diff --git "a/text/Domain_ids.tsv" "b/text/Domain_ids.tsv"
new file mode 100644--- /dev/null
+++ "b/text/Domain_ids.tsv"
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+At position 46 to 136, the domain is characterized as ATP-cone.
+At position 17 to 302, the domain is characterized as Protein kinase.
+At position 30 to 154, the domain is characterized as EamA 1.
+At position 206 to 324, the domain is characterized as EamA 2.
+At position 229 to 475, the domain is characterized as PPM-type phosphatase.
+At position 88 to 274, the domain is characterized as PXA.
+At position 390 to 529, the domain is characterized as RGS.
+At position 698 to 815, the domain is characterized as PX.
+At position 32 to 396, the domain is characterized as Protein kinase.
+At position 15 to 73, the domain is characterized as TRAM.
+At position 61 to 109, the domain is characterized as F-box.
+At position 170 to 212, the domain is characterized as CAP-Gly.
+At position 98 to 173, the domain is characterized as Smr.
+At position 28 to 142, the domain is characterized as CUB 1.
+At position 149 to 267, the domain is characterized as CUB 2.
+At position 277 to 427, the domain is characterized as F5/8 type C 1.
+At position 434 to 592, the domain is characterized as F5/8 type C 2.
+At position 642 to 802, the domain is characterized as MAM.
+At position 3 to 115, the domain is characterized as HIT.
+At position 1 to 58, the domain is characterized as HTH lacI-type.
+At position 19 to 79, the domain is characterized as HTH cro/C1-type.
+At position 164 to 380, the domain is characterized as Histidine kinase.
+At position 6 to 247, the domain is characterized as tr-type G.
+At position 19 to 607, the domain is characterized as Peptidase M2.
+At position 351 to 496, the domain is characterized as MATH.
+At position 4 to 368, the domain is characterized as Trm1 methyltransferase.
+At position 1 to 67, the domain is characterized as Core-binding (CB).
+At position 83 to 241, the domain is characterized as Tyr recombinase.
+At position 24 to 153, the domain is characterized as Bulb-type lectin.
+At position 292 to 344, the domain is characterized as EGF-like; atypical.
+At position 352 to 436, the domain is characterized as PAN.
+At position 521 to 795, the domain is characterized as Protein kinase.
+At position 130 to 225, the domain is characterized as Rhodanese.
+At position 1 to 72, the domain is characterized as S1-like.
+At position 219 to 246, the domain is characterized as PLD phosphodiesterase 1.
+At position 399 to 426, the domain is characterized as PLD phosphodiesterase 2.
+At position 27 to 70, the domain is characterized as LysM 1.
+At position 84 to 127, the domain is characterized as LysM 2.
+At position 147 to 190, the domain is characterized as LysM 3.
+At position 200 to 324, the domain is characterized as Peptidase C51.
+At position 163 to 248, the domain is characterized as PPIase FKBP-type.
+At position 90 to 181, the domain is characterized as Fibronectin type-III 1.
+At position 185 to 227, the domain is characterized as WR1.
+At position 330 to 417, the domain is characterized as Fibronectin type-III 2.
+At position 427 to 523, the domain is characterized as Fibronectin type-III 3.
+At position 619 to 710, the domain is characterized as Ig-like C2-type.
+At position 817 to 909, the domain is characterized as Fibronectin type-III 4.
+At position 187 to 354, the domain is characterized as tr-type G.
+At position 1 to 365, the domain is characterized as Trm1 methyltransferase.
+At position 291 to 453, the domain is characterized as Tyrosine-protein phosphatase.
+At position 35 to 324, the domain is characterized as ABC transmembrane type-1 1.
+At position 359 to 595, the domain is characterized as ABC transporter 1.
+At position 674 to 962, the domain is characterized as ABC transmembrane type-1 2.
+At position 999 to 1233, the domain is characterized as ABC transporter 2.
+At position 36 to 291, the domain is characterized as Protein kinase.
+At position 471 to 554, the domain is characterized as POLO box 1.
+At position 574 to 626, the domain is characterized as POLO box 2.
+At position 188 to 458, the domain is characterized as NR LBD.
+At position 15 to 194, the domain is characterized as Guanylate kinase-like.
+At position 44 to 207, the domain is characterized as Exonuclease.
+At position 248 to 326, the domain is characterized as GIY-YIG.
+At position 149 to 231, the domain is characterized as RRM 1.
+At position 259 to 337, the domain is characterized as RRM 2.
+At position 385 to 466, the domain is characterized as RRM 3.
+At position 23 to 180, the domain is characterized as Helicase ATP-binding.
+At position 426 to 588, the domain is characterized as Helicase C-terminal.
+At position 622 to 657, the domain is characterized as UVR.
+At position 14 to 97, the domain is characterized as GIY-YIG.
+At position 124 to 435, the domain is characterized as PPM-type phosphatase.
+At position 312 to 567, the domain is characterized as Protein kinase.
+At position 4 to 150, the domain is characterized as UBC core.
+At position 563 to 832, the domain is characterized as Protein kinase.
+At position 12 to 233, the domain is characterized as ABC transporter.
+At position 2 to 184, the domain is characterized as tr-type G.
+At position 110 to 194, the domain is characterized as PAZ.
+At position 436 to 760, the domain is characterized as Piwi.
+At position 578 to 733, the domain is characterized as STAS.
+At position 61 to 218, the domain is characterized as CP-type G.
+At position 314 to 548, the domain is characterized as NR LBD.
+At position 189 to 661, the domain is characterized as FERM.
+At position 380 to 476, the domain is characterized as PH.
+At position 119 to 308, the domain is characterized as ATP-grasp.
+At position 575 to 677, the domain is characterized as tRNA-binding.
+At position 61 to 162, the domain is characterized as Rieske.
+At position 75 to 292, the domain is characterized as Radical SAM core.
+At position 3 to 73, the domain is characterized as J.
+At position 14 to 105, the domain is characterized as Core-binding (CB).
+At position 126 to 309, the domain is characterized as Tyr recombinase.
+At position 43 to 226, the domain is characterized as MurNAc-LAA.
+At position 36 to 276, the domain is characterized as Radical SAM core.
+At position 146 to 318, the domain is characterized as Helicase ATP-binding.
+At position 396 to 543, the domain is characterized as Helicase C-terminal.
+At position 74 to 265, the domain is characterized as Macro.
+At position 3 to 167, the domain is characterized as EngA-type G 1.
+At position 205 to 380, the domain is characterized as EngA-type G 2.
+At position 381 to 465, the domain is characterized as KH-like.
+At position 10 to 214, the domain is characterized as tr-type G.
+At position 3 to 56, the domain is characterized as ClpX-type ZB.
+At position 44 to 137, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 180 to 210, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 357 to 496, the domain is characterized as DAGKc.
+At position 118 to 184, the domain is characterized as SAM.
+At position 1 to 61, the domain is characterized as HTH tetR-type.
+At position 185 to 369, the domain is characterized as Rho-GAP.
+At position 55 to 84, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 95 to 124, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 569 to 893, the domain is characterized as Reverse transcriptase.
+At position 1 to 159, the domain is characterized as Obg.
+At position 160 to 333, the domain is characterized as OBG-type G.
+At position 39 to 107, the domain is characterized as KH type-2.
+At position 111 to 322, the domain is characterized as Radical SAM core.
+At position 2 to 80, the domain is characterized as GST N-terminal.
+At position 82 to 215, the domain is characterized as GST C-terminal.
+At position 15 to 50, the domain is characterized as EF-hand 1.
+At position 81 to 116, the domain is characterized as EF-hand 2.
+At position 8 to 83, the domain is characterized as S1-like.
+At position 1 to 195, the domain is characterized as SMP-LTD.
+At position 18 to 133, the domain is characterized as Response regulatory.
+At position 507 to 582, the domain is characterized as PUA.
+At position 24 to 116, the domain is characterized as ARID.
+At position 17 to 105, the domain is characterized as Rhodanese.
+At position 141 to 322, the domain is characterized as Macro.
+At position 8 to 268, the domain is characterized as tr-type G.
+At position 44 to 83, the domain is characterized as EGF-like.
+At position 34 to 84, the domain is characterized as bHLH.
+At position 107 to 177, the domain is characterized as PAS 1.
+At position 262 to 332, the domain is characterized as PAS 2.
+At position 336 to 379, the domain is characterized as PAC.
+At position 23 to 75, the domain is characterized as bHLH.
+At position 38 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 31 to 88, the domain is characterized as Sushi.
+At position 103 to 345, the domain is characterized as Peptidase S1.
+At position 106 to 313, the domain is characterized as ATP-grasp.
+At position 315 to 361, the domain is characterized as G-patch.
+At position 33 to 105, the domain is characterized as Ig-like.
+At position 25 to 129, the domain is characterized as Phytocyanin.
+At position 7 to 174, the domain is characterized as Era-type G.
+At position 205 to 283, the domain is characterized as KH type-2.
+At position 31 to 205, the domain is characterized as EngB-type G.
+At position 1 to 107, the domain is characterized as Calponin-homology (CH).
+At position 187 to 249, the domain is characterized as LIM zinc-binding.
+At position 838 to 985, the domain is characterized as bMERB.
+At position 49 to 139, the domain is characterized as ATP-cone.
+At position 5 to 195, the domain is characterized as Glutamine amidotransferase type-1.
+At position 196 to 389, the domain is characterized as GMPS ATP-PPase.
+At position 21 to 149, the domain is characterized as RNase III.
+At position 176 to 245, the domain is characterized as DRBM.
+At position 4 to 165, the domain is characterized as EngA-type G 1.
+At position 180 to 357, the domain is characterized as EngA-type G 2.
+At position 358 to 443, the domain is characterized as KH-like.
+At position 24 to 308, the domain is characterized as Protein kinase.
+At position 16 to 80, the domain is characterized as TRAM.
+At position 688 to 762, the domain is characterized as Smr.
+At position 309 to 587, the domain is characterized as ABC transporter 1.
+At position 607 to 935, the domain is characterized as ABC transporter 2.
+At position 3 to 87, the domain is characterized as CS.
+At position 47 to 204, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 61, the domain is characterized as TGS.
+At position 4 to 235, the domain is characterized as ABC transporter.
+At position 17 to 80, the domain is characterized as S5 DRBM.
+At position 285 to 363, the domain is characterized as PUA.
+At position 42 to 95, the domain is characterized as TSP type-1.
+At position 99 to 136, the domain is characterized as LDL-receptor class A.
+At position 138 to 509, the domain is characterized as MACPF.
+At position 510 to 540, the domain is characterized as EGF-like.
+At position 24 to 139, the domain is characterized as MTTase N-terminal.
+At position 162 to 392, the domain is characterized as Radical SAM core.
+At position 395 to 465, the domain is characterized as TRAM.
+At position 55 to 288, the domain is characterized as Radical SAM core.
+At position 104 to 184, the domain is characterized as PRC barrel.
+At position 135 to 243, the domain is characterized as PET.
+At position 242 to 306, the domain is characterized as LIM zinc-binding 1.
+At position 307 to 367, the domain is characterized as LIM zinc-binding 2.
+At position 368 to 430, the domain is characterized as LIM zinc-binding 3.
+At position 114 to 323, the domain is characterized as ATP-grasp.
+At position 152 to 334, the domain is characterized as VWFA.
+At position 6 to 285, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 286 to 560, the domain is characterized as UvrD-like helicase C-terminal.
+At position 2 to 241, the domain is characterized as ABC transporter.
+At position 4 to 190, the domain is characterized as Flavodoxin-like.
+At position 46 to 264, the domain is characterized as Radical SAM core.
+At position 80 to 341, the domain is characterized as Protein kinase.
+At position 55 to 282, the domain is characterized as Radical SAM core.
+At position 31 to 302, the domain is characterized as GH18.
+At position 3 to 120, the domain is characterized as MTTase N-terminal.
+At position 143 to 375, the domain is characterized as Radical SAM core.
+At position 378 to 441, the domain is characterized as TRAM.
+At position 184 to 368, the domain is characterized as Macro.
+At position 126 to 310, the domain is characterized as ATP-grasp.
+At position 115 to 258, the domain is characterized as N-acetyltransferase.
+At position 8 to 290, the domain is characterized as tr-type G.
+At position 227 to 301, the domain is characterized as PUA.
+At position 8 to 68, the domain is characterized as HTH tetR-type.
+At position 43 to 327, the domain is characterized as Peptidase S1.
+At position 2 to 93, the domain is characterized as Glutaredoxin.
+At position 26 to 72, the domain is characterized as LRRNT.
+At position 371 to 424, the domain is characterized as LRRCT.
+At position 424 to 515, the domain is characterized as Ig-like C2-type.
+At position 525 to 617, the domain is characterized as Fibronectin type-III.
+At position 11 to 63, the domain is characterized as HTH myb-type 1.
+At position 64 to 118, the domain is characterized as HTH myb-type 2.
+At position 1 to 284, the domain is characterized as Deacetylase sirtuin-type.
+At position 132 to 226, the domain is characterized as Rhodanese.
+At position 1 to 380, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 145 to 239, the domain is characterized as GS beta-grasp.
+At position 246 to 571, the domain is characterized as GS catalytic.
+At position 277 to 355, the domain is characterized as PUA.
+At position 275 to 353, the domain is characterized as PUA.
+At position 98 to 332, the domain is characterized as Radical SAM core.
+At position 5 to 69, the domain is characterized as J.
+At position 6 to 70, the domain is characterized as J.
+At position 263 to 326, the domain is characterized as bZIP.
+At position 43 to 120, the domain is characterized as KH type-2.
+At position 30 to 139, the domain is characterized as Ig-like V-type 1.
+At position 145 to 236, the domain is characterized as Ig-like V-type 2.
+At position 322 to 518, the domain is characterized as B30.2/SPRY.
+At position 70 to 226, the domain is characterized as TIR.
+At position 97 to 162, the domain is characterized as S4 RNA-binding.
+At position 28 to 78, the domain is characterized as FHA.
+At position 90 to 261, the domain is characterized as Helicase ATP-binding.
+At position 285 to 433, the domain is characterized as Helicase C-terminal.
+At position 569 to 647, the domain is characterized as BRCT.
+At position 364 to 445, the domain is characterized as PDZ.
+At position 22 to 85, the domain is characterized as S5 DRBM.
+At position 37 to 85, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 84 to 170, the domain is characterized as Toprim.
+At position 12 to 154, the domain is characterized as Nudix hydrolase.
+At position 23 to 274, the domain is characterized as PPM-type phosphatase.
+At position 3 to 231, the domain is characterized as ABC transporter.
+At position 41 to 79, the domain is characterized as EGF-like 1.
+At position 80 to 120, the domain is characterized as EGF-like 2.
+At position 121 to 158, the domain is characterized as EGF-like 3.
+At position 160 to 197, the domain is characterized as EGF-like 4; calcium-binding.
+At position 199 to 236, the domain is characterized as EGF-like 5.
+At position 238 to 274, the domain is characterized as EGF-like 6; calcium-binding.
+At position 276 to 314, the domain is characterized as EGF-like 7.
+At position 316 to 352, the domain is characterized as EGF-like 8; calcium-binding.
+At position 353 to 391, the domain is characterized as EGF-like 9.
+At position 393 to 431, the domain is characterized as EGF-like 10; calcium-binding.
+At position 433 to 469, the domain is characterized as EGF-like 11; calcium-binding.
+At position 471 to 507, the domain is characterized as EGF-like 12; calcium-binding.
+At position 509 to 545, the domain is characterized as EGF-like 13; calcium-binding.
+At position 547 to 582, the domain is characterized as EGF-like 14; calcium-binding.
+At position 584 to 620, the domain is characterized as EGF-like 15; calcium-binding.
+At position 622 to 657, the domain is characterized as EGF-like 16; calcium-binding.
+At position 659 to 695, the domain is characterized as EGF-like 17; calcium-binding.
+At position 697 to 732, the domain is characterized as EGF-like 18.
+At position 736 to 772, the domain is characterized as EGF-like 19.
+At position 773 to 810, the domain is characterized as EGF-like 20.
+At position 812 to 849, the domain is characterized as EGF-like 21; calcium-binding.
+At position 851 to 887, the domain is characterized as EGF-like 22; calcium-binding.
+At position 889 to 924, the domain is characterized as EGF-like 23; calcium-binding.
+At position 926 to 962, the domain is characterized as EGF-like 24.
+At position 964 to 1000, the domain is characterized as EGF-like 25.
+At position 1002 to 1036, the domain is characterized as EGF-like 26.
+At position 1038 to 1084, the domain is characterized as EGF-like 27.
+At position 1086 to 1122, the domain is characterized as EGF-like 28.
+At position 1124 to 1160, the domain is characterized as EGF-like 29; calcium-binding.
+At position 1162 to 1205, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1207 to 1246, the domain is characterized as EGF-like 31.
+At position 1248 to 1289, the domain is characterized as EGF-like 32.
+At position 1291 to 1327, the domain is characterized as EGF-like 33.
+At position 1337 to 1375, the domain is characterized as EGF-like 34.
+At position 162 to 339, the domain is characterized as Helicase ATP-binding.
+At position 350 to 514, the domain is characterized as Helicase C-terminal.
+At position 1 to 181, the domain is characterized as KARI N-terminal Rossmann.
+At position 182 to 327, the domain is characterized as KARI C-terminal knotted.
+At position 37 to 724, the domain is characterized as Myosin motor.
+At position 728 to 748, the domain is characterized as IQ 1.
+At position 749 to 774, the domain is characterized as IQ 2.
+At position 782 to 971, the domain is characterized as TH1.
+At position 1101 to 1161, the domain is characterized as SH3.
+At position 10 to 70, the domain is characterized as Sm.
+At position 221 to 401, the domain is characterized as Helicase ATP-binding.
+At position 437 to 603, the domain is characterized as Helicase C-terminal.
+At position 4 to 193, the domain is characterized as Glutamine amidotransferase type-1.
+At position 194 to 384, the domain is characterized as GMPS ATP-PPase.
+At position 300 to 361, the domain is characterized as SH3.
+At position 2 to 91, the domain is characterized as PpiC.
+At position 43 to 207, the domain is characterized as Exonuclease.
+At position 9 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 199 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 190 to 249, the domain is characterized as CBS 1.
+At position 264 to 321, the domain is characterized as CBS 2.
+At position 12 to 52, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 53 to 99, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 106 to 147, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 148 to 196, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 33 to 279, the domain is characterized as CN hydrolase.
+At position 315 to 422, the domain is characterized as HIT.
+At position 136 to 319, the domain is characterized as Brix.
+At position 128 to 566, the domain is characterized as Urease.
+At position 9 to 277, the domain is characterized as tr-type G.
+At position 4 to 76, the domain is characterized as Sm.
+At position 656 to 912, the domain is characterized as Protein kinase.
+At position 11 to 85, the domain is characterized as U-box.
+At position 149 to 199, the domain is characterized as DHHC.
+At position 30 to 338, the domain is characterized as PPM-type phosphatase.
+At position 159 to 302, the domain is characterized as TRUD.
+At position 18 to 58, the domain is characterized as Saposin A-type 1.
+At position 59 to 142, the domain is characterized as Saposin B-type 1.
+At position 194 to 275, the domain is characterized as Saposin B-type 2.
+At position 311 to 392, the domain is characterized as Saposin B-type 3.
+At position 405 to 486, the domain is characterized as Saposin B-type 4.
+At position 488 to 524, the domain is characterized as Saposin A-type 2.
+At position 176 to 352, the domain is characterized as EngA-type G 2.
+At position 353 to 437, the domain is characterized as KH-like.
+At position 124 to 287, the domain is characterized as Integrase catalytic.
+At position 9 to 126, the domain is characterized as MSP.
+At position 1 to 243, the domain is characterized as Deacetylase sirtuin-type.
+At position 24 to 112, the domain is characterized as Ig-like.
+At position 281 to 491, the domain is characterized as NEL.
+At position 329 to 365, the domain is characterized as CBM1.
+At position 27 to 347, the domain is characterized as G-alpha.
+At position 2 to 93, the domain is characterized as ABM.
+At position 590 to 668, the domain is characterized as BRCT.
+At position 4 to 33, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 40 to 70, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 82 to 143, the domain is characterized as S4 RNA-binding.
+At position 219 to 392, the domain is characterized as PCI.
+At position 2 to 81, the domain is characterized as PUA.
+At position 402 to 524, the domain is characterized as RCK N-terminal.
+At position 25 to 176, the domain is characterized as Helicase ATP-binding.
+At position 429 to 591, the domain is characterized as Helicase C-terminal.
+At position 638 to 673, the domain is characterized as UVR.
+At position 5 to 235, the domain is characterized as ABC transporter.
+At position 71 to 184, the domain is characterized as Plastocyanin-like 1.
+At position 195 to 355, the domain is characterized as Plastocyanin-like 2.
+At position 431 to 551, the domain is characterized as Plastocyanin-like 3.
+At position 30 to 96, the domain is characterized as Sushi 1.
+At position 98 to 159, the domain is characterized as Sushi 2.
+At position 91 to 151, the domain is characterized as S4 RNA-binding.
+At position 41 to 97, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 97 to 329, the domain is characterized as Radical SAM core.
+At position 24 to 74, the domain is characterized as Clip.
+At position 110 to 364, the domain is characterized as Peptidase S1.
+At position 8 to 291, the domain is characterized as tr-type G.
+At position 112 to 344, the domain is characterized as ABC transporter.
+At position 250 to 438, the domain is characterized as GATase cobBQ-type.
+At position 5 to 81, the domain is characterized as GST N-terminal.
+At position 83 to 198, the domain is characterized as GST C-terminal.
+At position 54 to 238, the domain is characterized as BPL/LPL catalytic.
+At position 19 to 130, the domain is characterized as Thioredoxin 1.
+At position 131 to 251, the domain is characterized as Thioredoxin 2.
+At position 167 to 432, the domain is characterized as ABC transporter 1.
+At position 882 to 1125, the domain is characterized as ABC transporter 2.
+At position 27 to 214, the domain is characterized as RNase H type-2.
+At position 6 to 187, the domain is characterized as UmuC.
+At position 177 to 291, the domain is characterized as SPR.
+At position 24 to 106, the domain is characterized as Lipoyl-binding.
+At position 57 to 86, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 97 to 126, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 100, the domain is characterized as PE.
+At position 466 to 593, the domain is characterized as Guanylate cyclase.
+At position 1 to 277, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 278 to 562, the domain is characterized as UvrD-like helicase C-terminal.
+At position 16 to 269, the domain is characterized as Protein kinase.
+At position 291 to 334, the domain is characterized as UBA.
+At position 54 to 217, the domain is characterized as SIS.
+At position 132 to 194, the domain is characterized as t-SNARE coiled-coil homology.
+At position 19 to 81, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 140 to 202, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 43 to 297, the domain is characterized as Protein kinase.
+At position 298 to 350, the domain is characterized as AGC-kinase C-terminal.
+At position 8 to 234, the domain is characterized as Radical SAM core.
+At position 6 to 184, the domain is characterized as Guanylate kinase-like.
+At position 611 to 670, the domain is characterized as KH.
+At position 682 to 751, the domain is characterized as S1 motif.
+At position 69 to 231, the domain is characterized as CP-type G.
+At position 12 to 278, the domain is characterized as Protein kinase.
+At position 116 to 287, the domain is characterized as Helicase ATP-binding.
+At position 297 to 457, the domain is characterized as Helicase C-terminal.
+At position 17 to 362, the domain is characterized as tr-type G.
+At position 2 to 260, the domain is characterized as NodB homology.
+At position 3 to 153, the domain is characterized as Toprim.
+At position 64 to 374, the domain is characterized as AB hydrolase-1.
+At position 932 to 987, the domain is characterized as Bromo.
+At position 554 to 613, the domain is characterized as KH.
+At position 623 to 691, the domain is characterized as S1 motif.
+At position 108 to 245, the domain is characterized as MRH 1.
+At position 340 to 467, the domain is characterized as MRH 2.
+At position 204 to 267, the domain is characterized as bZIP.
+At position 33 to 203, the domain is characterized as Helicase ATP-binding.
+At position 214 to 375, the domain is characterized as Helicase C-terminal.
+At position 5 to 40, the domain is characterized as KOW.
+At position 13 to 99, the domain is characterized as KRAB.
+At position 9 to 244, the domain is characterized as ATP-grasp.
+At position 130 to 197, the domain is characterized as KH 1.
+At position 282 to 346, the domain is characterized as KH 2.
+At position 869 to 932, the domain is characterized as SAM.
+At position 365 to 600, the domain is characterized as NR LBD.
+At position 5 to 70, the domain is characterized as J.
+At position 40 to 219, the domain is characterized as Helicase ATP-binding.
+At position 245 to 390, the domain is characterized as Helicase C-terminal.
+At position 1 to 181, the domain is characterized as RNase H type-2.
+At position 1 to 76, the domain is characterized as Lipoyl-binding 1.
+At position 113 to 188, the domain is characterized as Lipoyl-binding 2.
+At position 242 to 279, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 35 to 131, the domain is characterized as PH.
+At position 9 to 310, the domain is characterized as Protein kinase.
+At position 309 to 385, the domain is characterized as Ubiquitin-like.
+At position 6 to 132, the domain is characterized as MATH.
+At position 2 to 77, the domain is characterized as Carrier.
+At position 533 to 708, the domain is characterized as Helicase ATP-binding.
+At position 883 to 1041, the domain is characterized as Helicase C-terminal.
+At position 19 to 93, the domain is characterized as PAS.
+At position 93 to 147, the domain is characterized as PAC 1.
+At position 232 to 281, the domain is characterized as PAC 2.
+At position 723 to 786, the domain is characterized as R3H.
+At position 1 to 177, the domain is characterized as Obg.
+At position 178 to 348, the domain is characterized as OBG-type G.
+At position 1046 to 1299, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 357, the domain is characterized as SAM-dependent MTase C5-type.
+At position 130 to 169, the domain is characterized as STI1 1.
+At position 492 to 531, the domain is characterized as STI1 2.
+At position 1 to 61, the domain is characterized as LCN-type CS-alpha/beta.
+At position 26 to 317, the domain is characterized as Protein kinase.
+At position 25 to 199, the domain is characterized as EngB-type G.
+At position 120 to 491, the domain is characterized as Protein kinase.
+At position 27 to 268, the domain is characterized as ABC transporter.
+At position 4 to 102, the domain is characterized as PTS EIIA type-3.
+At position 2 to 78, the domain is characterized as Cytochrome b5 heme-binding.
+At position 78 to 178, the domain is characterized as Fe2OG dioxygenase.
+At position 4 to 126, the domain is characterized as TsaA-like.
+At position 71 to 211, the domain is characterized as SCP.
+At position 447 to 538, the domain is characterized as RRM 1.
+At position 555 to 637, the domain is characterized as RRM 2.
+At position 42 to 105, the domain is characterized as S4 RNA-binding.
+At position 9 to 123, the domain is characterized as Response regulatory.
+At position 274 to 364, the domain is characterized as Ras-associating.
+At position 366 to 413, the domain is characterized as SARAH.
+At position 154 to 215, the domain is characterized as CBS 1.
+At position 238 to 296, the domain is characterized as CBS 2.
+At position 323 to 382, the domain is characterized as CBS 3.
+At position 439 to 508, the domain is characterized as CBS 4.
+At position 33 to 224, the domain is characterized as RNase H type-2.
+At position 74 to 121, the domain is characterized as bZIP.
+At position 27 to 204, the domain is characterized as BPL/LPL catalytic.
+At position 68 to 173, the domain is characterized as PRD 1.
+At position 174 to 282, the domain is characterized as PRD 2.
+At position 54 to 91, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 7 to 146, the domain is characterized as SprT-like.
+At position 232 to 306, the domain is characterized as U-box.
+At position 55 to 218, the domain is characterized as SIS.
+At position 5 to 122, the domain is characterized as WH1.
+At position 201 to 257, the domain is characterized as KBD.
+At position 308 to 416, the domain is characterized as SPR.
+At position 9 to 90, the domain is characterized as PDZ 1.
+At position 128 to 215, the domain is characterized as PDZ 2.
+At position 243 to 323, the domain is characterized as PDZ 3.
+At position 378 to 458, the domain is characterized as PDZ 4.
+At position 106 to 326, the domain is characterized as Radical SAM core.
+At position 5 to 227, the domain is characterized as Radical SAM core.
+At position 139 to 258, the domain is characterized as C2 1.
+At position 270 to 403, the domain is characterized as C2 2.
+At position 2 to 135, the domain is characterized as HTH marR-type.
+At position 91 to 284, the domain is characterized as DH.
+At position 301 to 459, the domain is characterized as PH.
+At position 484 to 613, the domain is characterized as C2.
+At position 647 to 845, the domain is characterized as Rho-GAP.
+At position 208 to 275, the domain is characterized as PAS 1.
+At position 348 to 414, the domain is characterized as PAS 2.
+At position 422 to 465, the domain is characterized as PAC.
+At position 60 to 223, the domain is characterized as SIS.
+At position 5 to 241, the domain is characterized as PABS.
+At position 160 to 253, the domain is characterized as PPIase FKBP-type.
+At position 13 to 194, the domain is characterized as tr-type G.
+At position 214 to 375, the domain is characterized as TrmE-type G.
+At position 253 to 317, the domain is characterized as EamA.
+At position 3 to 89, the domain is characterized as ACB.
+At position 8 to 181, the domain is characterized as Clp R.
+At position 246 to 413, the domain is characterized as W2.
+At position 3 to 73, the domain is characterized as RRM 1.
+At position 129 to 202, the domain is characterized as RRM 2.
+At position 97 to 190, the domain is characterized as SH2.
+At position 627 to 766, the domain is characterized as VPS9.
+At position 796 to 887, the domain is characterized as Ras-associating.
+At position 504 to 567, the domain is characterized as bZIP.
+At position 12 to 100, the domain is characterized as MtN3/slv 1.
+At position 136 to 221, the domain is characterized as MtN3/slv 2.
+At position 18 to 133, the domain is characterized as MTTase N-terminal.
+At position 150 to 391, the domain is characterized as Radical SAM core.
+At position 394 to 466, the domain is characterized as TRAM.
+At position 639 to 717, the domain is characterized as BRCT.
+At position 69 to 183, the domain is characterized as Plastocyanin-like 1.
+At position 469 to 562, the domain is characterized as Plastocyanin-like 3.
+At position 43 to 157, the domain is characterized as TBDR plug.
+At position 160 to 624, the domain is characterized as TBDR beta-barrel.
+At position 3 to 244, the domain is characterized as ABC transporter 1.
+At position 299 to 533, the domain is characterized as ABC transporter 2.
+At position 2 to 116, the domain is characterized as Response regulatory.
+At position 38 to 106, the domain is characterized as KH type-2.
+At position 98 to 163, the domain is characterized as S4 RNA-binding.
+At position 27 to 104, the domain is characterized as EMI.
+At position 98 to 133, the domain is characterized as EGF-like 1.
+At position 141 to 176, the domain is characterized as EGF-like 2.
+At position 184 to 219, the domain is characterized as EGF-like 3.
+At position 227 to 261, the domain is characterized as EGF-like 4.
+At position 274 to 304, the domain is characterized as EGF-like 5.
+At position 312 to 347, the domain is characterized as EGF-like 6.
+At position 401 to 436, the domain is characterized as EGF-like 7.
+At position 444 to 479, the domain is characterized as EGF-like 8.
+At position 487 to 522, the domain is characterized as EGF-like 9.
+At position 573 to 608, the domain is characterized as EGF-like 10.
+At position 616 to 653, the domain is characterized as EGF-like 11.
+At position 666 to 696, the domain is characterized as EGF-like 12.
+At position 709 to 739, the domain is characterized as EGF-like 13.
+At position 747 to 782, the domain is characterized as EGF-like 14.
+At position 795 to 825, the domain is characterized as EGF-like 15.
+At position 1 to 82, the domain is characterized as GST N-terminal.
+At position 89 to 213, the domain is characterized as GST C-terminal.
+At position 49 to 124, the domain is characterized as Carrier.
+At position 16 to 221, the domain is characterized as Radical SAM core.
+At position 24 to 170, the domain is characterized as VOC.
+At position 610 to 691, the domain is characterized as BRCT.
+At position 1590 to 1916, the domain is characterized as PIPK.
+At position 1 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 43 to 111, the domain is characterized as KH type-2.
+At position 169 to 341, the domain is characterized as OBG-type G.
+At position 39 to 117, the domain is characterized as RRM 1.
+At position 125 to 205, the domain is characterized as RRM 2.
+At position 284 to 362, the domain is characterized as RRM 3.
+At position 29 to 360, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 20 to 108, the domain is characterized as PPIase FKBP-type.
+At position 77 to 152, the domain is characterized as Carrier.
+At position 531 to 741, the domain is characterized as STAS.
+At position 226 to 279, the domain is characterized as HAMP.
+At position 320 to 556, the domain is characterized as Methyl-accepting transducer.
+At position 2 to 29, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 37 to 66, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 188, the domain is characterized as tr-type G.
+At position 52 to 210, the domain is characterized as Thioredoxin.
+At position 542 to 776, the domain is characterized as NR LBD.
+At position 30 to 164, the domain is characterized as Nudix hydrolase.
+At position 35 to 365, the domain is characterized as USP.
+At position 179 to 444, the domain is characterized as NR LBD.
+At position 198 to 324, the domain is characterized as RabBD.
+At position 827 to 950, the domain is characterized as C2 1.
+At position 967 to 1086, the domain is characterized as C2 2.
+At position 169 to 303, the domain is characterized as TIR.
+At position 257 to 331, the domain is characterized as POU-specific.
+At position 50 to 177, the domain is characterized as PH.
+At position 277 to 456, the domain is characterized as Helicase ATP-binding.
+At position 481 to 639, the domain is characterized as Helicase C-terminal.
+At position 32 to 341, the domain is characterized as Protein kinase.
+At position 206 to 348, the domain is characterized as VLRF1.
+At position 4 to 203, the domain is characterized as DPCK.
+At position 122 to 196, the domain is characterized as COMM.
+At position 90 to 256, the domain is characterized as Nudix hydrolase.
+At position 220 to 413, the domain is characterized as Helicase ATP-binding.
+At position 424 to 585, the domain is characterized as Helicase C-terminal.
+At position 43 to 293, the domain is characterized as Protein kinase.
+At position 308 to 476, the domain is characterized as VWFA.
+At position 21 to 92, the domain is characterized as RRM.
+At position 199 to 259, the domain is characterized as KH.
+At position 325 to 418, the domain is characterized as HD.
+At position 51 to 290, the domain is characterized as Radical SAM core.
+At position 3 to 119, the domain is characterized as Response regulatory.
+At position 152 to 346, the domain is characterized as CheB-type methylesterase.
+At position 29 to 231, the domain is characterized as DPCK.
+At position 25 to 145, the domain is characterized as Ricin B-type lectin 1.
+At position 158 to 296, the domain is characterized as Ricin B-type lectin 2.
+At position 93 to 310, the domain is characterized as Radical SAM core.
+At position 853 to 880, the domain is characterized as PLD phosphodiesterase 1.
+At position 1249 to 1276, the domain is characterized as PLD phosphodiesterase 2.
+At position 166 to 394, the domain is characterized as NR LBD.
+At position 51 to 176, the domain is characterized as TBDR plug.
+At position 187 to 908, the domain is characterized as TBDR beta-barrel.
+At position 29 to 202, the domain is characterized as FAD-binding PCMH-type.
+At position 74 to 389, the domain is characterized as IF rod.
+At position 2 to 142, the domain is characterized as PTS EIIA type-2.
+At position 286 to 376, the domain is characterized as HPr 1.
+At position 410 to 499, the domain is characterized as HPr 2.
+At position 25 to 249, the domain is characterized as Peptidase S1.
+At position 422 to 725, the domain is characterized as Reverse transcriptase.
+At position 16 to 156, the domain is characterized as CheW-like.
+At position 2 to 40, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 41 to 83, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 89 to 129, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 130 to 172, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 57 to 153, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 312 to 460, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 1654 to 1716, the domain is characterized as PWWP.
+At position 1788 to 1838, the domain is characterized as AWS.
+At position 1840 to 1957, the domain is characterized as SET.
+At position 1964 to 1980, the domain is characterized as Post-SET.
+At position 65 to 224, the domain is characterized as CP-type G.
+At position 165 to 255, the domain is characterized as 5'-3' exonuclease.
+At position 369 to 397, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 407 to 436, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 68, the domain is characterized as J.
+At position 66 to 330, the domain is characterized as Protein kinase.
+At position 4 to 57, the domain is characterized as ClpX-type ZB.
+At position 9 to 68, the domain is characterized as Sm.
+At position 3 to 147, the domain is characterized as Clp R.
+At position 5 to 53, the domain is characterized as SpoVT-AbrB 1.
+At position 82 to 125, the domain is characterized as SpoVT-AbrB 2.
+At position 3 to 35, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 37 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 216 to 312, the domain is characterized as PH 1.
+At position 409 to 503, the domain is characterized as PH 2.
+At position 23 to 65, the domain is characterized as CHCH.
+At position 126 to 253, the domain is characterized as Nudix hydrolase.
+At position 222 to 282, the domain is characterized as SH3.
+At position 254 to 393, the domain is characterized as Flavodoxin-like.
+At position 423 to 474, the domain is characterized as Rubredoxin-like.
+At position 53 to 112, the domain is characterized as EamA.
+At position 2 to 69, the domain is characterized as J.
+At position 36 to 158, the domain is characterized as RUN.
+At position 771 to 873, the domain is characterized as PH.
+At position 7 to 175, the domain is characterized as Era-type G.
+At position 206 to 283, the domain is characterized as KH type-2.
+At position 29 to 160, the domain is characterized as Nudix hydrolase.
+At position 19 to 64, the domain is characterized as F-box.
+At position 1 to 182, the domain is characterized as KARI N-terminal Rossmann.
+At position 183 to 328, the domain is characterized as KARI C-terminal knotted.
+At position 1 to 142, the domain is characterized as RNase H type-1.
+At position 1 to 67, the domain is characterized as HTH OST-type 1.
+At position 220 to 289, the domain is characterized as HTH OST-type 2.
+At position 330 to 398, the domain is characterized as HTH OST-type 3.
+At position 494 to 551, the domain is characterized as Tudor 1.
+At position 684 to 741, the domain is characterized as Tudor 2.
+At position 17 to 50, the domain is characterized as LRRNT.
+At position 421 to 474, the domain is characterized as LRRCT.
+At position 9 to 151, the domain is characterized as N-acetyltransferase.
+At position 244 to 503, the domain is characterized as Olfactomedin-like.
+At position 39 to 108, the domain is characterized as KH type-2.
+At position 1 to 158, the domain is characterized as Obg.
+At position 159 to 329, the domain is characterized as OBG-type G.
+At position 352 to 430, the domain is characterized as OCT.
+At position 89 to 149, the domain is characterized as S4 RNA-binding.
+At position 1 to 249, the domain is characterized as IMD.
+At position 340 to 403, the domain is characterized as SH3.
+At position 153 to 198, the domain is characterized as CAP-Gly 1.
+At position 253 to 286, the domain is characterized as CAP-Gly 2.
+At position 489 to 532, the domain is characterized as CAP-Gly 3.
+At position 589 to 947, the domain is characterized as USP.
+At position 38 to 149, the domain is characterized as sHSP.
+At position 104 to 180, the domain is characterized as UBX.
+At position 9 to 119, the domain is characterized as MTTase N-terminal.
+At position 136 to 373, the domain is characterized as Radical SAM core.
+At position 376 to 441, the domain is characterized as TRAM.
+At position 85 to 314, the domain is characterized as ABC transmembrane type-1.
+At position 25 to 239, the domain is characterized as tr-type G.
+At position 39 to 95, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 10 to 263, the domain is characterized as ABC transporter.
+At position 97 to 213, the domain is characterized as TBDR plug.
+At position 220 to 990, the domain is characterized as TBDR beta-barrel.
+At position 11 to 231, the domain is characterized as Radical SAM core.
+At position 3 to 139, the domain is characterized as PINc.
+At position 106 to 269, the domain is characterized as Helicase ATP-binding.
+At position 294 to 466, the domain is characterized as Helicase C-terminal.
+At position 94 to 386, the domain is characterized as ABC transmembrane type-1.
+At position 474 to 729, the domain is characterized as ABC transporter.
+At position 51 to 227, the domain is characterized as Helicase ATP-binding.
+At position 433 to 602, the domain is characterized as Helicase C-terminal.
+At position 630 to 722, the domain is characterized as Dicer dsRNA-binding fold.
+At position 895 to 1042, the domain is characterized as PAZ.
+At position 1277 to 1404, the domain is characterized as RNase III 1.
+At position 1665 to 1823, the domain is characterized as RNase III 2.
+At position 1848 to 1913, the domain is characterized as DRBM.
+At position 174 to 272, the domain is characterized as HTH araC/xylS-type.
+At position 2 to 303, the domain is characterized as Glutamine amidotransferase type-2.
+At position 377 to 516, the domain is characterized as SIS 1.
+At position 544 to 689, the domain is characterized as SIS 2.
+At position 99 to 154, the domain is characterized as CBS 1.
+At position 156 to 212, the domain is characterized as CBS 2.
+At position 83 to 178, the domain is characterized as Toprim.
+At position 39 to 148, the domain is characterized as tRNA-binding.
+At position 401 to 476, the domain is characterized as B5.
+At position 701 to 794, the domain is characterized as FDX-ACB.
+At position 47 to 111, the domain is characterized as SH3b 1.
+At position 116 to 178, the domain is characterized as SH3b 2.
+At position 146 to 525, the domain is characterized as GRAS.
+At position 3 to 166, the domain is characterized as N-acetyltransferase.
+At position 251 to 439, the domain is characterized as GATase cobBQ-type.
+At position 162 to 327, the domain is characterized as CP-type G.
+At position 20 to 137, the domain is characterized as AB hydrolase-1.
+At position 1050 to 1118, the domain is characterized as S1 motif.
+At position 1167 to 1262, the domain is characterized as SH2.
+At position 125 to 213, the domain is characterized as Ig-like C1-type.
+At position 1 to 76, the domain is characterized as Ubiquitin-like.
+At position 41 to 105, the domain is characterized as SH3b.
+At position 122 to 286, the domain is characterized as MurNAc-LAA.
+At position 106 to 268, the domain is characterized as JmjC.
+At position 26 to 137, the domain is characterized as sHSP.
+At position 18 to 106, the domain is characterized as Rhodanese.
+At position 7 to 201, the domain is characterized as AMMECR1.
+At position 5 to 220, the domain is characterized as ABC transporter.
+At position 1 to 163, the domain is characterized as CN hydrolase.
+At position 263 to 400, the domain is characterized as MPN.
+At position 7 to 156, the domain is characterized as Ferritin-like diiron.
+At position 303 to 551, the domain is characterized as Glutamine amidotransferase type-1.
+At position 79 to 137, the domain is characterized as TCP.
+At position 192 to 209, the domain is characterized as R.
+At position 686 to 799, the domain is characterized as SMC hinge.
+At position 64 to 310, the domain is characterized as ABC transporter.
+At position 14 to 224, the domain is characterized as START.
+At position 2 to 90, the domain is characterized as GST C-terminal.
+At position 29 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 9 to 88, the domain is characterized as PUA.
+At position 146 to 198, the domain is characterized as BSD.
+At position 179 to 381, the domain is characterized as Pentraxin (PTX).
+At position 598 to 657, the domain is characterized as KH.
+At position 669 to 738, the domain is characterized as S1 motif.
+At position 6 to 245, the domain is characterized as ABC transporter.
+At position 60 to 402, the domain is characterized as Kinesin motor.
+At position 61 to 165, the domain is characterized as THUMP.
+At position 24 to 59, the domain is characterized as EF-hand 1.
+At position 60 to 95, the domain is characterized as EF-hand 2.
+At position 97 to 132, the domain is characterized as EF-hand 3.
+At position 133 to 168, the domain is characterized as EF-hand 4.
+At position 2 to 235, the domain is characterized as PABS.
+At position 351 to 416, the domain is characterized as S4 RNA-binding.
+At position 13 to 140, the domain is characterized as Peptidase C39.
+At position 170 to 452, the domain is characterized as ABC transmembrane type-1.
+At position 486 to 722, the domain is characterized as ABC transporter.
+At position 122 to 365, the domain is characterized as Radical SAM core.
+At position 362 to 429, the domain is characterized as S4 RNA-binding.
+At position 357 to 399, the domain is characterized as CCT.
+At position 43 to 73, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 89 to 118, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 51 to 238, the domain is characterized as FAD-binding PCMH-type.
+At position 63 to 288, the domain is characterized as OBG-type G.
+At position 288 to 363, the domain is characterized as TGS.
+At position 8 to 282, the domain is characterized as tr-type G.
+At position 71 to 145, the domain is characterized as Lipoyl-binding.
+At position 5 to 341, the domain is characterized as Kinesin motor.
+At position 1 to 54, the domain is characterized as ClpX-type ZB.
+At position 70 to 258, the domain is characterized as RNase H type-2.
+At position 264 to 495, the domain is characterized as NR LBD.
+At position 1 to 141, the domain is characterized as Nudix hydrolase.
+At position 1 to 10, the domain is characterized as Gla.
+At position 11 to 20, the domain is characterized as Peptidase S1.
+At position 4 to 121, the domain is characterized as TIR.
+At position 41 to 139, the domain is characterized as Cyclin N-terminal.
+At position 55 to 284, the domain is characterized as Ferric oxidoreductase.
+At position 285 to 395, the domain is characterized as FAD-binding FR-type.
+At position 10 to 88, the domain is characterized as RRM.
+At position 99 to 293, the domain is characterized as ATP-grasp.
+At position 3 to 125, the domain is characterized as Peptidase C39.
+At position 154 to 436, the domain is characterized as ABC transmembrane type-1.
+At position 468 to 703, the domain is characterized as ABC transporter.
+At position 41 to 212, the domain is characterized as FAD-binding PCMH-type.
+At position 606 to 689, the domain is characterized as BRCT.
+At position 5 to 127, the domain is characterized as Glycine radical.
+At position 374 to 543, the domain is characterized as tr-type G.
+At position 129 to 567, the domain is characterized as Urease.
+At position 2 to 157, the domain is characterized as Thioredoxin.
+At position 4 to 252, the domain is characterized as ABC transporter.
+At position 1 to 141, the domain is characterized as Toprim.
+At position 7 to 205, the domain is characterized as DPCK.
+At position 4 to 167, the domain is characterized as EngA-type G 1.
+At position 175 to 350, the domain is characterized as EngA-type G 2.
+At position 351 to 435, the domain is characterized as KH-like.
+At position 277 to 350, the domain is characterized as Collagen-like.
+At position 357 to 457, the domain is characterized as SRCR.
+At position 8 to 229, the domain is characterized as Radical SAM core.
+At position 28 to 189, the domain is characterized as E1.
+At position 291 to 341, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 374 to 565, the domain is characterized as E2.
+At position 2 to 115, the domain is characterized as PINc.
+At position 2 to 218, the domain is characterized as Glutamine amidotransferase type-2.
+At position 284 to 423, the domain is characterized as SIS 1.
+At position 453 to 591, the domain is characterized as SIS 2.
+At position 30 to 91, the domain is characterized as PUB.
+At position 454 to 654, the domain is characterized as PAW.
+At position 26 to 116, the domain is characterized as Apple 1.
+At position 123 to 209, the domain is characterized as Apple 2.
+At position 221 to 725, the domain is characterized as ZP.
+At position 5 to 257, the domain is characterized as Pyruvate carboxyltransferase.
+At position 11 to 97, the domain is characterized as Acylphosphatase-like.
+At position 48 to 219, the domain is characterized as Helicase ATP-binding.
+At position 228 to 422, the domain is characterized as Helicase C-terminal.
+At position 25 to 248, the domain is characterized as Peptidase S1.
+At position 49 to 176, the domain is characterized as MARVEL.
+At position 78 to 173, the domain is characterized as Toprim.
+At position 563 to 664, the domain is characterized as tRNA-binding.
+At position 1 to 36, the domain is characterized as Pacifastin.
+At position 1 to 227, the domain is characterized as Peptidase S1.
+At position 17 to 214, the domain is characterized as Lon N-terminal.
+At position 605 to 787, the domain is characterized as Lon proteolytic.
+At position 252 to 393, the domain is characterized as C2.
+At position 595 to 630, the domain is characterized as PLD phosphodiesterase 1.
+At position 929 to 956, the domain is characterized as PLD phosphodiesterase 2.
+At position 42 to 135, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 178 to 208, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 23 to 244, the domain is characterized as Alpha-carbonic anhydrase.
+At position 9 to 253, the domain is characterized as ATP-grasp.
+At position 3 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 395, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 84, the domain is characterized as Core-binding (CB).
+At position 105 to 289, the domain is characterized as Tyr recombinase.
+At position 277 to 339, the domain is characterized as J.
+At position 92 to 199, the domain is characterized as PET.
+At position 234 to 297, the domain is characterized as LIM zinc-binding 1.
+At position 299 to 359, the domain is characterized as LIM zinc-binding 2.
+At position 362 to 421, the domain is characterized as LIM zinc-binding 3.
+At position 30 to 261, the domain is characterized as Laminin N-terminal.
+At position 262 to 331, the domain is characterized as Laminin EGF-like 1.
+At position 332 to 394, the domain is characterized as Laminin EGF-like 2.
+At position 395 to 448, the domain is characterized as Laminin EGF-like 3.
+At position 506 to 627, the domain is characterized as NTR.
+At position 273 to 422, the domain is characterized as YDG.
+At position 73 to 262, the domain is characterized as ABC transmembrane type-1.
+At position 177 to 347, the domain is characterized as Helicase ATP-binding.
+At position 375 to 519, the domain is characterized as Helicase C-terminal.
+At position 6 to 128, the domain is characterized as MATH.
+At position 8 to 146, the domain is characterized as MABP.
+At position 215 to 266, the domain is characterized as UMA.
+At position 316 to 595, the domain is characterized as ABC transporter 1.
+At position 615 to 944, the domain is characterized as ABC transporter 2.
+At position 5 to 185, the domain is characterized as KARI N-terminal Rossmann.
+At position 186 to 331, the domain is characterized as KARI C-terminal knotted.
+At position 3 to 72, the domain is characterized as HTH merR-type.
+At position 40 to 224, the domain is characterized as EngB-type G.
+At position 71 to 102, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 112 to 141, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 24 to 205, the domain is characterized as EngB-type G.
+At position 77 to 173, the domain is characterized as Fe2OG dioxygenase.
+At position 12 to 83, the domain is characterized as S1 motif.
+At position 21 to 56, the domain is characterized as EF-hand 1.
+At position 60 to 88, the domain is characterized as EF-hand 2.
+At position 90 to 125, the domain is characterized as EF-hand 3.
+At position 131 to 166, the domain is characterized as EF-hand 4.
+At position 3 to 70, the domain is characterized as PAS 1.
+At position 129 to 198, the domain is characterized as PAS 2.
+At position 199 to 251, the domain is characterized as PAC.
+At position 283 to 410, the domain is characterized as GGDEF.
+At position 4 to 186, the domain is characterized as tr-type G.
+At position 44 to 172, the domain is characterized as VIT.
+At position 299 to 467, the domain is characterized as VWFA.
+At position 160 to 306, the domain is characterized as TRUD.
+At position 1 to 145, the domain is characterized as MGS-like.
+At position 4 to 79, the domain is characterized as Carrier.
+At position 96 to 307, the domain is characterized as NR LBD.
+At position 403 to 485, the domain is characterized as RCK C-terminal.
+At position 36 to 198, the domain is characterized as SIS.
+At position 198 to 394, the domain is characterized as Peptidase M12B.
+At position 10 to 206, the domain is characterized as tr-type G.
+At position 38 to 69, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 2 to 92, the domain is characterized as ABM.
+At position 28 to 202, the domain is characterized as Exonuclease.
+At position 66 to 173, the domain is characterized as HTH APSES-type.
+At position 153 to 223, the domain is characterized as Bromo.
+At position 12 to 234, the domain is characterized as YjeF N-terminal.
+At position 53 to 142, the domain is characterized as PPIase FKBP-type.
+At position 26 to 219, the domain is characterized as GH16.
+At position 86 to 142, the domain is characterized as PAC.
+At position 177 to 396, the domain is characterized as PPM-type phosphatase.
+At position 546 to 653, the domain is characterized as STAS.
+At position 39 to 128, the domain is characterized as S1 motif.
+At position 56 to 138, the domain is characterized as SCAN box.
+At position 225 to 304, the domain is characterized as KRAB.
+At position 1 to 47, the domain is characterized as Gla.
+At position 230 to 497, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 48 to 168, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 187 to 295, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 337 to 504, the domain is characterized as tr-type G.
+At position 410 to 613, the domain is characterized as Helicase ATP-binding.
+At position 624 to 787, the domain is characterized as Helicase C-terminal.
+At position 147 to 223, the domain is characterized as RRM.
+At position 94 to 168, the domain is characterized as PRC barrel.
+At position 15 to 60, the domain is characterized as UBA.
+At position 276 to 341, the domain is characterized as SH3.
+At position 281 to 359, the domain is characterized as PUA.
+At position 33 to 253, the domain is characterized as Protein kinase.
+At position 32 to 70, the domain is characterized as EGF-like.
+At position 15 to 92, the domain is characterized as Ubiquitin-like.
+At position 198 to 261, the domain is characterized as bZIP.
+At position 352 to 412, the domain is characterized as S4 RNA-binding.
+At position 1 to 141, the domain is characterized as RNase H type-1.
+At position 46 to 110, the domain is characterized as Sushi 1.
+At position 111 to 168, the domain is characterized as Sushi 2.
+At position 169 to 230, the domain is characterized as Sushi 3.
+At position 232 to 295, the domain is characterized as Sushi 4.
+At position 277 to 354, the domain is characterized as PUA.
+At position 23 to 126, the domain is characterized as AB hydrolase-1.
+At position 52 to 149, the domain is characterized as SWIRM.
+At position 288 to 339, the domain is characterized as SANT.
+At position 201 to 425, the domain is characterized as tr-type G.
+At position 112 to 301, the domain is characterized as ATP-grasp.
+At position 46 to 223, the domain is characterized as EngB-type G.
+At position 206 to 393, the domain is characterized as DH.
+At position 422 to 521, the domain is characterized as PH 1.
+At position 643 to 740, the domain is characterized as PH 2.
+At position 174 to 281, the domain is characterized as PH.
+At position 640 to 818, the domain is characterized as C2 DOCK-type.
+At position 1605 to 2069, the domain is characterized as DOCKER.
+At position 141 to 336, the domain is characterized as ATP-grasp 1.
+At position 688 to 879, the domain is characterized as ATP-grasp 2.
+At position 952 to 1092, the domain is characterized as MGS-like.
+At position 21 to 257, the domain is characterized as ABC transporter 1.
+At position 256 to 511, the domain is characterized as ABC transporter 2.
+At position 663 to 824, the domain is characterized as Helicase ATP-binding.
+At position 842 to 999, the domain is characterized as Helicase C-terminal.
+At position 227 to 302, the domain is characterized as PUA.
+At position 310 to 356, the domain is characterized as G-patch.
+At position 205 to 379, the domain is characterized as MARVEL.
+At position 451 to 562, the domain is characterized as OCEL.
+At position 35 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 308 to 615, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 130 to 568, the domain is characterized as Urease.
+At position 91 to 282, the domain is characterized as ABC transmembrane type-1.
+At position 146 to 267, the domain is characterized as Peptidase C51.
+At position 5 to 184, the domain is characterized as Guanylate kinase-like.
+At position 15 to 220, the domain is characterized as Cytochrome b561.
+At position 32 to 330, the domain is characterized as F5/8 type A 1.
+At position 32 to 196, the domain is characterized as Plastocyanin-like 1.
+At position 206 to 330, the domain is characterized as Plastocyanin-like 2.
+At position 351 to 685, the domain is characterized as F5/8 type A 2.
+At position 351 to 529, the domain is characterized as Plastocyanin-like 3.
+At position 539 to 685, the domain is characterized as Plastocyanin-like 4.
+At position 824 to 1143, the domain is characterized as F5/8 type A 3.
+At position 824 to 992, the domain is characterized as Plastocyanin-like 5.
+At position 1001 to 1143, the domain is characterized as Plastocyanin-like 6.
+At position 1147 to 1298, the domain is characterized as F5/8 type C 1.
+At position 1303 to 1457, the domain is characterized as F5/8 type C 2.
+At position 2 to 31, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 39 to 68, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 263 to 325, the domain is characterized as t-SNARE coiled-coil homology.
+At position 81 to 365, the domain is characterized as ABC transmembrane type-1 1.
+At position 423 to 646, the domain is characterized as ABC transporter 1.
+At position 854 to 1153, the domain is characterized as ABC transmembrane type-1 2.
+At position 1208 to 1439, the domain is characterized as ABC transporter 2.
+At position 59 to 222, the domain is characterized as SIS.
+At position 47 to 120, the domain is characterized as KH type-2.
+At position 2 to 103, the domain is characterized as FAD-binding FR-type.
+At position 722 to 797, the domain is characterized as HSA.
+At position 985 to 1045, the domain is characterized as Myb-like.
+At position 35 to 326, the domain is characterized as YjeF C-terminal.
+At position 3 to 370, the domain is characterized as TTL.
+At position 14 to 55, the domain is characterized as JmjN.
+At position 79 to 169, the domain is characterized as ARID.
+At position 468 to 634, the domain is characterized as JmjC.
+At position 24 to 106, the domain is characterized as RH1.
+At position 130 to 201, the domain is characterized as RH2.
+At position 24 to 155, the domain is characterized as Ig-like.
+At position 3 to 221, the domain is characterized as ABC transporter.
+At position 2 to 124, the domain is characterized as PTS EIIA type-4.
+At position 157 to 320, the domain is characterized as PTS EIIB type-4.
+At position 674 to 871, the domain is characterized as Helicase ATP-binding.
+At position 1113 to 1277, the domain is characterized as Helicase C-terminal.
+At position 5 to 91, the domain is characterized as Acylphosphatase-like.
+At position 10 to 42, the domain is characterized as LisH.
+At position 149 to 253, the domain is characterized as HTH LytTR-type.
+At position 99 to 339, the domain is characterized as Radical SAM core.
+At position 108 to 165, the domain is characterized as FHA.
+At position 352 to 418, the domain is characterized as S4 RNA-binding.
+At position 3 to 58, the domain is characterized as bHLH.
+At position 300 to 512, the domain is characterized as PCI.
+At position 21 to 211, the domain is characterized as RNase H type-2.
+At position 10 to 125, the domain is characterized as MTTase N-terminal.
+At position 146 to 388, the domain is characterized as Radical SAM core.
+At position 390 to 462, the domain is characterized as TRAM.
+At position 220 to 311, the domain is characterized as PDZ.
+At position 349 to 401, the domain is characterized as Myosin N-terminal SH3-like.
+At position 405 to 1181, the domain is characterized as Myosin motor.
+At position 1184 to 1213, the domain is characterized as IQ.
+At position 23 to 158, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 4 to 68, the domain is characterized as J.
+At position 74 to 291, the domain is characterized as Radical SAM core.
+At position 49 to 155, the domain is characterized as Calponin-homology (CH).
+At position 592 to 672, the domain is characterized as BRCT.
+At position 1 to 36, the domain is characterized as EF-hand 1.
+At position 37 to 72, the domain is characterized as EF-hand 2.
+At position 74 to 109, the domain is characterized as EF-hand 3.
+At position 112 to 147, the domain is characterized as EF-hand 4.
+At position 10 to 285, the domain is characterized as tr-type G.
+At position 59 to 250, the domain is characterized as HD.
+At position 29 to 176, the domain is characterized as Thioredoxin.
+At position 8 to 43, the domain is characterized as EF-hand 1.
+At position 44 to 79, the domain is characterized as EF-hand 2.
+At position 81 to 116, the domain is characterized as EF-hand 3.
+At position 117 to 149, the domain is characterized as EF-hand 4.
+At position 28 to 63, the domain is characterized as EF-hand 1.
+At position 97 to 132, the domain is characterized as EF-hand 2.
+At position 133 to 168, the domain is characterized as EF-hand 3.
+At position 580 to 641, the domain is characterized as CBS 1.
+At position 676 to 734, the domain is characterized as CBS 2.
+At position 1 to 157, the domain is characterized as Obg.
+At position 158 to 330, the domain is characterized as OBG-type G.
+At position 335 to 411, the domain is characterized as OCT.
+At position 74 to 254, the domain is characterized as B30.2/SPRY.
+At position 81 to 176, the domain is characterized as Toprim.
+At position 7 to 131, the domain is characterized as Longin.
+At position 139 to 199, the domain is characterized as v-SNARE coiled-coil homology.
+At position 30 to 269, the domain is characterized as Laminin N-terminal.
+At position 270 to 325, the domain is characterized as Laminin EGF-like 1.
+At position 326 to 381, the domain is characterized as Laminin EGF-like 2.
+At position 382 to 428, the domain is characterized as Laminin EGF-like 3.
+At position 429 to 478, the domain is characterized as Laminin EGF-like 4.
+At position 505 to 673, the domain is characterized as Laminin IV type A.
+At position 708 to 756, the domain is characterized as Laminin EGF-like 5.
+At position 757 to 811, the domain is characterized as Laminin EGF-like 6.
+At position 812 to 867, the domain is characterized as Laminin EGF-like 7.
+At position 868 to 918, the domain is characterized as Laminin EGF-like 8.
+At position 919 to 966, the domain is characterized as Laminin EGF-like 9.
+At position 967 to 1014, the domain is characterized as Laminin EGF-like 10.
+At position 74 to 265, the domain is characterized as ABC transmembrane type-1.
+At position 21 to 78, the domain is characterized as Sushi 1.
+At position 79 to 136, the domain is characterized as Sushi 2.
+At position 137 to 193, the domain is characterized as Sushi 3.
+At position 64 to 133, the domain is characterized as S1 motif 1.
+At position 227 to 331, the domain is characterized as S1 motif 2.
+At position 36 to 189, the domain is characterized as PID.
+At position 3 to 107, the domain is characterized as PH.
+At position 126 to 230, the domain is characterized as IRS-type PTB.
+At position 3 to 87, the domain is characterized as YcgL.
+At position 118 to 230, the domain is characterized as DUF1279.
+At position 148 to 256, the domain is characterized as SEA.
+At position 531 to 578, the domain is characterized as GPS.
+At position 86 to 142, the domain is characterized as BRX 1.
+At position 274 to 329, the domain is characterized as BRX 2.
+At position 36 to 286, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 45 to 112, the domain is characterized as BTB.
+At position 147 to 249, the domain is characterized as BACK.
+At position 69 to 117, the domain is characterized as WAP.
+At position 1 to 48, the domain is characterized as ClpX-type ZB.
+At position 182 to 274, the domain is characterized as PH.
+At position 440 to 512, the domain is characterized as PAS.
+At position 102 to 247, the domain is characterized as N-acetyltransferase.
+At position 10 to 203, the domain is characterized as tr-type G.
+At position 35 to 184, the domain is characterized as C2 PI3K-type.
+At position 283 to 520, the domain is characterized as PIK helical.
+At position 605 to 871, the domain is characterized as PI3K/PI4K catalytic.
+At position 24 to 141, the domain is characterized as HD.
+At position 15 to 169, the domain is characterized as FAD-binding PCMH-type.
+At position 468 to 590, the domain is characterized as HD.
+At position 709 to 789, the domain is characterized as ACT 1.
+At position 816 to 890, the domain is characterized as ACT 2.
+At position 307 to 578, the domain is characterized as Protein kinase.
+At position 1 to 55, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 58 to 198, the domain is characterized as FAD-binding FR-type.
+At position 13 to 268, the domain is characterized as Protein kinase.
+At position 306 to 331, the domain is characterized as NAF.
+At position 97 to 170, the domain is characterized as PRC barrel.
+At position 12 to 137, the domain is characterized as RNase III.
+At position 162 to 231, the domain is characterized as DRBM.
+At position 178 to 412, the domain is characterized as NR LBD.
+At position 29 to 115, the domain is characterized as PNT.
+At position 482 to 501, the domain is characterized as UIM 1.
+At position 528 to 547, the domain is characterized as UIM 2.
+At position 564 to 583, the domain is characterized as UIM 3.
+At position 589 to 605, the domain is characterized as UIM 4.
+At position 27 to 367, the domain is characterized as Transferrin-like.
+At position 1 to 250, the domain is characterized as Deacetylase sirtuin-type.
+At position 32 to 79, the domain is characterized as F-box.
+At position 6 to 40, the domain is characterized as WW.
+At position 58 to 383, the domain is characterized as Peptidase A1.
+At position 4 to 204, the domain is characterized as DPCK.
+At position 83 to 182, the domain is characterized as Toprim.
+At position 2 to 182, the domain is characterized as KARI N-terminal Rossmann.
+At position 4 to 234, the domain is characterized as ABC transporter.
+At position 79 to 148, the domain is characterized as Cyclin N-terminal.
+At position 2 to 217, the domain is characterized as ABC transporter.
+At position 577 to 627, the domain is characterized as LRRCT.
+At position 670 to 813, the domain is characterized as TIR.
+At position 58 to 91, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 188 to 393, the domain is characterized as Histidine kinase.
+At position 17 to 111, the domain is characterized as Ig-like.
+At position 111 to 315, the domain is characterized as ATP-grasp.
+At position 321 to 414, the domain is characterized as BRCT.
+At position 10 to 207, the domain is characterized as tr-type G.
+At position 2 to 246, the domain is characterized as ABC transporter 1.
+At position 313 to 527, the domain is characterized as ABC transporter 2.
+At position 28 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 342 to 578, the domain is characterized as ABC transporter.
+At position 27 to 75, the domain is characterized as HNH.
+At position 177 to 274, the domain is characterized as Rhodanese.
+At position 210 to 273, the domain is characterized as KH.
+At position 336 to 429, the domain is characterized as HD.
+At position 25 to 113, the domain is characterized as RH1.
+At position 456 to 526, the domain is characterized as RH2.
+At position 14 to 195, the domain is characterized as PPIase cyclophilin-type.
+At position 22 to 272, the domain is characterized as ABC transporter.
+At position 11 to 90, the domain is characterized as RRM 1.
+At position 111 to 188, the domain is characterized as RRM 2.
+At position 289 to 364, the domain is characterized as RRM 3.
+At position 96 to 172, the domain is characterized as PRC barrel.
+At position 101 to 211, the domain is characterized as C-type lectin.
+At position 100 to 206, the domain is characterized as THUMP.
+At position 78 to 177, the domain is characterized as Fe2OG dioxygenase.
+At position 38 to 256, the domain is characterized as Radical SAM core.
+At position 542 to 644, the domain is characterized as tRNA-binding.
+At position 345 to 397, the domain is characterized as HAMP 1.
+At position 439 to 493, the domain is characterized as HAMP 2.
+At position 512 to 748, the domain is characterized as Methyl-accepting transducer.
+At position 34 to 288, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 4 to 63, the domain is characterized as CSD.
+At position 12 to 161, the domain is characterized as MPN.
+At position 149 to 187, the domain is characterized as F-box.
+At position 16 to 95, the domain is characterized as GIY-YIG.
+At position 208 to 243, the domain is characterized as UVR.
+At position 295 to 434, the domain is characterized as N-acetyltransferase.
+At position 8 to 118, the domain is characterized as MTTase N-terminal.
+At position 137 to 375, the domain is characterized as Radical SAM core.
+At position 378 to 443, the domain is characterized as TRAM.
+At position 3 to 117, the domain is characterized as Response regulatory.
+At position 142 to 246, the domain is characterized as HTH LytTR-type.
+At position 22 to 150, the domain is characterized as C-type lysozyme.
+At position 33 to 300, the domain is characterized as Pyruvate carboxyltransferase.
+At position 707 to 782, the domain is characterized as Smr.
+At position 58 to 174, the domain is characterized as MTTase N-terminal.
+At position 197 to 433, the domain is characterized as Radical SAM core.
+At position 436 to 504, the domain is characterized as TRAM.
+At position 1 to 64, the domain is characterized as TGS.
+At position 115 to 198, the domain is characterized as PDZ.
+At position 163 to 300, the domain is characterized as PH 1.
+At position 325 to 437, the domain is characterized as PH 2.
+At position 484 to 540, the domain is characterized as SU.
+At position 1 to 76, the domain is characterized as Ubiquitin-like 1.
+At position 77 to 152, the domain is characterized as Ubiquitin-like 2.
+At position 153 to 228, the domain is characterized as Ubiquitin-like 3.
+At position 229 to 304, the domain is characterized as Ubiquitin-like 4.
+At position 305 to 380, the domain is characterized as Ubiquitin-like 5.
+At position 17 to 46, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 70 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 227, the domain is characterized as Radical SAM core.
+At position 8 to 152, the domain is characterized as Flavodoxin-like.
+At position 210 to 457, the domain is characterized as FAD-binding FR-type.
+At position 94 to 157, the domain is characterized as S4 RNA-binding.
+At position 34 to 196, the domain is characterized as SIS.
+At position 533 to 621, the domain is characterized as MCM.
+At position 6 to 236, the domain is characterized as ABC transporter.
+At position 28 to 130, the domain is characterized as Phytocyanin.
+At position 279 to 357, the domain is characterized as PUA.
+At position 186 to 381, the domain is characterized as ATP-grasp 1.
+At position 742 to 954, the domain is characterized as ATP-grasp 2.
+At position 1026 to 1162, the domain is characterized as MGS-like.
+At position 328 to 481, the domain is characterized as N-acetyltransferase.
+At position 10 to 475, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 476 to 786, the domain is characterized as UvrD-like helicase C-terminal.
+At position 22 to 247, the domain is characterized as ABC transporter.
+At position 18 to 53, the domain is characterized as EF-hand.
+At position 100 to 173, the domain is characterized as PRC barrel.
+At position 11 to 78, the domain is characterized as H15.
+At position 8 to 90, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 173 to 347, the domain is characterized as PCI.
+At position 2 to 165, the domain is characterized as N-acetyltransferase.
+At position 33 to 301, the domain is characterized as Protein kinase 1.
+At position 302 to 371, the domain is characterized as AGC-kinase C-terminal.
+At position 417 to 674, the domain is characterized as Protein kinase 2.
+At position 2 to 135, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 5 to 92, the domain is characterized as Acylphosphatase-like.
+At position 2 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 218 to 386, the domain is characterized as Helicase ATP-binding.
+At position 586 to 736, the domain is characterized as Helicase C-terminal.
+At position 86 to 278, the domain is characterized as DCUN1.
+At position 3 to 147, the domain is characterized as Toprim.
+At position 31 to 148, the domain is characterized as Ig-like C2-type.
+At position 231 to 459, the domain is characterized as NR LBD.
+At position 32 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 310, the domain is characterized as Plastocyanin-like 2.
+At position 413 to 549, the domain is characterized as Plastocyanin-like 3.
+At position 250 to 437, the domain is characterized as GATase cobBQ-type.
+At position 35 to 126, the domain is characterized as IGFBP N-terminal.
+At position 216 to 298, the domain is characterized as Thyroglobulin type-1.
+At position 1 to 84, the domain is characterized as PDZ.
+At position 292 to 351, the domain is characterized as LIM zinc-binding.
+At position 29 to 190, the domain is characterized as CBM3.
+At position 291 to 428, the domain is characterized as Cohesin 1.
+At position 435 to 570, the domain is characterized as Cohesin 2.
+At position 668 to 801, the domain is characterized as Cohesin 3.
+At position 810 to 943, the domain is characterized as Cohesin 4.
+At position 952 to 1085, the domain is characterized as Cohesin 5.
+At position 1094 to 1227, the domain is characterized as Cohesin 6.
+At position 1236 to 1369, the domain is characterized as Cohesin 7.
+At position 1377 to 1511, the domain is characterized as Cohesin 8.
+At position 1709 to 1847, the domain is characterized as Cohesin 9.
+At position 5 to 137, the domain is characterized as HTH marR-type.
+At position 2 to 88, the domain is characterized as Core-binding (CB).
+At position 109 to 288, the domain is characterized as Tyr recombinase.
+At position 25 to 412, the domain is characterized as Helicase ATP-binding.
+At position 429 to 582, the domain is characterized as Helicase C-terminal.
+At position 632 to 667, the domain is characterized as UVR.
+At position 73 to 249, the domain is characterized as FAD-binding PCMH-type.
+At position 74 to 262, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 117, the domain is characterized as Response regulatory.
+At position 306 to 382, the domain is characterized as RRM.
+At position 187 to 374, the domain is characterized as Glutamine amidotransferase type-1.
+At position 62 to 232, the domain is characterized as Helicase ATP-binding.
+At position 243 to 404, the domain is characterized as Helicase C-terminal.
+At position 283 to 653, the domain is characterized as GRAS.
+At position 3 to 166, the domain is characterized as EngA-type G 1.
+At position 211 to 384, the domain is characterized as EngA-type G 2.
+At position 385 to 469, the domain is characterized as KH-like.
+At position 1 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 10 to 217, the domain is characterized as tr-type G.
+At position 1 to 37, the domain is characterized as Chitin-binding type R&R.
+At position 2 to 188, the domain is characterized as Glutamine amidotransferase type-2.
+At position 217 to 466, the domain is characterized as Asparagine synthetase.
+At position 2 to 104, the domain is characterized as Thioredoxin.
+At position 32 to 202, the domain is characterized as Helicase ATP-binding.
+At position 229 to 373, the domain is characterized as Helicase C-terminal.
+At position 128 to 169, the domain is characterized as UBA.
+At position 20 to 158, the domain is characterized as SprT-like.
+At position 25 to 280, the domain is characterized as Protein kinase.
+At position 302 to 326, the domain is characterized as NAF.
+At position 644 to 733, the domain is characterized as BRCT.
+At position 103 to 225, the domain is characterized as MPN.
+At position 13 to 260, the domain is characterized as CN hydrolase.
+At position 5 to 116, the domain is characterized as MTTase N-terminal.
+At position 140 to 370, the domain is characterized as Radical SAM core.
+At position 372 to 442, the domain is characterized as TRAM.
+At position 139 to 303, the domain is characterized as GAF.
+At position 510 to 721, the domain is characterized as Histidine kinase.
+At position 42 to 728, the domain is characterized as Myosin motor.
+At position 732 to 752, the domain is characterized as IQ 1.
+At position 753 to 778, the domain is characterized as IQ 2.
+At position 786 to 980, the domain is characterized as TH1.
+At position 1184 to 1243, the domain is characterized as SH3.
+At position 188 to 357, the domain is characterized as tr-type G.
+At position 83 to 177, the domain is characterized as GS beta-grasp.
+At position 184 to 509, the domain is characterized as GS catalytic.
+At position 59 to 221, the domain is characterized as TIR.
+At position 241 to 480, the domain is characterized as NB-ARC.
+At position 48 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 131 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 24 to 108, the domain is characterized as DEP.
+At position 282 to 322, the domain is characterized as Rho-GAP.
+At position 12 to 176, the domain is characterized as TIR.
+At position 191 to 447, the domain is characterized as NB-ARC.
+At position 43 to 180, the domain is characterized as Nudix hydrolase.
+At position 29 to 203, the domain is characterized as EngB-type G.
+At position 1 to 101, the domain is characterized as SSB.
+At position 1 to 68, the domain is characterized as REM-1 1.
+At position 149 to 226, the domain is characterized as REM-1 2.
+At position 229 to 349, the domain is characterized as C2.
+At position 849 to 1108, the domain is characterized as Protein kinase.
+At position 1109 to 1174, the domain is characterized as AGC-kinase C-terminal.
+At position 61 to 125, the domain is characterized as CSD.
+At position 19 to 234, the domain is characterized as Radical SAM core.
+At position 43 to 320, the domain is characterized as ZP.
+At position 133 to 327, the domain is characterized as ATP-grasp 1.
+At position 671 to 861, the domain is characterized as ATP-grasp 2.
+At position 930 to 1058, the domain is characterized as MGS-like.
+At position 3 to 274, the domain is characterized as DegV.
+At position 221 to 280, the domain is characterized as PAP-associated.
+At position 32 to 81, the domain is characterized as F-box.
+At position 372 to 421, the domain is characterized as FBD.
+At position 35 to 262, the domain is characterized as Cupin type-1 1.
+At position 311 to 460, the domain is characterized as Cupin type-1 2.
+At position 1 to 308, the domain is characterized as 5'-3' exonuclease.
+At position 394 to 630, the domain is characterized as 3'-5' exonuclease.
+At position 25 to 269, the domain is characterized as ABC transporter.
+At position 360 to 572, the domain is characterized as ABC transmembrane type-2.
+At position 7 to 39, the domain is characterized as LisH.
+At position 71 to 190, the domain is characterized as Rhodanese.
+At position 247 to 390, the domain is characterized as Tyrosine-protein phosphatase.
+At position 7 to 190, the domain is characterized as YrdC-like.
+At position 200 to 288, the domain is characterized as RCK C-terminal 1.
+At position 292 to 373, the domain is characterized as RCK C-terminal 2.
+At position 2 to 283, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 287 to 354, the domain is characterized as ACT.
+At position 20 to 87, the domain is characterized as LCN-type CS-alpha/beta.
+At position 122 to 429, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 1 to 59, the domain is characterized as HTH lysR-type.
+At position 354 to 521, the domain is characterized as tr-type G.
+At position 1116 to 1369, the domain is characterized as Glutamine amidotransferase type-1.
+At position 561 to 643, the domain is characterized as S1 motif.
+At position 209 to 500, the domain is characterized as GH10.
+At position 22 to 104, the domain is characterized as Lipoyl-binding.
+At position 83 to 215, the domain is characterized as FAS1.
+At position 39 to 94, the domain is characterized as FHA.
+At position 193 to 246, the domain is characterized as HAMP.
+At position 254 to 466, the domain is characterized as Histidine kinase.
+At position 3 to 66, the domain is characterized as J.
+At position 39 to 98, the domain is characterized as Ig-like C2-type 1.
+At position 127 to 196, the domain is characterized as Ig-like C2-type 2.
+At position 32 to 354, the domain is characterized as G-alpha.
+At position 46 to 86, the domain is characterized as LDL-receptor class A.
+At position 2 to 61, the domain is characterized as AFP-like.
+At position 287 to 362, the domain is characterized as PUA.
+At position 4 to 64, the domain is characterized as L27.
+At position 224 to 310, the domain is characterized as PDZ 1.
+At position 318 to 404, the domain is characterized as PDZ 2.
+At position 465 to 545, the domain is characterized as PDZ 3.
+At position 580 to 650, the domain is characterized as SH3.
+At position 721 to 896, the domain is characterized as Guanylate kinase-like.
+At position 104 to 287, the domain is characterized as ATP-grasp.
+At position 48 to 126, the domain is characterized as SCAN box.
+At position 164 to 237, the domain is characterized as KRAB.
+At position 11 to 74, the domain is characterized as S5 DRBM.
+At position 80 to 175, the domain is characterized as Toprim.
+At position 42 to 286, the domain is characterized as Peptidase S1.
+At position 6 to 59, the domain is characterized as ClpX-type ZB.
+At position 98 to 128, the domain is characterized as KOW.
+At position 44 to 142, the domain is characterized as Rieske.
+At position 29 to 106, the domain is characterized as Ig-like C2-type.
+At position 238 to 329, the domain is characterized as Fibronectin type-III.
+At position 32 to 91, the domain is characterized as 4Fe-4S.
+At position 108 to 137, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 138 to 167, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 9 to 280, the domain is characterized as tr-type G.
+At position 509 to 601, the domain is characterized as ELM2.
+At position 616 to 667, the domain is characterized as SANT.
+At position 269 to 390, the domain is characterized as SET.
+At position 21 to 341, the domain is characterized as Protein kinase.
+At position 342 to 408, the domain is characterized as AGC-kinase C-terminal.
+At position 45 to 76, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 50 to 113, the domain is characterized as S5 DRBM.
+At position 54 to 397, the domain is characterized as GH18.
+At position 2 to 78, the domain is characterized as Lipoyl-binding.
+At position 128 to 165, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 31 to 175, the domain is characterized as MARVEL.
+At position 163 to 279, the domain is characterized as HD.
+At position 384 to 553, the domain is characterized as tr-type G.
+At position 2 to 133, the domain is characterized as DAGKc.
+At position 42 to 110, the domain is characterized as J.
+At position 2 to 119, the domain is characterized as Response regulatory.
+At position 149 to 214, the domain is characterized as HTH luxR-type.
+At position 9 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 208 to 400, the domain is characterized as GMPS ATP-PPase.
+At position 20 to 117, the domain is characterized as Ig-like.
+At position 105 to 368, the domain is characterized as Protein kinase.
+At position 411 to 446, the domain is characterized as EF-hand 1.
+At position 447 to 482, the domain is characterized as EF-hand 2.
+At position 483 to 518, the domain is characterized as EF-hand 3.
+At position 520 to 553, the domain is characterized as EF-hand 4.
+At position 54 to 109, the domain is characterized as Death.
+At position 159 to 293, the domain is characterized as TIR.
+At position 2 to 228, the domain is characterized as ABC transporter.
+At position 14 to 80, the domain is characterized as PQ-loop 1.
+At position 178 to 233, the domain is characterized as PQ-loop 2.
+At position 15 to 134, the domain is characterized as PX.
+At position 100 to 301, the domain is characterized as ATP-grasp.
+At position 392 to 453, the domain is characterized as PWWP.
+At position 98 to 161, the domain is characterized as S4 RNA-binding.
+At position 97 to 384, the domain is characterized as tr-type G.
+At position 1 to 174, the domain is characterized as TCTP.
+At position 3 to 132, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 18 to 187, the domain is characterized as N-acetyltransferase.
+At position 242 to 296, the domain is characterized as bHLH.
+At position 22 to 224, the domain is characterized as Laminin G-like.
+At position 319 to 376, the domain is characterized as VWFC.
+At position 382 to 432, the domain is characterized as TSP type-1 1.
+At position 438 to 493, the domain is characterized as TSP type-1 2.
+At position 495 to 550, the domain is characterized as TSP type-1 3.
+At position 550 to 590, the domain is characterized as EGF-like 1.
+At position 649 to 693, the domain is characterized as EGF-like 2.
+At position 961 to 1173, the domain is characterized as TSP C-terminal.
+At position 120 to 365, the domain is characterized as Radical SAM core.
+At position 8 to 161, the domain is characterized as Exonuclease.
+At position 241 to 496, the domain is characterized as Helicase ATP-binding.
+At position 703 to 893, the domain is characterized as Helicase C-terminal.
+At position 169 to 254, the domain is characterized as PPIase FKBP-type.
+At position 8 to 126, the domain is characterized as C2 B9-type.
+At position 70 to 145, the domain is characterized as ACT.
+At position 4 to 73, the domain is characterized as HTH merR-type.
+At position 10 to 205, the domain is characterized as tr-type G.
+At position 168 to 259, the domain is characterized as CS.
+At position 44 to 73, the domain is characterized as EF-hand 2.
+At position 78 to 113, the domain is characterized as EF-hand 3.
+At position 114 to 149, the domain is characterized as EF-hand 4.
+At position 11 to 223, the domain is characterized as ABC transmembrane type-1.
+At position 293 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 81 to 171, the domain is characterized as CTCK.
+At position 90 to 154, the domain is characterized as J.
+At position 71 to 239, the domain is characterized as tr-type G.
+At position 463 to 499, the domain is characterized as EGF-like 1.
+At position 501 to 534, the domain is characterized as EGF-like 2.
+At position 650 to 684, the domain is characterized as EGF-like 3.
+At position 716 to 753, the domain is characterized as EGF-like 4.
+At position 29 to 74, the domain is characterized as SpoVT-AbrB.
+At position 9 to 62, the domain is characterized as LIM zinc-binding 1.
+At position 71 to 125, the domain is characterized as LIM zinc-binding 2.
+At position 68 to 186, the domain is characterized as MTTase N-terminal.
+At position 209 to 440, the domain is characterized as Radical SAM core.
+At position 442 to 505, the domain is characterized as TRAM.
+At position 20 to 97, the domain is characterized as Ubiquitin-like.
+At position 197 to 249, the domain is characterized as HAMP.
+At position 366 to 583, the domain is characterized as Histidine kinase.
+At position 104 to 176, the domain is characterized as PRC barrel.
+At position 504 to 533, the domain is characterized as IQ.
+At position 3 to 73, the domain is characterized as S4 RNA-binding.
+At position 128 to 250, the domain is characterized as MPN.
+At position 519 to 737, the domain is characterized as STAS.
+At position 43 to 155, the domain is characterized as FAD-binding FR-type.
+At position 2 to 242, the domain is characterized as ABC transporter.
+At position 43 to 313, the domain is characterized as Protein kinase.
+At position 3 to 57, the domain is characterized as MADS-box.
+At position 84 to 174, the domain is characterized as K-box.
+At position 31 to 149, the domain is characterized as MTTase N-terminal.
+At position 172 to 402, the domain is characterized as Radical SAM core.
+At position 405 to 468, the domain is characterized as TRAM.
+At position 17 to 56, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 57 to 101, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 107 to 148, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 149 to 191, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 47 to 67, the domain is characterized as IQ.
+At position 32 to 353, the domain is characterized as G-alpha.
+At position 6 to 244, the domain is characterized as ABC transporter.
+At position 6 to 92, the domain is characterized as Core-binding (CB).
+At position 113 to 292, the domain is characterized as Tyr recombinase.
+At position 7 to 117, the domain is characterized as MTTase N-terminal.
+At position 134 to 371, the domain is characterized as Radical SAM core.
+At position 374 to 440, the domain is characterized as TRAM.
+At position 246 to 470, the domain is characterized as Collagen IV NC1.
+At position 7 to 145, the domain is characterized as SprT-like.
+At position 1 to 99, the domain is characterized as Plastocyanin-like.
+At position 29 to 102, the domain is characterized as Importin N-terminal.
+At position 63 to 106, the domain is characterized as CWF21.
+At position 47 to 280, the domain is characterized as Radical SAM core.
+At position 4 to 124, the domain is characterized as MTTase N-terminal.
+At position 147 to 379, the domain is characterized as Radical SAM core.
+At position 382 to 444, the domain is characterized as TRAM.
+At position 41 to 343, the domain is characterized as AB hydrolase-1.
+At position 33 to 160, the domain is characterized as MARVEL.
+At position 5 to 143, the domain is characterized as SprT-like.
+At position 3 to 142, the domain is characterized as PTS EIIA type-2.
+At position 111 to 199, the domain is characterized as RRM.
+At position 1869 to 1986, the domain is characterized as SET.
+At position 1992 to 2008, the domain is characterized as Post-SET.
+At position 694 to 790, the domain is characterized as PilZ.
+At position 72 to 148, the domain is characterized as Biotinyl-binding.
+At position 10 to 231, the domain is characterized as ABC transporter.
+At position 36 to 132, the domain is characterized as BRCT.
+At position 208 to 399, the domain is characterized as Helicase ATP-binding.
+At position 427 to 579, the domain is characterized as Helicase C-terminal.
+At position 5 to 243, the domain is characterized as ABC transporter.
+At position 32 to 268, the domain is characterized as ABC transporter.
+At position 29 to 276, the domain is characterized as BAR.
+At position 520 to 593, the domain is characterized as SH3.
+At position 35 to 115, the domain is characterized as Doublecortin.
+At position 26 to 116, the domain is characterized as Ig-like C2-type 1.
+At position 115 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 260 to 373, the domain is characterized as Ig-like C2-type 3.
+At position 376 to 469, the domain is characterized as Ig-like C2-type 4.
+At position 474 to 564, the domain is characterized as Ig-like C2-type 5.
+At position 695 to 1040, the domain is characterized as Protein kinase; inactive.
+At position 195 to 453, the domain is characterized as Protein kinase.
+At position 290 to 541, the domain is characterized as Glutamine amidotransferase type-1.
+At position 144 to 432, the domain is characterized as ABC transmembrane type-1.
+At position 466 to 702, the domain is characterized as ABC transporter.
+At position 374 to 413, the domain is characterized as UBA 1.
+At position 424 to 470, the domain is characterized as UBA 2.
+At position 489 to 529, the domain is characterized as UBA 3.
+At position 125 to 175, the domain is characterized as DHHC.
+At position 141 to 305, the domain is characterized as JmjC.
+At position 329 to 535, the domain is characterized as PCI.
+At position 56 to 164, the domain is characterized as sHSP.
+At position 7 to 164, the domain is characterized as Obg.
+At position 165 to 345, the domain is characterized as OBG-type G.
+At position 363 to 441, the domain is characterized as OCT.
+At position 279 to 439, the domain is characterized as Helicase ATP-binding.
+At position 462 to 618, the domain is characterized as Helicase C-terminal.
+At position 20 to 233, the domain is characterized as Peptidase S1.
+At position 31 to 142, the domain is characterized as DOMON.
+At position 40 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 315 to 391, the domain is characterized as Ig-like C2-type 4.
+At position 413 to 472, the domain is characterized as Ig-like C2-type 5.
+At position 488 to 578, the domain is characterized as Ig-like C2-type 6.
+At position 1 to 129, the domain is characterized as C-type lysozyme.
+At position 12 to 101, the domain is characterized as ACB.
+At position 176 to 351, the domain is characterized as EngA-type G 2.
+At position 352 to 436, the domain is characterized as KH-like.
+At position 92 to 371, the domain is characterized as Protein kinase.
+At position 74 to 293, the domain is characterized as ABC transporter.
+At position 45 to 76, the domain is characterized as LRRNT.
+At position 301 to 353, the domain is characterized as LRRCT.
+At position 354 to 442, the domain is characterized as Ig-like C2-type.
+At position 36 to 140, the domain is characterized as Calponin-homology (CH) 1.
+At position 149 to 255, the domain is characterized as Calponin-homology (CH) 2.
+At position 776 to 811, the domain is characterized as EF-hand 1.
+At position 817 to 852, the domain is characterized as EF-hand 2.
+At position 13 to 209, the domain is characterized as DPCK.
+At position 1 to 99, the domain is characterized as SSB.
+At position 458 to 517, the domain is characterized as PAP-associated.
+At position 5 to 238, the domain is characterized as PABS.
+At position 220 to 464, the domain is characterized as CN hydrolase.
+At position 22 to 122, the domain is characterized as Fibronectin type-III 1.
+At position 124 to 224, the domain is characterized as Fibronectin type-III 2.
+At position 292 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 225 to 459, the domain is characterized as PABS.
+At position 46 to 114, the domain is characterized as BTB.
+At position 1 to 116, the domain is characterized as HTH marR-type.
+At position 40 to 109, the domain is characterized as EamA.
+At position 3 to 116, the domain is characterized as Response regulatory.
+At position 3 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 29 to 317, the domain is characterized as GH18.
+At position 121 to 165, the domain is characterized as LysM 1.
+At position 171 to 215, the domain is characterized as LysM 2.
+At position 295 to 339, the domain is characterized as LysM 3.
+At position 345 to 389, the domain is characterized as LysM 4.
+At position 4 to 185, the domain is characterized as UmuC.
+At position 50 to 117, the domain is characterized as BTB.
+At position 1 to 131, the domain is characterized as MSS4.
+At position 55 to 123, the domain is characterized as BTB.
+At position 25 to 251, the domain is characterized as Peptidase S1.
+At position 340 to 405, the domain is characterized as S4 RNA-binding.
+At position 47 to 197, the domain is characterized as FZ.
+At position 3 to 129, the domain is characterized as MATH.
+At position 28 to 97, the domain is characterized as GRAM.
+At position 163 to 538, the domain is characterized as Myotubularin phosphatase.
+At position 34 to 200, the domain is characterized as Helicase ATP-binding.
+At position 234 to 435, the domain is characterized as Helicase C-terminal.
+At position 20 to 142, the domain is characterized as C-type lysozyme.
+At position 3 to 124, the domain is characterized as MTTase N-terminal.
+At position 148 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 445, the domain is characterized as TRAM.
+At position 169 to 256, the domain is characterized as PPIase FKBP-type.
+At position 34 to 113, the domain is characterized as Chorismate mutase.
+At position 15 to 239, the domain is characterized as AB hydrolase-1.
+At position 39 to 150, the domain is characterized as tRNA-binding.
+At position 391 to 467, the domain is characterized as B5.
+At position 686 to 778, the domain is characterized as FDX-ACB.
+At position 3 to 225, the domain is characterized as tr-type G.
+At position 183 to 283, the domain is characterized as Fe2OG dioxygenase.
+At position 49 to 258, the domain is characterized as Protein kinase.
+At position 27 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 40 to 392, the domain is characterized as TTL.
+At position 1 to 228, the domain is characterized as ABC transporter.
+At position 289 to 356, the domain is characterized as Mop.
+At position 45 to 384, the domain is characterized as AB hydrolase-1.
+At position 103 to 286, the domain is characterized as ATP-grasp.
+At position 31 to 213, the domain is characterized as CNNM transmembrane.
+At position 232 to 292, the domain is characterized as CBS 1.
+At position 297 to 352, the domain is characterized as CBS 2.
+At position 364 to 425, the domain is characterized as CBS 3.
+At position 27 to 138, the domain is characterized as Rhodanese.
+At position 159 to 302, the domain is characterized as Tyrosine-protein phosphatase.
+At position 87 to 122, the domain is characterized as EF-hand 1.
+At position 123 to 158, the domain is characterized as EF-hand 2.
+At position 10 to 226, the domain is characterized as tr-type G.
+At position 269 to 539, the domain is characterized as F-BAR.
+At position 761 to 974, the domain is characterized as Rho-GAP.
+At position 25 to 90, the domain is characterized as J.
+At position 67 to 145, the domain is characterized as GIY-YIG.
+At position 255 to 290, the domain is characterized as UVR.
+At position 585 to 1069, the domain is characterized as Protein kinase.
+At position 2 to 229, the domain is characterized as Glutamine amidotransferase type-2.
+At position 301 to 440, the domain is characterized as SIS 1.
+At position 473 to 618, the domain is characterized as SIS 2.
+At position 32 to 355, the domain is characterized as G-alpha.
+At position 22 to 62, the domain is characterized as Chitin-binding type-1.
+At position 263 to 323, the domain is characterized as HTH myb-type.
+At position 4 to 54, the domain is characterized as Kazal-like.
+At position 9 to 480, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 507 to 796, the domain is characterized as UvrD-like helicase C-terminal.
+At position 426 to 641, the domain is characterized as ABC transporter 1.
+At position 667 to 993, the domain is characterized as ABC transporter 2.
+At position 10 to 286, the domain is characterized as tr-type G.
+At position 50 to 145, the domain is characterized as PH.
+At position 37 to 104, the domain is characterized as SAM.
+At position 662 to 868, the domain is characterized as Rho-GAP.
+At position 898 to 1105, the domain is characterized as START.
+At position 20 to 98, the domain is characterized as GIY-YIG.
+At position 207 to 242, the domain is characterized as UVR.
+At position 30 to 65, the domain is characterized as EF-hand 1.
+At position 135 to 170, the domain is characterized as EF-hand 2.
+At position 22 to 163, the domain is characterized as SprT-like.
+At position 1 to 61, the domain is characterized as MADS-box.
+At position 87 to 177, the domain is characterized as K-box.
+At position 31 to 148, the domain is characterized as MTTase N-terminal.
+At position 178 to 410, the domain is characterized as Radical SAM core.
+At position 413 to 477, the domain is characterized as TRAM.
+At position 5 to 52, the domain is characterized as SpoVT-AbrB 1.
+At position 81 to 124, the domain is characterized as SpoVT-AbrB 2.
+At position 62 to 213, the domain is characterized as CP-type G.
+At position 83 to 204, the domain is characterized as C2 1.
+At position 216 to 354, the domain is characterized as C2 2.
+At position 128 to 440, the domain is characterized as Peptidase S8.
+At position 449 to 588, the domain is characterized as P/Homo B.
+At position 258 to 356, the domain is characterized as Cytochrome c.
+At position 14 to 47, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 119 to 304, the domain is characterized as ATP-grasp.
+At position 15 to 153, the domain is characterized as Rhodanese 1.
+At position 155 to 243, the domain is characterized as Rhodanese 2.
+At position 2 to 74, the domain is characterized as J.
+At position 65 to 167, the domain is characterized as PA.
+At position 390 to 531, the domain is characterized as SEFIR.
+At position 659 to 730, the domain is characterized as PAS.
+At position 802 to 1031, the domain is characterized as Histidine kinase.
+At position 69 to 173, the domain is characterized as PRD 1.
+At position 174 to 283, the domain is characterized as PRD 2.
+At position 58 to 354, the domain is characterized as Protein kinase.
+At position 9 to 125, the domain is characterized as MTTase N-terminal.
+At position 135 to 364, the domain is characterized as Radical SAM core.
+At position 367 to 434, the domain is characterized as TRAM.
+At position 31 to 311, the domain is characterized as FERM.
+At position 1 to 58, the domain is characterized as HTH lysR-type.
+At position 1 to 85, the domain is characterized as Core-binding (CB).
+At position 106 to 285, the domain is characterized as Tyr recombinase.
+At position 36 to 139, the domain is characterized as Ig-like V-type.
+At position 1 to 147, the domain is characterized as MGS-like.
+At position 38 to 237, the domain is characterized as PBC.
+At position 2 to 37, the domain is characterized as EF-hand 1.
+At position 38 to 73, the domain is characterized as EF-hand 2.
+At position 11 to 71, the domain is characterized as Sm.
+At position 7 to 244, the domain is characterized as ABC transporter.
+At position 183 to 279, the domain is characterized as CRM 1.
+At position 301 to 397, the domain is characterized as CRM 2.
+At position 12 to 197, the domain is characterized as Ku.
+At position 135 to 257, the domain is characterized as MPN.
+At position 2 to 123, the domain is characterized as PTS EIIA type-4.
+At position 346 to 399, the domain is characterized as bHLH.
+At position 58 to 283, the domain is characterized as Radical SAM core.
+At position 119 to 442, the domain is characterized as SAC.
+At position 902 to 971, the domain is characterized as RRM.
+At position 463 to 723, the domain is characterized as Protein kinase.
+At position 2 to 145, the domain is characterized as Ferritin-like diiron.
+At position 313 to 463, the domain is characterized as PI-PLC X-box.
+At position 565 to 681, the domain is characterized as PI-PLC Y-box.
+At position 684 to 809, the domain is characterized as C2.
+At position 24 to 123, the domain is characterized as Ig-like 1.
+At position 132 to 230, the domain is characterized as Ig-like 2.
+At position 240 to 323, the domain is characterized as Ig-like 3.
+At position 338 to 432, the domain is characterized as Ig-like 4.
+At position 440 to 534, the domain is characterized as Ig-like 5.
+At position 539 to 632, the domain is characterized as Ig-like 6.
+At position 644 to 744, the domain is characterized as Fibronectin type-III.
+At position 752 to 919, the domain is characterized as MAM.
+At position 164 to 334, the domain is characterized as Helicase ATP-binding.
+At position 490 to 685, the domain is characterized as Helicase C-terminal.
+At position 3 to 169, the domain is characterized as DHFR.
+At position 18 to 225, the domain is characterized as Radical SAM core.
+At position 7 to 70, the domain is characterized as TGS.
+At position 35 to 296, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 65 to 109, the domain is characterized as LysM.
+At position 225 to 243, the domain is characterized as UIM.
+At position 630 to 690, the domain is characterized as PWWP.
+At position 11 to 134, the domain is characterized as Rhodanese.
+At position 66 to 273, the domain is characterized as HD.
+At position 28 to 138, the domain is characterized as sHSP.
+At position 58 to 174, the domain is characterized as Thioredoxin.
+At position 21 to 153, the domain is characterized as MPN.
+At position 379 to 478, the domain is characterized as Zinc-hook.
+At position 19 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 23 to 151, the domain is characterized as EamA 1.
+At position 198 to 325, the domain is characterized as EamA 2.
+At position 1 to 63, the domain is characterized as HTH dtxR-type.
+At position 35 to 170, the domain is characterized as Thioredoxin.
+At position 295 to 397, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 230 to 292, the domain is characterized as t-SNARE coiled-coil homology.
+At position 158 to 304, the domain is characterized as TRUD.
+At position 444 to 516, the domain is characterized as PAS.
+At position 54 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 93 to 122, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 286 to 381, the domain is characterized as SH2.
+At position 376 to 425, the domain is characterized as SOCS box.
+At position 33 to 122, the domain is characterized as GOLD.
+At position 581 to 683, the domain is characterized as tRNA-binding.
+At position 32 to 155, the domain is characterized as AB hydrolase-1.
+At position 8 to 139, the domain is characterized as HTH marR-type.
+At position 305 to 377, the domain is characterized as PDZ 1.
+At position 876 to 957, the domain is characterized as PDZ 2.
+At position 106 to 289, the domain is characterized as Integrase catalytic.
+At position 1 to 73, the domain is characterized as Core-binding (CB).
+At position 90 to 244, the domain is characterized as Tyr recombinase.
+At position 192 to 276, the domain is characterized as RCK C-terminal 1.
+At position 279 to 361, the domain is characterized as RCK C-terminal 2.
+At position 77 to 162, the domain is characterized as Cytochrome c.
+At position 1 to 247, the domain is characterized as Deacetylase sirtuin-type.
+At position 1 to 80, the domain is characterized as Cytochrome b5 heme-binding.
+At position 354 to 406, the domain is characterized as bHLH.
+At position 177 to 249, the domain is characterized as KH 1.
+At position 634 to 702, the domain is characterized as KH 2.
+At position 712 to 771, the domain is characterized as KH 3.
+At position 782 to 851, the domain is characterized as KH 4.
+At position 861 to 929, the domain is characterized as KH 5.
+At position 939 to 1001, the domain is characterized as KH 6.
+At position 1153 to 1216, the domain is characterized as KH 7.
+At position 10 to 73, the domain is characterized as S5 DRBM.
+At position 3 to 163, the domain is characterized as Thioredoxin.
+At position 47 to 273, the domain is characterized as AB hydrolase-1.
+At position 43 to 214, the domain is characterized as uDENN.
+At position 246 to 373, the domain is characterized as cDENN.
+At position 375 to 499, the domain is characterized as dDENN.
+At position 232 to 291, the domain is characterized as SH3.
+At position 41 to 133, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 136 to 286, the domain is characterized as FAD-binding FR-type.
+At position 5 to 254, the domain is characterized as ABC transporter.
+At position 102 to 165, the domain is characterized as bZIP.
+At position 1 to 48, the domain is characterized as L27 1.
+At position 49 to 107, the domain is characterized as L27 2.
+At position 130 to 209, the domain is characterized as PDZ.
+At position 215 to 284, the domain is characterized as SH3.
+At position 338 to 525, the domain is characterized as Guanylate kinase-like.
+At position 6 to 230, the domain is characterized as ABC transporter.
+At position 96 to 468, the domain is characterized as GT44.
+At position 567 to 774, the domain is characterized as Peptidase C80.
+At position 13 to 785, the domain is characterized as ABC transporter.
+At position 170 to 294, the domain is characterized as Rhodanese.
+At position 432 to 794, the domain is characterized as USP.
+At position 58 to 161, the domain is characterized as THUMP.
+At position 2 to 90, the domain is characterized as HPr.
+At position 30 to 94, the domain is characterized as BTB.
+At position 360 to 457, the domain is characterized as BEN.
+At position 22 to 105, the domain is characterized as SWIB/MDM2.
+At position 499 to 567, the domain is characterized as SoHo.
+At position 683 to 742, the domain is characterized as SH3 1.
+At position 745 to 805, the domain is characterized as SH3 2.
+At position 946 to 1005, the domain is characterized as SH3 3.
+At position 827 to 907, the domain is characterized as KHA.
+At position 146 to 329, the domain is characterized as CheB-type methylesterase.
+At position 24 to 76, the domain is characterized as TIL.
+At position 4 to 130, the domain is characterized as PINc.
+At position 20 to 138, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 262, the domain is characterized as Ig-like C2-type 2.
+At position 276 to 386, the domain is characterized as Ig-like C2-type 3.
+At position 401 to 539, the domain is characterized as Ig-like C2-type 4.
+At position 545 to 661, the domain is characterized as Ig-like C2-type 5.
+At position 676 to 803, the domain is characterized as Ig-like C2-type 6.
+At position 813 to 945, the domain is characterized as Ig-like C2-type 7.
+At position 949 to 1097, the domain is characterized as Ig-like C2-type 8.
+At position 83 to 394, the domain is characterized as IF rod.
+At position 31 to 66, the domain is characterized as EF-hand 1.
+At position 100 to 135, the domain is characterized as EF-hand 2.
+At position 71 to 182, the domain is characterized as FAD-binding FR-type.
+At position 26 to 71, the domain is characterized as EGF-like 1; atypical.
+At position 173 to 213, the domain is characterized as EGF-like 2; calcium-binding.
+At position 214 to 253, the domain is characterized as EGF-like 3; calcium-binding.
+At position 254 to 293, the domain is characterized as EGF-like 4; calcium-binding.
+At position 294 to 333, the domain is characterized as EGF-like 5; calcium-binding.
+At position 334 to 378, the domain is characterized as EGF-like 6; calcium-binding.
+At position 541 to 607, the domain is characterized as SAM.
+At position 13 to 236, the domain is characterized as RMT2.
+At position 10 to 86, the domain is characterized as S1-like.
+At position 25 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 160, the domain is characterized as Obg.
+At position 161 to 326, the domain is characterized as OBG-type G.
+At position 3 to 140, the domain is characterized as B12-binding.
+At position 63 to 200, the domain is characterized as GAF 1.
+At position 231 to 369, the domain is characterized as GAF 2.
+At position 383 to 578, the domain is characterized as Histidine kinase.
+At position 6 to 62, the domain is characterized as HTH lysR-type.
+At position 490 to 662, the domain is characterized as Helicase C-terminal.
+At position 2 to 161, the domain is characterized as Thioredoxin.
+At position 68 to 215, the domain is characterized as HD.
+At position 216 to 379, the domain is characterized as TrmE-type G.
+At position 42 to 147, the domain is characterized as Ig-like C2-type.
+At position 165 to 299, the domain is characterized as FZ.
+At position 312 to 391, the domain is characterized as Kringle.
+At position 473 to 746, the domain is characterized as Protein kinase.
+At position 133 to 328, the domain is characterized as ATP-grasp 1.
+At position 675 to 866, the domain is characterized as ATP-grasp 2.
+At position 948 to 1093, the domain is characterized as MGS-like.
+At position 269 to 835, the domain is characterized as PPM-type phosphatase.
+At position 152 to 344, the domain is characterized as Histidine kinase.
+At position 704 to 978, the domain is characterized as Protein kinase.
+At position 120 to 358, the domain is characterized as Radical SAM core.
+At position 150 to 274, the domain is characterized as Fe2OG dioxygenase.
+At position 145 to 240, the domain is characterized as PpiC.
+At position 23 to 329, the domain is characterized as PPM-type phosphatase.
+At position 22 to 100, the domain is characterized as GIY-YIG.
+At position 209 to 244, the domain is characterized as UVR.
+At position 88 to 212, the domain is characterized as N-terminal Ras-GEF.
+At position 243 to 513, the domain is characterized as Ras-GEF.
+At position 648 to 735, the domain is characterized as Ras-associating.
+At position 6 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 43 to 154, the domain is characterized as THUMP.
+At position 211 to 491, the domain is characterized as ABC transmembrane type-1.
+At position 524 to 760, the domain is characterized as ABC transporter.
+At position 33 to 259, the domain is characterized as ABC transmembrane type-2.
+At position 1 to 85, the domain is characterized as YcgL.
+At position 93 to 258, the domain is characterized as CRAL-TRIO.
+At position 126 to 221, the domain is characterized as Rhodanese.
+At position 492 to 606, the domain is characterized as Toprim.
+At position 1018 to 1290, the domain is characterized as Autotransporter.
+At position 138 to 196, the domain is characterized as HTH luxR-type.
+At position 49 to 132, the domain is characterized as RRM 1.
+At position 188 to 270, the domain is characterized as RRM 2.
+At position 2 to 145, the domain is characterized as PTS EIIA type-2.
+At position 81 to 435, the domain is characterized as Peptidase A1.
+At position 54 to 159, the domain is characterized as Cadherin 1.
+At position 160 to 268, the domain is characterized as Cadherin 2.
+At position 269 to 383, the domain is characterized as Cadherin 3.
+At position 384 to 486, the domain is characterized as Cadherin 4.
+At position 487 to 612, the domain is characterized as Cadherin 5.
+At position 309 to 588, the domain is characterized as ABC transporter 1.
+At position 608 to 937, the domain is characterized as ABC transporter 2.
+At position 451 to 559, the domain is characterized as Peptidase S74.
+At position 11 to 162, the domain is characterized as N-acetyltransferase.
+At position 6 to 238, the domain is characterized as ABC transporter.
+At position 219 to 436, the domain is characterized as Letm1 RBD.
+At position 40 to 147, the domain is characterized as HPt.
+At position 40 to 122, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 6 to 265, the domain is characterized as ABC transporter.
+At position 453 to 585, the domain is characterized as Ricin B-type lectin.
+At position 24 to 119, the domain is characterized as Ig-like.
+At position 1 to 36, the domain is characterized as Chitin-binding type-1.
+At position 28 to 211, the domain is characterized as Radical SAM core.
+At position 48 to 168, the domain is characterized as Calponin-homology (CH).
+At position 208 to 281, the domain is characterized as GAR.
+At position 14 to 81, the domain is characterized as HTH HARE-type.
+At position 2 to 234, the domain is characterized as ABC transporter.
+At position 293 to 358, the domain is characterized as Mop.
+At position 3 to 188, the domain is characterized as YrdC-like.
+At position 88 to 279, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 250 to 439, the domain is characterized as GATase cobBQ-type.
+At position 637 to 717, the domain is characterized as S1 motif.
+At position 21 to 111, the domain is characterized as RRM 1.
+At position 110 to 187, the domain is characterized as RRM 2.
+At position 239 to 335, the domain is characterized as BEN.
+At position 93 to 175, the domain is characterized as PRC barrel.
+At position 18 to 113, the domain is characterized as HPt.
+At position 93 to 312, the domain is characterized as Radical SAM core.
+At position 109 to 314, the domain is characterized as ATP-grasp.
+At position 113 to 205, the domain is characterized as Ig-like C1-type.
+At position 2 to 120, the domain is characterized as TRM112.
+At position 183 to 348, the domain is characterized as DDE Tnp4.
+At position 1 to 107, the domain is characterized as MSP.
+At position 141 to 347, the domain is characterized as ATP-grasp.
+At position 32 to 230, the domain is characterized as PNPLA.
+At position 36 to 88, the domain is characterized as bHLH.
+At position 2 to 91, the domain is characterized as ABM.
+At position 2 to 60, the domain is characterized as IBB.
+At position 210 to 329, the domain is characterized as PAZ.
+At position 498 to 799, the domain is characterized as Piwi.
+At position 626 to 1169, the domain is characterized as WAPL.
+At position 26 to 183, the domain is characterized as Helicase ATP-binding.
+At position 431 to 593, the domain is characterized as Helicase C-terminal.
+At position 631 to 666, the domain is characterized as UVR.
+At position 51 to 155, the domain is characterized as Calponin-homology (CH) 1.
+At position 164 to 270, the domain is characterized as Calponin-homology (CH) 2.
+At position 766 to 801, the domain is characterized as EF-hand 1.
+At position 807 to 842, the domain is characterized as EF-hand 2.
+At position 35 to 172, the domain is characterized as Thioredoxin.
+At position 476 to 645, the domain is characterized as tr-type G.
+At position 33 to 144, the domain is characterized as CUB 1.
+At position 154 to 268, the domain is characterized as CUB 2.
+At position 297 to 415, the domain is characterized as NTR.
+At position 70 to 122, the domain is characterized as LIM zinc-binding 1.
+At position 131 to 184, the domain is characterized as LIM zinc-binding 2.
+At position 614 to 720, the domain is characterized as tRNA-binding.
+At position 576 to 678, the domain is characterized as tRNA-binding.
+At position 74 to 163, the domain is characterized as Rieske.
+At position 5 to 142, the domain is characterized as TsaA-like.
+At position 64 to 221, the domain is characterized as CP-type G.
+At position 37 to 284, the domain is characterized as NIT.
+At position 323 to 384, the domain is characterized as ANTAR.
+At position 5 to 78, the domain is characterized as PAS.
+At position 136 to 349, the domain is characterized as Histidine kinase.
+At position 209 to 272, the domain is characterized as KH.
+At position 335 to 428, the domain is characterized as HD.
+At position 12 to 60, the domain is characterized as F-box.
+At position 192 to 380, the domain is characterized as Rho-GAP.
+At position 14 to 293, the domain is characterized as YjeF C-terminal.
+At position 111 to 380, the domain is characterized as Helicase ATP-binding.
+At position 408 to 566, the domain is characterized as Helicase C-terminal.
+At position 158 to 256, the domain is characterized as HTH araC/xylS-type.
+At position 1 to 82, the domain is characterized as CN hydrolase.
+At position 31 to 300, the domain is characterized as GP-PDE.
+At position 85 to 281, the domain is characterized as Lon N-terminal.
+At position 668 to 850, the domain is characterized as Lon proteolytic.
+At position 38 to 152, the domain is characterized as TBDR plug.
+At position 155 to 614, the domain is characterized as TBDR beta-barrel.
+At position 74 to 168, the domain is characterized as Toprim.
+At position 96 to 156, the domain is characterized as S4 RNA-binding.
+At position 1 to 104, the domain is characterized as SSB.
+At position 77 to 239, the domain is characterized as TNase-like.
+At position 40 to 212, the domain is characterized as EngB-type G.
+At position 33 to 143, the domain is characterized as MTTase N-terminal.
+At position 161 to 398, the domain is characterized as Radical SAM core.
+At position 401 to 467, the domain is characterized as TRAM.
+At position 32 to 207, the domain is characterized as BPL/LPL catalytic.
+At position 189 to 235, the domain is characterized as LysM.
+At position 123 to 318, the domain is characterized as ATP-grasp.
+At position 162 to 201, the domain is characterized as Pentapeptide repeat 1.
+At position 202 to 241, the domain is characterized as Pentapeptide repeat 2.
+At position 247 to 286, the domain is characterized as Pentapeptide repeat 3.
+At position 287 to 326, the domain is characterized as Pentapeptide repeat 4.
+At position 159 to 331, the domain is characterized as OBG-type G.
+At position 345 to 424, the domain is characterized as OCT.
+At position 31 to 70, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 71 to 117, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 124 to 165, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 166 to 214, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 407 to 577, the domain is characterized as tr-type G.
+At position 187 to 268, the domain is characterized as RRM.
+At position 444 to 589, the domain is characterized as CID.
+At position 638 to 672, the domain is characterized as SAP.
+At position 6 to 69, the domain is characterized as SH3.
+At position 246 to 280, the domain is characterized as WW 1.
+At position 299 to 333, the domain is characterized as WW 2.
+At position 411 to 444, the domain is characterized as WW 3.
+At position 496 to 612, the domain is characterized as PH.
+At position 697 to 886, the domain is characterized as Rho-GAP.
+At position 130 to 458, the domain is characterized as SAC.
+At position 173 to 249, the domain is characterized as RRM.
+At position 376 to 491, the domain is characterized as Rhodanese.
+At position 36 to 67, the domain is characterized as LRRNT.
+At position 338 to 361, the domain is characterized as LRRCT.
+At position 419 to 517, the domain is characterized as Fibronectin type-III.
+At position 32 to 357, the domain is characterized as G-alpha.
+At position 6 to 257, the domain is characterized as ABC transporter 1.
+At position 287 to 526, the domain is characterized as ABC transporter 2.
+At position 609 to 668, the domain is characterized as CBS 1.
+At position 827 to 882, the domain is characterized as CBS 2.
+At position 3 to 81, the domain is characterized as Ubiquitin-like.
+At position 133 to 294, the domain is characterized as FCP1 homology.
+At position 1 to 147, the domain is characterized as UBC core.
+At position 247 to 414, the domain is characterized as W2.
+At position 322 to 358, the domain is characterized as CBM1.
+At position 25 to 79, the domain is characterized as G-patch.
+At position 39 to 133, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 30 to 61, the domain is characterized as LRRNT 1.
+At position 309 to 357, the domain is characterized as LRRCT 1.
+At position 394 to 428, the domain is characterized as LRRNT 2.
+At position 674 to 722, the domain is characterized as LRRCT 2.
+At position 383 to 624, the domain is characterized as NR LBD.
+At position 3 to 186, the domain is characterized as PBC.
+At position 4 to 287, the domain is characterized as Protein kinase.
+At position 39 to 153, the domain is characterized as tRNA-binding.
+At position 379 to 454, the domain is characterized as B5.
+At position 174 to 332, the domain is characterized as Cupin type-1 1.
+At position 391 to 548, the domain is characterized as Cupin type-1 2.
+At position 550 to 635, the domain is characterized as RWP-RK.
+At position 834 to 916, the domain is characterized as PB1.
+At position 32 to 159, the domain is characterized as Calponin-homology (CH).
+At position 201 to 273, the domain is characterized as GAR.
+At position 92 to 170, the domain is characterized as S4 RNA-binding.
+At position 494 to 620, the domain is characterized as Guanylate cyclase.
+At position 10 to 204, the domain is characterized as tr-type G.
+At position 14 to 92, the domain is characterized as RRM.
+At position 416 to 550, the domain is characterized as YTH.
+At position 261 to 530, the domain is characterized as Protein kinase 1.
+At position 531 to 599, the domain is characterized as AGC-kinase C-terminal.
+At position 623 to 886, the domain is characterized as Protein kinase 2.
+At position 29 to 139, the domain is characterized as sHSP.
+At position 65 to 165, the domain is characterized as THUMP.
+At position 1 to 76, the domain is characterized as Carrier.
+At position 414 to 473, the domain is characterized as LIM zinc-binding 1.
+At position 474 to 534, the domain is characterized as LIM zinc-binding 2.
+At position 535 to 603, the domain is characterized as LIM zinc-binding 3.
+At position 200 to 297, the domain is characterized as PH 1.
+At position 348 to 443, the domain is characterized as PH 2.
+At position 14 to 42, the domain is characterized as EF-hand 1.
+At position 84 to 119, the domain is characterized as EF-hand 3.
+At position 120 to 151, the domain is characterized as EF-hand 4.
+At position 28 to 286, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 26 to 97, the domain is characterized as IGFBP N-terminal.
+At position 100 to 166, the domain is characterized as VWFC.
+At position 197 to 242, the domain is characterized as TSP type-1.
+At position 255 to 329, the domain is characterized as CTCK.
+At position 549 to 608, the domain is characterized as KH.
+At position 618 to 686, the domain is characterized as S1 motif.
+At position 78 to 126, the domain is characterized as F-box.
+At position 13 to 92, the domain is characterized as GIY-YIG.
+At position 204 to 239, the domain is characterized as UVR.
+At position 161 to 339, the domain is characterized as OBG-type G.
+At position 360 to 438, the domain is characterized as OCT.
+At position 300 to 539, the domain is characterized as NR LBD.
+At position 24 to 177, the domain is characterized as Helicase ATP-binding.
+At position 428 to 594, the domain is characterized as Helicase C-terminal.
+At position 620 to 655, the domain is characterized as UVR.
+At position 3 to 237, the domain is characterized as ABC transporter.
+At position 42 to 77, the domain is characterized as EF-hand 2.
+At position 182 to 217, the domain is characterized as EF-hand 3.
+At position 219 to 252, the domain is characterized as EF-hand 4.
+At position 317 to 352, the domain is characterized as EF-hand 5.
+At position 80 to 176, the domain is characterized as Toprim.
+At position 93 to 156, the domain is characterized as S4 RNA-binding.
+At position 369 to 391, the domain is characterized as WH2.
+At position 671 to 863, the domain is characterized as ATP-grasp 2.
+At position 930 to 1028, the domain is characterized as MGS-like.
+At position 4 to 124, the domain is characterized as RabBD.
+At position 227 to 488, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 352 to 419, the domain is characterized as S4 RNA-binding.
+At position 40 to 167, the domain is characterized as ALOG.
+At position 29 to 117, the domain is characterized as Cystatin.
+At position 538 to 612, the domain is characterized as Carrier.
+At position 56 to 149, the domain is characterized as BLUF 1.
+At position 205 to 333, the domain is characterized as Guanylate cyclase 1.
+At position 471 to 563, the domain is characterized as BLUF 2.
+At position 619 to 748, the domain is characterized as Guanylate cyclase 2.
+At position 8 to 294, the domain is characterized as tr-type G.
+At position 8 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 236 to 421, the domain is characterized as FAD-binding PCMH-type.
+At position 54 to 82, the domain is characterized as ITAM.
+At position 146 to 367, the domain is characterized as Radical SAM core.
+At position 498 to 665, the domain is characterized as tr-type G.
+At position 2 to 181, the domain is characterized as KARI N-terminal Rossmann.
+At position 16 to 139, the domain is characterized as EamA 1.
+At position 188 to 313, the domain is characterized as EamA 2.
+At position 206 to 476, the domain is characterized as MHD.
+At position 121 to 450, the domain is characterized as SAC.
+At position 10 to 77, the domain is characterized as NAC-A/B.
+At position 23 to 103, the domain is characterized as Ig-like C2-type.
+At position 106 to 203, the domain is characterized as Fibronectin type-III 1.
+At position 204 to 304, the domain is characterized as Fibronectin type-III 2.
+At position 1 to 146, the domain is characterized as CID.
+At position 102 to 237, the domain is characterized as ZU5.
+At position 415 to 494, the domain is characterized as Death.
+At position 1 to 88, the domain is characterized as HPr.
+At position 48 to 308, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 206 to 339, the domain is characterized as GGDEF.
+At position 36 to 118, the domain is characterized as Doublecortin 1.
+At position 152 to 231, the domain is characterized as Doublecortin 2.
+At position 179 to 352, the domain is characterized as EngA-type G 2.
+At position 228 to 288, the domain is characterized as HTH myb-type.
+At position 11 to 291, the domain is characterized as tr-type G.
+At position 19 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 213 to 411, the domain is characterized as GMPS ATP-PPase.
+At position 5 to 79, the domain is characterized as TFIIS N-terminal.
+At position 148 to 264, the domain is characterized as TFIIS central.
+At position 2 to 123, the domain is characterized as TRM112.
+At position 98 to 164, the domain is characterized as S4 RNA-binding.
+At position 18 to 408, the domain is characterized as GRAS.
+At position 13 to 94, the domain is characterized as Death.
+At position 206 to 476, the domain is characterized as Protein kinase.
+At position 4 to 191, the domain is characterized as Flavodoxin-like.
+At position 262 to 344, the domain is characterized as Toprim.
+At position 64 to 373, the domain is characterized as AB hydrolase-1.
+At position 469 to 617, the domain is characterized as N-acetyltransferase.
+At position 704 to 774, the domain is characterized as Bromo.
+At position 348 to 782, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1272 to 1582, the domain is characterized as PKS/mFAS DH.
+At position 1640 to 1716, the domain is characterized as Carrier 1.
+At position 1741 to 1815, the domain is characterized as Carrier 2.
+At position 126 to 158, the domain is characterized as LisH.
+At position 164 to 221, the domain is characterized as CTLH.
+At position 40 to 82, the domain is characterized as EGF-like.
+At position 122 to 170, the domain is characterized as Fibronectin type-II.
+At position 290 to 514, the domain is characterized as ABC transmembrane type-1.
+At position 403 to 581, the domain is characterized as Helicase ATP-binding.
+At position 592 to 753, the domain is characterized as Helicase C-terminal.
+At position 107 to 160, the domain is characterized as bHLH.
+At position 178 to 250, the domain is characterized as PAS 1.
+At position 357 to 427, the domain is characterized as PAS 2.
+At position 432 to 475, the domain is characterized as PAC.
+At position 20 to 163, the domain is characterized as SprT-like.
+At position 605 to 685, the domain is characterized as BRCT.
+At position 15 to 276, the domain is characterized as Protein kinase.
+At position 306 to 513, the domain is characterized as MCM.
+At position 11 to 280, the domain is characterized as tr-type G.
+At position 93 to 188, the domain is characterized as TAFH.
+At position 57 to 264, the domain is characterized as SEC7.
+At position 412 to 551, the domain is characterized as PH.
+At position 1 to 242, the domain is characterized as ABC transporter.
+At position 272 to 334, the domain is characterized as SAM.
+At position 80 to 297, the domain is characterized as Radical SAM core.
+At position 309 to 355, the domain is characterized as G-patch.
+At position 8 to 273, the domain is characterized as tr-type G.
+At position 221 to 269, the domain is characterized as RPE1 insert.
+At position 6 to 245, the domain is characterized as ABC transporter 1.
+At position 262 to 507, the domain is characterized as ABC transporter 2.
+At position 8 to 325, the domain is characterized as Kinesin motor.
+At position 20 to 138, the domain is characterized as MTTase N-terminal.
+At position 162 to 398, the domain is characterized as Radical SAM core.
+At position 401 to 464, the domain is characterized as TRAM.
+At position 634 to 738, the domain is characterized as Cytochrome c.
+At position 43 to 118, the domain is characterized as KH type-2.
+At position 5 to 172, the domain is characterized as Era-type G.
+At position 203 to 279, the domain is characterized as KH type-2.
+At position 12 to 47, the domain is characterized as EF-hand 1.
+At position 49 to 84, the domain is characterized as EF-hand 2.
+At position 216 to 377, the domain is characterized as TrmE-type G.
+At position 97 to 160, the domain is characterized as S4 RNA-binding.
+At position 13 to 180, the domain is characterized as TIR.
+At position 89 to 150, the domain is characterized as S4 RNA-binding.
+At position 235 to 287, the domain is characterized as HAMP.
+At position 302 to 519, the domain is characterized as Histidine kinase.
+At position 291 to 542, the domain is characterized as Glutamine amidotransferase type-1.
+At position 366 to 481, the domain is characterized as Rhodanese.
+At position 37 to 278, the domain is characterized as ABC transporter.
+At position 31 to 418, the domain is characterized as Helicase ATP-binding.
+At position 435 to 601, the domain is characterized as Helicase C-terminal.
+At position 627 to 662, the domain is characterized as UVR.
+At position 29 to 75, the domain is characterized as F-box.
+At position 378 to 428, the domain is characterized as FBD.
+At position 171 to 257, the domain is characterized as Toprim.
+At position 251 to 343, the domain is characterized as Enkurin.
+At position 183 to 260, the domain is characterized as RCK C-terminal 1.
+At position 268 to 352, the domain is characterized as RCK C-terminal 2.
+At position 65 to 223, the domain is characterized as CP-type G.
+At position 546 to 599, the domain is characterized as bHLH.
+At position 2 to 126, the domain is characterized as ApaG.
+At position 58 to 111, the domain is characterized as Kazal-like.
+At position 117 to 217, the domain is characterized as SRCR.
+At position 218 to 262, the domain is characterized as LDL-receptor class A 1.
+At position 263 to 299, the domain is characterized as LDL-receptor class A 2.
+At position 362 to 595, the domain is characterized as Peptidase S1.
+At position 82 to 177, the domain is characterized as Toprim.
+At position 231 to 294, the domain is characterized as bZIP.
+At position 105 to 168, the domain is characterized as bZIP.
+At position 9 to 121, the domain is characterized as Pru.
+At position 13 to 120, the domain is characterized as PH.
+At position 192 to 295, the domain is characterized as DEUBAD.
+At position 108 to 172, the domain is characterized as J.
+At position 22 to 311, the domain is characterized as FERM.
+At position 361 to 458, the domain is characterized as ERCC4.
+At position 149 to 416, the domain is characterized as GH84.
+At position 562 to 644, the domain is characterized as S1 motif.
+At position 166 to 241, the domain is characterized as HTH crp-type.
+At position 11 to 191, the domain is characterized as PBS-linker.
+At position 556 to 670, the domain is characterized as Fe2OG dioxygenase.
+At position 39 to 154, the domain is characterized as tRNA-binding.
+At position 404 to 483, the domain is characterized as B5.
+At position 694 to 790, the domain is characterized as FDX-ACB.
+At position 8 to 108, the domain is characterized as SSB.
+At position 53 to 270, the domain is characterized as uDENN.
+At position 289 to 452, the domain is characterized as cDENN.
+At position 454 to 619, the domain is characterized as dDENN.
+At position 809 to 969, the domain is characterized as RUN 1.
+At position 973 to 1081, the domain is characterized as PLAT.
+At position 1155 to 1306, the domain is characterized as RUN 2.
+At position 1 to 133, the domain is characterized as ABC transmembrane type-1.
+At position 581 to 706, the domain is characterized as DBINO.
+At position 830 to 1002, the domain is characterized as Helicase ATP-binding.
+At position 1403 to 1563, the domain is characterized as Helicase C-terminal.
+At position 53 to 261, the domain is characterized as TNase-like.
+At position 42 to 99, the domain is characterized as Collagen-like.
+At position 134 to 245, the domain is characterized as C-type lectin.
+At position 132 to 318, the domain is characterized as Histidine kinase.
+At position 693 to 776, the domain is characterized as BRCT.
+At position 171 to 323, the domain is characterized as C-CAP/cofactor C-like.
+At position 10 to 65, the domain is characterized as L27.
+At position 93 to 175, the domain is characterized as PDZ.
+At position 6 to 41, the domain is characterized as EF-hand 1.
+At position 595 to 630, the domain is characterized as EF-hand 2.
+At position 45 to 249, the domain is characterized as Helicase ATP-binding.
+At position 283 to 437, the domain is characterized as Helicase C-terminal.
+At position 30 to 133, the domain is characterized as Cadherin 1.
+At position 134 to 242, the domain is characterized as Cadherin 2.
+At position 243 to 350, the domain is characterized as Cadherin 3.
+At position 351 to 454, the domain is characterized as Cadherin 4.
+At position 455 to 564, the domain is characterized as Cadherin 5.
+At position 571 to 677, the domain is characterized as Cadherin 6.
+At position 159 to 341, the domain is characterized as OBG-type G.
+At position 237 to 341, the domain is characterized as HD.
+At position 25 to 300, the domain is characterized as Protein kinase.
+At position 228 to 443, the domain is characterized as Asparagine synthetase.
+At position 1 to 81, the domain is characterized as Sm.
+At position 283 to 319, the domain is characterized as DFDF.
+At position 101 to 202, the domain is characterized as PH.
+At position 193 to 311, the domain is characterized as C2.
+At position 371 to 563, the domain is characterized as Ras-GAP.
+At position 291 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 30 to 60, the domain is characterized as LRRNT.
+At position 358 to 412, the domain is characterized as LRRCT.
+At position 412 to 502, the domain is characterized as Ig-like C2-type.
+At position 140 to 329, the domain is characterized as ABC transmembrane type-1.
+At position 10 to 101, the domain is characterized as BRCT.
+At position 130 to 190, the domain is characterized as Myb-like.
+At position 66 to 201, the domain is characterized as MPN.
+At position 8 to 41, the domain is characterized as WW 1.
+At position 53 to 86, the domain is characterized as WW 2.
+At position 158 to 257, the domain is characterized as PH.
+At position 26 to 100, the domain is characterized as REM-1.
+At position 111 to 460, the domain is characterized as BRO1.
+At position 515 to 593, the domain is characterized as PDZ.
+At position 162 to 215, the domain is characterized as PPIase FKBP-type.
+At position 214 to 374, the domain is characterized as Helicase C-terminal.
+At position 119 to 203, the domain is characterized as PNT.
+At position 53 to 283, the domain is characterized as Radical SAM core.
+At position 13 to 357, the domain is characterized as YjeF C-terminal.
+At position 2 to 321, the domain is characterized as Glutamine amidotransferase type-2.
+At position 393 to 532, the domain is characterized as SIS 1.
+At position 565 to 710, the domain is characterized as SIS 2.
+At position 68 to 175, the domain is characterized as C-type lectin.
+At position 17 to 274, the domain is characterized as Protein kinase.
+At position 495 to 800, the domain is characterized as CNH.
+At position 26 to 253, the domain is characterized as Peptidase S1.
+At position 204 to 256, the domain is characterized as HAMP.
+At position 261 to 331, the domain is characterized as PAS.
+At position 314 to 378, the domain is characterized as PAC.
+At position 382 to 600, the domain is characterized as Histidine kinase.
+At position 70 to 116, the domain is characterized as F-box.
+At position 84 to 463, the domain is characterized as PRONE.
+At position 241 to 377, the domain is characterized as GAF 1.
+At position 409 to 548, the domain is characterized as GAF 2.
+At position 578 to 902, the domain is characterized as PDEase.
+At position 109 to 300, the domain is characterized as ATP-grasp.
+At position 61 to 121, the domain is characterized as SH3.
+At position 127 to 224, the domain is characterized as SH2.
+At position 245 to 498, the domain is characterized as Protein kinase.
+At position 19 to 209, the domain is characterized as Albumin 1.
+At position 210 to 402, the domain is characterized as Albumin 2.
+At position 403 to 600, the domain is characterized as Albumin 3.
+At position 173 to 450, the domain is characterized as NR LBD.
+At position 3 to 220, the domain is characterized as tr-type G.
+At position 6 to 150, the domain is characterized as PHTF.
+At position 309 to 503, the domain is characterized as PCI.
+At position 213 to 273, the domain is characterized as HTH myb-type.
+At position 63 to 168, the domain is characterized as PH.
+At position 193 to 297, the domain is characterized as IRS-type PTB.
+At position 58 to 118, the domain is characterized as MADS-box.
+At position 29 to 268, the domain is characterized as Peptidase S1.
+At position 398 to 563, the domain is characterized as Helicase ATP-binding.
+At position 699 to 866, the domain is characterized as Helicase C-terminal.
+At position 1 to 120, the domain is characterized as Peptidase M12B.
+At position 126 to 214, the domain is characterized as Disintegrin.
+At position 360 to 416, the domain is characterized as EGF-like.
+At position 172 to 358, the domain is characterized as Glutamine amidotransferase type-1.
+At position 334 to 397, the domain is characterized as bZIP.
+At position 169 to 234, the domain is characterized as HTH luxR-type.
+At position 27 to 225, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 72, the domain is characterized as F-box.
+At position 620 to 785, the domain is characterized as SSD.
+At position 1 to 110, the domain is characterized as WH1.
+At position 68 to 195, the domain is characterized as MATH.
+At position 214 to 521, the domain is characterized as USP.
+At position 160 to 327, the domain is characterized as OBG-type G.
+At position 102 to 786, the domain is characterized as Peptidase M13.
+At position 408 to 483, the domain is characterized as B5.
+At position 708 to 800, the domain is characterized as FDX-ACB.
+At position 1 to 87, the domain is characterized as Acylphosphatase-like.
+At position 7 to 55, the domain is characterized as F-box.
+At position 1 to 116, the domain is characterized as Response regulatory.
+At position 162 to 352, the domain is characterized as CheB-type methylesterase.
+At position 1 to 155, the domain is characterized as PPIase cyclophilin-type.
+At position 119 to 198, the domain is characterized as RRM.
+At position 393 to 543, the domain is characterized as NTF2.
+At position 572 to 626, the domain is characterized as TAP-C.
+At position 13 to 103, the domain is characterized as Acylphosphatase-like.
+At position 243 to 320, the domain is characterized as TFIIS N-terminal.
+At position 223 to 381, the domain is characterized as TrmE-type G.
+At position 325 to 608, the domain is characterized as ABC transmembrane type-1 1.
+At position 644 to 868, the domain is characterized as ABC transporter 1.
+At position 975 to 1256, the domain is characterized as ABC transmembrane type-1 2.
+At position 1293 to 1527, the domain is characterized as ABC transporter 2.
+At position 1731 to 1830, the domain is characterized as Calx-beta.
+At position 2060 to 2174, the domain is characterized as C-type lectin.
+At position 25 to 258, the domain is characterized as Peptidase S1.
+At position 8 to 285, the domain is characterized as EndoU.
+At position 157 to 303, the domain is characterized as TRUD.
+At position 212 to 558, the domain is characterized as USP.
+At position 229 to 419, the domain is characterized as Helicase ATP-binding.
+At position 430 to 590, the domain is characterized as Helicase C-terminal.
+At position 801 to 963, the domain is characterized as SUN.
+At position 305 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 103 to 184, the domain is characterized as RRM.
+At position 103 to 353, the domain is characterized as Protein kinase.
+At position 35 to 115, the domain is characterized as Inhibitor I9.
+At position 125 to 397, the domain is characterized as Peptidase S8.
+At position 33 to 223, the domain is characterized as GH11.
+At position 275 to 310, the domain is characterized as CBM1.
+At position 195 to 263, the domain is characterized as POTRA.
+At position 91 to 167, the domain is characterized as WWE.
+At position 50 to 79, the domain is characterized as IQ.
+At position 72 to 149, the domain is characterized as BAG.
+At position 10 to 69, the domain is characterized as Sm.
+At position 135 to 303, the domain is characterized as N-acetyltransferase.
+At position 43 to 78, the domain is characterized as EF-hand.
+At position 79 to 174, the domain is characterized as Toprim.
+At position 3 to 476, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 528 to 824, the domain is characterized as UvrD-like helicase C-terminal.
+At position 37 to 182, the domain is characterized as FAS1.
+At position 360 to 415, the domain is characterized as SOCS box.
+At position 16 to 377, the domain is characterized as GH18.
+At position 8 to 130, the domain is characterized as MsrB.
+At position 13 to 304, the domain is characterized as Protein kinase.
+At position 14 to 198, the domain is characterized as UmuC.
+At position 9 to 276, the domain is characterized as tr-type G.
+At position 46 to 157, the domain is characterized as THUMP.
+At position 2 to 159, the domain is characterized as Thioredoxin.
+At position 13 to 188, the domain is characterized as EngB-type G.
+At position 26 to 69, the domain is characterized as CAP-Gly.
+At position 37 to 269, the domain is characterized as Peptidase S1.
+At position 173 to 202, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 14 to 115, the domain is characterized as AB hydrolase-1.
+At position 28 to 100, the domain is characterized as Collagen-like.
+At position 127 to 247, the domain is characterized as C-type lectin.
+At position 9 to 236, the domain is characterized as ATP-grasp.
+At position 404 to 482, the domain is characterized as Rhodanese.
+At position 31 to 81, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 2 to 200, the domain is characterized as DPCK.
+At position 30 to 208, the domain is characterized as Peptidase M12A.
+At position 203 to 244, the domain is characterized as EGF-like.
+At position 3 to 240, the domain is characterized as ABC transporter.
+At position 94 to 165, the domain is characterized as PRC barrel.
+At position 24 to 231, the domain is characterized as MRH.
+At position 108 to 356, the domain is characterized as NR LBD.
+At position 232 to 418, the domain is characterized as PCI.
+At position 12 to 162, the domain is characterized as PPIase cyclophilin-type.
+At position 670 to 955, the domain is characterized as Protein kinase.
+At position 956 to 1042, the domain is characterized as AGC-kinase C-terminal.
+At position 21 to 92, the domain is characterized as KRAB.
+At position 26 to 83, the domain is characterized as 4Fe-4S Wbl-type.
+At position 2 to 68, the domain is characterized as HMA.
+At position 219 to 375, the domain is characterized as TrmE-type G.
+At position 8 to 65, the domain is characterized as HTH lysR-type.
+At position 329 to 564, the domain is characterized as PPM-type phosphatase.
+At position 212 to 387, the domain is characterized as EngA-type G 2.
+At position 388 to 472, the domain is characterized as KH-like.
+At position 21 to 100, the domain is characterized as GIY-YIG.
+At position 210 to 245, the domain is characterized as UVR.
+At position 218 to 428, the domain is characterized as Helicase ATP-binding.
+At position 480 to 638, the domain is characterized as Helicase C-terminal.
+At position 6 to 152, the domain is characterized as MGS-like.
+At position 30 to 142, the domain is characterized as HD.
+At position 6 to 326, the domain is characterized as Hcy-binding.
+At position 359 to 620, the domain is characterized as Pterin-binding.
+At position 650 to 747, the domain is characterized as B12-binding N-terminal.
+At position 760 to 895, the domain is characterized as B12-binding.
+At position 911 to 1253, the domain is characterized as AdoMet activation.
+At position 95 to 169, the domain is characterized as PRC barrel.
+At position 21 to 101, the domain is characterized as Importin N-terminal.
+At position 19 to 179, the domain is characterized as PNPLA.
+At position 6 to 90, the domain is characterized as PB1.
+At position 811 to 860, the domain is characterized as UBA.
+At position 23 to 111, the domain is characterized as Fibronectin type-III 1.
+At position 112 to 207, the domain is characterized as Fibronectin type-III 2.
+At position 203 to 288, the domain is characterized as Fibronectin type-III 3.
+At position 291 to 378, the domain is characterized as Fibronectin type-III 4.
+At position 379 to 471, the domain is characterized as Fibronectin type-III 5.
+At position 467 to 552, the domain is characterized as Fibronectin type-III 6.
+At position 556 to 641, the domain is characterized as Fibronectin type-III 7.
+At position 642 to 729, the domain is characterized as Fibronectin type-III 8.
+At position 730 to 829, the domain is characterized as Fibronectin type-III 9.
+At position 819 to 906, the domain is characterized as Fibronectin type-III 10.
+At position 909 to 1001, the domain is characterized as Fibronectin type-III 11.
+At position 995 to 1083, the domain is characterized as Fibronectin type-III 12.
+At position 1087 to 1175, the domain is characterized as Fibronectin type-III 13.
+At position 1173 to 1260, the domain is characterized as Fibronectin type-III 14.
+At position 1260 to 1356, the domain is characterized as Fibronectin type-III 15.
+At position 1357 to 1448, the domain is characterized as Fibronectin type-III 16.
+At position 1458 to 1554, the domain is characterized as Fibronectin type-III 17.
+At position 1703 to 1963, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 80, the domain is characterized as Ubiquitin-like.
+At position 387 to 426, the domain is characterized as UBA.
+At position 5 to 240, the domain is characterized as tr-type G.
+At position 24 to 241, the domain is characterized as ABC transporter.
+At position 104 to 175, the domain is characterized as SUI1.
+At position 7 to 203, the domain is characterized as Peptidase M12B.
+At position 211 to 291, the domain is characterized as Disintegrin.
+At position 93 to 144, the domain is characterized as bHLH.
+At position 355 to 421, the domain is characterized as S4 RNA-binding.
+At position 68 to 251, the domain is characterized as MACPF.
+At position 76 to 143, the domain is characterized as RRM 1.
+At position 150 to 231, the domain is characterized as RRM 2.
+At position 12 to 64, the domain is characterized as F-box.
+At position 996 to 1042, the domain is characterized as G-patch.
+At position 29 to 293, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 28 to 83, the domain is characterized as Sushi 1.
+At position 84 to 141, the domain is characterized as Sushi 2.
+At position 156 to 398, the domain is characterized as Peptidase S1.
+At position 41 to 277, the domain is characterized as AB hydrolase-1.
+At position 5 to 240, the domain is characterized as ABC transporter 1.
+At position 250 to 492, the domain is characterized as ABC transporter 2.
+At position 2 to 73, the domain is characterized as U-box.
+At position 41 to 339, the domain is characterized as GP-PDE 1.
+At position 355 to 654, the domain is characterized as GP-PDE 2.
+At position 563 to 833, the domain is characterized as Protein kinase.
+At position 19 to 134, the domain is characterized as RNase III.
+At position 161 to 229, the domain is characterized as DRBM.
+At position 54 to 388, the domain is characterized as A to I editase.
+At position 144 to 335, the domain is characterized as CheB-type methylesterase.
+At position 20 to 183, the domain is characterized as Exonuclease.
+At position 435 to 493, the domain is characterized as Prospero-type homeo.
+At position 494 to 593, the domain is characterized as Prospero.
+At position 62 to 166, the domain is characterized as THUMP.
+At position 405 to 483, the domain is characterized as Rhodanese.
+At position 19 to 73, the domain is characterized as MADS-box.
+At position 103 to 193, the domain is characterized as K-box.
+At position 1 to 129, the domain is characterized as Plastocyanin-like.
+At position 50 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 96 to 125, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 455 to 622, the domain is characterized as tr-type G.
+At position 13 to 159, the domain is characterized as UBC core.
+At position 42 to 149, the domain is characterized as Ig-like C2-type 1.
+At position 152 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 252 to 340, the domain is characterized as Ig-like C2-type 3.
+At position 346 to 433, the domain is characterized as Ig-like C2-type 4.
+At position 468 to 578, the domain is characterized as Fibronectin type-III 1.
+At position 586 to 681, the domain is characterized as Fibronectin type-III 2.
+At position 77 to 184, the domain is characterized as Calponin-homology (CH).
+At position 1 to 73, the domain is characterized as Carrier.
+At position 80 to 114, the domain is characterized as Tify.
+At position 14 to 208, the domain is characterized as KARI N-terminal Rossmann.
+At position 209 to 344, the domain is characterized as KARI C-terminal knotted 1.
+At position 345 to 487, the domain is characterized as KARI C-terminal knotted 2.
+At position 214 to 256, the domain is characterized as CAP-Gly.
+At position 15 to 208, the domain is characterized as KARI N-terminal Rossmann.
+At position 345 to 484, the domain is characterized as KARI C-terminal knotted 2.
+At position 11 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 393, the domain is characterized as GMPS ATP-PPase.
+At position 114 to 310, the domain is characterized as HD-GYP.
+At position 20 to 287, the domain is characterized as CN hydrolase.
+At position 4 to 184, the domain is characterized as UmuC.
+At position 270 to 468, the domain is characterized as B30.2/SPRY.
+At position 69 to 103, the domain is characterized as SAP.
+At position 104 to 233, the domain is characterized as TIR.
+At position 153 to 230, the domain is characterized as RRM 1.
+At position 250 to 328, the domain is characterized as RRM 2.
+At position 445 to 508, the domain is characterized as RRM 3.
+At position 8 to 288, the domain is characterized as tr-type G.
+At position 302 to 541, the domain is characterized as START.
+At position 51 to 118, the domain is characterized as BTB.
+At position 158 to 236, the domain is characterized as BACK.
+At position 4 to 120, the domain is characterized as Response regulatory.
+At position 82 to 175, the domain is characterized as PH.
+At position 350 to 486, the domain is characterized as DAGKc.
+At position 1853 to 1916, the domain is characterized as SAM.
+At position 114 to 228, the domain is characterized as SET.
+At position 216 to 368, the domain is characterized as TrmE-type G.
+At position 58 to 172, the domain is characterized as OmpA-like.
+At position 34 to 113, the domain is characterized as Inhibitor I9.
+At position 126 to 400, the domain is characterized as Peptidase S8.
+At position 223 to 381, the domain is characterized as FCP1 homology.
+At position 66 to 144, the domain is characterized as RRM.
+At position 214 to 236, the domain is characterized as DAZ.
+At position 313 to 390, the domain is characterized as Toprim.
+At position 15 to 73, the domain is characterized as NAC-A/B.
+At position 135 to 174, the domain is characterized as UBA.
+At position 7 to 140, the domain is characterized as B12-binding.
+At position 135 to 252, the domain is characterized as PilZ.
+At position 805 to 870, the domain is characterized as HTH luxR-type.
+At position 1 to 112, the domain is characterized as WH1.
+At position 153 to 352, the domain is characterized as Peptidase M12A.
+At position 354 to 466, the domain is characterized as CUB 1.
+At position 467 to 579, the domain is characterized as CUB 2.
+At position 579 to 620, the domain is characterized as EGF-like 1; calcium-binding.
+At position 623 to 735, the domain is characterized as CUB 3.
+At position 735 to 775, the domain is characterized as EGF-like 2; calcium-binding.
+At position 779 to 891, the domain is characterized as CUB 4.
+At position 892 to 1008, the domain is characterized as CUB 5.
+At position 21 to 189, the domain is characterized as N-acetyltransferase.
+At position 112 to 235, the domain is characterized as MPN.
+At position 38 to 151, the domain is characterized as GOLD.
+At position 21 to 96, the domain is characterized as Peptidase A2.
+At position 111 to 156, the domain is characterized as G-patch.
+At position 20 to 410, the domain is characterized as Helicase ATP-binding.
+At position 425 to 591, the domain is characterized as Helicase C-terminal.
+At position 5 to 121, the domain is characterized as MTTase N-terminal.
+At position 143 to 373, the domain is characterized as Radical SAM core.
+At position 376 to 439, the domain is characterized as TRAM.
+At position 164 to 279, the domain is characterized as RNase III 1.
+At position 411 to 511, the domain is characterized as RNase III 2.
+At position 21 to 317, the domain is characterized as Protein kinase.
+At position 7 to 151, the domain is characterized as N-acetyltransferase.
+At position 27 to 192, the domain is characterized as Laminin G-like.
+At position 286 to 325, the domain is characterized as EGF-like 1.
+At position 326 to 363, the domain is characterized as EGF-like 2; calcium-binding.
+At position 379 to 419, the domain is characterized as EGF-like 3; calcium-binding.
+At position 420 to 462, the domain is characterized as EGF-like 4.
+At position 731 to 945, the domain is characterized as TSP C-terminal.
+At position 22 to 245, the domain is characterized as Peptidase S1.
+At position 378 to 469, the domain is characterized as RRM 1.
+At position 486 to 568, the domain is characterized as RRM 2.
+At position 3 to 619, the domain is characterized as PFL.
+At position 626 to 749, the domain is characterized as Glycine radical.
+At position 26 to 193, the domain is characterized as 3'-5' exonuclease.
+At position 231 to 312, the domain is characterized as HRDC.
+At position 3 to 121, the domain is characterized as Response regulatory.
+At position 154 to 348, the domain is characterized as CheB-type methylesterase.
+At position 10 to 64, the domain is characterized as HTH lacI-type.
+At position 1 to 88, the domain is characterized as GLUE N-terminal.
+At position 105 to 138, the domain is characterized as GLUE C-terminal.
+At position 127 to 294, the domain is characterized as Helicase ATP-binding.
+At position 354 to 526, the domain is characterized as Helicase C-terminal.
+At position 938 to 1001, the domain is characterized as Tudor.
+At position 125 to 184, the domain is characterized as P-type.
+At position 131 to 228, the domain is characterized as PpiC.
+At position 349 to 531, the domain is characterized as N-acetyltransferase.
+At position 17 to 121, the domain is characterized as PH.
+At position 23 to 166, the domain is characterized as VOC 1.
+At position 197 to 355, the domain is characterized as VOC 2.
+At position 3 to 51, the domain is characterized as F-box.
+At position 471 to 637, the domain is characterized as Mic1.
+At position 32 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 14 to 345, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 358 to 684, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 54 to 195, the domain is characterized as Fido.
+At position 1 to 193, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 79, the domain is characterized as PUA.
+At position 205 to 262, the domain is characterized as LIM zinc-binding 1.
+At position 263 to 322, the domain is characterized as LIM zinc-binding 2.
+At position 328 to 387, the domain is characterized as LIM zinc-binding 3.
+At position 388 to 447, the domain is characterized as LIM zinc-binding 4.
+At position 448 to 505, the domain is characterized as LIM zinc-binding 5.
+At position 21 to 50, the domain is characterized as LRRNT.
+At position 142 to 193, the domain is characterized as LRRCT.
+At position 35 to 161, the domain is characterized as EamA.
+At position 2 to 129, the domain is characterized as HTH rrf2-type.
+At position 20 to 35, the domain is characterized as HhH.
+At position 3 to 160, the domain is characterized as N-acetyltransferase.
+At position 228 to 329, the domain is characterized as HD.
+At position 4 to 171, the domain is characterized as Era-type G.
+At position 202 to 280, the domain is characterized as KH type-2.
+At position 29 to 162, the domain is characterized as Ephrin RBD.
+At position 104 to 166, the domain is characterized as S4 RNA-binding.
+At position 429 to 492, the domain is characterized as bZIP.
+At position 74 to 281, the domain is characterized as Rab-GAP TBC.
+At position 3 to 201, the domain is characterized as DPCK.
+At position 140 to 196, the domain is characterized as bZIP.
+At position 567 to 700, the domain is characterized as MHD1.
+At position 981 to 1097, the domain is characterized as MHD2.
+At position 25 to 106, the domain is characterized as RRM.
+At position 276 to 350, the domain is characterized as PUA.
+At position 3 to 130, the domain is characterized as PINc.
+At position 8 to 158, the domain is characterized as Exonuclease.
+At position 664 to 724, the domain is characterized as SH3.
+At position 16 to 95, the domain is characterized as Ubiquitin-like.
+At position 10 to 70, the domain is characterized as Kazal-like 1.
+At position 71 to 121, the domain is characterized as Kazal-like 2.
+At position 170 to 426, the domain is characterized as MHD.
+At position 182 to 318, the domain is characterized as C2.
+At position 829 to 862, the domain is characterized as WW 1.
+At position 1018 to 1051, the domain is characterized as WW 2.
+At position 1271 to 1606, the domain is characterized as HECT.
+At position 25 to 72, the domain is characterized as WAP.
+At position 27 to 80, the domain is characterized as TSP type-1 1.
+At position 83 to 121, the domain is characterized as LDL-receptor class A.
+At position 124 to 456, the domain is characterized as MACPF.
+At position 457 to 487, the domain is characterized as EGF-like.
+At position 500 to 549, the domain is characterized as TSP type-1 2.
+At position 569 to 628, the domain is characterized as Sushi 1.
+At position 629 to 690, the domain is characterized as Sushi 2.
+At position 271 to 373, the domain is characterized as RAMA.
+At position 9 to 241, the domain is characterized as ATP-grasp.
+At position 340 to 393, the domain is characterized as TSP type-1.
+At position 12 to 109, the domain is characterized as Yippee.
+At position 14 to 80, the domain is characterized as HMA 1.
+At position 112 to 176, the domain is characterized as HMA 2.
+At position 843 to 920, the domain is characterized as Carrier.
+At position 94 to 193, the domain is characterized as BRICHOS.
+At position 40 to 198, the domain is characterized as SIS.
+At position 59 to 361, the domain is characterized as FERM.
+At position 389 to 564, the domain is characterized as Helicase ATP-binding.
+At position 736 to 895, the domain is characterized as Helicase C-terminal.
+At position 63 to 179, the domain is characterized as PH.
+At position 213 to 317, the domain is characterized as IRS-type PTB.
+At position 10 to 187, the domain is characterized as Ku.
+At position 37 to 151, the domain is characterized as sHSP.
+At position 115 to 276, the domain is characterized as TNase-like.
+At position 2 to 65, the domain is characterized as HMA.
+At position 1 to 360, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 8 to 86, the domain is characterized as RRM.
+At position 26 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 309 to 359, the domain is characterized as bHLH.
+At position 6 to 246, the domain is characterized as ABC transporter.
+At position 64 to 207, the domain is characterized as MH1.
+At position 261 to 426, the domain is characterized as MH2.
+At position 68 to 103, the domain is characterized as EF-hand 1.
+At position 104 to 139, the domain is characterized as EF-hand 2.
+At position 151 to 186, the domain is characterized as EF-hand 3.
+At position 188 to 223, the domain is characterized as EF-hand 4.
+At position 229 to 264, the domain is characterized as EF-hand 5.
+At position 265 to 300, the domain is characterized as EF-hand 6.
+At position 533 to 728, the domain is characterized as Glutamine amidotransferase type-1.
+At position 17 to 46, the domain is characterized as RIIa.
+At position 278 to 376, the domain is characterized as Fe2OG dioxygenase.
+At position 46 to 128, the domain is characterized as SCAN box.
+At position 148 to 229, the domain is characterized as PRC barrel.
+At position 3 to 162, the domain is characterized as Flavodoxin-like.
+At position 99 to 332, the domain is characterized as Radical SAM core.
+At position 25 to 107, the domain is characterized as Lipoyl-binding.
+At position 112 to 147, the domain is characterized as EF-hand 1.
+At position 149 to 183, the domain is characterized as EF-hand 2.
+At position 45 to 175, the domain is characterized as C2 1.
+At position 183 to 304, the domain is characterized as C2 2.
+At position 345 to 552, the domain is characterized as VWFA.
+At position 14 to 97, the domain is characterized as RRM 1.
+At position 105 to 184, the domain is characterized as RRM 2.
+At position 35 to 338, the domain is characterized as PPM-type phosphatase.
+At position 15 to 219, the domain is characterized as Cytochrome b561.
+At position 115 to 229, the domain is characterized as SET.
+At position 29 to 216, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 64, the domain is characterized as CSD.
+At position 387 to 546, the domain is characterized as PA14.
+At position 16 to 93, the domain is characterized as S4 RNA-binding.
+At position 378 to 585, the domain is characterized as MCM.
+At position 10 to 207, the domain is characterized as DPCK.
+At position 607 to 781, the domain is characterized as PCI.
+At position 33 to 98, the domain is characterized as NAC-A/B.
+At position 26 to 267, the domain is characterized as ABC transporter.
+At position 22 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 21 to 319, the domain is characterized as tr-type G.
+At position 24 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 180 to 270, the domain is characterized as 5'-3' exonuclease.
+At position 308 to 468, the domain is characterized as 3'-5' exonuclease.
+At position 522 to 705, the domain is characterized as Flavodoxin-like.
+At position 758 to 1004, the domain is characterized as FAD-binding FR-type.
+At position 34 to 128, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 131 to 271, the domain is characterized as FAD-binding FR-type.
+At position 65 to 271, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 137, the domain is characterized as MGS-like.
+At position 3 to 181, the domain is characterized as Guanylate kinase-like.
+At position 20 to 92, the domain is characterized as Chitin-binding type R&R.
+At position 5 to 47, the domain is characterized as CHCH.
+At position 103 to 293, the domain is characterized as ATP-grasp.
+At position 4 to 95, the domain is characterized as Core-binding (CB).
+At position 116 to 298, the domain is characterized as Tyr recombinase.
+At position 9 to 135, the domain is characterized as EamA 1.
+At position 186 to 313, the domain is characterized as EamA 2.
+At position 343 to 414, the domain is characterized as Ubiquitin-like.
+At position 197 to 282, the domain is characterized as KH.
+At position 323 to 416, the domain is characterized as HD.
+At position 19 to 105, the domain is characterized as PDZ.
+At position 496 to 529, the domain is characterized as WW.
+At position 10 to 65, the domain is characterized as bHLH.
+At position 86 to 121, the domain is characterized as Orange.
+At position 100 to 164, the domain is characterized as KH 1.
+At position 185 to 251, the domain is characterized as KH 2.
+At position 275 to 339, the domain is characterized as KH 3.
+At position 376 to 443, the domain is characterized as KH 4.
+At position 7 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 231 to 416, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 93, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 5 to 65, the domain is characterized as HTH iclR-type.
+At position 80 to 249, the domain is characterized as IclR-ED.
+At position 29 to 104, the domain is characterized as Importin N-terminal.
+At position 136 to 297, the domain is characterized as CRAL-TRIO.
+At position 71 to 291, the domain is characterized as Radical SAM core.
+At position 533 to 640, the domain is characterized as CBM20.
+At position 11 to 60, the domain is characterized as Myosin N-terminal SH3-like.
+At position 65 to 735, the domain is characterized as Myosin motor.
+At position 738 to 767, the domain is characterized as IQ 1.
+At position 761 to 790, the domain is characterized as IQ 2.
+At position 786 to 815, the domain is characterized as IQ 3.
+At position 809 to 838, the domain is characterized as IQ 4.
+At position 834 to 863, the domain is characterized as IQ 5.
+At position 857 to 886, the domain is characterized as IQ 6.
+At position 1163 to 1472, the domain is characterized as Dilute.
+At position 29 to 58, the domain is characterized as LRRNT.
+At position 305 to 357, the domain is characterized as LRRCT.
+At position 409 to 504, the domain is characterized as Fibronectin type-III.
+At position 1 to 63, the domain is characterized as TGS.
+At position 32 to 220, the domain is characterized as RNase H type-2.
+At position 30 to 89, the domain is characterized as VWFC.
+At position 1232 to 1466, the domain is characterized as Fibrillar collagen NC1.
+At position 1106 to 1230, the domain is characterized as PH.
+At position 10 to 197, the domain is characterized as RNase H type-2.
+At position 72 to 89, the domain is characterized as EF-hand 2.
+At position 95 to 130, the domain is characterized as EF-hand 3.
+At position 132 to 163, the domain is characterized as EF-hand 4.
+At position 12 to 179, the domain is characterized as MPN.
+At position 168 to 421, the domain is characterized as MHD.
+At position 24 to 54, the domain is characterized as LRRNT.
+At position 579 to 630, the domain is characterized as LRRCT.
+At position 673 to 816, the domain is characterized as TIR.
+At position 33 to 92, the domain is characterized as LIM zinc-binding 1.
+At position 92 to 154, the domain is characterized as LIM zinc-binding 2.
+At position 7 to 329, the domain is characterized as DhaK.
+At position 575 to 634, the domain is characterized as KH.
+At position 646 to 718, the domain is characterized as S1 motif.
+At position 25 to 352, the domain is characterized as Transferrin-like 1.
+At position 364 to 693, the domain is characterized as Transferrin-like 2.
+At position 1 to 42, the domain is characterized as KRAB.
+At position 31 to 272, the domain is characterized as ABC transporter.
+At position 57 to 141, the domain is characterized as RRM.
+At position 12 to 279, the domain is characterized as Protein kinase.
+At position 1 to 102, the domain is characterized as SSB.
+At position 12 to 201, the domain is characterized as RNase H type-2.
+At position 12 to 70, the domain is characterized as TRAM.
+At position 245 to 322, the domain is characterized as U-box.
+At position 175 to 364, the domain is characterized as ABC transmembrane type-1.
+At position 156 to 274, the domain is characterized as C2.
+At position 174 to 258, the domain is characterized as 5'-3' exonuclease.
+At position 93 to 155, the domain is characterized as S4 RNA-binding.
+At position 20 to 119, the domain is characterized as CFEM.
+At position 39 to 305, the domain is characterized as Septin-type G.
+At position 7 to 663, the domain is characterized as PFL.
+At position 670 to 789, the domain is characterized as Glycine radical.
+At position 6 to 128, the domain is characterized as CMP/dCMP-type deaminase.
+At position 320 to 370, the domain is characterized as bHLH.
+At position 36 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 413 to 577, the domain is characterized as Helicase ATP-binding.
+At position 602 to 775, the domain is characterized as Helicase C-terminal.
+At position 138 to 166, the domain is characterized as ITAM.
+At position 154 to 217, the domain is characterized as bZIP.
+At position 40 to 279, the domain is characterized as Peptidase S1.
+At position 99 to 337, the domain is characterized as Radical SAM core.
+At position 63 to 169, the domain is characterized as THUMP.
+At position 591 to 669, the domain is characterized as BRCT.
+At position 5 to 239, the domain is characterized as ABC transporter.
+At position 446 to 568, the domain is characterized as HD.
+At position 688 to 764, the domain is characterized as ACT 1.
+At position 794 to 863, the domain is characterized as ACT 2.
+At position 18 to 102, the domain is characterized as GS beta-grasp.
+At position 110 to 473, the domain is characterized as GS catalytic.
+At position 132 to 251, the domain is characterized as PAZ.
+At position 298 to 418, the domain is characterized as RNase III 1.
+At position 613 to 734, the domain is characterized as RNase III 2.
+At position 84 to 406, the domain is characterized as Asparaginase/glutaminase.
+At position 124 to 313, the domain is characterized as ATP-grasp.
+At position 113 to 341, the domain is characterized as Radical SAM core.
+At position 27 to 311, the domain is characterized as GH18.
+At position 134 to 193, the domain is characterized as SH3 1.
+At position 196 to 259, the domain is characterized as SH3 2.
+At position 452 to 513, the domain is characterized as SH3 3.
+At position 833 to 892, the domain is characterized as SH3 4.
+At position 140 to 390, the domain is characterized as Protein kinase.
+At position 2 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 85 to 163, the domain is characterized as RRM 1.
+At position 165 to 245, the domain is characterized as RRM 2.
+At position 584 to 673, the domain is characterized as BRCT.
+At position 1 to 87, the domain is characterized as PTS EIIB type-1.
+At position 107 to 461, the domain is characterized as PTS EIIC type-1.
+At position 45 to 741, the domain is characterized as GH81.
+At position 96 to 213, the domain is characterized as PX.
+At position 1 to 107, the domain is characterized as SSB.
+At position 102 to 283, the domain is characterized as DH.
+At position 313 to 411, the domain is characterized as PH.
+At position 3 to 127, the domain is characterized as ApaG.
+At position 52 to 172, the domain is characterized as RGS.
+At position 187 to 449, the domain is characterized as Protein kinase.
+At position 450 to 515, the domain is characterized as AGC-kinase C-terminal.
+At position 4 to 201, the domain is characterized as DPCK.
+At position 45 to 98, the domain is characterized as HTH cro/C1-type.
+At position 47 to 118, the domain is characterized as KH type-2.
+At position 118 to 500, the domain is characterized as Protein kinase.
+At position 7 to 158, the domain is characterized as N-acetyltransferase.
+At position 5 to 187, the domain is characterized as tr-type G.
+At position 98 to 162, the domain is characterized as PWWP.
+At position 29 to 148, the domain is characterized as NEAT.
+At position 2 to 120, the domain is characterized as MTTase N-terminal.
+At position 144 to 374, the domain is characterized as Radical SAM core.
+At position 377 to 440, the domain is characterized as TRAM.
+At position 100 to 222, the domain is characterized as MPN.
+At position 6 to 251, the domain is characterized as ABC transporter.
+At position 96 to 257, the domain is characterized as CRAL-TRIO.
+At position 7 to 189, the domain is characterized as tr-type G.
+At position 7 to 67, the domain is characterized as Chromo.
+At position 1025 to 1164, the domain is characterized as Peptidase S59.
+At position 84 to 136, the domain is characterized as HTH cro/C1-type.
+At position 282 to 441, the domain is characterized as FCP1 homology.
+At position 6 to 74, the domain is characterized as NAC-A/B.
+At position 5 to 153, the domain is characterized as Jacalin-type lectin 1.
+At position 160 to 301, the domain is characterized as Jacalin-type lectin 2.
+At position 311 to 453, the domain is characterized as Jacalin-type lectin 3.
+At position 19 to 54, the domain is characterized as CBM1.
+At position 38 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 6 to 107, the domain is characterized as Calponin-homology (CH).
+At position 188 to 281, the domain is characterized as EB1 C-terminal.
+At position 6 to 203, the domain is characterized as CYTH.
+At position 5 to 49, the domain is characterized as SpoVT-AbrB 1.
+At position 78 to 121, the domain is characterized as SpoVT-AbrB 2.
+At position 342 to 419, the domain is characterized as SPOR.
+At position 6 to 83, the domain is characterized as TFIIS N-terminal.
+At position 138 to 254, the domain is characterized as TFIIS central.
+At position 27 to 512, the domain is characterized as Sema.
+At position 864 to 959, the domain is characterized as IPT/TIG 1.
+At position 961 to 1045, the domain is characterized as IPT/TIG 2.
+At position 1048 to 1147, the domain is characterized as IPT/TIG 3.
+At position 1150 to 1236, the domain is characterized as IPT/TIG 4.
+At position 285 to 375, the domain is characterized as HPr.
+At position 375 to 532, the domain is characterized as F5/8 type C.
+At position 160 to 335, the domain is characterized as TRUD.
+At position 190 to 377, the domain is characterized as Helicase ATP-binding.
+At position 406 to 554, the domain is characterized as Helicase C-terminal.
+At position 23 to 283, the domain is characterized as OBG-type G.
+At position 304 to 387, the domain is characterized as TGS.
+At position 47 to 292, the domain is characterized as GH16.
+At position 291 to 406, the domain is characterized as CBM-cenC.
+At position 296 to 338, the domain is characterized as CUE.
+At position 76 to 301, the domain is characterized as Radical SAM core.
+At position 2 to 69, the domain is characterized as Biotinyl-binding.
+At position 2 to 169, the domain is characterized as Era-type G.
+At position 200 to 276, the domain is characterized as KH type-2.
+At position 5 to 267, the domain is characterized as Pyruvate carboxyltransferase.
+At position 38 to 124, the domain is characterized as ACT 1.
+At position 134 to 214, the domain is characterized as ACT 2.
+At position 283 to 358, the domain is characterized as ACT 3.
+At position 361 to 441, the domain is characterized as ACT 4.
+At position 95 to 195, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 7 to 135, the domain is characterized as RNase III.
+At position 160 to 229, the domain is characterized as DRBM.
+At position 61 to 189, the domain is characterized as CID.
+At position 236 to 357, the domain is characterized as SEA 1.
+At position 579 to 692, the domain is characterized as SEA 2.
+At position 14 to 249, the domain is characterized as ABC transporter 1.
+At position 264 to 506, the domain is characterized as ABC transporter 2.
+At position 38 to 359, the domain is characterized as G-alpha.
+At position 16 to 94, the domain is characterized as GIY-YIG.
+At position 1 to 445, the domain is characterized as Biotin carboxylation.
+At position 120 to 316, the domain is characterized as ATP-grasp.
+At position 526 to 601, the domain is characterized as Biotinyl-binding.
+At position 180 to 377, the domain is characterized as Peptidase M12B.
+At position 7 to 67, the domain is characterized as HTH tetR-type.
+At position 6 to 149, the domain is characterized as Nudix hydrolase.
+At position 70 to 122, the domain is characterized as bHLH.
+At position 12 to 136, the domain is characterized as Rhodanese.
+At position 109 to 160, the domain is characterized as bHLH.
+At position 3 to 243, the domain is characterized as ABC transporter.
+At position 6 to 173, the domain is characterized as Era-type G.
+At position 204 to 281, the domain is characterized as KH type-2.
+At position 17 to 94, the domain is characterized as GIY-YIG.
+At position 199 to 234, the domain is characterized as UVR.
+At position 160 to 334, the domain is characterized as OBG-type G.
+At position 20 to 316, the domain is characterized as Protein kinase.
+At position 1 to 183, the domain is characterized as KARI N-terminal Rossmann.
+At position 184 to 329, the domain is characterized as KARI C-terminal knotted.
+At position 672 to 862, the domain is characterized as ATP-grasp 2.
+At position 931 to 1068, the domain is characterized as MGS-like.
+At position 292 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 131 to 308, the domain is characterized as Urease.
+At position 684 to 719, the domain is characterized as Anaphylatoxin-like.
+At position 1507 to 1650, the domain is characterized as NTR.
+At position 165 to 243, the domain is characterized as Toprim.
+At position 137 to 376, the domain is characterized as Radical SAM core.
+At position 20 to 299, the domain is characterized as Protein kinase.
+At position 41 to 103, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 193, the domain is characterized as Ig-like C2-type 2.
+At position 230 to 297, the domain is characterized as Ig-like C2-type 3.
+At position 325 to 378, the domain is characterized as Ig-like C2-type 4.
+At position 412 to 464, the domain is characterized as Ig-like C2-type 5.
+At position 31 to 88, the domain is characterized as SLH 1.
+At position 89 to 152, the domain is characterized as SLH 2.
+At position 153 to 216, the domain is characterized as SLH 3.
+At position 233 to 339, the domain is characterized as HTH APSES-type.
+At position 29 to 283, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 108 to 162, the domain is characterized as bHLH.
+At position 4 to 141, the domain is characterized as ADF-H.
+At position 5 to 55, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 269 to 304, the domain is characterized as EF-hand 1.
+At position 270 to 359, the domain is characterized as EH 1.
+At position 306 to 338, the domain is characterized as EF-hand 2.
+At position 600 to 689, the domain is characterized as EH 2.
+At position 633 to 668, the domain is characterized as EF-hand 3.
+At position 246 to 440, the domain is characterized as GATase cobBQ-type.
+At position 136 to 577, the domain is characterized as Urease.
+At position 112 to 294, the domain is characterized as ATP-grasp.
+At position 9 to 218, the domain is characterized as YjeF N-terminal.
+At position 224 to 507, the domain is characterized as YjeF C-terminal.
+At position 7 to 253, the domain is characterized as SET.
+At position 496 to 606, the domain is characterized as CNA-B 1.
+At position 607 to 717, the domain is characterized as CNA-B 2.
+At position 8 to 125, the domain is characterized as Response regulatory.
+At position 183 to 375, the domain is characterized as CheB-type methylesterase.
+At position 47 to 309, the domain is characterized as Protein kinase.
+At position 160 to 245, the domain is characterized as PPIase FKBP-type.
+At position 675 to 751, the domain is characterized as RRM.
+At position 85 to 206, the domain is characterized as FZ.
+At position 378 to 490, the domain is characterized as Rhodanese.
+At position 14 to 89, the domain is characterized as Sm.
+At position 275 to 355, the domain is characterized as PUA.
+At position 1 to 165, the domain is characterized as EngA-type G 1.
+At position 227 to 400, the domain is characterized as EngA-type G 2.
+At position 401 to 485, the domain is characterized as KH-like.
+At position 247 to 306, the domain is characterized as SH3 1.
+At position 307 to 364, the domain is characterized as SH3 2.
+At position 63 to 739, the domain is characterized as Myosin motor.
+At position 742 to 763, the domain is characterized as IQ 1.
+At position 764 to 787, the domain is characterized as IQ 2.
+At position 788 to 817, the domain is characterized as IQ 3.
+At position 1212 to 1310, the domain is characterized as PH 1.
+At position 1392 to 1497, the domain is characterized as PH 2.
+At position 1547 to 1695, the domain is characterized as MyTH4.
+At position 1700 to 2044, the domain is characterized as FERM.
+At position 191 to 314, the domain is characterized as MsrB.
+At position 83 to 174, the domain is characterized as ACB.
+At position 384 to 526, the domain is characterized as GOLD.
+At position 193 to 293, the domain is characterized as Fe2OG dioxygenase.
+At position 5 to 63, the domain is characterized as TRAM.
+At position 2 to 401, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 122 to 341, the domain is characterized as Radical SAM core.
+At position 271 to 359, the domain is characterized as PDZ 1.
+At position 461 to 546, the domain is characterized as PDZ 2.
+At position 590 to 677, the domain is characterized as PDZ 3.
+At position 68 to 243, the domain is characterized as FAD-binding PCMH-type.
+At position 19 to 237, the domain is characterized as Glutamine amidotransferase type-2.
+At position 161 to 246, the domain is characterized as PPIase FKBP-type.
+At position 49 to 81, the domain is characterized as LisH.
+At position 19 to 71, the domain is characterized as HTH cro/C1-type.
+At position 1 to 43, the domain is characterized as C-type lectin.
+At position 26 to 121, the domain is characterized as Fibronectin type-III.
+At position 56 to 194, the domain is characterized as FAS1 1.
+At position 250 to 384, the domain is characterized as FAS1 2.
+At position 31 to 177, the domain is characterized as VOC.
+At position 69 to 144, the domain is characterized as ACT.
+At position 52 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 65 to 141, the domain is characterized as Carrier 1.
+At position 1178 to 1255, the domain is characterized as Carrier 2.
+At position 1740 to 1813, the domain is characterized as Carrier 3.
+At position 133 to 274, the domain is characterized as Fatty acid hydroxylase.
+At position 206 to 381, the domain is characterized as EngA-type G 2.
+At position 382 to 466, the domain is characterized as KH-like.
+At position 162 to 566, the domain is characterized as PUM-HD.
+At position 160 to 625, the domain is characterized as TBDR beta-barrel.
+At position 27 to 203, the domain is characterized as BPL/LPL catalytic.
+At position 102 to 224, the domain is characterized as MPN.
+At position 110 to 432, the domain is characterized as PDEase.
+At position 82 to 227, the domain is characterized as Flavodoxin-like.
+At position 277 to 543, the domain is characterized as FAD-binding FR-type.
+At position 464 to 614, the domain is characterized as N-acetyltransferase.
+At position 4 to 50, the domain is characterized as Agenet-like 1.
+At position 63 to 115, the domain is characterized as Agenet-like 2.
+At position 222 to 251, the domain is characterized as KH 1.
+At position 285 to 314, the domain is characterized as KH 2.
+At position 433 to 488, the domain is characterized as Kazal-like.
+At position 16 to 96, the domain is characterized as Ubiquitin-like.
+At position 30 to 174, the domain is characterized as F5/8 type C.
+At position 180 to 360, the domain is characterized as Laminin G-like 1.
+At position 367 to 544, the domain is characterized as Laminin G-like 2.
+At position 546 to 583, the domain is characterized as EGF-like 1.
+At position 584 to 790, the domain is characterized as Fibrinogen C-terminal.
+At position 791 to 956, the domain is characterized as Laminin G-like 3.
+At position 957 to 995, the domain is characterized as EGF-like 2.
+At position 1013 to 1199, the domain is characterized as Laminin G-like 4.
+At position 186 to 355, the domain is characterized as tr-type G.
+At position 8 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 222, the domain is characterized as ABC transporter 1.
+At position 290 to 516, the domain is characterized as ABC transporter 2.
+At position 548 to 672, the domain is characterized as STAS.
+At position 96 to 331, the domain is characterized as Radical SAM core.
+At position 100 to 460, the domain is characterized as Rab-GAP TBC.
+At position 179 to 209, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 2275 to 2596, the domain is characterized as PIPK.
+At position 10 to 210, the domain is characterized as tr-type G.
+At position 15 to 161, the domain is characterized as UBC core.
+At position 180 to 452, the domain is characterized as GH84.
+At position 916 to 1001, the domain is characterized as Fibronectin type-III.
+At position 283 to 360, the domain is characterized as PUA.
+At position 10 to 84, the domain is characterized as Carrier.
+At position 49 to 227, the domain is characterized as BPL/LPL catalytic.
+At position 7 to 129, the domain is characterized as MsrB.
+At position 9 to 87, the domain is characterized as GST N-terminal.
+At position 92 to 209, the domain is characterized as GST C-terminal.
+At position 70 to 105, the domain is characterized as EF-hand 1.
+At position 106 to 141, the domain is characterized as EF-hand 2.
+At position 157 to 192, the domain is characterized as EF-hand 3.
+At position 194 to 229, the domain is characterized as EF-hand 4.
+At position 235 to 270, the domain is characterized as EF-hand 5.
+At position 271 to 306, the domain is characterized as EF-hand 6.
+At position 593 to 671, the domain is characterized as BRCT.
+At position 1 to 83, the domain is characterized as BMV.
+At position 212 to 601, the domain is characterized as Peptidase S53.
+At position 193 to 379, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 112, the domain is characterized as MTTase N-terminal.
+At position 128 to 365, the domain is characterized as Radical SAM core.
+At position 368 to 434, the domain is characterized as TRAM.
+At position 94 to 165, the domain is characterized as SUI1.
+At position 517 to 619, the domain is characterized as CXC.
+At position 626 to 741, the domain is characterized as SET.
+At position 17 to 59, the domain is characterized as CHCH 1.
+At position 60 to 102, the domain is characterized as CHCH 2.
+At position 51 to 362, the domain is characterized as AB hydrolase-1.
+At position 34 to 212, the domain is characterized as Eph LBD.
+At position 331 to 441, the domain is characterized as Fibronectin type-III 1.
+At position 442 to 537, the domain is characterized as Fibronectin type-III 2.
+At position 631 to 944, the domain is characterized as Protein kinase.
+At position 961 to 1025, the domain is characterized as SAM.
+At position 67 to 158, the domain is characterized as ABM.
+At position 551 to 610, the domain is characterized as KH.
+At position 620 to 688, the domain is characterized as S1 motif.
+At position 244 to 431, the domain is characterized as GATase cobBQ-type.
+At position 6 to 295, the domain is characterized as Protein kinase.
+At position 29 to 73, the domain is characterized as Fibronectin type-II 1.
+At position 74 to 120, the domain is characterized as Fibronectin type-II 2.
+At position 39 to 81, the domain is characterized as Fibronectin type-I.
+At position 82 to 120, the domain is characterized as EGF-like.
+At position 126 to 208, the domain is characterized as Kringle 1.
+At position 214 to 296, the domain is characterized as Kringle 2.
+At position 311 to 561, the domain is characterized as Peptidase S1.
+At position 134 to 339, the domain is characterized as ATP-grasp.
+At position 357 to 433, the domain is characterized as Cytochrome b5 heme-binding.
+At position 27 to 141, the domain is characterized as Ig-like V-type.
+At position 355 to 633, the domain is characterized as Protein kinase.
+At position 41 to 298, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 5 to 295, the domain is characterized as FERM.
+At position 1 to 63, the domain is characterized as G-alpha.
+At position 1 to 183, the domain is characterized as YrdC-like.
+At position 16 to 93, the domain is characterized as RRM 1.
+At position 195 to 270, the domain is characterized as RRM 2.
+At position 1 to 350, the domain is characterized as SPX.
+At position 605 to 806, the domain is characterized as EXS.
+At position 16 to 309, the domain is characterized as Protein kinase.
+At position 29 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 6 to 233, the domain is characterized as Radical SAM core.
+At position 1 to 81, the domain is characterized as YcgL.
+At position 106 to 274, the domain is characterized as CP-type G.
+At position 12 to 66, the domain is characterized as HTH cro/C1-type.
+At position 11 to 46, the domain is characterized as EF-hand 1.
+At position 80 to 115, the domain is characterized as EF-hand 2.
+At position 120 to 155, the domain is characterized as EF-hand 3.
+At position 156 to 191, the domain is characterized as EF-hand 4.
+At position 28 to 96, the domain is characterized as Ig-like C2-type 1.
+At position 91 to 184, the domain is characterized as Ig-like C2-type 2.
+At position 190 to 281, the domain is characterized as Ig-like C2-type 3.
+At position 287 to 381, the domain is characterized as Ig-like C2-type 4.
+At position 389 to 493, the domain is characterized as Ig-like C2-type 5.
+At position 569 to 945, the domain is characterized as Protein kinase.
+At position 397 to 474, the domain is characterized as B5.
+At position 693 to 786, the domain is characterized as FDX-ACB.
+At position 54 to 175, the domain is characterized as RGS.
+At position 191 to 455, the domain is characterized as Protein kinase.
+At position 456 to 523, the domain is characterized as AGC-kinase C-terminal.
+At position 558 to 658, the domain is characterized as PH.
+At position 94 to 146, the domain is characterized as bHLH.
+At position 59 to 122, the domain is characterized as S5 DRBM.
+At position 105 to 274, the domain is characterized as Helicase ATP-binding.
+At position 285 to 463, the domain is characterized as Helicase C-terminal.
+At position 156 to 363, the domain is characterized as ATP-grasp.
+At position 182 to 277, the domain is characterized as CS.
+At position 312 to 395, the domain is characterized as SGS.
+At position 1 to 75, the domain is characterized as S1-like.
+At position 198 to 268, the domain is characterized as HARP 1.
+At position 284 to 355, the domain is characterized as HARP 2.
+At position 402 to 557, the domain is characterized as Helicase ATP-binding.
+At position 672 to 825, the domain is characterized as Helicase C-terminal.
+At position 10 to 92, the domain is characterized as GIY-YIG.
+At position 521 to 648, the domain is characterized as Guanylate cyclase.
+At position 7 to 185, the domain is characterized as Guanylate kinase-like.
+At position 12 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 206 to 395, the domain is characterized as GMPS ATP-PPase.
+At position 431 to 597, the domain is characterized as Helicase C-terminal.
+At position 633 to 668, the domain is characterized as UVR.
+At position 315 to 373, the domain is characterized as CBS 1.
+At position 377 to 435, the domain is characterized as CBS 2.
+At position 293 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 29 to 91, the domain is characterized as SH3b 1.
+At position 102 to 164, the domain is characterized as SH3b 2.
+At position 181 to 243, the domain is characterized as SH3b 3.
+At position 258 to 320, the domain is characterized as SH3b 4.
+At position 346 to 514, the domain is characterized as MurNAc-LAA.
+At position 28 to 66, the domain is characterized as LRRNT.
+At position 197 to 370, the domain is characterized as EngA-type G 2.
+At position 371 to 455, the domain is characterized as KH-like.
+At position 2 to 115, the domain is characterized as Thioredoxin.
+At position 267 to 348, the domain is characterized as PUA.
+At position 11 to 160, the domain is characterized as Ferritin-like diiron.
+At position 23 to 74, the domain is characterized as Rubredoxin-like.
+At position 48 to 159, the domain is characterized as TBDR plug.
+At position 170 to 661, the domain is characterized as TBDR beta-barrel.
+At position 85 to 175, the domain is characterized as K-box.
+At position 4 to 119, the domain is characterized as VOC.
+At position 1 to 73, the domain is characterized as RRM 1.
+At position 79 to 149, the domain is characterized as RRM 2.
+At position 400 to 838, the domain is characterized as Urease.
+At position 49 to 307, the domain is characterized as GB1/RHD3-type G.
+At position 18 to 96, the domain is characterized as RRM 1.
+At position 106 to 182, the domain is characterized as RRM 2.
+At position 199 to 276, the domain is characterized as RRM 3.
+At position 302 to 378, the domain is characterized as RRM 4.
+At position 22 to 157, the domain is characterized as Obg.
+At position 158 to 353, the domain is characterized as OBG-type G.
+At position 1612 to 1819, the domain is characterized as Rap-GAP.
+At position 168 to 293, the domain is characterized as Nudix hydrolase.
+At position 25 to 97, the domain is characterized as S4 RNA-binding.
+At position 70 to 183, the domain is characterized as Plastocyanin-like 1.
+At position 195 to 357, the domain is characterized as Plastocyanin-like 2.
+At position 466 to 563, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 223, the domain is characterized as Peptidase S1.
+At position 130 to 324, the domain is characterized as AMMECR1.
+At position 6 to 78, the domain is characterized as KRAB.
+At position 137 to 439, the domain is characterized as NB-ARC.
+At position 5 to 108, the domain is characterized as PH.
+At position 150 to 408, the domain is characterized as Protein kinase.
+At position 409 to 480, the domain is characterized as AGC-kinase C-terminal.
+At position 420 to 734, the domain is characterized as FERM.
+At position 126 to 460, the domain is characterized as Rab-GAP TBC.
+At position 107 to 280, the domain is characterized as Helicase ATP-binding.
+At position 291 to 464, the domain is characterized as Helicase C-terminal.
+At position 1 to 145, the domain is characterized as Ferritin-like diiron.
+At position 215 to 376, the domain is characterized as TrmE-type G.
+At position 197 to 387, the domain is characterized as GMPS ATP-PPase.
+At position 51 to 281, the domain is characterized as Radical SAM core.
+At position 2 to 190, the domain is characterized as Glutamine amidotransferase type-1.
+At position 19 to 148, the domain is characterized as RNase III.
+At position 174 to 243, the domain is characterized as DRBM.
+At position 32 to 229, the domain is characterized as PNPLA.
+At position 32 to 104, the domain is characterized as Ubiquitin-like 1.
+At position 109 to 187, the domain is characterized as Ubiquitin-like 2.
+At position 257 to 542, the domain is characterized as PI3K/PI4K catalytic.
+At position 247 to 352, the domain is characterized as RRM Nup35-type.
+At position 4 to 169, the domain is characterized as EngA-type G 1.
+At position 178 to 353, the domain is characterized as EngA-type G 2.
+At position 354 to 439, the domain is characterized as KH-like.
+At position 41 to 85, the domain is characterized as Gla.
+At position 86 to 122, the domain is characterized as EGF-like 1; calcium-binding.
+At position 127 to 168, the domain is characterized as EGF-like 2.
+At position 193 to 432, the domain is characterized as Peptidase S1.
+At position 93 to 477, the domain is characterized as PRONE.
+At position 71 to 149, the domain is characterized as GIY-YIG.
+At position 259 to 294, the domain is characterized as UVR.
+At position 104 to 154, the domain is characterized as DHHC.
+At position 28 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 555 to 614, the domain is characterized as KH.
+At position 624 to 692, the domain is characterized as S1 motif.
+At position 151 to 316, the domain is characterized as Helicase ATP-binding.
+At position 457 to 608, the domain is characterized as Helicase C-terminal.
+At position 833 to 885, the domain is characterized as SANT.
+At position 2 to 225, the domain is characterized as ABC transporter.
+At position 157 to 279, the domain is characterized as C2 1.
+At position 291 to 426, the domain is characterized as C2 2.
+At position 369 to 579, the domain is characterized as TRUD.
+At position 9 to 154, the domain is characterized as N-acetyltransferase.
+At position 121 to 327, the domain is characterized as ATP-grasp.
+At position 571 to 648, the domain is characterized as S1 motif.
+At position 413 to 582, the domain is characterized as tr-type G.
+At position 137 to 201, the domain is characterized as J.
+At position 23 to 90, the domain is characterized as Importin N-terminal.
+At position 216 to 297, the domain is characterized as KH.
+At position 342 to 435, the domain is characterized as HD.
+At position 93 to 132, the domain is characterized as Agouti.
+At position 62 to 320, the domain is characterized as Protein kinase.
+At position 20 to 118, the domain is characterized as Ig-like.
+At position 154 to 297, the domain is characterized as PPC.
+At position 3 to 282, the domain is characterized as DegV.
+At position 711 to 786, the domain is characterized as Smr.
+At position 6 to 51, the domain is characterized as F-box.
+At position 2 to 88, the domain is characterized as GST N-terminal.
+At position 90 to 208, the domain is characterized as GST C-terminal.
+At position 139 to 390, the domain is characterized as Alpha-carbonic anhydrase.
+At position 134 to 255, the domain is characterized as Peptidase C51.
+At position 79 to 393, the domain is characterized as Peptidase A1.
+At position 21 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 1 to 81, the domain is characterized as Ubiquitin-like.
+At position 1 to 71, the domain is characterized as S1-like.
+At position 101 to 317, the domain is characterized as ATP-grasp.
+At position 2 to 261, the domain is characterized as NodB homology.
+At position 1 to 84, the domain is characterized as YcgL.
+At position 1 to 275, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 269 to 583, the domain is characterized as UvrD-like helicase C-terminal.
+At position 94 to 154, the domain is characterized as S4 RNA-binding.
+At position 132 to 189, the domain is characterized as HTH cro/C1-type.
+At position 30 to 156, the domain is characterized as C-type lectin.
+At position 162 to 232, the domain is characterized as Sushi.
+At position 312 to 351, the domain is characterized as EGF-like; calcium-binding.
+At position 127 to 217, the domain is characterized as RRM.
+At position 83 to 367, the domain is characterized as Protein kinase.
+At position 92 to 167, the domain is characterized as PRC barrel.
+At position 7 to 237, the domain is characterized as ABC transporter.
+At position 44 to 362, the domain is characterized as GP-PDE.
+At position 212 to 370, the domain is characterized as Cupin type-1 1.
+At position 422 to 583, the domain is characterized as Cupin type-1 2.
+At position 12 to 295, the domain is characterized as Protein kinase.
+At position 197 to 293, the domain is characterized as PH.
+At position 284 to 404, the domain is characterized as C2.
+At position 458 to 650, the domain is characterized as Ras-GAP.
+At position 37 to 100, the domain is characterized as S4 RNA-binding.
+At position 22 to 210, the domain is characterized as Albumin 1.
+At position 211 to 403, the domain is characterized as Albumin 2.
+At position 404 to 599, the domain is characterized as Albumin 3.
+At position 462 to 631, the domain is characterized as tr-type G.
+At position 415 to 584, the domain is characterized as tr-type G.
+At position 5 to 242, the domain is characterized as tr-type G.
+At position 281 to 407, the domain is characterized as AB hydrolase-1.
+At position 485 to 546, the domain is characterized as SH3.
+At position 558 to 697, the domain is characterized as PID.
+At position 1 to 361, the domain is characterized as GH18.
+At position 253 to 446, the domain is characterized as GATase cobBQ-type.
+At position 183 to 327, the domain is characterized as KARI C-terminal knotted.
+At position 74 to 385, the domain is characterized as IF rod.
+At position 41 to 265, the domain is characterized as Radical SAM core.
+At position 93 to 212, the domain is characterized as EamA.
+At position 22 to 116, the domain is characterized as HTH La-type RNA-binding.
+At position 119 to 197, the domain is characterized as RRM.
+At position 438 to 551, the domain is characterized as xRRM.
+At position 7 to 133, the domain is characterized as Longin.
+At position 4 to 254, the domain is characterized as Protein kinase.
+At position 52 to 189, the domain is characterized as RUN.
+At position 8 to 287, the domain is characterized as tr-type G.
+At position 752 to 838, the domain is characterized as SUEL-type lectin.
+At position 433 to 600, the domain is characterized as Helicase ATP-binding.
+At position 831 to 990, the domain is characterized as Helicase C-terminal.
+At position 7 to 81, the domain is characterized as S1-like.
+At position 127 to 298, the domain is characterized as Helicase ATP-binding.
+At position 308 to 468, the domain is characterized as Helicase C-terminal.
+At position 27 to 126, the domain is characterized as PWI.
+At position 1 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 66, the domain is characterized as IF rod.
+At position 485 to 682, the domain is characterized as DH.
+At position 723 to 825, the domain is characterized as PH.
+At position 6 to 122, the domain is characterized as Response regulatory.
+At position 142 to 207, the domain is characterized as HTH luxR-type.
+At position 273 to 347, the domain is characterized as U-box.
+At position 63 to 98, the domain is characterized as EF-hand 1.
+At position 99 to 132, the domain is characterized as EF-hand 2.
+At position 289 to 377, the domain is characterized as ABM.
+At position 298 to 505, the domain is characterized as Histidine kinase.
+At position 7 to 250, the domain is characterized as ABC transporter.
+At position 7 to 120, the domain is characterized as DMAP1-binding.
+At position 348 to 419, the domain is characterized as Ubiquitin-like.
+At position 50 to 279, the domain is characterized as Radical SAM core.
+At position 344 to 580, the domain is characterized as Methyl-accepting transducer.
+At position 17 to 30, the domain is characterized as CRIB.
+At position 6 to 80, the domain is characterized as S1-like.
+At position 329 to 499, the domain is characterized as tr-type G.
+At position 18 to 64, the domain is characterized as F-box.
+At position 593 to 681, the domain is characterized as BRCT.
+At position 28 to 129, the domain is characterized as AB hydrolase-1.
+At position 92 to 153, the domain is characterized as S4 RNA-binding.
+At position 1 to 276, the domain is characterized as SMP-LTD.
+At position 354 to 438, the domain is characterized as KH-like.
+At position 420 to 576, the domain is characterized as Exonuclease.
+At position 14 to 112, the domain is characterized as Ras-associating.
+At position 146 to 1016, the domain is characterized as Myosin motor.
+At position 1021 to 1041, the domain is characterized as IQ 1.
+At position 1042 to 1071, the domain is characterized as IQ 2.
+At position 1074 to 1103, the domain is characterized as IQ 3.
+At position 1115 to 1144, the domain is characterized as IQ 4.
+At position 1138 to 1167, the domain is characterized as IQ 5.
+At position 2063 to 2251, the domain is characterized as Rho-GAP.
+At position 232 to 479, the domain is characterized as Ku.
+At position 236 to 406, the domain is characterized as Helicase ATP-binding.
+At position 427 to 583, the domain is characterized as Helicase C-terminal.
+At position 806 to 886, the domain is characterized as HRDC.
+At position 27 to 254, the domain is characterized as Peptidase S1.
+At position 7 to 131, the domain is characterized as ApaG.
+At position 124 to 187, the domain is characterized as bZIP.
+At position 18 to 53, the domain is characterized as EF-hand 1.
+At position 57 to 85, the domain is characterized as EF-hand 2.
+At position 87 to 122, the domain is characterized as EF-hand 3.
+At position 128 to 163, the domain is characterized as EF-hand 4.
+At position 2 to 77, the domain is characterized as Lipoyl-binding.
+At position 112 to 149, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 60 to 249, the domain is characterized as Brix.
+At position 124 to 502, the domain is characterized as Protein kinase.
+At position 65 to 150, the domain is characterized as SAND.
+At position 20 to 274, the domain is characterized as Protein kinase.
+At position 23 to 205, the domain is characterized as EngB-type G.
+At position 33 to 96, the domain is characterized as Sushi 1.
+At position 97 to 159, the domain is characterized as Sushi 2.
+At position 160 to 225, the domain is characterized as Sushi 3.
+At position 226 to 285, the domain is characterized as Sushi 4.
+At position 21 to 66, the domain is characterized as WAP.
+At position 133 to 326, the domain is characterized as ATP-grasp.
+At position 1 to 39, the domain is characterized as HYR 1.
+At position 40 to 123, the domain is characterized as HYR 2.
+At position 124 to 207, the domain is characterized as HYR 3.
+At position 208 to 292, the domain is characterized as HYR 4.
+At position 293 to 376, the domain is characterized as HYR 5.
+At position 377 to 460, the domain is characterized as HYR 6.
+At position 461 to 544, the domain is characterized as HYR 7.
+At position 546 to 629, the domain is characterized as HYR 8.
+At position 630 to 713, the domain is characterized as HYR 9.
+At position 714 to 797, the domain is characterized as HYR 10.
+At position 798 to 881, the domain is characterized as HYR 11.
+At position 882 to 966, the domain is characterized as HYR 12.
+At position 967 to 1050, the domain is characterized as HYR 13.
+At position 1051 to 1133, the domain is characterized as HYR 14.
+At position 1134 to 1200, the domain is characterized as HYR 15.
+At position 256 to 433, the domain is characterized as Helicase ATP-binding.
+At position 651 to 812, the domain is characterized as Helicase C-terminal.
+At position 840 to 935, the domain is characterized as Dicer dsRNA-binding fold.
+At position 1189 to 1318, the domain is characterized as PAZ.
+At position 1342 to 1518, the domain is characterized as RNase III 1.
+At position 1559 to 1707, the domain is characterized as RNase III 2.
+At position 1733 to 1796, the domain is characterized as DRBM 1.
+At position 1831 to 1906, the domain is characterized as DRBM 2.
+At position 99 to 142, the domain is characterized as LysM.
+At position 208 to 275, the domain is characterized as GRAM.
+At position 713 to 874, the domain is characterized as TLDc.
+At position 345 to 411, the domain is characterized as S4 RNA-binding.
+At position 2 to 82, the domain is characterized as GST N-terminal.
+At position 88 to 230, the domain is characterized as GST C-terminal.
+At position 254 to 418, the domain is characterized as Helicase ATP-binding.
+At position 15 to 178, the domain is characterized as TIR.
+At position 210 to 480, the domain is characterized as NB-ARC.
+At position 456 to 674, the domain is characterized as FtsK.
+At position 46 to 208, the domain is characterized as Helicase ATP-binding.
+At position 325 to 481, the domain is characterized as Helicase C-terminal.
+At position 1006 to 1046, the domain is characterized as HNH.
+At position 374 to 806, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1295 to 1605, the domain is characterized as PKS/mFAS DH.
+At position 1670 to 1747, the domain is characterized as Carrier 1.
+At position 1798 to 1875, the domain is characterized as Carrier 2.
+At position 4 to 82, the domain is characterized as Carrier.
+At position 479 to 799, the domain is characterized as Protein kinase.
+At position 1 to 96, the domain is characterized as CRM.
+At position 134 to 581, the domain is characterized as Urease.
+At position 5 to 47, the domain is characterized as SpoVT-AbrB 1.
+At position 76 to 119, the domain is characterized as SpoVT-AbrB 2.
+At position 152 to 324, the domain is characterized as Helicase ATP-binding.
+At position 403 to 554, the domain is characterized as Helicase C-terminal.
+At position 11 to 79, the domain is characterized as HTH gntR-type.
+At position 68 to 111, the domain is characterized as F-box.
+At position 146 to 276, the domain is characterized as SEC7.
+At position 100 to 181, the domain is characterized as PDZ.
+At position 63 to 234, the domain is characterized as Helicase ATP-binding.
+At position 245 to 406, the domain is characterized as Helicase C-terminal.
+At position 443 to 814, the domain is characterized as USP.
+At position 860 to 1033, the domain is characterized as Exonuclease.
+At position 3 to 92, the domain is characterized as ABM.
+At position 27 to 114, the domain is characterized as Ig-like.
+At position 10 to 133, the domain is characterized as RNase III.
+At position 52 to 260, the domain is characterized as YjeF N-terminal.
+At position 170 to 396, the domain is characterized as TRUD.
+At position 555 to 730, the domain is characterized as Helicase ATP-binding.
+At position 897 to 1057, the domain is characterized as Helicase C-terminal.
+At position 227 to 431, the domain is characterized as Peptidase M12B.
+At position 437 to 524, the domain is characterized as Disintegrin.
+At position 662 to 699, the domain is characterized as EGF-like.
+At position 302 to 384, the domain is characterized as Helicase ATP-binding; first part.
+At position 433 to 507, the domain is characterized as H15.
+At position 701 to 859, the domain is characterized as Helicase ATP-binding; second part.
+At position 1505 to 1663, the domain is characterized as Helicase C-terminal.
+At position 15 to 257, the domain is characterized as ABC transporter.
+At position 316 to 519, the domain is characterized as ABC transmembrane type-2.
+At position 35 to 193, the domain is characterized as Cupin type-1 1.
+At position 228 to 383, the domain is characterized as Cupin type-1 2.
+At position 28 to 280, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 37 to 307, the domain is characterized as Deacetylase sirtuin-type.
+At position 201 to 374, the domain is characterized as EngA-type G 2.
+At position 375 to 459, the domain is characterized as KH-like.
+At position 24 to 239, the domain is characterized as tr-type G.
+At position 101 to 339, the domain is characterized as NR LBD.
+At position 3 to 246, the domain is characterized as ABC transporter.
+At position 25 to 100, the domain is characterized as REM-1 1.
+At position 113 to 194, the domain is characterized as REM-1 2.
+At position 200 to 281, the domain is characterized as REM-1 3.
+At position 308 to 471, the domain is characterized as C2.
+At position 617 to 876, the domain is characterized as Protein kinase.
+At position 877 to 944, the domain is characterized as AGC-kinase C-terminal.
+At position 8 to 179, the domain is characterized as PCI.
+At position 215 to 250, the domain is characterized as EF-hand 1.
+At position 405 to 440, the domain is characterized as EF-hand 2.
+At position 27 to 110, the domain is characterized as Ig-like C2-type.
+At position 112 to 219, the domain is characterized as Fibronectin type-III 1.
+At position 220 to 317, the domain is characterized as Fibronectin type-III 2.
+At position 23 to 104, the domain is characterized as Lipoyl-binding.
+At position 185 to 360, the domain is characterized as EngA-type G 2.
+At position 361 to 445, the domain is characterized as KH-like.
+At position 368 to 519, the domain is characterized as N-acetyltransferase.
+At position 20 to 128, the domain is characterized as PH.
+At position 142 to 177, the domain is characterized as EF-hand 1.
+At position 178 to 214, the domain is characterized as EF-hand 2.
+At position 226 to 246, the domain is characterized as EF-hand 3.
+At position 299 to 444, the domain is characterized as PI-PLC X-box.
+At position 602 to 715, the domain is characterized as PI-PLC Y-box.
+At position 716 to 844, the domain is characterized as C2.
+At position 184 to 467, the domain is characterized as ABC transmembrane type-1.
+At position 500 to 736, the domain is characterized as ABC transporter.
+At position 2 to 109, the domain is characterized as HIT.
+At position 551 to 622, the domain is characterized as J.
+At position 147 to 465, the domain is characterized as Peptidase S8.
+At position 6 to 128, the domain is characterized as RNase III.
+At position 155 to 225, the domain is characterized as DRBM.
+At position 38 to 117, the domain is characterized as RRM.
+At position 27 to 146, the domain is characterized as Ricin B-type lectin 1.
+At position 117 to 250, the domain is characterized as Ricin B-type lectin 2.
+At position 5 to 73, the domain is characterized as J.
+At position 19 to 103, the domain is characterized as LIM zinc-binding.
+At position 909 to 1042, the domain is characterized as MATH.
+At position 591 to 670, the domain is characterized as BRCT.
+At position 265 to 369, the domain is characterized as PH.
+At position 383 to 568, the domain is characterized as Rho-GAP.
+At position 713 to 771, the domain is characterized as SH3.
+At position 350 to 417, the domain is characterized as S4 RNA-binding.
+At position 73 to 268, the domain is characterized as TR mART core.
+At position 1 to 125, the domain is characterized as ApaG.
+At position 34 to 189, the domain is characterized as SIS.
+At position 150 to 260, the domain is characterized as FAD-binding FR-type.
+At position 240 to 274, the domain is characterized as SAP.
+At position 2 to 204, the domain is characterized as ABC transporter.
+At position 22 to 92, the domain is characterized as IGFBP N-terminal.
+At position 74 to 136, the domain is characterized as Kazal-like.
+At position 344 to 447, the domain is characterized as PDZ.
+At position 35 to 277, the domain is characterized as GB1/RHD3-type G.
+At position 130 to 244, the domain is characterized as PilZ.
+At position 46 to 80, the domain is characterized as WW.
+At position 19 to 96, the domain is characterized as Ubiquitin-like.
+At position 40 to 158, the domain is characterized as tRNA-binding.
+At position 397 to 468, the domain is characterized as B5.
+At position 691 to 772, the domain is characterized as FDX-ACB.
+At position 201 to 377, the domain is characterized as OTU.
+At position 764 to 841, the domain is characterized as BRCT.
+At position 294 to 546, the domain is characterized as Glutamine amidotransferase type-1.
+At position 573 to 632, the domain is characterized as KH.
+At position 642 to 717, the domain is characterized as S1 motif.
+At position 341 to 464, the domain is characterized as PLAT.
+At position 1 to 201, the domain is characterized as DHFR.
+At position 870 to 899, the domain is characterized as IQ 1.
+At position 893 to 922, the domain is characterized as IQ 2.
+At position 48 to 109, the domain is characterized as KH.
+At position 253 to 428, the domain is characterized as Helicase ATP-binding.
+At position 440 to 601, the domain is characterized as Helicase C-terminal.
+At position 1 to 132, the domain is characterized as ADF-H.
+At position 3 to 170, the domain is characterized as Era-type G.
+At position 201 to 278, the domain is characterized as KH type-2.
+At position 102 to 153, the domain is characterized as HTH myb-type 1.
+At position 154 to 208, the domain is characterized as HTH myb-type 2.
+At position 145 to 274, the domain is characterized as Fatty acid hydroxylase.
+At position 192 to 266, the domain is characterized as RRM.
+At position 4 to 119, the domain is characterized as MTTase N-terminal.
+At position 38 to 73, the domain is characterized as EF-hand 1.
+At position 77 to 108, the domain is characterized as EF-hand 2.
+At position 6 to 74, the domain is characterized as HTH gntR-type.
+At position 40 to 325, the domain is characterized as Protein kinase.
+At position 3 to 88, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 92 to 121, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 342, the domain is characterized as IF rod.
+At position 375 to 493, the domain is characterized as LTD.
+At position 166 to 270, the domain is characterized as Cadherin 1.
+At position 271 to 375, the domain is characterized as Cadherin 2.
+At position 376 to 479, the domain is characterized as Cadherin 3.
+At position 480 to 581, the domain is characterized as Cadherin 4.
+At position 582 to 682, the domain is characterized as Cadherin 5.
+At position 683 to 784, the domain is characterized as Cadherin 6.
+At position 785 to 892, the domain is characterized as Cadherin 7.
+At position 893 to 1000, the domain is characterized as Cadherin 8.
+At position 1251 to 1287, the domain is characterized as EGF-like 1.
+At position 1333 to 1526, the domain is characterized as Laminin G-like 1.
+At position 1529 to 1568, the domain is characterized as EGF-like 2.
+At position 1577 to 1732, the domain is characterized as Laminin G-like 2.
+At position 1734 to 1771, the domain is characterized as EGF-like 3.
+At position 1776 to 1808, the domain is characterized as EGF-like 4.
+At position 2171 to 2218, the domain is characterized as GPS.
+At position 1087 to 1147, the domain is characterized as v-SNARE coiled-coil homology.
+At position 7 to 60, the domain is characterized as F-box.
+At position 19 to 125, the domain is characterized as Ig-like V-type.
+At position 42 to 95, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 97 to 151, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 410 to 737, the domain is characterized as NACHT.
+At position 2 to 219, the domain is characterized as Glutamine amidotransferase type-2.
+At position 250 to 639, the domain is characterized as Asparagine synthetase.
+At position 7 to 132, the domain is characterized as RNase III.
+At position 157 to 226, the domain is characterized as DRBM.
+At position 404 to 605, the domain is characterized as 3'-5' exonuclease.
+At position 153 to 408, the domain is characterized as ABC transporter 1.
+At position 850 to 1093, the domain is characterized as ABC transporter 2.
+At position 30 to 303, the domain is characterized as EndoU.
+At position 711 to 1026, the domain is characterized as Protein kinase.
+At position 1029 to 1163, the domain is characterized as KEN.
+At position 46 to 222, the domain is characterized as Collagen-like.
+At position 260 to 374, the domain is characterized as C-type lectin.
+At position 8 to 146, the domain is characterized as DAC.
+At position 51 to 113, the domain is characterized as J.
+At position 1 to 79, the domain is characterized as Ubiquitin-like.
+At position 188 to 228, the domain is characterized as UBA 1.
+At position 274 to 317, the domain is characterized as STI1.
+At position 370 to 410, the domain is characterized as UBA 2.
+At position 1 to 66, the domain is characterized as TGS.
+At position 319 to 405, the domain is characterized as PPIase FKBP-type.
+At position 34 to 100, the domain is characterized as PQ-loop 1.
+At position 184 to 243, the domain is characterized as PQ-loop 2.
+At position 17 to 77, the domain is characterized as HTH tetR-type.
+At position 29 to 75, the domain is characterized as CHCH.
+At position 63 to 235, the domain is characterized as FAD-binding PCMH-type.
+At position 147 to 212, the domain is characterized as HTH luxR-type.
+At position 13 to 146, the domain is characterized as UBC core.
+At position 2 to 229, the domain is characterized as ABC transporter.
+At position 894 to 971, the domain is characterized as RRM.
+At position 4 to 140, the domain is characterized as SprT-like.
+At position 181 to 321, the domain is characterized as Helicase ATP-binding.
+At position 330 to 508, the domain is characterized as Helicase C-terminal.
+At position 17 to 300, the domain is characterized as ABC transmembrane type-1.
+At position 335 to 571, the domain is characterized as ABC transporter.
+At position 8 to 260, the domain is characterized as Pyruvate carboxyltransferase.
+At position 18 to 205, the domain is characterized as YrdC-like.
+At position 123 to 156, the domain is characterized as WW 1.
+At position 164 to 197, the domain is characterized as WW 2.
+At position 10 to 134, the domain is characterized as Cyclin N-terminal.
+At position 36 to 122, the domain is characterized as Inhibitor I9.
+At position 131 to 421, the domain is characterized as Peptidase S8.
+At position 122 to 294, the domain is characterized as Helicase ATP-binding.
+At position 360 to 511, the domain is characterized as Helicase C-terminal.
+At position 1 to 66, the domain is characterized as RGS.
+At position 292 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 271 to 345, the domain is characterized as U-box.
+At position 296 to 443, the domain is characterized as N-acetyltransferase.
+At position 5 to 58, the domain is characterized as ClpX-type ZB.
+At position 679 to 876, the domain is characterized as ATP-grasp 2.
+At position 943 to 1080, the domain is characterized as MGS-like.
+At position 194 to 446, the domain is characterized as Olfactomedin-like.
+At position 285 to 410, the domain is characterized as Nop.
+At position 51 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 90 to 119, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 15 to 81, the domain is characterized as PQ-loop 1.
+At position 149 to 204, the domain is characterized as PQ-loop 2.
+At position 116 to 179, the domain is characterized as bZIP.
+At position 91 to 157, the domain is characterized as S4 RNA-binding.
+At position 361 to 404, the domain is characterized as LysM 1.
+At position 429 to 472, the domain is characterized as LysM 2.
+At position 497 to 540, the domain is characterized as LysM 3.
+At position 565 to 608, the domain is characterized as LysM 4.
+At position 631 to 674, the domain is characterized as LysM 5.
+At position 693 to 736, the domain is characterized as LysM 6.
+At position 13 to 91, the domain is characterized as GIY-YIG.
+At position 202 to 237, the domain is characterized as UVR.
+At position 14 to 77, the domain is characterized as S5 DRBM.
+At position 599 to 726, the domain is characterized as PH.
+At position 948 to 1146, the domain is characterized as Rho-GAP.
+At position 229 to 321, the domain is characterized as RRM.
+At position 6 to 84, the domain is characterized as RRM.
+At position 143 to 299, the domain is characterized as PPIase cyclophilin-type.
+At position 35 to 65, the domain is characterized as LRRNT.
+At position 196 to 251, the domain is characterized as LRRCT.
+At position 102 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 5 to 205, the domain is characterized as N-acetyltransferase.
+At position 145 to 209, the domain is characterized as KH 1.
+At position 234 to 300, the domain is characterized as KH 2.
+At position 323 to 387, the domain is characterized as KH 3.
+At position 425 to 492, the domain is characterized as KH 4.
+At position 1 to 343, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 281 to 587, the domain is characterized as UvrD-like helicase C-terminal.
+At position 49 to 239, the domain is characterized as Rho-GAP.
+At position 97 to 179, the domain is characterized as RRM 1.
+At position 182 to 261, the domain is characterized as RRM 2.
+At position 98 to 409, the domain is characterized as IF rod.
+At position 4 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 49 to 728, the domain is characterized as Myosin motor.
+At position 786 to 973, the domain is characterized as TH1.
+At position 1084 to 1145, the domain is characterized as SH3.
+At position 8 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 206 to 398, the domain is characterized as GMPS ATP-PPase.
+At position 31 to 214, the domain is characterized as SIS.
+At position 14 to 78, the domain is characterized as NAC-A/B.
+At position 137 to 176, the domain is characterized as UBA.
+At position 7 to 101, the domain is characterized as Ig-like.
+At position 1074 to 1209, the domain is characterized as TIR.
+At position 274 to 667, the domain is characterized as USP.
+At position 407 to 491, the domain is characterized as B5.
+At position 713 to 806, the domain is characterized as FDX-ACB.
+At position 66 to 210, the domain is characterized as SCP.
+At position 12 to 71, the domain is characterized as SH3.
+At position 2 to 50, the domain is characterized as F-box.
+At position 930 to 1057, the domain is characterized as MGS-like.
+At position 24 to 230, the domain is characterized as PNPLA.
+At position 1 to 131, the domain is characterized as MGS-like.
+At position 49 to 165, the domain is characterized as Thioredoxin.
+At position 31 to 99, the domain is characterized as BTB.
+At position 126 to 159, the domain is characterized as WW 1.
+At position 186 to 219, the domain is characterized as WW 2.
+At position 7 to 197, the domain is characterized as RNase H type-2.
+At position 179 to 343, the domain is characterized as SUN.
+At position 134 to 215, the domain is characterized as PDZ 2.
+At position 25 to 137, the domain is characterized as RWD.
+At position 296 to 539, the domain is characterized as Protein kinase 1.
+At position 590 to 1001, the domain is characterized as Protein kinase 2.
+At position 24 to 265, the domain is characterized as ABC transporter.
+At position 92 to 205, the domain is characterized as Response regulatory.
+At position 26 to 162, the domain is characterized as ENTH.
+At position 7 to 64, the domain is characterized as PWWP.
+At position 73 to 220, the domain is characterized as Tyrosine-protein phosphatase.
+At position 3 to 50, the domain is characterized as F-box.
+At position 71 to 252, the domain is characterized as FBA.
+At position 22 to 197, the domain is characterized as EngB-type G.
+At position 20 to 194, the domain is characterized as Exonuclease.
+At position 8 to 238, the domain is characterized as ABC transporter.
+At position 15 to 698, the domain is characterized as Myosin motor.
+At position 774 to 957, the domain is characterized as TH1.
+At position 1123 to 1182, the domain is characterized as SH3.
+At position 401 to 558, the domain is characterized as N-acetyltransferase.
+At position 67 to 175, the domain is characterized as TBDR plug.
+At position 180 to 760, the domain is characterized as TBDR beta-barrel.
+At position 215 to 394, the domain is characterized as PCI.
+At position 5 to 57, the domain is characterized as HTH myb-type 1.
+At position 58 to 112, the domain is characterized as HTH myb-type 2.
+At position 156 to 288, the domain is characterized as Calponin-homology (CH).
+At position 1489 to 1623, the domain is characterized as CKK.
+At position 46 to 75, the domain is characterized as IQ.
+At position 692 to 1029, the domain is characterized as HECT.
+At position 40 to 84, the domain is characterized as Gla.
+At position 85 to 121, the domain is characterized as EGF-like 1; calcium-binding.
+At position 126 to 167, the domain is characterized as EGF-like 2.
+At position 192 to 431, the domain is characterized as Peptidase S1.
+At position 61 to 124, the domain is characterized as S5 DRBM.
+At position 34 to 145, the domain is characterized as C-type lectin.
+At position 43 to 136, the domain is characterized as ARID.
+At position 358 to 448, the domain is characterized as ELM2.
+At position 9 to 62, the domain is characterized as C-type lectin.
+At position 647 to 718, the domain is characterized as KHA.
+At position 598 to 674, the domain is characterized as BRCT.
+At position 18 to 149, the domain is characterized as VHS.
+At position 258 to 277, the domain is characterized as UIM 1.
+At position 301 to 320, the domain is characterized as UIM 2.
+At position 31 to 253, the domain is characterized as Peptidase S1.
+At position 1 to 105, the domain is characterized as HSR.
+At position 181 to 280, the domain is characterized as SAND.
+At position 39 to 369, the domain is characterized as USP.
+At position 714 to 981, the domain is characterized as Protein kinase.
+At position 28 to 212, the domain is characterized as RNase H type-2.
+At position 140 to 412, the domain is characterized as ABC transporter 1.
+At position 488 to 700, the domain is characterized as ABC transmembrane type-2 1.
+At position 806 to 1058, the domain is characterized as ABC transporter 2.
+At position 1131 to 1345, the domain is characterized as ABC transmembrane type-2 2.
+At position 50 to 268, the domain is characterized as Radical SAM core.
+At position 248 to 448, the domain is characterized as PCI.
+At position 56 to 340, the domain is characterized as Protein kinase.
+At position 2 to 239, the domain is characterized as ABC transporter.
+At position 73 to 222, the domain is characterized as GAF 1.
+At position 254 to 431, the domain is characterized as GAF 2.
+At position 483 to 816, the domain is characterized as PDEase.
+At position 3 to 317, the domain is characterized as Hcy-binding.
+At position 395 to 672, the domain is characterized as Protein kinase.
+At position 27 to 297, the domain is characterized as Septin-type G.
+At position 34 to 47, the domain is characterized as CRIB.
+At position 111 to 283, the domain is characterized as CP-type G.
+At position 356 to 553, the domain is characterized as MIF4G.
+At position 648 to 764, the domain is characterized as MI.
+At position 556 to 615, the domain is characterized as KH.
+At position 625 to 693, the domain is characterized as S1 motif.
+At position 2 to 103, the domain is characterized as Thioredoxin.
+At position 6 to 247, the domain is characterized as ABC transporter 1.
+At position 304 to 537, the domain is characterized as ABC transporter 2.
+At position 120 to 352, the domain is characterized as Radical SAM core.
+At position 544 to 830, the domain is characterized as MYST-type HAT.
+At position 202 to 254, the domain is characterized as bZIP.
+At position 9 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 224 to 643, the domain is characterized as Peptidase S53.
+At position 17 to 248, the domain is characterized as Radical SAM core.
+At position 8 to 76, the domain is characterized as DRBM 1.
+At position 95 to 162, the domain is characterized as DRBM 2.
+At position 236 to 502, the domain is characterized as Protein kinase.
+At position 2 to 180, the domain is characterized as PBS-linker.
+At position 234 to 286, the domain is characterized as CpcD-like.
+At position 51 to 322, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 2 to 48, the domain is characterized as F-box.
+At position 212 to 268, the domain is characterized as FBD.
+At position 12 to 72, the domain is characterized as HTH tetR-type.
+At position 14 to 160, the domain is characterized as UBC core.
+At position 42 to 219, the domain is characterized as EngB-type G.
+At position 158 to 441, the domain is characterized as Velvet.
+At position 16 to 182, the domain is characterized as FAD-binding PCMH-type.
+At position 300 to 391, the domain is characterized as PDZ 1.
+At position 414 to 500, the domain is characterized as PDZ 2.
+At position 26 to 106, the domain is characterized as GS beta-grasp.
+At position 113 to 373, the domain is characterized as GS catalytic.
+At position 201 to 236, the domain is characterized as UVR.
+At position 60 to 118, the domain is characterized as Tudor-knot.
+At position 169 to 440, the domain is characterized as MYST-type HAT.
+At position 34 to 164, the domain is characterized as N-terminal Ras-GEF.
+At position 204 to 452, the domain is characterized as Ras-GEF.
+At position 54 to 270, the domain is characterized as Radical SAM core.
+At position 32 to 105, the domain is characterized as CSD.
+At position 24 to 87, the domain is characterized as BTB.
+At position 5 to 170, the domain is characterized as Exonuclease.
+At position 351 to 455, the domain is characterized as Cadherin 4.
+At position 456 to 565, the domain is characterized as Cadherin 5.
+At position 581 to 678, the domain is characterized as Cadherin 6.
+At position 21 to 140, the domain is characterized as Bulb-type lectin.
+At position 276 to 312, the domain is characterized as EGF-like.
+At position 331 to 417, the domain is characterized as PAN.
+At position 498 to 785, the domain is characterized as Protein kinase.
+At position 579 to 679, the domain is characterized as Fibronectin type-III.
+At position 52 to 112, the domain is characterized as SH3.
+At position 118 to 214, the domain is characterized as SH2.
+At position 235 to 488, the domain is characterized as Protein kinase.
+At position 68 to 190, the domain is characterized as PX.
+At position 534 to 647, the domain is characterized as Calponin-homology (CH).
+At position 252 to 442, the domain is characterized as GATase cobBQ-type.
+At position 4 to 133, the domain is characterized as RNase III.
+At position 158 to 226, the domain is characterized as DRBM.
+At position 205 to 281, the domain is characterized as KH type-2.
+At position 314 to 596, the domain is characterized as Protein kinase.
+At position 54 to 117, the domain is characterized as S5 DRBM.
+At position 56 to 367, the domain is characterized as IF rod.
+At position 4 to 278, the domain is characterized as DegV.
+At position 12 to 75, the domain is characterized as S5 DRBM.
+At position 27 to 515, the domain is characterized as Sema.
+At position 563 to 655, the domain is characterized as IPT/TIG 1.
+At position 657 to 739, the domain is characterized as IPT/TIG 2.
+At position 742 to 836, the domain is characterized as IPT/TIG 3.
+At position 1078 to 1345, the domain is characterized as Protein kinase.
+At position 24 to 128, the domain is characterized as ARID.
+At position 427 to 593, the domain is characterized as JmjC.
+At position 50 to 206, the domain is characterized as PPIase cyclophilin-type.
+At position 7 to 61, the domain is characterized as HTH cro/C1-type.
+At position 607 to 691, the domain is characterized as BRCT.
+At position 4 to 234, the domain is characterized as CN hydrolase.
+At position 13 to 100, the domain is characterized as PDZ.
+At position 317 to 500, the domain is characterized as Helicase ATP-binding.
+At position 512 to 675, the domain is characterized as Helicase C-terminal.
+At position 137 to 440, the domain is characterized as NB-ARC.
+At position 74 to 302, the domain is characterized as ABC transmembrane type-1.
+At position 23 to 254, the domain is characterized as AB hydrolase-1.
+At position 1 to 82, the domain is characterized as DIX.
+At position 249 to 321, the domain is characterized as PDZ.
+At position 422 to 496, the domain is characterized as DEP.
+At position 16 to 328, the domain is characterized as FERM.
+At position 47 to 92, the domain is characterized as Gla.
+At position 93 to 129, the domain is characterized as EGF-like 1; calcium-binding.
+At position 130 to 171, the domain is characterized as EGF-like 2.
+At position 227 to 459, the domain is characterized as Peptidase S1.
+At position 194 to 314, the domain is characterized as Fe2OG dioxygenase.
+At position 2 to 181, the domain is characterized as tr-type G.
+At position 458 to 639, the domain is characterized as Helicase ATP-binding.
+At position 714 to 879, the domain is characterized as Helicase C-terminal.
+At position 98 to 285, the domain is characterized as uDENN FNIP1/2-type.
+At position 293 to 683, the domain is characterized as cDENN FNIP1/2-type.
+At position 690 to 767, the domain is characterized as dDENN FNIP1/2-type.
+At position 45 to 243, the domain is characterized as FAD-binding PCMH-type.
+At position 569 to 680, the domain is characterized as CNA-B 1.
+At position 681 to 791, the domain is characterized as CNA-B 2.
+At position 792 to 901, the domain is characterized as CNA-B 3.
+At position 902 to 1012, the domain is characterized as CNA-B 4.
+At position 1013 to 1123, the domain is characterized as CNA-B 5.
+At position 35 to 69, the domain is characterized as EF-hand 1.
+At position 70 to 105, the domain is characterized as EF-hand 2.
+At position 107 to 142, the domain is characterized as EF-hand 3.
+At position 151 to 186, the domain is characterized as EF-hand 4.
+At position 155 to 205, the domain is characterized as DHHC.
+At position 1 to 127, the domain is characterized as ENTH.
+At position 2 to 183, the domain is characterized as Glutamine amidotransferase type-1.
+At position 9 to 65, the domain is characterized as HTH myb-type 1.
+At position 66 to 116, the domain is characterized as HTH myb-type 2.
+At position 1 to 64, the domain is characterized as Jacalin-type lectin 1.
+At position 71 to 217, the domain is characterized as Jacalin-type lectin 2.
+At position 353 to 456, the domain is characterized as CBM2.
+At position 18 to 82, the domain is characterized as Chitin-binding type R&R.
+At position 27 to 140, the domain is characterized as KRAB.
+At position 301 to 586, the domain is characterized as Protein kinase.
+At position 551 to 614, the domain is characterized as KH.
+At position 182 to 267, the domain is characterized as PDZ.
+At position 68 to 195, the domain is characterized as TBDR plug.
+At position 203 to 999, the domain is characterized as TBDR beta-barrel.
+At position 74 to 126, the domain is characterized as HAMP.
+At position 153 to 346, the domain is characterized as Histidine kinase.
+At position 7 to 241, the domain is characterized as SET.
+At position 180 to 353, the domain is characterized as EngA-type G 2.
+At position 100 to 339, the domain is characterized as Radical SAM core.
+At position 179 to 303, the domain is characterized as Fatty acid hydroxylase.
+At position 149 to 223, the domain is characterized as POU-specific.
+At position 117 to 306, the domain is characterized as ATP-grasp.
+At position 173 to 436, the domain is characterized as Protein kinase.
+At position 61 to 236, the domain is characterized as uDENN FNIP1/2-type.
+At position 244 to 620, the domain is characterized as cDENN FNIP1/2-type.
+At position 634 to 712, the domain is characterized as dDENN FNIP1/2-type.
+At position 122 to 272, the domain is characterized as GAF 1.
+At position 304 to 461, the domain is characterized as GAF 2.
+At position 494 to 818, the domain is characterized as PDEase.
+At position 1 to 88, the domain is characterized as CARD.
+At position 163 to 476, the domain is characterized as NACHT.
+At position 28 to 76, the domain is characterized as WAP 1.
+At position 82 to 130, the domain is characterized as WAP 2.
+At position 23 to 118, the domain is characterized as HTH arsR-type.
+At position 78 to 237, the domain is characterized as CP-type G.
+At position 145 to 220, the domain is characterized as Carrier.
+At position 1079 to 1616, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 50 to 253, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 67, the domain is characterized as F-box.
+At position 101 to 277, the domain is characterized as FBA.
+At position 205 to 241, the domain is characterized as CBM1.
+At position 5 to 89, the domain is characterized as BMC.
+At position 508 to 597, the domain is characterized as Spaetzle.
+At position 17 to 99, the domain is characterized as PDZ.
+At position 755 to 935, the domain is characterized as Flavodoxin-like.
+At position 990 to 1237, the domain is characterized as FAD-binding FR-type.
+At position 343 to 394, the domain is characterized as HAMP.
+At position 399 to 635, the domain is characterized as Methyl-accepting transducer.
+At position 41 to 282, the domain is characterized as MIF4G 1.
+At position 446 to 634, the domain is characterized as MIF4G 2.
+At position 649 to 855, the domain is characterized as MIF4G 3.
+At position 70 to 122, the domain is characterized as SANT.
+At position 359 to 446, the domain is characterized as SWIRM.
+At position 12 to 261, the domain is characterized as Glutamine amidotransferase type-2.
+At position 1 to 59, the domain is characterized as TGS.
+At position 44 to 212, the domain is characterized as FAD-binding PCMH-type.
+At position 81 to 212, the domain is characterized as PX.
+At position 219 to 328, the domain is characterized as PH.
+At position 459 to 486, the domain is characterized as PLD phosphodiesterase 1.
+At position 891 to 918, the domain is characterized as PLD phosphodiesterase 2.
+At position 16 to 104, the domain is characterized as Rhodanese.
+At position 1 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 24 to 260, the domain is characterized as ABC transporter 1.
+At position 270 to 510, the domain is characterized as ABC transporter 2.
+At position 223 to 280, the domain is characterized as Collagen-like.
+At position 47 to 315, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 201, the domain is characterized as CNNM transmembrane.
+At position 220 to 281, the domain is characterized as CBS 1.
+At position 284 to 341, the domain is characterized as CBS 2.
+At position 15 to 242, the domain is characterized as AB hydrolase-1.
+At position 112 to 383, the domain is characterized as Dynamin-type G.
+At position 619 to 710, the domain is characterized as GED.
+At position 80 to 264, the domain is characterized as ABC transmembrane type-1.
+At position 10 to 134, the domain is characterized as CMP/dCMP-type deaminase.
+At position 54 to 84, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 94 to 123, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 15 to 206, the domain is characterized as PNPLA.
+At position 172 to 316, the domain is characterized as FCP1 homology.
+At position 1 to 164, the domain is characterized as PX.
+At position 419 to 575, the domain is characterized as Exonuclease.
+At position 24 to 81, the domain is characterized as PWWP.
+At position 845 to 986, the domain is characterized as CID.
+At position 7 to 54, the domain is characterized as SpoVT-AbrB 1.
+At position 83 to 126, the domain is characterized as SpoVT-AbrB 2.
+At position 1498 to 1721, the domain is characterized as JmjC.
+At position 19 to 239, the domain is characterized as Radical SAM core.
+At position 1 to 127, the domain is characterized as GAF.
+At position 213 to 543, the domain is characterized as Kinesin motor.
+At position 146 to 350, the domain is characterized as ATP-grasp.
+At position 134 to 184, the domain is characterized as DHHC.
+At position 24 to 279, the domain is characterized as Protein kinase.
+At position 307 to 392, the domain is characterized as POLO box.
+At position 10 to 56, the domain is characterized as F-box.
+At position 278 to 408, the domain is characterized as ApaG.
+At position 76 to 304, the domain is characterized as Radical SAM core.
+At position 56 to 95, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 96 to 140, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 146 to 187, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 188 to 230, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 88 to 196, the domain is characterized as sHSP.
+At position 54 to 304, the domain is characterized as Peptidase S6.
+At position 1029 to 1295, the domain is characterized as Autotransporter.
+At position 19 to 129, the domain is characterized as Response regulatory.
+At position 517 to 569, the domain is characterized as HTH bat-type.
+At position 5 to 134, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 538 to 614, the domain is characterized as BRCT.
+At position 71 to 161, the domain is characterized as Rieske.
+At position 1 to 235, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 105 to 288, the domain is characterized as tr-type G.
+At position 1 to 181, the domain is characterized as TCTP.
+At position 155 to 303, the domain is characterized as TRUD.
+At position 108 to 368, the domain is characterized as Protein kinase.
+At position 448 to 483, the domain is characterized as EF-hand 2.
+At position 490 to 525, the domain is characterized as EF-hand 3.
+At position 528 to 555, the domain is characterized as EF-hand 4.
+At position 9 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 203 to 395, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 189, the domain is characterized as Flavodoxin-like.
+At position 77 to 317, the domain is characterized as ABC transporter.
+At position 415 to 673, the domain is characterized as ABC transmembrane type-2.
+At position 114 to 143, the domain is characterized as IQ.
+At position 82 to 142, the domain is characterized as SH3.
+At position 150 to 246, the domain is characterized as SH2.
+At position 271 to 527, the domain is characterized as Protein kinase.
+At position 32 to 272, the domain is characterized as ABC transporter.
+At position 52 to 98, the domain is characterized as Gla.
+At position 25 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 122 to 211, the domain is characterized as Ig-like C2-type 2.
+At position 233 to 322, the domain is characterized as Ig-like C2-type 3.
+At position 327 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 31 to 206, the domain is characterized as BPL/LPL catalytic.
+At position 82 to 154, the domain is characterized as RRM 1.
+At position 156 to 237, the domain is characterized as RRM 2.
+At position 606 to 888, the domain is characterized as Protein kinase.
+At position 35 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 216 to 309, the domain is characterized as Ig-like C2-type 2.
+At position 319 to 406, the domain is characterized as Ig-like C2-type 3.
+At position 596 to 957, the domain is characterized as Protein kinase.
+At position 12 to 194, the domain is characterized as tr-type G.
+At position 241 to 481, the domain is characterized as CN hydrolase.
+At position 93 to 154, the domain is characterized as S4 RNA-binding.
+At position 1 to 56, the domain is characterized as HTH lacI-type.
+At position 276 to 496, the domain is characterized as Fibrinogen C-terminal.
+At position 391 to 644, the domain is characterized as Protein kinase.
+At position 3 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 201 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 9 to 130, the domain is characterized as Arf-GAP.
+At position 131 to 232, the domain is characterized as PH 1.
+At position 254 to 360, the domain is characterized as PH 2.
+At position 2 to 88, the domain is characterized as Carrier.
+At position 45 to 80, the domain is characterized as EF-hand 1.
+At position 127 to 162, the domain is characterized as EF-hand 3.
+At position 164 to 199, the domain is characterized as EF-hand 4.
+At position 12 to 89, the domain is characterized as GIY-YIG.
+At position 21 to 205, the domain is characterized as EngB-type G.
+At position 3 to 119, the domain is characterized as MTTase N-terminal.
+At position 377 to 437, the domain is characterized as TRAM.
+At position 2 to 1158, the domain is characterized as Zinc-hook.
+At position 518 to 635, the domain is characterized as SMC hinge.
+At position 92 to 168, the domain is characterized as WWE.
+At position 8 to 227, the domain is characterized as Radical SAM core.
+At position 7 to 99, the domain is characterized as PH.
+At position 357 to 422, the domain is characterized as S4 RNA-binding.
+At position 27 to 61, the domain is characterized as EF-hand.
+At position 129 to 290, the domain is characterized as TNase-like.
+At position 291 to 546, the domain is characterized as Glutamine amidotransferase type-1.
+At position 31 to 124, the domain is characterized as GOLD.
+At position 12 to 214, the domain is characterized as ABC transporter.
+At position 85 to 256, the domain is characterized as FAD-binding PCMH-type.
+At position 1011 to 1116, the domain is characterized as Calponin-homology (CH).
+At position 21 to 115, the domain is characterized as Ig-like.
+At position 366 to 397, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 85 to 167, the domain is characterized as RRM 1.
+At position 297 to 369, the domain is characterized as RRM 3.
+At position 77 to 361, the domain is characterized as Protein kinase.
+At position 2 to 223, the domain is characterized as ABC transporter.
+At position 103 to 165, the domain is characterized as S4 RNA-binding.
+At position 103 to 332, the domain is characterized as Radical SAM core.
+At position 628 to 762, the domain is characterized as C2.
+At position 153 to 473, the domain is characterized as Peptidase S8.
+At position 481 to 618, the domain is characterized as P/Homo B.
+At position 36 to 202, the domain is characterized as FAD-binding PCMH-type.
+At position 153 to 333, the domain is characterized as Helicase ATP-binding.
+At position 344 to 506, the domain is characterized as Helicase C-terminal.
+At position 176 to 250, the domain is characterized as POU-specific.
+At position 178 to 228, the domain is characterized as LRRCT.
+At position 230 to 332, the domain is characterized as Ig-like.
+At position 678 to 729, the domain is characterized as GPS.
+At position 81 to 184, the domain is characterized as FAD-binding FR-type.
+At position 9 to 167, the domain is characterized as YEATS.
+At position 123 to 501, the domain is characterized as Protein kinase.
+At position 8 to 243, the domain is characterized as ABC transporter 1.
+At position 254 to 499, the domain is characterized as ABC transporter 2.
+At position 214 to 371, the domain is characterized as TrmE-type G.
+At position 20 to 288, the domain is characterized as Protein kinase.
+At position 52 to 242, the domain is characterized as PIK helical.
+At position 535 to 801, the domain is characterized as PI3K/PI4K catalytic.
+At position 83 to 366, the domain is characterized as Protein kinase.
+At position 25 to 274, the domain is characterized as ABC transporter.
+At position 535 to 824, the domain is characterized as Protein kinase.
+At position 882 to 1012, the domain is characterized as Guanylate cyclase.
+At position 22 to 270, the domain is characterized as GH16.
+At position 184 to 451, the domain is characterized as MHD.
+At position 75 to 144, the domain is characterized as S1 motif.
+At position 710 to 785, the domain is characterized as Smr.
+At position 63 to 126, the domain is characterized as S5 DRBM.
+At position 81 to 175, the domain is characterized as Toprim.
+At position 602 to 655, the domain is characterized as bHLH.
+At position 11 to 85, the domain is characterized as S1-like.
+At position 169 to 362, the domain is characterized as ABC transmembrane type-1.
+At position 66 to 150, the domain is characterized as GST N-terminal.
+At position 159 to 308, the domain is characterized as GST C-terminal.
+At position 323 to 409, the domain is characterized as RRM.
+At position 7 to 103, the domain is characterized as PilZ.
+At position 610 to 639, the domain is characterized as IQ.
+At position 10 to 70, the domain is characterized as HTH tetR-type.
+At position 197 to 365, the domain is characterized as PCI.
+At position 74 to 354, the domain is characterized as Protein kinase.
+At position 34 to 111, the domain is characterized as Inhibitor I9.
+At position 116 to 379, the domain is characterized as Peptidase S8.
+At position 226 to 266, the domain is characterized as P-type.
+At position 271 to 542, the domain is characterized as ZP.
+At position 30 to 89, the domain is characterized as Cystatin.
+At position 59 to 387, the domain is characterized as PORR.
+At position 6 to 120, the domain is characterized as Response regulatory.
+At position 145 to 374, the domain is characterized as Sigma-54 factor interaction.
+At position 22 to 116, the domain is characterized as Ig-like V-type.
+At position 154 to 242, the domain is characterized as Ig-like C1-type.
+At position 24 to 91, the domain is characterized as POTRA 1.
+At position 92 to 172, the domain is characterized as POTRA 2.
+At position 175 to 263, the domain is characterized as POTRA 3.
+At position 266 to 344, the domain is characterized as POTRA 4.
+At position 347 to 421, the domain is characterized as POTRA 5.
+At position 5 to 245, the domain is characterized as ABC transporter.
+At position 6 to 103, the domain is characterized as Fibronectin type-III 1.
+At position 109 to 207, the domain is characterized as Fibronectin type-III 2.
+At position 211 to 308, the domain is characterized as Fibronectin type-III 3.
+At position 45 to 114, the domain is characterized as POTRA.
+At position 60 to 116, the domain is characterized as FHA.
+At position 167 to 433, the domain is characterized as Protein kinase.
+At position 85 to 414, the domain is characterized as Asparaginase/glutaminase.
+At position 2 to 119, the domain is characterized as MTTase N-terminal.
+At position 142 to 374, the domain is characterized as Radical SAM core.
+At position 377 to 439, the domain is characterized as TRAM.
+At position 38 to 155, the domain is characterized as EamA.
+At position 5 to 194, the domain is characterized as AMMECR1.
+At position 211 to 283, the domain is characterized as RRM.
+At position 114 to 164, the domain is characterized as DHHC.
+At position 66 to 328, the domain is characterized as Protein kinase.
+At position 6 to 231, the domain is characterized as ABC transporter.
+At position 1736 to 1806, the domain is characterized as Bromo.
+At position 18 to 209, the domain is characterized as RNase H type-2.
+At position 573 to 681, the domain is characterized as Cadherin 6.
+At position 235 to 353, the domain is characterized as C2 1.
+At position 399 to 516, the domain is characterized as C2 2.
+At position 550 to 671, the domain is characterized as C2 3.
+At position 42 to 74, the domain is characterized as ShKT.
+At position 278 to 353, the domain is characterized as B5.
+At position 34 to 306, the domain is characterized as Septin-type G.
+At position 14 to 122, the domain is characterized as PET.
+At position 124 to 189, the domain is characterized as LIM zinc-binding 1.
+At position 189 to 249, the domain is characterized as LIM zinc-binding 2.
+At position 249 to 313, the domain is characterized as LIM zinc-binding 3.
+At position 146 to 221, the domain is characterized as SANT.
+At position 1 to 80, the domain is characterized as GST N-terminal.
+At position 89 to 210, the domain is characterized as GST C-terminal.
+At position 14 to 129, the domain is characterized as PH.
+At position 19 to 148, the domain is characterized as C-type lysozyme.
+At position 17 to 148, the domain is characterized as Galectin 1.
+At position 228 to 356, the domain is characterized as Galectin 2.
+At position 129 to 373, the domain is characterized as NR LBD.
+At position 19 to 274, the domain is characterized as Protein kinase.
+At position 309 to 336, the domain is characterized as NAF.
+At position 19 to 132, the domain is characterized as Ig-like V-type.
+At position 44 to 215, the domain is characterized as Helicase ATP-binding.
+At position 226 to 385, the domain is characterized as Helicase C-terminal.
+At position 824 to 914, the domain is characterized as PKD.
+At position 1 to 64, the domain is characterized as Fibronectin type-III.
+At position 187 to 450, the domain is characterized as Protein kinase.
+At position 421 to 500, the domain is characterized as SAM.
+At position 2 to 72, the domain is characterized as S1-like.
+At position 572 to 667, the domain is characterized as SH2.
+At position 8 to 124, the domain is characterized as Response regulatory.
+At position 161 to 422, the domain is characterized as NR LBD.
+At position 299 to 483, the domain is characterized as Helicase ATP-binding.
+At position 521 to 678, the domain is characterized as Helicase C-terminal.
+At position 3 to 89, the domain is characterized as Acylphosphatase-like.
+At position 358 to 418, the domain is characterized as S4 RNA-binding.
+At position 327 to 605, the domain is characterized as ABC transporter 1.
+At position 625 to 953, the domain is characterized as ABC transporter 2.
+At position 221 to 237, the domain is characterized as UIM.
+At position 1 to 45, the domain is characterized as F-box.
+At position 437 to 559, the domain is characterized as HD.
+At position 676 to 762, the domain is characterized as ACT 1.
+At position 789 to 865, the domain is characterized as ACT 2.
+At position 447 to 644, the domain is characterized as DH.
+At position 684 to 786, the domain is characterized as PH.
+At position 27 to 73, the domain is characterized as WAP 1.
+At position 74 to 121, the domain is characterized as WAP 2.
+At position 1 to 150, the domain is characterized as MGS-like.
+At position 82 to 179, the domain is characterized as Fibronectin type-III.
+At position 216 to 285, the domain is characterized as Ubiquitin-like.
+At position 520 to 702, the domain is characterized as Rho-GAP.
+At position 1040 to 1293, the domain is characterized as Glutamine amidotransferase type-1.
+At position 45 to 278, the domain is characterized as Radical SAM core.
+At position 586 to 668, the domain is characterized as BRCT.
+At position 73 to 289, the domain is characterized as Radical SAM core.
+At position 62 to 184, the domain is characterized as NEAT.
+At position 15 to 269, the domain is characterized as ABC transporter 1.
+At position 314 to 564, the domain is characterized as ABC transporter 2.
+At position 42 to 117, the domain is characterized as PTS EIIB type-1.
+At position 134 to 344, the domain is characterized as ATP-grasp.
+At position 333 to 396, the domain is characterized as SAM.
+At position 403 to 476, the domain is characterized as U-box.
+At position 73 to 170, the domain is characterized as SRCR.
+At position 182 to 424, the domain is characterized as Peptidase S1.
+At position 5 to 147, the domain is characterized as RNase H type-1.
+At position 1 to 101, the domain is characterized as Glutaredoxin.
+At position 5 to 220, the domain is characterized as Radical SAM core.
+At position 398 to 567, the domain is characterized as tr-type G.
+At position 305 to 402, the domain is characterized as SWIRM.
+At position 522 to 573, the domain is characterized as SANT.
+At position 6 to 236, the domain is characterized as Radical SAM core.
+At position 14 to 290, the domain is characterized as Helicase ATP-binding.
+At position 224 to 683, the domain is characterized as Trm1 methyltransferase.
+At position 188 to 384, the domain is characterized as Histidine kinase.
+At position 75 to 384, the domain is characterized as Peptidase A1.
+At position 67 to 224, the domain is characterized as CP-type G.
+At position 72 to 257, the domain is characterized as RNase H type-2.
+At position 28 to 137, the domain is characterized as sHSP.
+At position 5 to 81, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 81 to 121, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 144 to 171, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 187 to 216, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 263 to 319, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 9 to 141, the domain is characterized as Galectin.
+At position 63 to 158, the domain is characterized as SH2.
+At position 700 to 843, the domain is characterized as VPS9.
+At position 865 to 962, the domain is characterized as Ras-associating.
+At position 107 to 290, the domain is characterized as ATP-grasp.
+At position 32 to 210, the domain is characterized as Eph LBD.
+At position 628 to 889, the domain is characterized as Protein kinase.
+At position 918 to 982, the domain is characterized as SAM.
+At position 20 to 272, the domain is characterized as Pyruvate carboxyltransferase.
+At position 4 to 75, the domain is characterized as KRAB.
+At position 40 to 204, the domain is characterized as FAD-binding PCMH-type.
+At position 23 to 306, the domain is characterized as Protein kinase.
+At position 423 to 528, the domain is characterized as Glutaredoxin.
+At position 55 to 95, the domain is characterized as EGF-like.
+At position 45 to 125, the domain is characterized as POTRA.
+At position 12 to 115, the domain is characterized as UmuC.
+At position 687 to 716, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 743 to 773, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 7 to 97, the domain is characterized as WWE 1.
+At position 98 to 174, the domain is characterized as WWE 2.
+At position 31 to 161, the domain is characterized as MATH.
+At position 200 to 267, the domain is characterized as BTB.
+At position 19 to 209, the domain is characterized as RNase H type-2.
+At position 1 to 189, the domain is characterized as Protein kinase.
+At position 48 to 111, the domain is characterized as S5 DRBM.
+At position 1314 to 1425, the domain is characterized as PH.
+At position 636 to 727, the domain is characterized as Fe2OG dioxygenase.
+At position 575 to 851, the domain is characterized as Protein kinase.
+At position 854 to 984, the domain is characterized as KEN.
+At position 193 to 380, the domain is characterized as Glutamine amidotransferase type-1.
+At position 60 to 95, the domain is characterized as EF-hand 1.
+At position 96 to 131, the domain is characterized as EF-hand 2.
+At position 124 to 194, the domain is characterized as KH.
+At position 2 to 47, the domain is characterized as F-box.
+At position 2 to 118, the domain is characterized as C2 B9-type.
+At position 474 to 700, the domain is characterized as ABC transporter.
+At position 46 to 161, the domain is characterized as C-type lectin.
+At position 2 to 79, the domain is characterized as Carrier.
+At position 234 to 289, the domain is characterized as FF.
+At position 81 to 257, the domain is characterized as FAD-binding PCMH-type.
+At position 1046 to 1298, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 224, the domain is characterized as Miro 1.
+At position 240 to 275, the domain is characterized as EF-hand 1.
+At position 388 to 423, the domain is characterized as EF-hand 2.
+At position 505 to 671, the domain is characterized as Miro 2.
+At position 5 to 65, the domain is characterized as L27.
+At position 134 to 221, the domain is characterized as PDZ 1.
+At position 248 to 328, the domain is characterized as PDZ 2.
+At position 365 to 453, the domain is characterized as PDZ 3.
+At position 553 to 639, the domain is characterized as PDZ 4.
+At position 686 to 758, the domain is characterized as PDZ 5.
+At position 1070 to 1162, the domain is characterized as PDZ 6.
+At position 1241 to 1324, the domain is characterized as PDZ 7.
+At position 1464 to 1547, the domain is characterized as PDZ 8.
+At position 1560 to 1642, the domain is characterized as PDZ 9.
+At position 1703 to 1789, the domain is characterized as PDZ 10.
+At position 47 to 82, the domain is characterized as EF-hand 2.
+At position 120 to 155, the domain is characterized as EF-hand 4.
+At position 98 to 330, the domain is characterized as Radical SAM core.
+At position 26 to 136, the domain is characterized as Bulb-type lectin 1.
+At position 150 to 260, the domain is characterized as Bulb-type lectin 2.
+At position 81 to 299, the domain is characterized as Radical SAM core.
+At position 6 to 148, the domain is characterized as Nudix hydrolase.
+At position 43 to 148, the domain is characterized as Cadherin 1.
+At position 149 to 257, the domain is characterized as Cadherin 2.
+At position 258 to 365, the domain is characterized as Cadherin 3.
+At position 374 to 469, the domain is characterized as Cadherin 4.
+At position 470 to 579, the domain is characterized as Cadherin 5.
+At position 594 to 691, the domain is characterized as Cadherin 6.
+At position 11 to 193, the domain is characterized as tr-type G.
+At position 494 to 610, the domain is characterized as HD.
+At position 734 to 815, the domain is characterized as ACT 1.
+At position 845 to 926, the domain is characterized as ACT 2.
+At position 38 to 290, the domain is characterized as Protein kinase.
+At position 1 to 90, the domain is characterized as Chorismate mutase.
+At position 99 to 361, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 339 to 413, the domain is characterized as ACT-like.
+At position 106 to 289, the domain is characterized as Tyr recombinase.
+At position 130 to 209, the domain is characterized as Cytochrome c 1.
+At position 219 to 300, the domain is characterized as Cytochrome c 2.
+At position 64 to 202, the domain is characterized as Flavodoxin-like.
+At position 234 to 448, the domain is characterized as FAD-binding FR-type.
+At position 41 to 104, the domain is characterized as S5 DRBM.
+At position 9 to 691, the domain is characterized as Myosin motor.
+At position 729 to 913, the domain is characterized as TH1.
+At position 1053 to 1111, the domain is characterized as SH3.
+At position 106 to 344, the domain is characterized as Radical SAM core.
+At position 2 to 244, the domain is characterized as ABC transporter.
+At position 135 to 233, the domain is characterized as Rhodanese.
+At position 55 to 118, the domain is characterized as S5 DRBM.
+At position 21 to 130, the domain is characterized as PH.
+At position 140 to 175, the domain is characterized as EF-hand 1.
+At position 176 to 211, the domain is characterized as EF-hand 2.
+At position 296 to 440, the domain is characterized as PI-PLC X-box.
+At position 492 to 609, the domain is characterized as PI-PLC Y-box.
+At position 609 to 737, the domain is characterized as C2.
+At position 641 to 811, the domain is characterized as Helicase ATP-binding.
+At position 886 to 1064, the domain is characterized as Helicase C-terminal.
+At position 45 to 282, the domain is characterized as Radical SAM core.
+At position 1 to 40, the domain is characterized as Peptidase S1.
+At position 181 to 297, the domain is characterized as Ig-like V-type.
+At position 304 to 394, the domain is characterized as Ig-like C1-type.
+At position 35 to 139, the domain is characterized as Gnk2-homologous 1.
+At position 144 to 248, the domain is characterized as Gnk2-homologous 2.
+At position 9 to 72, the domain is characterized as S5 DRBM.
+At position 1 to 125, the domain is characterized as MGS-like.
+At position 578 to 662, the domain is characterized as Smr.
+At position 12 to 144, the domain is characterized as ENTH.
+At position 202 to 221, the domain is characterized as UIM 1.
+At position 229 to 248, the domain is characterized as UIM 2.
+At position 160 to 249, the domain is characterized as 5'-3' exonuclease.
+At position 301 to 356, the domain is characterized as HAMP.
+At position 364 to 592, the domain is characterized as Histidine kinase.
+At position 390 to 594, the domain is characterized as DDHD.
+At position 3 to 50, the domain is characterized as RsgI N-terminal anti-sigma.
+At position 22 to 115, the domain is characterized as Ig-like.
+At position 53 to 99, the domain is characterized as Gla.
+At position 27 to 202, the domain is characterized as BPL/LPL catalytic.
+At position 3 to 149, the domain is characterized as UBC core.
+At position 93 to 294, the domain is characterized as Peptidase M12A.
+At position 289 to 329, the domain is characterized as EGF-like.
+At position 340 to 450, the domain is characterized as CUB 1.
+At position 503 to 614, the domain is characterized as CUB 2.
+At position 8 to 161, the domain is characterized as Tyrosine-protein phosphatase.
+At position 36 to 294, the domain is characterized as Protein kinase.
+At position 122 to 240, the domain is characterized as PilZ.
+At position 54 to 130, the domain is characterized as Cytochrome b5 heme-binding.
+At position 164 to 255, the domain is characterized as CS.
+At position 272 to 384, the domain is characterized as FAD-binding FR-type.
+At position 92 to 168, the domain is characterized as PRC barrel.
+At position 4 to 241, the domain is characterized as ABC transporter.
+At position 19 to 182, the domain is characterized as PPIase cyclophilin-type.
+At position 564 to 678, the domain is characterized as Fe2OG dioxygenase.
+At position 57 to 206, the domain is characterized as RUN.
+At position 8 to 220, the domain is characterized as ABC transporter.
+At position 298 to 320, the domain is characterized as RRM.
+At position 97 to 176, the domain is characterized as PRC barrel.
+At position 69 to 303, the domain is characterized as NodB homology.
+At position 255 to 305, the domain is characterized as LIM zinc-binding.
+At position 47 to 226, the domain is characterized as Helicase ATP-binding.
+At position 264 to 411, the domain is characterized as Helicase C-terminal.
+At position 11 to 57, the domain is characterized as F-box.
+At position 1 to 44, the domain is characterized as F-box.
+At position 4 to 284, the domain is characterized as Protein kinase.
+At position 183 to 235, the domain is characterized as HAMP.
+At position 243 to 449, the domain is characterized as Histidine kinase.
+At position 3 to 38, the domain is characterized as EF-hand 1.
+At position 28 to 210, the domain is characterized as BPL/LPL catalytic.
+At position 21 to 244, the domain is characterized as Phosphagen kinase C-terminal.
+At position 86 to 203, the domain is characterized as SET.
+At position 186 to 294, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 115 to 233, the domain is characterized as C2.
+At position 285 to 344, the domain is characterized as bHLH.
+At position 533 to 733, the domain is characterized as FtsK.
+At position 4 to 106, the domain is characterized as Glutaredoxin.
+At position 1 to 44, the domain is characterized as Stress-response A/B barrel.
+At position 1 to 276, the domain is characterized as tr-type G.
+At position 30 to 214, the domain is characterized as SIS.
+At position 50 to 161, the domain is characterized as TBDR plug.
+At position 171 to 758, the domain is characterized as TBDR beta-barrel.
+At position 3 to 69, the domain is characterized as J.
+At position 137 to 251, the domain is characterized as RRM 1.
+At position 259 to 339, the domain is characterized as RRM 2.
+At position 27 to 117, the domain is characterized as UPAR/Ly6.
+At position 16 to 87, the domain is characterized as KRAB.
+At position 3 to 244, the domain is characterized as ABC transporter.
+At position 7 to 253, the domain is characterized as PABS.
+At position 42 to 104, the domain is characterized as S4 RNA-binding.
+At position 39 to 257, the domain is characterized as RNase H type-2.
+At position 75 to 224, the domain is characterized as GAF 1.
+At position 256 to 433, the domain is characterized as GAF 2.
+At position 486 to 819, the domain is characterized as PDEase.
+At position 524 to 625, the domain is characterized as SMC hinge.
+At position 1 to 159, the domain is characterized as sHSP.
+At position 40 to 447, the domain is characterized as G-alpha.
+At position 3 to 139, the domain is characterized as DAGKc.
+At position 38 to 274, the domain is characterized as AB hydrolase-1.
+At position 41 to 109, the domain is characterized as BTB.
+At position 413 to 568, the domain is characterized as Exonuclease.
+At position 178 to 351, the domain is characterized as EngA-type G 2.
+At position 704 to 779, the domain is characterized as Smr.
+At position 46 to 144, the domain is characterized as Cyclin N-terminal.
+At position 357 to 414, the domain is characterized as S4 RNA-binding.
+At position 35 to 144, the domain is characterized as sHSP.
+At position 404 to 659, the domain is characterized as Protein kinase.
+At position 53 to 276, the domain is characterized as Radical SAM core.
+At position 29 to 64, the domain is characterized as EF-hand 1.
+At position 98 to 133, the domain is characterized as EF-hand 2.
+At position 134 to 169, the domain is characterized as EF-hand 3.
+At position 167 to 251, the domain is characterized as Ig-like C2-type.
+At position 34 to 99, the domain is characterized as NAC-A/B.
+At position 51 to 129, the domain is characterized as RRM.
+At position 38 to 153, the domain is characterized as Response regulatory.
+At position 91 to 168, the domain is characterized as S4 RNA-binding.
+At position 160 to 406, the domain is characterized as Protein kinase.
+At position 94 to 140, the domain is characterized as F-box.
+At position 6 to 241, the domain is characterized as ABC transporter 1.
+At position 252 to 497, the domain is characterized as ABC transporter 2.
+At position 1817 to 1934, the domain is characterized as SET.
+At position 1940 to 1956, the domain is characterized as Post-SET.
+At position 134 to 453, the domain is characterized as Peptidase S8.
+At position 461 to 601, the domain is characterized as P/Homo B.
+At position 869 to 913, the domain is characterized as PLAC.
+At position 8 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 14 to 181, the domain is characterized as 3'-5' exonuclease.
+At position 219 to 300, the domain is characterized as HRDC.
+At position 327 to 505, the domain is characterized as PCI.
+At position 222 to 306, the domain is characterized as Death.
+At position 35 to 116, the domain is characterized as Inhibitor I9.
+At position 126 to 397, the domain is characterized as Peptidase S8.
+At position 17 to 93, the domain is characterized as IGFBP N-terminal.
+At position 154 to 229, the domain is characterized as Sm.
+At position 4 to 153, the domain is characterized as ADF-H.
+At position 151 to 471, the domain is characterized as Protein kinase.
+At position 4 to 266, the domain is characterized as Pyruvate carboxyltransferase.
+At position 411 to 463, the domain is characterized as TSP type-1.
+At position 296 to 567, the domain is characterized as Radical SAM core.
+At position 31 to 94, the domain is characterized as HMA.
+At position 46 to 207, the domain is characterized as PCI.
+At position 171 to 420, the domain is characterized as ABC transporter 1.
+At position 884 to 1127, the domain is characterized as ABC transporter 2.
+At position 212 to 286, the domain is characterized as POU-specific.
+At position 281 to 330, the domain is characterized as bHLH.
+At position 1 to 62, the domain is characterized as TGS.
+At position 184 to 358, the domain is characterized as EngA-type G 2.
+At position 359 to 443, the domain is characterized as KH-like.
+At position 1634 to 1842, the domain is characterized as Rap-GAP.
+At position 2 to 73, the domain is characterized as S1-like.
+At position 542 to 841, the domain is characterized as Peptidase M60.
+At position 126 to 199, the domain is characterized as PDZ.
+At position 306 to 383, the domain is characterized as SWIB/MDM2.
+At position 625 to 706, the domain is characterized as BRCT.
+At position 158 to 208, the domain is characterized as DHHC.
+At position 31 to 85, the domain is characterized as HTH myb-type.
+At position 24 to 197, the domain is characterized as EngB-type G.
+At position 122 to 246, the domain is characterized as RRM 1.
+At position 250 to 326, the domain is characterized as RRM 2.
+At position 401 to 480, the domain is characterized as RRM 3.
+At position 38 to 156, the domain is characterized as Response regulatory.
+At position 417 to 459, the domain is characterized as CCT.
+At position 1 to 504, the domain is characterized as GRAD1.
+At position 201 to 279, the domain is characterized as KH type-2.
+At position 105 to 300, the domain is characterized as ATP-grasp.
+At position 133 to 168, the domain is characterized as QLQ.
+At position 196 to 240, the domain is characterized as WRC.
+At position 5 to 280, the domain is characterized as tr-type G.
+At position 1 to 75, the domain is characterized as MAM.
+At position 2 to 74, the domain is characterized as Fibronectin type-III 1.
+At position 196 to 286, the domain is characterized as Fibronectin type-III 2.
+At position 291 to 386, the domain is characterized as Fibronectin type-III 3.
+At position 1 to 101, the domain is characterized as Cadherin 1.
+At position 102 to 216, the domain is characterized as Cadherin 2.
+At position 217 to 296, the domain is characterized as Cadherin 3.
+At position 27 to 201, the domain is characterized as EngB-type G.
+At position 87 to 272, the domain is characterized as RNase H type-2.
+At position 22 to 101, the domain is characterized as GST N-terminal.
+At position 106 to 231, the domain is characterized as GST C-terminal.
+At position 11 to 76, the domain is characterized as J.
+At position 178 to 249, the domain is characterized as RRM.
+At position 26 to 63, the domain is characterized as LDL-receptor class A.
+At position 67 to 281, the domain is characterized as Radical SAM core.
+At position 1 to 72, the domain is characterized as Disintegrin.
+At position 505 to 739, the domain is characterized as ABC transporter 1.
+At position 1322 to 1557, the domain is characterized as ABC transporter 2.
+At position 252 to 278, the domain is characterized as HhH.
+At position 10 to 278, the domain is characterized as tr-type G.
+At position 266 to 321, the domain is characterized as DEK-C.
+At position 325 to 466, the domain is characterized as Tyrosine-protein phosphatase.
+At position 37 to 193, the domain is characterized as SIS.
+At position 184 to 467, the domain is characterized as Dynamin-type G.
+At position 36 to 164, the domain is characterized as Nudix hydrolase.
+At position 259 to 546, the domain is characterized as Protein kinase.
+At position 586 to 692, the domain is characterized as tRNA-binding.
+At position 30 to 98, the domain is characterized as HTH gntR-type.
+At position 40 to 318, the domain is characterized as tr-type G.
+At position 175 to 228, the domain is characterized as HAMP.
+At position 367 to 566, the domain is characterized as Histidine kinase.
+At position 134 to 194, the domain is characterized as HTH luxR-type.
+At position 44 to 224, the domain is characterized as BPL/LPL catalytic.
+At position 472 to 601, the domain is characterized as ADD.
+At position 741 to 924, the domain is characterized as Helicase ATP-binding.
+At position 1122 to 1290, the domain is characterized as Helicase C-terminal.
+At position 18 to 132, the domain is characterized as Cadherin 1.
+At position 133 to 243, the domain is characterized as Cadherin 2.
+At position 244 to 351, the domain is characterized as Cadherin 3.
+At position 353 to 472, the domain is characterized as Cadherin 4.
+At position 473 to 583, the domain is characterized as Cadherin 5.
+At position 589 to 695, the domain is characterized as Cadherin 6.
+At position 400 to 656, the domain is characterized as Protein kinase.
+At position 101 to 335, the domain is characterized as Radical SAM core.
+At position 163 to 478, the domain is characterized as Protein kinase.
+At position 61 to 253, the domain is characterized as B30.2/SPRY.
+At position 9 to 254, the domain is characterized as ATP-grasp.
+At position 287 to 431, the domain is characterized as SIS 1.
+At position 459 to 600, the domain is characterized as SIS 2.
+At position 7 to 156, the domain is characterized as NAC.
+At position 38 to 328, the domain is characterized as FAE.
+At position 70 to 219, the domain is characterized as GAF 1.
+At position 251 to 428, the domain is characterized as GAF 2.
+At position 481 to 814, the domain is characterized as PDEase.
+At position 192 to 272, the domain is characterized as G5.
+At position 355 to 419, the domain is characterized as S4 RNA-binding.
+At position 72 to 288, the domain is characterized as Radical SAM core.
+At position 39 to 109, the domain is characterized as KH type-2.
+At position 75 to 213, the domain is characterized as Exonuclease.
+At position 31 to 134, the domain is characterized as CBM2.
+At position 144 to 229, the domain is characterized as Fibronectin type-III.
+At position 240 to 619, the domain is characterized as GH18.
+At position 97 to 184, the domain is characterized as PB1.
+At position 16 to 143, the domain is characterized as MSP.
+At position 505 to 631, the domain is characterized as SMC hinge.
+At position 21 to 262, the domain is characterized as ABC transporter.
+At position 33 to 307, the domain is characterized as Pyruvate carboxyltransferase.
+At position 17 to 86, the domain is characterized as KH type-2.
+At position 76 to 201, the domain is characterized as Nudix hydrolase.
+At position 320 to 541, the domain is characterized as VWFA.
+At position 557 to 639, the domain is characterized as Cache 1.
+At position 889 to 934, the domain is characterized as Cache 2.
+At position 13 to 48, the domain is characterized as EF-hand 1.
+At position 50 to 85, the domain is characterized as EF-hand 2.
+At position 1 to 67, the domain is characterized as REM-1 1.
+At position 142 to 219, the domain is characterized as REM-1 2.
+At position 225 to 343, the domain is characterized as C2.
+At position 814 to 1073, the domain is characterized as Protein kinase.
+At position 1074 to 1139, the domain is characterized as AGC-kinase C-terminal.
+At position 2 to 114, the domain is characterized as MTTase N-terminal.
+At position 132 to 363, the domain is characterized as Radical SAM core.
+At position 23 to 991, the domain is characterized as Zinc-hook.
+At position 110 to 277, the domain is characterized as Helicase ATP-binding.
+At position 288 to 465, the domain is characterized as Helicase C-terminal.
+At position 1 to 134, the domain is characterized as RNase III.
+At position 16 to 257, the domain is characterized as ABC transporter.
+At position 31 to 204, the domain is characterized as EngB-type G.
+At position 557 to 657, the domain is characterized as tRNA-binding.
+At position 141 to 349, the domain is characterized as ATP-grasp.
+At position 24 to 325, the domain is characterized as Protein kinase.
+At position 5 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 115 to 355, the domain is characterized as Radical SAM core.
+At position 62 to 297, the domain is characterized as AB hydrolase-1.
+At position 34 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 132 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 233 to 321, the domain is characterized as Ig-like C2-type 3.
+At position 89 to 264, the domain is characterized as Helicase ATP-binding.
+At position 292 to 437, the domain is characterized as Helicase C-terminal.
+At position 96 to 157, the domain is characterized as S4 RNA-binding.
+At position 2 to 157, the domain is characterized as DHFR.
+At position 119 to 313, the domain is characterized as ATP-grasp.
+At position 64 to 99, the domain is characterized as EF-hand 1.
+At position 150 to 185, the domain is characterized as EF-hand 3.
+At position 189 to 224, the domain is characterized as EF-hand 4.
+At position 230 to 265, the domain is characterized as EF-hand 5.
+At position 266 to 301, the domain is characterized as EF-hand 6.
+At position 2 to 77, the domain is characterized as GIY-YIG.
+At position 16 to 124, the domain is characterized as PH.
+At position 134 to 169, the domain is characterized as EF-hand 1.
+At position 170 to 205, the domain is characterized as EF-hand 2.
+At position 206 to 237, the domain is characterized as EF-hand 3.
+At position 290 to 435, the domain is characterized as PI-PLC X-box.
+At position 530 to 646, the domain is characterized as PI-PLC Y-box.
+At position 646 to 773, the domain is characterized as C2.
+At position 8 to 243, the domain is characterized as Glutamine amidotransferase type-1.
+At position 163 to 225, the domain is characterized as t-SNARE coiled-coil homology.
+At position 2 to 63, the domain is characterized as LIM zinc-binding.
+At position 401 to 567, the domain is characterized as N-acetyltransferase.
+At position 4 to 126, the domain is characterized as N-terminal Ras-GEF.
+At position 154 to 387, the domain is characterized as Ras-GEF.
+At position 426 to 461, the domain is characterized as EF-hand 1.
+At position 463 to 490, the domain is characterized as EF-hand 2.
+At position 95 to 149, the domain is characterized as bHLH.
+At position 28 to 100, the domain is characterized as KRAB.
+At position 656 to 720, the domain is characterized as CBS 1.
+At position 752 to 812, the domain is characterized as CBS 2.
+At position 17 to 232, the domain is characterized as ABC transporter.
+At position 9 to 508, the domain is characterized as Peptidase S8.
+At position 67 to 287, the domain is characterized as Radical SAM core.
+At position 1 to 168, the domain is characterized as TCTP.
+At position 104 to 141, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 5 to 120, the domain is characterized as MTTase N-terminal.
+At position 137 to 382, the domain is characterized as Radical SAM core.
+At position 385 to 453, the domain is characterized as TRAM.
+At position 14 to 314, the domain is characterized as Protein kinase.
+At position 7 to 196, the domain is characterized as RNase H type-2.
+At position 702 to 817, the domain is characterized as GAE.
+At position 16 to 144, the domain is characterized as VHS.
+At position 165 to 184, the domain is characterized as UIM.
+At position 202 to 261, the domain is characterized as SH3.
+At position 360 to 377, the domain is characterized as ITAM.
+At position 13 to 67, the domain is characterized as HTH cro/C1-type.
+At position 129 to 233, the domain is characterized as Ig-like C1-type.
+At position 7 to 42, the domain is characterized as EF-hand 1.
+At position 43 to 78, the domain is characterized as EF-hand 2.
+At position 80 to 115, the domain is characterized as EF-hand 3.
+At position 116 to 151, the domain is characterized as EF-hand 4.
+At position 30 to 121, the domain is characterized as HTH La-type RNA-binding.
+At position 127 to 205, the domain is characterized as RRM.
+At position 461 to 574, the domain is characterized as xRRM.
+At position 14 to 125, the domain is characterized as BMC circularly permuted 1.
+At position 126 to 225, the domain is characterized as BMC circularly permuted 2.
+At position 5 to 94, the domain is characterized as CS.
+At position 284 to 362, the domain is characterized as PUA.
+At position 772 to 858, the domain is characterized as SUEL-type lectin.
+At position 424 to 660, the domain is characterized as Ras-GEF.
+At position 5 to 188, the domain is characterized as VWFA.
+At position 211 to 230, the domain is characterized as UIM 1.
+At position 282 to 301, the domain is characterized as UIM 2.
+At position 368 to 397, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 148 to 218, the domain is characterized as Bromo.
+At position 602 to 681, the domain is characterized as BRCT.
+At position 66 to 101, the domain is characterized as EF-hand 1.
+At position 103 to 138, the domain is characterized as EF-hand 2.
+At position 139 to 174, the domain is characterized as EF-hand 3.
+At position 176 to 209, the domain is characterized as EF-hand 4.
+At position 181 to 234, the domain is characterized as HAMP.
+At position 253 to 489, the domain is characterized as Methyl-accepting transducer.
+At position 71 to 257, the domain is characterized as RNase H type-2.
+At position 45 to 111, the domain is characterized as Importin N-terminal.
+At position 232 to 465, the domain is characterized as ABC transporter.
+At position 65 to 143, the domain is characterized as GIY-YIG.
+At position 253 to 288, the domain is characterized as UVR.
+At position 17 to 99, the domain is characterized as Lipoyl-binding.
+At position 316 to 607, the domain is characterized as Protein kinase.
+At position 40 to 314, the domain is characterized as Pyruvate carboxyltransferase.
+At position 8 to 189, the domain is characterized as UmuC.
+At position 379 to 469, the domain is characterized as Toprim.
+At position 591 to 672, the domain is characterized as BRCT.
+At position 4 to 114, the domain is characterized as STAS.
+At position 194 to 286, the domain is characterized as PpiC.
+At position 133 to 228, the domain is characterized as Rhodanese.
+At position 19 to 134, the domain is characterized as Ig-like 1.
+At position 143 to 232, the domain is characterized as Ig-like 2.
+At position 242 to 350, the domain is characterized as Ig-like 3.
+At position 403 to 559, the domain is characterized as TIR.
+At position 82 to 198, the domain is characterized as Calponin-homology (CH).
+At position 228 to 402, the domain is characterized as DH.
+At position 426 to 547, the domain is characterized as PH.
+At position 772 to 859, the domain is characterized as PB1.
+At position 28 to 199, the domain is characterized as EngB-type G.
+At position 5 to 127, the domain is characterized as MsrB.
+At position 66 to 204, the domain is characterized as Flavodoxin-like.
+At position 239 to 453, the domain is characterized as FAD-binding FR-type.
+At position 19 to 149, the domain is characterized as CID.
+At position 316 to 444, the domain is characterized as C2.
+At position 505 to 721, the domain is characterized as Ras-GAP.
+At position 433 to 543, the domain is characterized as SCP2.
+At position 1 to 155, the domain is characterized as HTH marR-type.
+At position 84 to 365, the domain is characterized as FERM.
+At position 30 to 201, the domain is characterized as Chitin-binding type-4.
+At position 438 to 479, the domain is characterized as Chitin-binding type-3.
+At position 1 to 64, the domain is characterized as LCN-type CS-alpha/beta.
+At position 563 to 645, the domain is characterized as S1 motif.
+At position 599 to 773, the domain is characterized as PCI.
+At position 78 to 157, the domain is characterized as PRC barrel.
+At position 50 to 154, the domain is characterized as Calponin-homology (CH) 1.
+At position 163 to 269, the domain is characterized as Calponin-homology (CH) 2.
+At position 765 to 800, the domain is characterized as EF-hand 1.
+At position 806 to 841, the domain is characterized as EF-hand 2.
+At position 78 to 107, the domain is characterized as EGF-like.
+At position 40 to 422, the domain is characterized as Helicase ATP-binding.
+At position 443 to 605, the domain is characterized as Helicase C-terminal.
+At position 46 to 142, the domain is characterized as SH2.
+At position 177 to 224, the domain is characterized as SOCS box.
+At position 103 to 135, the domain is characterized as EGF-like 1.
+At position 137 to 177, the domain is characterized as EGF-like 2; calcium-binding.
+At position 6 to 138, the domain is characterized as HTH marR-type.
+At position 340 to 411, the domain is characterized as ACT-like 1.
+At position 433 to 504, the domain is characterized as ACT-like 2.
+At position 349 to 414, the domain is characterized as S4 RNA-binding.
+At position 12 to 51, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 52 to 98, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 105 to 146, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 147 to 195, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 59 to 113, the domain is characterized as J.
+At position 541 to 796, the domain is characterized as STAS.
+At position 54 to 307, the domain is characterized as EAL.
+At position 6 to 242, the domain is characterized as ABC transporter.
+At position 1 to 94, the domain is characterized as HIG1.
+At position 60 to 311, the domain is characterized as Protein kinase.
+At position 329 to 370, the domain is characterized as UBA.
+At position 746 to 795, the domain is characterized as KA1.
+At position 31 to 105, the domain is characterized as Ubiquitin-like.
+At position 562 to 607, the domain is characterized as UBA.
+At position 6 to 56, the domain is characterized as Kazal-like.
+At position 1 to 21, the domain is characterized as Pacifastin.
+At position 40 to 79, the domain is characterized as VM.
+At position 156 to 316, the domain is characterized as TRUD.
+At position 152 to 465, the domain is characterized as IF rod.
+At position 468 to 898, the domain is characterized as FH2.
+At position 84 to 270, the domain is characterized as RNase H type-2.
+At position 6 to 186, the domain is characterized as UmuC.
+At position 46 to 136, the domain is characterized as DEP.
+At position 580 to 668, the domain is characterized as PB1.
+At position 2 to 113, the domain is characterized as Thioredoxin.
+At position 90 to 177, the domain is characterized as LITAF.
+At position 14 to 94, the domain is characterized as GIY-YIG.
+At position 206 to 241, the domain is characterized as UVR.
+At position 73 to 245, the domain is characterized as FAD-binding PCMH-type.
+At position 296 to 464, the domain is characterized as Helicase ATP-binding.
+At position 634 to 808, the domain is characterized as Helicase C-terminal.
+At position 1 to 77, the domain is characterized as Carrier.
+At position 196 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 44 to 111, the domain is characterized as BTB.
+At position 146 to 248, the domain is characterized as BACK.
+At position 268 to 405, the domain is characterized as MPN.
+At position 13 to 419, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 48 to 284, the domain is characterized as FAD-binding PCMH-type.
+At position 665 to 696, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 4 to 239, the domain is characterized as ABC transporter.
+At position 585 to 807, the domain is characterized as Rho-GAP.
+At position 1262 to 1474, the domain is characterized as Roc.
+At position 2049 to 2342, the domain is characterized as Protein kinase.
+At position 2412 to 2536, the domain is characterized as RGS.
+At position 29 to 150, the domain is characterized as NEAT.
+At position 330 to 415, the domain is characterized as PDZ.
+At position 159 to 409, the domain is characterized as Protein kinase.
+At position 434 to 508, the domain is characterized as U-box.
+At position 112 to 296, the domain is characterized as ATP-grasp.
+At position 261 to 471, the domain is characterized as NEL.
+At position 777 to 919, the domain is characterized as Peptidase S59.
+At position 358 to 480, the domain is characterized as RCK N-terminal.
+At position 9 to 94, the domain is characterized as Core-binding (CB).
+At position 115 to 299, the domain is characterized as Tyr recombinase.
+At position 98 to 161, the domain is characterized as bZIP.
+At position 35 to 221, the domain is characterized as BPL/LPL catalytic.
+At position 746 to 799, the domain is characterized as Myb-like.
+At position 3 to 79, the domain is characterized as SH3.
+At position 113 to 301, the domain is characterized as Rho-GAP.
+At position 333 to 428, the domain is characterized as SH2 1.
+At position 624 to 718, the domain is characterized as SH2 2.
+At position 101 to 316, the domain is characterized as RNase H type-2.
+At position 171 to 374, the domain is characterized as CP-type G.
+At position 10 to 156, the domain is characterized as N-acetyltransferase 1.
+At position 162 to 303, the domain is characterized as N-acetyltransferase 2.
+At position 153 to 207, the domain is characterized as bHLH.
+At position 217 to 302, the domain is characterized as KH.
+At position 343 to 436, the domain is characterized as HD.
+At position 5 to 275, the domain is characterized as CN hydrolase.
+At position 21 to 87, the domain is characterized as S1 motif 1.
+At position 105 to 171, the domain is characterized as S1 motif 2.
+At position 192 to 260, the domain is characterized as S1 motif 3.
+At position 277 to 347, the domain is characterized as S1 motif 4.
+At position 364 to 434, the domain is characterized as S1 motif 5.
+At position 451 to 520, the domain is characterized as S1 motif 6.
+At position 32 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 142 to 251, the domain is characterized as Gnk2-homologous 2.
+At position 361 to 641, the domain is characterized as Protein kinase.
+At position 80 to 148, the domain is characterized as DRBM 1.
+At position 292 to 359, the domain is characterized as DRBM 2.
+At position 488 to 656, the domain is characterized as Helicase ATP-binding.
+At position 697 to 870, the domain is characterized as Helicase C-terminal.
+At position 693 to 1014, the domain is characterized as Protein kinase 1.
+At position 1057 to 1309, the domain is characterized as Protein kinase 2.
+At position 220 to 316, the domain is characterized as PH 1.
+At position 413 to 507, the domain is characterized as PH 2.
+At position 1 to 94, the domain is characterized as Pyrin.
+At position 463 to 850, the domain is characterized as USP.
+At position 897 to 1070, the domain is characterized as Exonuclease.
+At position 335 to 579, the domain is characterized as Clu.
+At position 38 to 94, the domain is characterized as EF-hand 1; degenerate.
+At position 181 to 216, the domain is characterized as EF-hand 4.
+At position 421 to 579, the domain is characterized as SSD.
+At position 22 to 68, the domain is characterized as F-box.
+At position 375 to 433, the domain is characterized as FBD.
+At position 251 to 333, the domain is characterized as Toprim.
+At position 196 to 373, the domain is characterized as Helicase ATP-binding.
+At position 402 to 550, the domain is characterized as Helicase C-terminal.
+At position 5 to 74, the domain is characterized as J.
+At position 7 to 73, the domain is characterized as J.
+At position 143 to 377, the domain is characterized as Radical SAM core.
+At position 380 to 447, the domain is characterized as TRAM.
+At position 403 to 549, the domain is characterized as MATH.
+At position 3 to 182, the domain is characterized as KARI N-terminal Rossmann.
+At position 1 to 166, the domain is characterized as PfpI endopeptidase.
+At position 580 to 682, the domain is characterized as tRNA-binding.
+At position 814 to 879, the domain is characterized as HTH luxR-type.
+At position 552 to 611, the domain is characterized as KH.
+At position 621 to 689, the domain is characterized as S1 motif.
+At position 476 to 618, the domain is characterized as SEFIR.
+At position 7 to 123, the domain is characterized as Calponin-homology (CH).
+At position 223 to 271, the domain is characterized as F-box.
+At position 85 to 161, the domain is characterized as S4 RNA-binding.
+At position 160 to 310, the domain is characterized as TRUD.
+At position 167 to 269, the domain is characterized as YkuD.
+At position 577 to 635, the domain is characterized as Prospero-type homeo.
+At position 636 to 735, the domain is characterized as Prospero.
+At position 16 to 81, the domain is characterized as CBS 1.
+At position 331 to 391, the domain is characterized as CBS 2.
+At position 91 to 169, the domain is characterized as RRM 1.
+At position 179 to 247, the domain is characterized as RRM 2.
+At position 303 to 379, the domain is characterized as RRM 3.
+At position 393 to 471, the domain is characterized as RRM 4.
+At position 46 to 101, the domain is characterized as F-box.
+At position 36 to 129, the domain is characterized as Link.
+At position 135 to 247, the domain is characterized as CUB.
+At position 47 to 191, the domain is characterized as SCP.
+At position 10 to 68, the domain is characterized as TRAM.
+At position 13 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 51 to 112, the domain is characterized as SH3.
+At position 120 to 212, the domain is characterized as SH2.
+At position 230 to 488, the domain is characterized as Protein kinase.
+At position 59 to 136, the domain is characterized as RRM 1.
+At position 146 to 223, the domain is characterized as RRM 2.
+At position 239 to 316, the domain is characterized as RRM 3.
+At position 342 to 419, the domain is characterized as RRM 4.
+At position 588 to 665, the domain is characterized as PABC.
+At position 4 to 87, the domain is characterized as GST N-terminal.
+At position 92 to 217, the domain is characterized as GST C-terminal.
+At position 285 to 356, the domain is characterized as S1 motif.
+At position 596 to 759, the domain is characterized as Helicase ATP-binding.
+At position 777 to 957, the domain is characterized as Helicase C-terminal.
+At position 47 to 234, the domain is characterized as RNase H type-2.
+At position 83 to 286, the domain is characterized as ABC transmembrane type-1.
+At position 199 to 299, the domain is characterized as HTH araC/xylS-type.
+At position 18 to 98, the domain is characterized as Ubiquitin-like.
+At position 333 to 377, the domain is characterized as UBA.
+At position 286 to 432, the domain is characterized as N-acetyltransferase.
+At position 13 to 286, the domain is characterized as YjeF C-terminal.
+At position 2 to 183, the domain is characterized as GMPS ATP-PPase.
+At position 218 to 353, the domain is characterized as GGDEF.
+At position 44 to 298, the domain is characterized as Protein kinase.
+At position 299 to 351, the domain is characterized as AGC-kinase C-terminal.
+At position 48 to 232, the domain is characterized as Glutamine amidotransferase type-1.
+At position 144 to 193, the domain is characterized as bHLH.
+At position 429 to 543, the domain is characterized as Toprim.
+At position 138 to 270, the domain is characterized as Nudix hydrolase.
+At position 53 to 142, the domain is characterized as Cyclin N-terminal.
+At position 418 to 533, the domain is characterized as Toprim.
+At position 616 to 692, the domain is characterized as Carrier 1.
+At position 1700 to 1776, the domain is characterized as Carrier 2.
+At position 31 to 146, the domain is characterized as Plastocyanin-like 1.
+At position 156 to 303, the domain is characterized as Plastocyanin-like 2.
+At position 363 to 498, the domain is characterized as Plastocyanin-like 3.
+At position 40 to 92, the domain is characterized as LIM zinc-binding 1.
+At position 101 to 153, the domain is characterized as LIM zinc-binding 2.
+At position 162 to 212, the domain is characterized as LIM zinc-binding 3.
+At position 221 to 275, the domain is characterized as LIM zinc-binding 4.
+At position 221 to 281, the domain is characterized as KH.
+At position 347 to 440, the domain is characterized as HD.
+At position 14 to 98, the domain is characterized as GS beta-grasp.
+At position 106 to 468, the domain is characterized as GS catalytic.
+At position 387 to 578, the domain is characterized as PNPLA.
+At position 6 to 147, the domain is characterized as RNase H type-1.
+At position 111 to 483, the domain is characterized as Peptidase S8.
+At position 809 to 1083, the domain is characterized as Autotransporter.
+At position 4 to 246, the domain is characterized as CN hydrolase.
+At position 11 to 285, the domain is characterized as tr-type G.
+At position 13 to 115, the domain is characterized as IRS-type PTB.
+At position 280 to 358, the domain is characterized as PUA.
+At position 61 to 188, the domain is characterized as Thioredoxin.
+At position 1 to 154, the domain is characterized as BPL/LPL catalytic.
+At position 177 to 352, the domain is characterized as EngA-type G 2.
+At position 353 to 438, the domain is characterized as KH-like.
+At position 28 to 195, the domain is characterized as Chitin-binding type-4.
+At position 426 to 468, the domain is characterized as Chitin-binding type-3.
+At position 152 to 462, the domain is characterized as NB-ARC.
+At position 10 to 62, the domain is characterized as LIM zinc-binding 1.
+At position 71 to 121, the domain is characterized as LIM zinc-binding 2.
+At position 135 to 184, the domain is characterized as LIM zinc-binding 3.
+At position 193 to 243, the domain is characterized as LIM zinc-binding 4.
+At position 252 to 303, the domain is characterized as LIM zinc-binding 5.
+At position 6 to 188, the domain is characterized as RNase H type-2.
+At position 72 to 189, the domain is characterized as Thioredoxin.
+At position 7 to 186, the domain is characterized as Guanylate kinase-like.
+At position 22 to 195, the domain is characterized as EngB-type G.
+At position 2 to 56, the domain is characterized as ClpX-type ZB.
+At position 2 to 99, the domain is characterized as Ig-like 1.
+At position 113 to 210, the domain is characterized as Ig-like 2.
+At position 272 to 364, the domain is characterized as Chromo 1.
+At position 389 to 452, the domain is characterized as Chromo 2.
+At position 493 to 663, the domain is characterized as Helicase ATP-binding.
+At position 792 to 943, the domain is characterized as Helicase C-terminal.
+At position 173 to 548, the domain is characterized as USP.
+At position 3 to 194, the domain is characterized as Glutamine amidotransferase type-1.
+At position 195 to 385, the domain is characterized as GMPS ATP-PPase.
+At position 256 to 518, the domain is characterized as UvrD-like helicase C-terminal.
+At position 3 to 78, the domain is characterized as Carrier.
+At position 14 to 67, the domain is characterized as bHLH.
+At position 84 to 154, the domain is characterized as PAS 1.
+At position 230 to 300, the domain is characterized as PAS 2.
+At position 304 to 347, the domain is characterized as PAC.
+At position 7 to 94, the domain is characterized as Acylphosphatase-like.
+At position 29 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 39 to 164, the domain is characterized as SCP.
+At position 218 to 252, the domain is characterized as WW 1.
+At position 603 to 637, the domain is characterized as WW 2.
+At position 10 to 290, the domain is characterized as tr-type G.
+At position 140 to 438, the domain is characterized as ABC transmembrane type-1 1.
+At position 474 to 710, the domain is characterized as ABC transporter 1.
+At position 801 to 1124, the domain is characterized as ABC transmembrane type-1 2.
+At position 1159 to 1395, the domain is characterized as ABC transporter 2.
+At position 17 to 88, the domain is characterized as S1 motif.
+At position 32 to 419, the domain is characterized as FERM.
+At position 438 to 543, the domain is characterized as SH2; atypical.
+At position 583 to 857, the domain is characterized as Protein kinase 1.
+At position 875 to 1153, the domain is characterized as Protein kinase 2.
+At position 144 to 179, the domain is characterized as EF-hand 3.
+At position 54 to 113, the domain is characterized as SH3 1.
+At position 312 to 449, the domain is characterized as ZU5.
+At position 649 to 719, the domain is characterized as SH3 2.
+At position 145 to 205, the domain is characterized as v-SNARE coiled-coil homology.
+At position 34 to 319, the domain is characterized as Protein kinase.
+At position 31 to 99, the domain is characterized as J.
+At position 21 to 54, the domain is characterized as EF-hand.
+At position 105 to 249, the domain is characterized as PI-PLC X-box.
+At position 294 to 410, the domain is characterized as PI-PLC Y-box.
+At position 414 to 541, the domain is characterized as C2.
+At position 580 to 681, the domain is characterized as tRNA-binding.
+At position 23 to 95, the domain is characterized as Sm.
+At position 123 to 246, the domain is characterized as OTU.
+At position 24 to 105, the domain is characterized as Lipoyl-binding.
+At position 4 to 55, the domain is characterized as Rubredoxin-like.
+At position 29 to 129, the domain is characterized as Cystatin.
+At position 19 to 315, the domain is characterized as Protein kinase.
+At position 310 to 421, the domain is characterized as SWIRM.
+At position 925 to 977, the domain is characterized as SANT.
+At position 40 to 307, the domain is characterized as CN hydrolase.
+At position 77 to 268, the domain is characterized as ABC transmembrane type-1.
+At position 410 to 495, the domain is characterized as PDZ 1.
+At position 532 to 617, the domain is characterized as PDZ 2.
+At position 31 to 60, the domain is characterized as LRRNT.
+At position 261 to 312, the domain is characterized as LRRCT.
+At position 7 to 201, the domain is characterized as MHYT.
+At position 255 to 319, the domain is characterized as PAS.
+At position 402 to 536, the domain is characterized as GGDEF.
+At position 545 to 798, the domain is characterized as EAL.
+At position 187 to 237, the domain is characterized as bHLH.
+At position 72 to 222, the domain is characterized as N-acetyltransferase.
+At position 191 to 276, the domain is characterized as RCK C-terminal 1.
+At position 223 to 288, the domain is characterized as BTB.
+At position 635 to 687, the domain is characterized as HTH psq-type.
+At position 1 to 230, the domain is characterized as VWFA.
+At position 152 to 226, the domain is characterized as Doublecortin.
+At position 4 to 120, the domain is characterized as MTTase N-terminal.
+At position 136 to 365, the domain is characterized as Radical SAM core.
+At position 368 to 431, the domain is characterized as TRAM.
+At position 97 to 157, the domain is characterized as S4 RNA-binding.
+At position 173 to 274, the domain is characterized as PpiC 1.
+At position 283 to 383, the domain is characterized as PpiC 2.
+At position 1 to 48, the domain is characterized as F-box.
+At position 18 to 81, the domain is characterized as S5 DRBM.
+At position 94 to 166, the domain is characterized as Kringle.
+At position 171 to 272, the domain is characterized as SRCR 1.
+At position 281 to 382, the domain is characterized as SRCR 2.
+At position 388 to 488, the domain is characterized as SRCR 3.
+At position 501 to 602, the domain is characterized as SRCR 4.
+At position 632 to 875, the domain is characterized as Peptidase S1.
+At position 27 to 119, the domain is characterized as Ig-like V-type.
+At position 127 to 219, the domain is characterized as Ig-like C2-type 1.
+At position 227 to 312, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 229, the domain is characterized as ABC transporter.
+At position 289 to 352, the domain is characterized as Mop.
+At position 1 to 120, the domain is characterized as C-type lysozyme.
+At position 402 to 483, the domain is characterized as Disintegrin.
+At position 4 to 47, the domain is characterized as LEM-like.
+At position 1 to 100, the domain is characterized as FAD-binding FR-type.
+At position 227 to 315, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 902 to 962, the domain is characterized as SH3.
+At position 3 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 26 to 261, the domain is characterized as ABC transporter.
+At position 1 to 189, the domain is characterized as AMMECR1.
+At position 74 to 141, the domain is characterized as RRM 1.
+At position 148 to 229, the domain is characterized as RRM 2.
+At position 31 to 243, the domain is characterized as MIF4G.
+At position 1 to 69, the domain is characterized as Biotinyl-binding.
+At position 45 to 119, the domain is characterized as RRM.
+At position 1 to 69, the domain is characterized as HTH merR-type.
+At position 90 to 295, the domain is characterized as VWFA.
+At position 3 to 168, the domain is characterized as EngA-type G 1.
+At position 181 to 354, the domain is characterized as EngA-type G 2.
+At position 355 to 439, the domain is characterized as KH-like.
+At position 60 to 214, the domain is characterized as Tyrosine-protein phosphatase.
+At position 61 to 318, the domain is characterized as AB hydrolase-1.
+At position 331 to 440, the domain is characterized as SCP2.
+At position 47 to 195, the domain is characterized as SCP.
+At position 393 to 422, the domain is characterized as IQ.
+At position 14 to 132, the domain is characterized as MTTase N-terminal.
+At position 155 to 386, the domain is characterized as Radical SAM core.
+At position 388 to 456, the domain is characterized as TRAM.
+At position 8 to 94, the domain is characterized as Acylphosphatase-like.
+At position 26 to 105, the domain is characterized as GIY-YIG.
+At position 215 to 250, the domain is characterized as UVR.
+At position 1 to 390, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 27 to 80, the domain is characterized as Tudor-knot.
+At position 220 to 496, the domain is characterized as MYST-type HAT.
+At position 8 to 169, the domain is characterized as YEATS.
+At position 1 to 137, the domain is characterized as HTH marR-type.
+At position 75 to 103, the domain is characterized as ITAM.
+At position 1 to 129, the domain is characterized as Peptidase C39.
+At position 158 to 440, the domain is characterized as ABC transmembrane type-1.
+At position 472 to 707, the domain is characterized as ABC transporter.
+At position 174 to 261, the domain is characterized as PPIase FKBP-type.
+At position 2 to 84, the domain is characterized as GST N-terminal.
+At position 86 to 212, the domain is characterized as GST C-terminal.
+At position 272 to 431, the domain is characterized as EF-1-gamma C-terminal.
+At position 18 to 46, the domain is characterized as EF-hand 1.
+At position 1 to 119, the domain is characterized as C2.
+At position 164 to 250, the domain is characterized as 5'-3' exonuclease.
+At position 1 to 147, the domain is characterized as BAH.
+At position 148 to 259, the domain is characterized as ELM2.
+At position 266 to 318, the domain is characterized as SANT.
+At position 258 to 484, the domain is characterized as tr-type G.
+At position 75 to 147, the domain is characterized as Bromo 1.
+At position 369 to 441, the domain is characterized as Bromo 2.
+At position 601 to 683, the domain is characterized as NET.
+At position 482 to 666, the domain is characterized as PNPLA.
+At position 466 to 538, the domain is characterized as PAS.
+At position 43 to 125, the domain is characterized as GOLD.
+At position 104 to 273, the domain is characterized as CP-type G.
+At position 19 to 137, the domain is characterized as MTTase N-terminal.
+At position 160 to 392, the domain is characterized as Radical SAM core.
+At position 393 to 456, the domain is characterized as TRAM.
+At position 140 to 207, the domain is characterized as KH.
+At position 32 to 223, the domain is characterized as RNase H type-2.
+At position 10 to 89, the domain is characterized as RRM 1.
+At position 208 to 282, the domain is characterized as RRM 2.
+At position 185 to 369, the domain is characterized as Brix.
+At position 8 to 242, the domain is characterized as ABC transporter.
+At position 142 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 441, the domain is characterized as TRAM.
+At position 117 to 152, the domain is characterized as EF-hand 4.
+At position 92 to 138, the domain is characterized as Clip.
+At position 186 to 432, the domain is characterized as Peptidase S1.
+At position 705 to 788, the domain is characterized as BRCT.
+At position 18 to 149, the domain is characterized as VOC 1.
+At position 180 to 338, the domain is characterized as VOC 2.
+At position 57 to 91, the domain is characterized as WW.
+At position 117 to 331, the domain is characterized as AB hydrolase-1.
+At position 227 to 247, the domain is characterized as ELK.
+At position 29 to 264, the domain is characterized as ABC transporter 1.
+At position 264 to 515, the domain is characterized as ABC transporter 2.
+At position 7 to 67, the domain is characterized as CSD.
+At position 8 to 189, the domain is characterized as tr-type G.
+At position 65 to 170, the domain is characterized as PRD 1.
+At position 171 to 280, the domain is characterized as PRD 2.
+At position 1 to 80, the domain is characterized as Carrier.
+At position 21 to 80, the domain is characterized as LIM zinc-binding 1.
+At position 80 to 140, the domain is characterized as LIM zinc-binding 2.
+At position 149 to 208, the domain is characterized as LIM zinc-binding 3.
+At position 208 to 268, the domain is characterized as LIM zinc-binding 4.
+At position 615 to 683, the domain is characterized as HP.
+At position 197 to 429, the domain is characterized as Fibrinogen C-terminal.
+At position 89 to 259, the domain is characterized as Helicase ATP-binding.
+At position 269 to 429, the domain is characterized as Helicase C-terminal.
+At position 249 to 304, the domain is characterized as DEK-C.
+At position 308 to 449, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 63, the domain is characterized as HTH lysR-type.
+At position 3 to 131, the domain is characterized as Nudix hydrolase.
+At position 1 to 60, the domain is characterized as TGS.
+At position 9 to 70, the domain is characterized as HTH tetR-type.
+At position 7 to 150, the domain is characterized as Tyrosine-protein phosphatase.
+At position 102 to 185, the domain is characterized as MEIS N-terminal.
+At position 478 to 607, the domain is characterized as Ricin B-type lectin.
+At position 18 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 391 to 441, the domain is characterized as GPS.
+At position 65 to 275, the domain is characterized as YjeF N-terminal.
+At position 47 to 111, the domain is characterized as Disintegrin.
+At position 11 to 128, the domain is characterized as Response regulatory.
+At position 170 to 358, the domain is characterized as CheB-type methylesterase.
+At position 1 to 64, the domain is characterized as SAM.
+At position 218 to 541, the domain is characterized as Kinesin motor.
+At position 22 to 139, the domain is characterized as C-type lectin.
+At position 140 to 175, the domain is characterized as EGF-like.
+At position 178 to 239, the domain is characterized as Sushi 1.
+At position 240 to 301, the domain is characterized as Sushi 2.
+At position 303 to 364, the domain is characterized as Sushi 3.
+At position 366 to 427, the domain is characterized as Sushi 4.
+At position 429 to 490, the domain is characterized as Sushi 5.
+At position 491 to 549, the domain is characterized as Sushi 6.
+At position 86 to 299, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 47 to 87, the domain is characterized as Chaplin.
+At position 4 to 184, the domain is characterized as Guanylate kinase-like.
+At position 4 to 334, the domain is characterized as Protein kinase.
+At position 64 to 143, the domain is characterized as PDZ.
+At position 323 to 503, the domain is characterized as RGSL.
+At position 742 to 931, the domain is characterized as DH.
+At position 973 to 1087, the domain is characterized as PH.
+At position 128 to 212, the domain is characterized as PDZ.
+At position 96 to 222, the domain is characterized as Fe2OG dioxygenase.
+At position 15 to 49, the domain is characterized as EF-hand 1.
+At position 85 to 120, the domain is characterized as EF-hand 3.
+At position 121 to 156, the domain is characterized as EF-hand 4.
+At position 157 to 189, the domain is characterized as EF-hand 5.
+At position 191 to 226, the domain is characterized as EF-hand 6.
+At position 227 to 243, the domain is characterized as EF-hand 7.
+At position 9 to 61, the domain is characterized as HTH myb-type 1.
+At position 62 to 116, the domain is characterized as HTH myb-type 2.
+At position 240 to 299, the domain is characterized as SH3 1.
+At position 352 to 430, the domain is characterized as PB1.
+At position 458 to 517, the domain is characterized as SH3 2.
+At position 201 to 397, the domain is characterized as Peptidase M12B.
+At position 405 to 491, the domain is characterized as Disintegrin.
+At position 574 to 652, the domain is characterized as BRCT.
+At position 6 to 140, the domain is characterized as RNase III.
+At position 166 to 231, the domain is characterized as DRBM.
+At position 54 to 309, the domain is characterized as PPM-type phosphatase.
+At position 1316 to 1489, the domain is characterized as Helicase ATP-binding.
+At position 1663 to 1813, the domain is characterized as Helicase C-terminal.
+At position 28 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 234 to 321, the domain is characterized as Ig-like C2-type 3.
+At position 327 to 414, the domain is characterized as Ig-like C2-type 4.
+At position 450 to 557, the domain is characterized as Fibronectin type-III 1.
+At position 565 to 660, the domain is characterized as Fibronectin type-III 2.
+At position 67 to 291, the domain is characterized as Radical SAM core.
+At position 15 to 102, the domain is characterized as GS beta-grasp.
+At position 109 to 446, the domain is characterized as GS catalytic.
+At position 132 to 335, the domain is characterized as ATP-grasp.
+At position 46 to 630, the domain is characterized as Peptidase M2 1.
+At position 649 to 1228, the domain is characterized as Peptidase M2 2.
+At position 18 to 163, the domain is characterized as Thioredoxin.
+At position 164 to 249, the domain is characterized as PPIase FKBP-type.
+At position 7 to 220, the domain is characterized as ABC transporter.
+At position 195 to 293, the domain is characterized as HTH araC/xylS-type.
+At position 185 to 371, the domain is characterized as Glutamine amidotransferase type-1.
+At position 32 to 110, the domain is characterized as Inhibitor I9.
+At position 114 to 580, the domain is characterized as Peptidase S8.
+At position 353 to 437, the domain is characterized as PA.
+At position 4 to 122, the domain is characterized as MTTase N-terminal.
+At position 366 to 432, the domain is characterized as TRAM.
+At position 143 to 350, the domain is characterized as ATP-grasp.
+At position 132 to 233, the domain is characterized as C-type lectin.
+At position 306 to 330, the domain is characterized as NAF.
+At position 429 to 595, the domain is characterized as Helicase C-terminal.
+At position 626 to 661, the domain is characterized as UVR.
+At position 6 to 265, the domain is characterized as Pterin-binding.
+At position 281 to 566, the domain is characterized as Reverse transcriptase.
+At position 8 to 277, the domain is characterized as tr-type G.
+At position 43 to 184, the domain is characterized as FAS1 1.
+At position 268 to 411, the domain is characterized as FAS1 2.
+At position 3 to 69, the domain is characterized as NAC-A/B.
+At position 87 to 305, the domain is characterized as Radical SAM core.
+At position 4 to 149, the domain is characterized as PTS EIIA type-2.
+At position 168 to 264, the domain is characterized as PTS EIIB type-2.
+At position 298 to 675, the domain is characterized as PTS EIIC type-2.
+At position 6 to 97, the domain is characterized as HIG1.
+At position 11 to 69, the domain is characterized as Chromo.
+At position 600 to 732, the domain is characterized as B12-binding.
+At position 3 to 198, the domain is characterized as tr-type G.
+At position 220 to 379, the domain is characterized as TrmE-type G.
+At position 252 to 444, the domain is characterized as GATase cobBQ-type.
+At position 58 to 221, the domain is characterized as SIS.
+At position 24 to 287, the domain is characterized as BAR.
+At position 335 to 395, the domain is characterized as SH3.
+At position 26 to 60, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 451 to 573, the domain is characterized as HD.
+At position 693 to 777, the domain is characterized as ACT 1.
+At position 800 to 876, the domain is characterized as ACT 2.
+At position 46 to 161, the domain is characterized as sHSP.
+At position 7 to 68, the domain is characterized as HTH tetR-type.
+At position 19 to 155, the domain is characterized as Plastocyanin-like 1.
+At position 156 to 339, the domain is characterized as Plastocyanin-like 2.
+At position 340 to 521, the domain is characterized as Plastocyanin-like 3.
+At position 9 to 251, the domain is characterized as ATP-grasp.
+At position 30 to 89, the domain is characterized as SH3.
+At position 99 to 432, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 17 to 250, the domain is characterized as ABC transporter.
+At position 13 to 218, the domain is characterized as Cytochrome b561.
+At position 339 to 438, the domain is characterized as Rhodanese.
+At position 78 to 276, the domain is characterized as B30.2/SPRY.
+At position 23 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 161, the domain is characterized as FeoB-type G.
+At position 76 to 284, the domain is characterized as ABC transmembrane type-1.
+At position 85 to 158, the domain is characterized as J.
+At position 445 to 507, the domain is characterized as SANT 1.
+At position 548 to 603, the domain is characterized as SANT 2.
+At position 117 to 382, the domain is characterized as AB hydrolase-1.
+At position 20 to 170, the domain is characterized as N-acetyltransferase.
+At position 21 to 67, the domain is characterized as F-box.
+At position 44 to 145, the domain is characterized as Expansin-like EG45.
+At position 429 to 536, the domain is characterized as SH2.
+At position 563 to 690, the domain is characterized as PTB.
+At position 9 to 191, the domain is characterized as tr-type G.
+At position 5 to 127, the domain is characterized as OTU.
+At position 168 to 283, the domain is characterized as SET.
+At position 38 to 172, the domain is characterized as Nudix hydrolase.
+At position 82 to 161, the domain is characterized as Cytochrome b5 heme-binding.
+At position 138 to 385, the domain is characterized as ABC transporter 1.
+At position 481 to 757, the domain is characterized as ABC transmembrane type-2 1.
+At position 924 to 1166, the domain is characterized as ABC transporter 2.
+At position 1256 to 1529, the domain is characterized as ABC transmembrane type-2 2.
+At position 18 to 51, the domain is characterized as LRRNT.
+At position 241 to 287, the domain is characterized as LRRCT.
+At position 288 to 375, the domain is characterized as Ig-like.
+At position 859 to 1155, the domain is characterized as ABC transmembrane type-1 2.
+At position 1211 to 1444, the domain is characterized as ABC transporter 2.
+At position 44 to 131, the domain is characterized as BRCT.
+At position 419 to 653, the domain is characterized as UmuC.
+At position 17 to 92, the domain is characterized as Sm.
+At position 806 to 1025, the domain is characterized as PARP catalytic.
+At position 622 to 813, the domain is characterized as FtsK.
+At position 210 to 446, the domain is characterized as NR LBD.
+At position 6 to 222, the domain is characterized as ABC transporter.
+At position 1 to 102, the domain is characterized as Glutaredoxin.
+At position 97 to 169, the domain is characterized as PRC barrel.
+At position 304 to 334, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 353 to 382, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 140 to 346, the domain is characterized as ATP-grasp.
+At position 28 to 257, the domain is characterized as Velvet.
+At position 19 to 91, the domain is characterized as RBD.
+At position 310 to 570, the domain is characterized as Protein kinase.
+At position 8 to 87, the domain is characterized as RRM 1.
+At position 101 to 170, the domain is characterized as RRM 2.
+At position 247 to 321, the domain is characterized as U-box.
+At position 5 to 51, the domain is characterized as SpoVT-AbrB 1.
+At position 77 to 120, the domain is characterized as SpoVT-AbrB 2.
+At position 169 to 251, the domain is characterized as RRM 1.
+At position 373 to 450, the domain is characterized as RRM 2.
+At position 454 to 528, the domain is characterized as RRM 3.
+At position 778 to 957, the domain is characterized as SPOC.
+At position 114 to 173, the domain is characterized as CBS 1.
+At position 179 to 237, the domain is characterized as CBS 2.
+At position 12 to 248, the domain is characterized as Protein kinase.
+At position 12 to 115, the domain is characterized as PH.
+At position 160 to 264, the domain is characterized as IRS-type PTB.
+At position 4 to 300, the domain is characterized as YjeF C-terminal.
+At position 1 to 73, the domain is characterized as S1-like.
+At position 578 to 664, the domain is characterized as Carrier.
+At position 7 to 70, the domain is characterized as S5 DRBM.
+At position 15 to 205, the domain is characterized as RNase H type-2.
+At position 53 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 1 to 229, the domain is characterized as Radical SAM core.
+At position 24 to 240, the domain is characterized as BAR.
+At position 610 to 683, the domain is characterized as SH3.
+At position 5 to 308, the domain is characterized as ABC transporter.
+At position 430 to 479, the domain is characterized as bHLH.
+At position 120 to 233, the domain is characterized as C-type lectin.
+At position 30 to 220, the domain is characterized as Spondin.
+At position 276 to 330, the domain is characterized as TSP type-1.
+At position 3 to 280, the domain is characterized as DegV.
+At position 561 to 592, the domain is characterized as Chromo.
+At position 845 to 877, the domain is characterized as LisH.
+At position 46 to 263, the domain is characterized as Radical SAM core.
+At position 6 to 150, the domain is characterized as Nudix hydrolase.
+At position 628 to 803, the domain is characterized as Helicase ATP-binding.
+At position 829 to 976, the domain is characterized as Helicase C-terminal.
+At position 1164 to 1244, the domain is characterized as HRDC.
+At position 56 to 127, the domain is characterized as Chitin-binding type R&R.
+At position 2 to 63, the domain is characterized as HTH asnC-type.
+At position 85 to 281, the domain is characterized as MACPF.
+At position 87 to 394, the domain is characterized as Peptidase A1.
+At position 76 to 139, the domain is characterized as Tudor.
+At position 72 to 213, the domain is characterized as Nudix hydrolase.
+At position 243 to 390, the domain is characterized as Helicase C-terminal.
+At position 33 to 137, the domain is characterized as Cadherin 1.
+At position 138 to 246, the domain is characterized as Cadherin 2.
+At position 247 to 351, the domain is characterized as Cadherin 3.
+At position 352 to 456, the domain is characterized as Cadherin 4.
+At position 457 to 566, the domain is characterized as Cadherin 5.
+At position 574 to 687, the domain is characterized as Cadherin 6.
+At position 14 to 200, the domain is characterized as YrdC-like.
+At position 38 to 68, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 103 to 134, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 136 to 165, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 8 to 207, the domain is characterized as DPCK.
+At position 70 to 308, the domain is characterized as Radical SAM core.
+At position 7 to 128, the domain is characterized as Peptidase C39.
+At position 157 to 439, the domain is characterized as ABC transmembrane type-1.
+At position 471 to 706, the domain is characterized as ABC transporter.
+At position 273 to 308, the domain is characterized as EF-hand 1.
+At position 341 to 376, the domain is characterized as EF-hand 2.
+At position 5 to 239, the domain is characterized as tr-type G.
+At position 61 to 114, the domain is characterized as HAMP.
+At position 129 to 348, the domain is characterized as Histidine kinase.
+At position 9 to 69, the domain is characterized as HTH tetR-type.
+At position 6 to 101, the domain is characterized as ASCH.
+At position 283 to 361, the domain is characterized as PUA.
+At position 13 to 199, the domain is characterized as YrdC-like.
+At position 7 to 188, the domain is characterized as UmuC.
+At position 160 to 337, the domain is characterized as OBG-type G.
+At position 25 to 75, the domain is characterized as LIM zinc-binding 1.
+At position 84 to 137, the domain is characterized as LIM zinc-binding 2.
+At position 165 to 258, the domain is characterized as PDZ.
+At position 339 to 604, the domain is characterized as Protein kinase.
+At position 660 to 749, the domain is characterized as BRCT.
+At position 16 to 96, the domain is characterized as PB1.
+At position 133 to 150, the domain is characterized as Pseudo-CRIB.
+At position 157 to 250, the domain is characterized as PDZ.
+At position 14 to 94, the domain is characterized as PDZ 1.
+At position 154 to 234, the domain is characterized as PDZ 2.
+At position 18 to 131, the domain is characterized as Pru.
+At position 277 to 390, the domain is characterized as DEUBAD.
+At position 235 to 510, the domain is characterized as Protein kinase.
+At position 27 to 414, the domain is characterized as Helicase ATP-binding.
+At position 628 to 663, the domain is characterized as UVR.
+At position 36 to 155, the domain is characterized as Ig-like V-type.
+At position 157 to 252, the domain is characterized as Link 1.
+At position 257 to 354, the domain is characterized as Link 2.
+At position 647 to 683, the domain is characterized as EGF-like.
+At position 683 to 811, the domain is characterized as C-type lectin.
+At position 814 to 874, the domain is characterized as Sushi.
+At position 60 to 165, the domain is characterized as THUMP.
+At position 11 to 232, the domain is characterized as Peptidase C83.
+At position 447 to 481, the domain is characterized as PLD phosphodiesterase.
+At position 233 to 332, the domain is characterized as MaoC-like.
+At position 17 to 63, the domain is characterized as F-box.
+At position 1 to 93, the domain is characterized as Pyrin.
+At position 140 to 210, the domain is characterized as FISNA.
+At position 220 to 536, the domain is characterized as NACHT.
+At position 37 to 142, the domain is characterized as Ig-like C2-type 1.
+At position 154 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 251 to 339, the domain is characterized as Ig-like C2-type 3.
+At position 345 to 432, the domain is characterized as Ig-like C2-type 4.
+At position 462 to 570, the domain is characterized as Fibronectin type-III 1.
+At position 578 to 673, the domain is characterized as Fibronectin type-III 2.
+At position 192 to 473, the domain is characterized as Protein kinase.
+At position 5 to 217, the domain is characterized as tr-type G.
+At position 1 to 131, the domain is characterized as C-type lectin.
+At position 48 to 134, the domain is characterized as Core-binding (CB).
+At position 163 to 346, the domain is characterized as Tyr recombinase.
+At position 201 to 286, the domain is characterized as KH.
+At position 327 to 420, the domain is characterized as HD.
+At position 352 to 672, the domain is characterized as Protein kinase.
+At position 673 to 754, the domain is characterized as AGC-kinase C-terminal.
+At position 76 to 385, the domain is characterized as Peptidase A1.
+At position 6 to 191, the domain is characterized as Guanylate kinase-like.
+At position 193 to 457, the domain is characterized as SF4 helicase.
+At position 17 to 87, the domain is characterized as HTH gntR-type.
+At position 2 to 191, the domain is characterized as Glutamine amidotransferase type-2.
+At position 213 to 536, the domain is characterized as Asparagine synthetase.
+At position 76 to 434, the domain is characterized as Peptidase A1.
+At position 6 to 95, the domain is characterized as KRAB.
+At position 152 to 256, the domain is characterized as PB1.
+At position 3 to 65, the domain is characterized as SH3.
+At position 35 to 163, the domain is characterized as Nudix hydrolase.
+At position 11 to 415, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 22 to 304, the domain is characterized as Protein kinase.
+At position 22 to 76, the domain is characterized as CHCH.
+At position 16 to 121, the domain is characterized as Core-binding (CB).
+At position 169 to 354, the domain is characterized as Tyr recombinase.
+At position 95 to 185, the domain is characterized as K-box.
+At position 14 to 242, the domain is characterized as AB hydrolase-1.
+At position 87 to 307, the domain is characterized as Glutamine amidotransferase type-2.
+At position 130 to 291, the domain is characterized as CRAL-TRIO.
+At position 767 to 855, the domain is characterized as Death.
+At position 21 to 74, the domain is characterized as TIL.
+At position 20 to 489, the domain is characterized as Sema.
+At position 841 to 934, the domain is characterized as IPT/TIG 1.
+At position 936 to 1021, the domain is characterized as IPT/TIG 2.
+At position 1024 to 1123, the domain is characterized as IPT/TIG 3.
+At position 1126 to 1212, the domain is characterized as IPT/TIG 4.
+At position 68 to 327, the domain is characterized as Protein kinase.
+At position 20 to 109, the domain is characterized as GST N-terminal.
+At position 115 to 249, the domain is characterized as GST C-terminal.
+At position 144 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 453, the domain is characterized as TRAM.
+At position 74 to 417, the domain is characterized as Calpain catalytic.
+At position 649 to 683, the domain is characterized as EF-hand 1.
+At position 692 to 725, the domain is characterized as EF-hand 2.
+At position 722 to 757, the domain is characterized as EF-hand 3.
+At position 787 to 821, the domain is characterized as EF-hand 4.
+At position 102 to 152, the domain is characterized as DHHC.
+At position 104 to 190, the domain is characterized as Ras-associating.
+At position 232 to 340, the domain is characterized as PH.
+At position 437 to 533, the domain is characterized as SH2.
+At position 78 to 172, the domain is characterized as Fe2OG dioxygenase.
+At position 173 to 258, the domain is characterized as PPIase FKBP-type.
+At position 123 to 306, the domain is characterized as Brix.
+At position 75 to 176, the domain is characterized as Glutaredoxin.
+At position 96 to 159, the domain is characterized as S4 RNA-binding.
+At position 17 to 208, the domain is characterized as tr-type G.
+At position 3 to 240, the domain is characterized as ABC transporter 1.
+At position 250 to 494, the domain is characterized as ABC transporter 2.
+At position 5 to 402, the domain is characterized as BRO1.
+At position 5 to 247, the domain is characterized as ABC transporter.
+At position 7 to 176, the domain is characterized as Era-type G.
+At position 33 to 222, the domain is characterized as RNase H type-2.
+At position 137 to 319, the domain is characterized as tr-type G.
+At position 435 to 510, the domain is characterized as B5.
+At position 727 to 818, the domain is characterized as FDX-ACB.
+At position 9 to 77, the domain is characterized as NAC-A/B.
+At position 126 to 216, the domain is characterized as RRM.
+At position 66 to 133, the domain is characterized as BTB.
+At position 168 to 270, the domain is characterized as BACK.
+At position 27 to 215, the domain is characterized as Protein kinase.
+At position 175 to 204, the domain is characterized as GS.
+At position 205 to 495, the domain is characterized as Protein kinase.
+At position 54 to 158, the domain is characterized as THUMP.
+At position 246 to 414, the domain is characterized as TLDc.
+At position 5 to 196, the domain is characterized as Flavodoxin-like.
+At position 15 to 87, the domain is characterized as J.
+At position 1 to 57, the domain is characterized as HTH lysR-type.
+At position 50 to 138, the domain is characterized as PPIase FKBP-type 1.
+At position 167 to 253, the domain is characterized as PPIase FKBP-type 2.
+At position 108 to 308, the domain is characterized as ATP-grasp.
+At position 1 to 192, the domain is characterized as Macro.
+At position 241 to 276, the domain is characterized as EF-hand 1.
+At position 293 to 328, the domain is characterized as EF-hand 2.
+At position 20 to 279, the domain is characterized as Protein kinase.
+At position 331 to 429, the domain is characterized as PH.
+At position 3 to 85, the domain is characterized as PDZ.
+At position 256 to 315, the domain is characterized as LIM zinc-binding.
+At position 265 to 368, the domain is characterized as PH.
+At position 380 to 564, the domain is characterized as Rho-GAP.
+At position 25 to 266, the domain is characterized as ABC transporter.
+At position 54 to 170, the domain is characterized as Expansin-like EG45.
+At position 180 to 259, the domain is characterized as Expansin-like CBD.
+At position 24 to 117, the domain is characterized as Ig-like.
+At position 7 to 136, the domain is characterized as RNase III.
+At position 162 to 232, the domain is characterized as DRBM.
+At position 281 to 390, the domain is characterized as PAZ.
+At position 555 to 852, the domain is characterized as Piwi.
+At position 55 to 245, the domain is characterized as TNase-like.
+At position 106 to 417, the domain is characterized as IF rod.
+At position 281 to 321, the domain is characterized as Rho-GAP.
+At position 39 to 110, the domain is characterized as KH type-2.
+At position 291 to 541, the domain is characterized as Glutamine amidotransferase type-1.
+At position 125 to 369, the domain is characterized as RGS 1.
+At position 379 to 505, the domain is characterized as RGS 2.
+At position 94 to 144, the domain is characterized as DHHC.
+At position 15 to 91, the domain is characterized as KRAB.
+At position 54 to 156, the domain is characterized as THUMP.
+At position 388 to 470, the domain is characterized as Rhodanese.
+At position 203 to 238, the domain is characterized as UVR.
+At position 10 to 64, the domain is characterized as HTH cro/C1-type.
+At position 295 to 684, the domain is characterized as USP.
+At position 2 to 69, the domain is characterized as SH3 1.
+At position 70 to 127, the domain is characterized as SH3 2.
+At position 393 to 455, the domain is characterized as SH3 3.
+At position 3 to 146, the domain is characterized as Clp R.
+At position 108 to 202, the domain is characterized as PB1.
+At position 6 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 201 to 393, the domain is characterized as GMPS ATP-PPase.
+At position 15 to 347, the domain is characterized as Kinesin motor.
+At position 12 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 509 to 800, the domain is characterized as UvrD-like helicase C-terminal.
+At position 337 to 405, the domain is characterized as HP.
+At position 13 to 248, the domain is characterized as PABS.
+At position 92 to 214, the domain is characterized as Thioredoxin 1.
+At position 649 to 799, the domain is characterized as Thioredoxin 2.
+At position 4 to 96, the domain is characterized as Acylphosphatase-like.
+At position 55 to 469, the domain is characterized as USP.
+At position 93 to 404, the domain is characterized as IF rod.
+At position 576 to 658, the domain is characterized as S1 motif.
+At position 3 to 83, the domain is characterized as GST N-terminal.
+At position 85 to 208, the domain is characterized as GST C-terminal.
+At position 255 to 354, the domain is characterized as BEN.
+At position 15 to 201, the domain is characterized as RNase H type-2.
+At position 35 to 181, the domain is characterized as F5/8 type C.
+At position 187 to 368, the domain is characterized as Laminin G-like 1.
+At position 373 to 552, the domain is characterized as Laminin G-like 2.
+At position 554 to 591, the domain is characterized as EGF-like 1.
+At position 592 to 798, the domain is characterized as Fibrinogen C-terminal.
+At position 799 to 963, the domain is characterized as Laminin G-like 3.
+At position 964 to 1002, the domain is characterized as EGF-like 2.
+At position 1023 to 1214, the domain is characterized as Laminin G-like 4.
+At position 5 to 266, the domain is characterized as Pyruvate carboxyltransferase.
+At position 256 to 353, the domain is characterized as TAFH.
+At position 642 to 691, the domain is characterized as Histone-fold.
+At position 316 to 396, the domain is characterized as Histone-fold.
+At position 6 to 285, the domain is characterized as CN hydrolase.
+At position 6 to 221, the domain is characterized as ABC transporter.
+At position 4 to 182, the domain is characterized as Guanylate kinase-like.
+At position 152 to 272, the domain is characterized as C2 1.
+At position 283 to 416, the domain is characterized as C2 2.
+At position 94 to 320, the domain is characterized as Radical SAM core.
+At position 17 to 241, the domain is characterized as ABC transporter.
+At position 230 to 459, the domain is characterized as NR LBD.
+At position 316 to 397, the domain is characterized as RCK C-terminal 1.
+At position 398 to 483, the domain is characterized as RCK C-terminal 2.
+At position 8 to 190, the domain is characterized as tr-type G.
+At position 170 to 286, the domain is characterized as THUMP.
+At position 22 to 156, the domain is characterized as VOC 1.
+At position 184 to 338, the domain is characterized as VOC 2.
+At position 350 to 428, the domain is characterized as OCT.
+At position 466 to 516, the domain is characterized as DHHC.
+At position 22 to 79, the domain is characterized as HTH lysR-type.
+At position 77 to 506, the domain is characterized as PPM-type phosphatase.
+At position 84 to 301, the domain is characterized as RNase H type-2.
+At position 50 to 208, the domain is characterized as SIS.
+At position 602 to 680, the domain is characterized as BRCT.
+At position 217 to 298, the domain is characterized as BCNT-C.
+At position 124 to 214, the domain is characterized as Ig-like C1-type.
+At position 22 to 238, the domain is characterized as tr-type G.
+At position 504 to 554, the domain is characterized as DHHC.
+At position 31 to 146, the domain is characterized as C-type lectin.
+At position 14 to 94, the domain is characterized as Core-binding (CB).
+At position 112 to 328, the domain is characterized as Tyr recombinase.
+At position 35 to 137, the domain is characterized as Gnk2-homologous 1.
+At position 145 to 254, the domain is characterized as Gnk2-homologous 2.
+At position 4 to 85, the domain is characterized as PB1.
+At position 913 to 957, the domain is characterized as UBA.
+At position 214 to 367, the domain is characterized as TrmE-type G.
+At position 115 to 354, the domain is characterized as Radical SAM core.
+At position 25 to 194, the domain is characterized as Integrase catalytic.
+At position 11 to 175, the domain is characterized as TIR.
+At position 190 to 443, the domain is characterized as NB-ARC.
+At position 958 to 1051, the domain is characterized as PB1.
+At position 16 to 139, the domain is characterized as MsrB.
+At position 44 to 90, the domain is characterized as Gla.
+At position 108 to 187, the domain is characterized as Kringle 1.
+At position 213 to 292, the domain is characterized as Kringle 2.
+At position 365 to 619, the domain is characterized as Peptidase S1.
+At position 76 to 125, the domain is characterized as F-box.
+At position 34 to 95, the domain is characterized as HTH dtxR-type.
+At position 9 to 83, the domain is characterized as U-box.
+At position 196 to 385, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 165, the domain is characterized as Thioredoxin.
+At position 154 to 303, the domain is characterized as TRUD.
+At position 84 to 302, the domain is characterized as Radical SAM core.
+At position 526 to 656, the domain is characterized as RCK N-terminal.
+At position 78 to 308, the domain is characterized as MIF4G.
+At position 543 to 666, the domain is characterized as MI.
+At position 720 to 904, the domain is characterized as W2.
+At position 78 to 180, the domain is characterized as PH.
+At position 194 to 295, the domain is characterized as Ras-associating.
+At position 365 to 551, the domain is characterized as Rho-GAP.
+At position 32 to 418, the domain is characterized as Helicase ATP-binding.
+At position 436 to 631, the domain is characterized as Helicase C-terminal.
+At position 656 to 691, the domain is characterized as UVR.
+At position 6 to 46, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 47 to 89, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 95 to 136, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 138 to 180, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 18 to 164, the domain is characterized as Thioredoxin.
+At position 401 to 523, the domain is characterized as RCK N-terminal.
+At position 22 to 152, the domain is characterized as SIS.
+At position 181 to 231, the domain is characterized as DHHC.
+At position 76 to 249, the domain is characterized as CRAL-TRIO.
+At position 275 to 383, the domain is characterized as GOLD.
+At position 12 to 490, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 510 to 818, the domain is characterized as UvrD-like helicase C-terminal.
+At position 7 to 85, the domain is characterized as RRM.
+At position 64 to 243, the domain is characterized as FAD-binding PCMH-type.
+At position 45 to 212, the domain is characterized as SprT-like.
+At position 216 to 312, the domain is characterized as PH.
+At position 196 to 269, the domain is characterized as RRM.
+At position 27 to 95, the domain is characterized as HTH gntR-type.
+At position 69 to 136, the domain is characterized as GRAM.
+At position 326 to 497, the domain is characterized as VASt.
+At position 234 to 442, the domain is characterized as Helicase ATP-binding.
+At position 480 to 626, the domain is characterized as Helicase C-terminal.
+At position 102 to 182, the domain is characterized as PRC barrel.
+At position 17 to 146, the domain is characterized as N-acetyltransferase 1.
+At position 156 to 296, the domain is characterized as N-acetyltransferase 2.
+At position 930 to 1072, the domain is characterized as MGS-like.
+At position 167 to 482, the domain is characterized as Peptidase S8.
+At position 490 to 628, the domain is characterized as P/Homo B.
+At position 3 to 58, the domain is characterized as HTH deoR-type.
+At position 98 to 208, the domain is characterized as C-type lectin.
+At position 32 to 73, the domain is characterized as JmjN.
+At position 97 to 187, the domain is characterized as ARID.
+At position 453 to 619, the domain is characterized as JmjC.
+At position 145 to 207, the domain is characterized as t-SNARE coiled-coil homology.
+At position 22 to 103, the domain is characterized as Lipoyl-binding.
+At position 1 to 155, the domain is characterized as Flo11.
+At position 1 to 65, the domain is characterized as TGS.
+At position 1 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 543 to 601, the domain is characterized as CBS 1.
+At position 724 to 781, the domain is characterized as CBS 2.
+At position 1 to 412, the domain is characterized as USP.
+At position 467 to 657, the domain is characterized as DH.
+At position 715 to 877, the domain is characterized as PH.
+At position 938 to 1279, the domain is characterized as CNH.
+At position 78 to 180, the domain is characterized as Fe2OG dioxygenase.
+At position 51 to 189, the domain is characterized as Nudix hydrolase.
+At position 24 to 83, the domain is characterized as FHA.
+At position 105 to 181, the domain is characterized as BRCT.
+At position 68 to 361, the domain is characterized as Protein kinase.
+At position 126 to 220, the domain is characterized as Rhodanese.
+At position 7 to 153, the domain is characterized as MPN.
+At position 37 to 72, the domain is characterized as EF-hand 1.
+At position 73 to 108, the domain is characterized as EF-hand 2.
+At position 110 to 145, the domain is characterized as EF-hand 3.
+At position 146 to 181, the domain is characterized as EF-hand 4.
+At position 2 to 83, the domain is characterized as Glutaredoxin.
+At position 1 to 43, the domain is characterized as Chitin-binding type-1.
+At position 4 to 126, the domain is characterized as RNase III.
+At position 153 to 226, the domain is characterized as DRBM.
+At position 3 to 197, the domain is characterized as DPCK.
+At position 4 to 96, the domain is characterized as GST N-terminal.
+At position 105 to 227, the domain is characterized as GST C-terminal.
+At position 177 to 221, the domain is characterized as DSL.
+At position 226 to 254, the domain is characterized as EGF-like 1.
+At position 257 to 285, the domain is characterized as EGF-like 2.
+At position 292 to 325, the domain is characterized as EGF-like 3.
+At position 332 to 363, the domain is characterized as EGF-like 4; calcium-binding.
+At position 370 to 402, the domain is characterized as EGF-like 5.
+At position 409 to 440, the domain is characterized as EGF-like 6.
+At position 447 to 478, the domain is characterized as EGF-like 7; calcium-binding.
+At position 485 to 516, the domain is characterized as EGF-like 8.
+At position 24 to 67, the domain is characterized as CUE.
+At position 360 to 511, the domain is characterized as N-acetyltransferase.
+At position 64 to 359, the domain is characterized as Protein kinase.
+At position 14 to 89, the domain is characterized as S1-like.
+At position 67 to 220, the domain is characterized as Cupin type-1.
+At position 202 to 256, the domain is characterized as HAMP.
+At position 275 to 511, the domain is characterized as Methyl-accepting transducer.
+At position 136 to 235, the domain is characterized as PpiC.
+At position 13 to 163, the domain is characterized as MPN.
+At position 27 to 278, the domain is characterized as Protein kinase.
+At position 437 to 484, the domain is characterized as SARAH.
+At position 54 to 89, the domain is characterized as EF-hand 2.
+At position 50 to 277, the domain is characterized as BPL/LPL catalytic.
+At position 610 to 690, the domain is characterized as BRCT.
+At position 30 to 59, the domain is characterized as EGF-like 1; truncated.
+At position 61 to 106, the domain is characterized as EGF-like 2.
+At position 106 to 150, the domain is characterized as EGF-like 3.
+At position 153 to 193, the domain is characterized as EGF-like 4.
+At position 29 to 97, the domain is characterized as GRAM.
+At position 1 to 86, the domain is characterized as PTS EIIB type-1.
+At position 103 to 459, the domain is characterized as PTS EIIC type-1.
+At position 480 to 584, the domain is characterized as PTS EIIA type-1.
+At position 26 to 214, the domain is characterized as RNase H type-2.
+At position 6 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 4 to 114, the domain is characterized as MTTase N-terminal.
+At position 131 to 369, the domain is characterized as Radical SAM core.
+At position 372 to 437, the domain is characterized as TRAM.
+At position 3 to 91, the domain is characterized as Acylphosphatase-like.
+At position 44 to 202, the domain is characterized as PCI.
+At position 9 to 288, the domain is characterized as tr-type G.
+At position 9 to 238, the domain is characterized as PABS.
+At position 1 to 171, the domain is characterized as Macro.
+At position 100 to 336, the domain is characterized as Radical SAM core.
+At position 112 to 367, the domain is characterized as Protein kinase.
+At position 412 to 447, the domain is characterized as EF-hand 1.
+At position 450 to 481, the domain is characterized as EF-hand 2.
+At position 482 to 517, the domain is characterized as EF-hand 3.
+At position 7 to 243, the domain is characterized as ABC transporter.
+At position 7 to 129, the domain is characterized as RNase III.
+At position 156 to 226, the domain is characterized as DRBM.
+At position 649 to 704, the domain is characterized as HTH myb-type.
+At position 27 to 315, the domain is characterized as GH16.
+At position 10 to 191, the domain is characterized as tr-type G.
+At position 3 to 187, the domain is characterized as Glutamine amidotransferase type-1.
+At position 47 to 174, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 314 to 368, the domain is characterized as HAMP.
+At position 385 to 596, the domain is characterized as Histidine kinase.
+At position 185 to 295, the domain is characterized as Ig-like.
+At position 7 to 72, the domain is characterized as J.
+At position 23 to 72, the domain is characterized as FHA-like.
+At position 173 to 278, the domain is characterized as HIT.
+At position 1 to 236, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 188 to 363, the domain is characterized as EngA-type G 2.
+At position 364 to 448, the domain is characterized as KH-like.
+At position 5 to 246, the domain is characterized as ABC transporter 1.
+At position 295 to 527, the domain is characterized as ABC transporter 2.
+At position 540 to 720, the domain is characterized as DUF724.
+At position 24 to 225, the domain is characterized as Pentraxin (PTX).
+At position 127 to 240, the domain is characterized as LRAT.
+At position 1 to 228, the domain is characterized as Radical SAM core.
+At position 337 to 427, the domain is characterized as BRCT.
+At position 352 to 435, the domain is characterized as KH-like.
+At position 606 to 673, the domain is characterized as PAS.
+At position 28 to 339, the domain is characterized as GH18.
+At position 428 to 502, the domain is characterized as Smr.
+At position 26 to 108, the domain is characterized as UPAR/Ly6.
+At position 1 to 55, the domain is characterized as TRAM.
+At position 2 to 63, the domain is characterized as LCN-type CS-alpha/beta.
+At position 123 to 217, the domain is characterized as Rhodanese.
+At position 25 to 112, the domain is characterized as Ig-like C1-type.
+At position 2 to 237, the domain is characterized as PABS.
+At position 288 to 384, the domain is characterized as PDZ.
+At position 23 to 286, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 229 to 309, the domain is characterized as Toprim.
+At position 14 to 235, the domain is characterized as tr-type G.
+At position 359 to 435, the domain is characterized as RRM.
+At position 2 to 141, the domain is characterized as RNase H type-1.
+At position 57 to 161, the domain is characterized as THUMP.
+At position 63 to 167, the domain is characterized as THUMP.
+At position 2 to 65, the domain is characterized as LCN-type CS-alpha/beta.
+At position 39 to 74, the domain is characterized as EF-hand 1.
+At position 78 to 110, the domain is characterized as EF-hand 2.
+At position 9 to 278, the domain is characterized as Protein kinase.
+At position 128 to 452, the domain is characterized as Peptidase S8.
+At position 460 to 596, the domain is characterized as P/Homo B.
+At position 9 to 278, the domain is characterized as tr-type G.
+At position 11 to 156, the domain is characterized as N-acetyltransferase.
+At position 30 to 137, the domain is characterized as Thioredoxin.
+At position 1 to 101, the domain is characterized as GRAM.
+At position 124 to 499, the domain is characterized as Myotubularin phosphatase.
+At position 202 to 288, the domain is characterized as RCK C-terminal 1.
+At position 290 to 373, the domain is characterized as RCK C-terminal 2.
+At position 4 to 128, the domain is characterized as Toprim.
+At position 12 to 73, the domain is characterized as Sm.
+At position 17 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 212 to 420, the domain is characterized as GMPS ATP-PPase.
+At position 18 to 166, the domain is characterized as Thioredoxin.
+At position 1 to 46, the domain is characterized as CSD.
+At position 413 to 758, the domain is characterized as Peptidase A1.
+At position 92 to 152, the domain is characterized as S4 RNA-binding.
+At position 77 to 176, the domain is characterized as Fe2OG dioxygenase.
+At position 21 to 100, the domain is characterized as Chorismate mutase.
+At position 9 to 262, the domain is characterized as Protein kinase.
+At position 288 to 329, the domain is characterized as UBA.
+At position 29 to 79, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 27 to 142, the domain is characterized as MTTase N-terminal.
+At position 165 to 395, the domain is characterized as Radical SAM core.
+At position 398 to 468, the domain is characterized as TRAM.
+At position 8 to 255, the domain is characterized as ABC transporter.
+At position 4 to 77, the domain is characterized as ACT.
+At position 51 to 160, the domain is characterized as Fibronectin type-III.
+At position 392 to 561, the domain is characterized as tr-type G.
+At position 203 to 376, the domain is characterized as EngA-type G 2.
+At position 377 to 461, the domain is characterized as KH-like.
+At position 1 to 105, the domain is characterized as Calponin-homology (CH).
+At position 2 to 173, the domain is characterized as Glutamine amidotransferase type-1.
+At position 65 to 127, the domain is characterized as KH 1.
+At position 136 to 199, the domain is characterized as KH 2.
+At position 310 to 375, the domain is characterized as Tudor.
+At position 278 to 387, the domain is characterized as Fido.
+At position 42 to 230, the domain is characterized as GH11.
+At position 28 to 119, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 161 to 191, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 97 to 156, the domain is characterized as LIM zinc-binding 1.
+At position 156 to 216, the domain is characterized as LIM zinc-binding 2.
+At position 224 to 283, the domain is characterized as LIM zinc-binding 3.
+At position 283 to 343, the domain is characterized as LIM zinc-binding 4.
+At position 710 to 778, the domain is characterized as HP.
+At position 7 to 163, the domain is characterized as PPIase cyclophilin-type.
+At position 52 to 289, the domain is characterized as PABS.
+At position 101 to 153, the domain is characterized as bHLH.
+At position 86 to 486, the domain is characterized as FH2.
+At position 199 to 320, the domain is characterized as SET.
+At position 146 to 240, the domain is characterized as Rhodanese.
+At position 199 to 273, the domain is characterized as U-box.
+At position 79 to 251, the domain is characterized as PCI.
+At position 206 to 235, the domain is characterized as IQ.
+At position 4 to 24, the domain is characterized as ELK.
+At position 624 to 712, the domain is characterized as BRCT.
+At position 59 to 217, the domain is characterized as TNase-like.
+At position 13 to 165, the domain is characterized as Tyrosine-protein phosphatase.
+At position 80 to 108, the domain is characterized as ITAM.
+At position 12 to 91, the domain is characterized as GIY-YIG.
+At position 16 to 207, the domain is characterized as KARI N-terminal Rossmann.
+At position 208 to 343, the domain is characterized as KARI C-terminal knotted 1.
+At position 344 to 483, the domain is characterized as KARI C-terminal knotted 2.
+At position 69 to 290, the domain is characterized as Radical SAM core.
+At position 44 to 159, the domain is characterized as Calponin-homology (CH).
+At position 685 to 710, the domain is characterized as WW.
+At position 745 to 774, the domain is characterized as IQ 1.
+At position 775 to 804, the domain is characterized as IQ 2.
+At position 805 to 834, the domain is characterized as IQ 3.
+At position 835 to 864, the domain is characterized as IQ 4.
+At position 1004 to 1237, the domain is characterized as Ras-GAP.
+At position 157 to 356, the domain is characterized as Peptidase M12A.
+At position 358 to 470, the domain is characterized as CUB 1.
+At position 471 to 583, the domain is characterized as CUB 2.
+At position 583 to 624, the domain is characterized as EGF-like 1; calcium-binding.
+At position 627 to 739, the domain is characterized as CUB 3.
+At position 739 to 779, the domain is characterized as EGF-like 2; calcium-binding.
+At position 783 to 895, the domain is characterized as CUB 4.
+At position 896 to 1012, the domain is characterized as CUB 5.
+At position 33 to 251, the domain is characterized as Fibrinogen C-terminal.
+At position 259 to 420, the domain is characterized as PH.
+At position 441 to 561, the domain is characterized as Arf-GAP.
+At position 23 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 5 to 75, the domain is characterized as HTH merR-type.
+At position 14 to 96, the domain is characterized as RH1.
+At position 119 to 184, the domain is characterized as RH2.
+At position 26 to 340, the domain is characterized as Transferrin-like 1.
+At position 353 to 685, the domain is characterized as Transferrin-like 2.
+At position 27 to 134, the domain is characterized as Rieske.
+At position 14 to 116, the domain is characterized as Calponin-homology (CH).
+At position 180 to 250, the domain is characterized as EB1 C-terminal.
+At position 20 to 55, the domain is characterized as CBM1.
+At position 131 to 419, the domain is characterized as Peptidase S8.
+At position 135 to 344, the domain is characterized as ATP-grasp.
+At position 73 to 385, the domain is characterized as Peptidase A1.
+At position 600 to 680, the domain is characterized as BRCT.
+At position 69 to 149, the domain is characterized as Cytochrome c 1.
+At position 170 to 248, the domain is characterized as Cytochrome c 2.
+At position 94 to 197, the domain is characterized as BRICHOS.
+At position 3 to 63, the domain is characterized as LIM zinc-binding.
+At position 204 to 263, the domain is characterized as SH3.
+At position 26 to 502, the domain is characterized as PPM-type phosphatase.
+At position 46 to 174, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 69 to 304, the domain is characterized as AB hydrolase-1.
+At position 5 to 165, the domain is characterized as Flavodoxin-like.
+At position 25 to 150, the domain is characterized as Plastocyanin-like 1.
+At position 162 to 306, the domain is characterized as Plastocyanin-like 2.
+At position 373 to 498, the domain is characterized as Plastocyanin-like 3.
+At position 21 to 103, the domain is characterized as Lipoyl-binding.
+At position 38 to 107, the domain is characterized as KH type-2.
+At position 55 to 145, the domain is characterized as Ig-like C2-type.
+At position 169 to 303, the domain is characterized as FZ.
+At position 316 to 394, the domain is characterized as Kringle.
+At position 56 to 173, the domain is characterized as Rhodanese 1.
+At position 224 to 338, the domain is characterized as Rhodanese 2.
+At position 31 to 216, the domain is characterized as BPL/LPL catalytic.
+At position 356 to 763, the domain is characterized as Peptidase S8.
+At position 1080 to 1363, the domain is characterized as ABC transmembrane type-1.
+At position 1518 to 1756, the domain is characterized as ABC transporter.
+At position 52 to 87, the domain is characterized as EF-hand 2.
+At position 123 to 239, the domain is characterized as Calponin-homology (CH) 1.
+At position 267 to 378, the domain is characterized as Calponin-homology (CH) 2.
+At position 397 to 506, the domain is characterized as Calponin-homology (CH) 3.
+At position 518 to 627, the domain is characterized as Calponin-homology (CH) 4.
+At position 209 to 297, the domain is characterized as Ig-like C1-type.
+At position 19 to 59, the domain is characterized as Saposin A-type 1.
+At position 60 to 144, the domain is characterized as Saposin B-type 1.
+At position 180 to 258, the domain is characterized as Saposin B-type 2.
+At position 290 to 370, the domain is characterized as Saposin B-type 3.
+At position 392 to 473, the domain is characterized as Saposin B-type 4.
+At position 475 to 515, the domain is characterized as Saposin A-type 2.
+At position 3 to 120, the domain is characterized as Response regulatory.
+At position 165 to 357, the domain is characterized as CheB-type methylesterase.
+At position 396 to 829, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1329 to 1640, the domain is characterized as PKS/mFAS DH.
+At position 1747 to 1824, the domain is characterized as Carrier.
+At position 94 to 166, the domain is characterized as PRC barrel.
+At position 54 to 224, the domain is characterized as Helicase ATP-binding.
+At position 235 to 396, the domain is characterized as Helicase C-terminal.
+At position 15 to 148, the domain is characterized as MARVEL 1.
+At position 153 to 304, the domain is characterized as MARVEL 2.
+At position 3 to 144, the domain is characterized as RNase H type-1.
+At position 315 to 627, the domain is characterized as ABC transporter 1.
+At position 647 to 975, the domain is characterized as ABC transporter 2.
+At position 241 to 452, the domain is characterized as Ku.
+At position 570 to 604, the domain is characterized as SAP.
+At position 5 to 108, the domain is characterized as PINc.
+At position 291 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 141 to 184, the domain is characterized as CUE.
+At position 92 to 155, the domain is characterized as S4 RNA-binding.
+At position 25 to 59, the domain is characterized as Chitin-binding type-1.
+At position 32 to 136, the domain is characterized as GS beta-grasp.
+At position 143 to 500, the domain is characterized as GS catalytic.
+At position 2 to 87, the domain is characterized as Core-binding (CB).
+At position 108 to 292, the domain is characterized as Tyr recombinase.
+At position 18 to 146, the domain is characterized as EamA 1.
+At position 175 to 300, the domain is characterized as EamA 2.
+At position 1119 to 1242, the domain is characterized as Rab-GAP TBC.
+At position 67 to 251, the domain is characterized as SMP-LTD.
+At position 245 to 366, the domain is characterized as C2 1.
+At position 426 to 543, the domain is characterized as C2 2.
+At position 32 to 143, the domain is characterized as C-type lectin.
+At position 88 to 178, the domain is characterized as K-box.
+At position 22 to 197, the domain is characterized as PI-PLC X-box.
+At position 6 to 129, the domain is characterized as MsrB.
+At position 223 to 298, the domain is characterized as RRM.
+At position 423 to 509, the domain is characterized as Rieske.
+At position 120 to 158, the domain is characterized as LRRCT.
+At position 200 to 262, the domain is characterized as t-SNARE coiled-coil homology.
+At position 30 to 89, the domain is characterized as 4Fe-4S.
+At position 107 to 136, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 137 to 166, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 312 to 358, the domain is characterized as G-patch.
+At position 9 to 69, the domain is characterized as Sm.
+At position 33 to 83, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 31 to 270, the domain is characterized as ABC transporter.
+At position 206 to 294, the domain is characterized as Ig-like C1-type.
+At position 49 to 112, the domain is characterized as S5 DRBM.
+At position 32 to 100, the domain is characterized as BTB.
+At position 215 to 314, the domain is characterized as Fe2OG dioxygenase.
+At position 34 to 101, the domain is characterized as NAC-A/B.
+At position 3 to 198, the domain is characterized as RNase H type-2.
+At position 69 to 130, the domain is characterized as SH3.
+At position 150 to 454, the domain is characterized as Protein kinase.
+At position 24 to 63, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 64 to 108, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 114 to 155, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 156 to 198, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 1 to 170, the domain is characterized as Macro.
+At position 244 to 435, the domain is characterized as GATase cobBQ-type.
+At position 1 to 131, the domain is characterized as RNase III.
+At position 157 to 220, the domain is characterized as DRBM.
+At position 42 to 104, the domain is characterized as KH 1.
+At position 144 to 209, the domain is characterized as KH 2.
+At position 387 to 451, the domain is characterized as KH 3.
+At position 351 to 750, the domain is characterized as PIPK.
+At position 221 to 375, the domain is characterized as TrmE-type G.
+At position 516 to 753, the domain is characterized as NR LBD.
+At position 31 to 116, the domain is characterized as Inhibitor I9.
+At position 120 to 628, the domain is characterized as Peptidase S8.
+At position 398 to 480, the domain is characterized as PA.
+At position 604 to 776, the domain is characterized as PCI.
+At position 334 to 589, the domain is characterized as Protein kinase.
+At position 4 to 391, the domain is characterized as Kinesin motor.
+At position 133 to 266, the domain is characterized as TIR.
+At position 175 to 351, the domain is characterized as EngA-type G 2.
+At position 490 to 659, the domain is characterized as tr-type G.
+At position 161 to 329, the domain is characterized as OBG-type G.
+At position 440 to 562, the domain is characterized as HD.
+At position 679 to 760, the domain is characterized as ACT 1.
+At position 788 to 861, the domain is characterized as ACT 2.
+At position 258 to 317, the domain is characterized as SH3.
+At position 45 to 85, the domain is characterized as LDL-receptor class A.
+At position 1 to 49, the domain is characterized as VWFA 1.
+At position 67 to 156, the domain is characterized as Fibronectin type-III 1.
+At position 158 to 250, the domain is characterized as Fibronectin type-III 2.
+At position 251 to 340, the domain is characterized as Fibronectin type-III 3.
+At position 342 to 432, the domain is characterized as Fibronectin type-III 4.
+At position 434 to 521, the domain is characterized as Fibronectin type-III 5.
+At position 523 to 613, the domain is characterized as Fibronectin type-III 6.
+At position 633 to 805, the domain is characterized as VWFA 2.
+At position 821 to 910, the domain is characterized as Fibronectin type-III 7.
+At position 133 to 185, the domain is characterized as Kazal-like.
+At position 314 to 380, the domain is characterized as Thyroglobulin type-1.
+At position 25 to 61, the domain is characterized as LRRNT.
+At position 219 to 275, the domain is characterized as LRRCT.
+At position 277 to 370, the domain is characterized as Ig-like C2-type.
+At position 101 to 191, the domain is characterized as PRC barrel.
+At position 704 to 782, the domain is characterized as TFIIS N-terminal.
+At position 263 to 457, the domain is characterized as GATase cobBQ-type.
+At position 51 to 223, the domain is characterized as 3'-5' exonuclease.
+At position 522 to 688, the domain is characterized as Helicase ATP-binding.
+At position 713 to 866, the domain is characterized as Helicase C-terminal.
+At position 1115 to 1194, the domain is characterized as HRDC.
+At position 30 to 253, the domain is characterized as AB hydrolase-1.
+At position 18 to 145, the domain is characterized as EamA.
+At position 131 to 163, the domain is characterized as KOW.
+At position 4 to 239, the domain is characterized as ABC transporter 1.
+At position 252 to 495, the domain is characterized as ABC transporter 2.
+At position 62 to 178, the domain is characterized as RGS.
+At position 20 to 177, the domain is characterized as UBC core.
+At position 136 to 243, the domain is characterized as Cadherin 1.
+At position 244 to 355, the domain is characterized as Cadherin 2.
+At position 356 to 471, the domain is characterized as Cadherin 3.
+At position 472 to 579, the domain is characterized as Cadherin 4.
+At position 580 to 694, the domain is characterized as Cadherin 5.
+At position 325 to 504, the domain is characterized as Helicase ATP-binding.
+At position 540 to 690, the domain is characterized as Helicase C-terminal.
+At position 39 to 103, the domain is characterized as CSD.
+At position 2 to 100, the domain is characterized as FAD-binding FR-type.
+At position 1 to 71, the domain is characterized as DRBM 1.
+At position 86 to 155, the domain is characterized as DRBM 2.
+At position 169 to 237, the domain is characterized as DRBM 3.
+At position 1244 to 1531, the domain is characterized as Autotransporter.
+At position 37 to 62, the domain is characterized as LBH.
+At position 34 to 292, the domain is characterized as Protein kinase.
+At position 874 to 909, the domain is characterized as UVR.
+At position 168 to 393, the domain is characterized as TRUD.
+At position 20 to 54, the domain is characterized as Pacifastin 1.
+At position 57 to 92, the domain is characterized as Pacifastin 2.
+At position 24 to 236, the domain is characterized as Radical SAM core.
+At position 1 to 162, the domain is characterized as BUB1 N-terminal.
+At position 222 to 520, the domain is characterized as Protein kinase.
+At position 80 to 172, the domain is characterized as HIG1.
+At position 206 to 262, the domain is characterized as HAMP.
+At position 270 to 472, the domain is characterized as Histidine kinase.
+At position 133 to 306, the domain is characterized as ELMO.
+At position 31 to 208, the domain is characterized as CP-type G.
+At position 134 to 163, the domain is characterized as IQ.
+At position 517 to 710, the domain is characterized as SEC7.
+At position 774 to 866, the domain is characterized as PH.
+At position 260 to 612, the domain is characterized as Kinesin motor.
+At position 347 to 424, the domain is characterized as OCT.
+At position 377 to 442, the domain is characterized as TRAM.
+At position 8 to 98, the domain is characterized as CS.
+At position 1 to 145, the domain is characterized as N-acetyltransferase.
+At position 22 to 156, the domain is characterized as MPN.
+At position 23 to 140, the domain is characterized as Response regulatory.
+At position 23 to 105, the domain is characterized as Lipoyl-binding.
+At position 5 to 90, the domain is characterized as Core-binding (CB).
+At position 111 to 310, the domain is characterized as Tyr recombinase.
+At position 29 to 194, the domain is characterized as PPIase cyclophilin-type.
+At position 104 to 201, the domain is characterized as BRICHOS.
+At position 15 to 91, the domain is characterized as Carrier 1.
+At position 1404 to 1478, the domain is characterized as Carrier 2.
+At position 1943 to 2017, the domain is characterized as Carrier 3.
+At position 35 to 263, the domain is characterized as ATP-grasp.
+At position 8 to 285, the domain is characterized as tr-type G.
+At position 484 to 691, the domain is characterized as MCM.
+At position 27 to 136, the domain is characterized as Thioredoxin 1.
+At position 351 to 477, the domain is characterized as Thioredoxin 2.
+At position 9 to 124, the domain is characterized as MTTase N-terminal.
+At position 134 to 364, the domain is characterized as Radical SAM core.
+At position 367 to 433, the domain is characterized as TRAM.
+At position 51 to 360, the domain is characterized as AB hydrolase-1.
+At position 126 to 281, the domain is characterized as PA14.
+At position 205 to 225, the domain is characterized as ELK.
+At position 23 to 272, the domain is characterized as Pyruvate carboxyltransferase.
+At position 638 to 716, the domain is characterized as BRCT.
+At position 222 to 397, the domain is characterized as CRAL-TRIO.
+At position 20 to 173, the domain is characterized as MARVEL.
+At position 351 to 415, the domain is characterized as S4 RNA-binding.
+At position 139 to 489, the domain is characterized as PUM-HD.
+At position 257 to 397, the domain is characterized as Flavodoxin-like.
+At position 125 to 248, the domain is characterized as Nudix hydrolase.
+At position 160 to 323, the domain is characterized as OBG-type G.
+At position 199 to 388, the domain is characterized as Helicase ATP-binding.
+At position 399 to 559, the domain is characterized as Helicase C-terminal.
+At position 29 to 344, the domain is characterized as GH18.
+At position 23 to 202, the domain is characterized as Josephin.
+At position 282 to 483, the domain is characterized as PNPLA.
+At position 99 to 173, the domain is characterized as RRM 1.
+At position 190 to 267, the domain is characterized as RRM 2.
+At position 379 to 476, the domain is characterized as RRM 3.
+At position 492 to 580, the domain is characterized as RRM 4.
+At position 3 to 128, the domain is characterized as EamA 1.
+At position 139 to 274, the domain is characterized as EamA 2.
+At position 8 to 176, the domain is characterized as Era-type G.
+At position 199 to 283, the domain is characterized as KH type-2.
+At position 331 to 686, the domain is characterized as PUM-HD.
+At position 379 to 451, the domain is characterized as PAS.
+At position 11 to 88, the domain is characterized as RRM.
+At position 678 to 869, the domain is characterized as ATP-grasp 2.
+At position 936 to 1077, the domain is characterized as MGS-like.
+At position 2 to 29, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 323, the domain is characterized as GH10.
+At position 23 to 101, the domain is characterized as Ig-like C2-type 1.
+At position 188 to 271, the domain is characterized as Ig-like C2-type 2.
+At position 287 to 374, the domain is characterized as Ig-like C2-type 3.
+At position 380 to 463, the domain is characterized as Ig-like C2-type 4.
+At position 473 to 556, the domain is characterized as Ig-like C2-type 5.
+At position 566 to 651, the domain is characterized as Ig-like C2-type 6.
+At position 659 to 744, the domain is characterized as Ig-like C2-type 7.
+At position 752 to 834, the domain is characterized as Ig-like C2-type 8.
+At position 24 to 55, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 56 to 85, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 100 to 133, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 20 to 222, the domain is characterized as ABC transporter.
+At position 12 to 73, the domain is characterized as HTH asnC-type.
+At position 33 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 231 to 283, the domain is characterized as CVC.
+At position 98 to 337, the domain is characterized as Radical SAM core.
+At position 20 to 78, the domain is characterized as TRAM.
+At position 1 to 66, the domain is characterized as CSD.
+At position 215 to 598, the domain is characterized as GRAS.
+At position 2 to 217, the domain is characterized as Glutamine amidotransferase type-2.
+At position 283 to 422, the domain is characterized as SIS 1.
+At position 455 to 597, the domain is characterized as SIS 2.
+At position 412 to 520, the domain is characterized as Fe2OG dioxygenase.
+At position 16 to 241, the domain is characterized as Radical SAM core.
+At position 166 to 364, the domain is characterized as B30.2/SPRY.
+At position 134 to 261, the domain is characterized as Thioredoxin 1.
+At position 270 to 384, the domain is characterized as Thioredoxin 2.
+At position 378 to 506, the domain is characterized as Thioredoxin 3.
+At position 75 to 147, the domain is characterized as Inhibitor I9.
+At position 153 to 459, the domain is characterized as Peptidase S8.
+At position 114 to 241, the domain is characterized as OmpA-like.
+At position 112 to 325, the domain is characterized as ATP-grasp.
+At position 117 to 233, the domain is characterized as DOMON.
+At position 24 to 277, the domain is characterized as Protein kinase.
+At position 130 to 235, the domain is characterized as Fe2OG dioxygenase.
+At position 116 to 183, the domain is characterized as COMM.
+At position 96 to 160, the domain is characterized as KH 1.
+At position 181 to 247, the domain is characterized as KH 2.
+At position 271 to 335, the domain is characterized as KH 3.
+At position 372 to 439, the domain is characterized as KH 4.
+At position 21 to 216, the domain is characterized as Ch-type lysozyme.
+At position 130 to 197, the domain is characterized as COMM.
+At position 36 to 114, the domain is characterized as RRM.
+At position 91 to 317, the domain is characterized as Radical SAM core.
+At position 6 to 148, the domain is characterized as SprT-like.
+At position 2 to 144, the domain is characterized as RNase H type-1.
+At position 380 to 478, the domain is characterized as Zinc-hook.
+At position 633 to 733, the domain is characterized as tRNA-binding.
+At position 411 to 614, the domain is characterized as Helicase ATP-binding.
+At position 625 to 783, the domain is characterized as Helicase C-terminal.
+At position 13 to 75, the domain is characterized as KH 1.
+At position 97 to 162, the domain is characterized as KH 2.
+At position 279 to 343, the domain is characterized as KH 3.
+At position 289 to 521, the domain is characterized as NR LBD.
+At position 519 to 647, the domain is characterized as B12-binding.
+At position 72 to 204, the domain is characterized as DCD.
+At position 7 to 78, the domain is characterized as KRAB.
+At position 1 to 114, the domain is characterized as MTTase N-terminal.
+At position 136 to 367, the domain is characterized as Radical SAM core.
+At position 370 to 431, the domain is characterized as TRAM.
+At position 8 to 171, the domain is characterized as Exonuclease.
+At position 350 to 625, the domain is characterized as Protein kinase.
+At position 274 to 336, the domain is characterized as SAM.
+At position 521 to 609, the domain is characterized as Spaetzle.
+At position 29 to 161, the domain is characterized as ENTH.
+At position 8 to 239, the domain is characterized as ABC transporter.
+At position 33 to 273, the domain is characterized as ABC transporter 1.
+At position 751 to 978, the domain is characterized as ABC transporter 2.
+At position 20 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 228, the domain is characterized as Ig-like C2-type 2.
+At position 29 to 130, the domain is characterized as CUB.
+At position 1058 to 1177, the domain is characterized as N-terminal Ras-GEF.
+At position 1316 to 1549, the domain is characterized as Ras-GEF.
+At position 7 to 127, the domain is characterized as MTTase N-terminal.
+At position 151 to 378, the domain is characterized as Radical SAM core.
+At position 381 to 443, the domain is characterized as TRAM.
+At position 15 to 209, the domain is characterized as AMMECR1.
+At position 140 to 198, the domain is characterized as CBS 1.
+At position 225 to 283, the domain is characterized as CBS 2.
+At position 310 to 369, the domain is characterized as CBS 3.
+At position 454 to 533, the domain is characterized as CBS 4.
+At position 3 to 123, the domain is characterized as MTTase N-terminal.
+At position 148 to 381, the domain is characterized as Radical SAM core.
+At position 384 to 446, the domain is characterized as TRAM.
+At position 1 to 227, the domain is characterized as Radical SAM core.
+At position 9 to 128, the domain is characterized as MTTase N-terminal.
+At position 149 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 455, the domain is characterized as TRAM.
+At position 1634 to 2179, the domain is characterized as FAT.
+At position 2287 to 2595, the domain is characterized as PI3K/PI4K catalytic.
+At position 2603 to 2635, the domain is characterized as FATC.
+At position 73 to 319, the domain is characterized as AB hydrolase-1.
+At position 99 to 328, the domain is characterized as NR LBD.
+At position 171 to 354, the domain is characterized as Glutamine amidotransferase type-1.
+At position 366 to 469, the domain is characterized as Fibronectin type-III 1.
+At position 1853 to 1943, the domain is characterized as Fibronectin type-III 2.
+At position 1945 to 2061, the domain is characterized as Fibronectin type-III 3.
+At position 41 to 120, the domain is characterized as Expansin-like CBD.
+At position 68 to 143, the domain is characterized as ACT.
+At position 30 to 108, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 108 to 147, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 245 to 301, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 203 to 327, the domain is characterized as Fe2OG dioxygenase.
+At position 233 to 436, the domain is characterized as PNPLA.
+At position 286 to 362, the domain is characterized as B5.
+At position 182 to 503, the domain is characterized as Peptidase S8.
+At position 512 to 646, the domain is characterized as P/Homo B.
+At position 233 to 264, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 282 to 311, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 571 to 600, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 601 to 629, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 2 to 230, the domain is characterized as ABC transporter.
+At position 70 to 219, the domain is characterized as Ferritin-like diiron.
+At position 42 to 102, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 202, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 300, the domain is characterized as Ig-like C2-type 3.
+At position 13 to 130, the domain is characterized as MTTase N-terminal.
+At position 164 to 396, the domain is characterized as Radical SAM core.
+At position 399 to 462, the domain is characterized as TRAM.
+At position 556 to 752, the domain is characterized as VWFA.
+At position 15 to 78, the domain is characterized as S5 DRBM.
+At position 1 to 134, the domain is characterized as MGS-like.
+At position 45 to 176, the domain is characterized as Cyclin N-terminal.
+At position 30 to 43, the domain is characterized as CRIB.
+At position 233 to 444, the domain is characterized as PCI.
+At position 66 to 115, the domain is characterized as bHLH.
+At position 4 to 180, the domain is characterized as PfpI endopeptidase.
+At position 79 to 308, the domain is characterized as Radical SAM core.
+At position 1 to 108, the domain is characterized as SSB.
+At position 3 to 63, the domain is characterized as LIM zinc-binding 1.
+At position 110 to 170, the domain is characterized as LIM zinc-binding 2.
+At position 26 to 191, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 259, the domain is characterized as OBG-type G.
+At position 281 to 364, the domain is characterized as TGS.
+At position 24 to 281, the domain is characterized as Protein kinase.
+At position 24 to 199, the domain is characterized as EngB-type G.
+At position 10 to 242, the domain is characterized as Nudix hydrolase.
+At position 577 to 606, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 112 to 204, the domain is characterized as Ig-like C1-type.
+At position 171 to 271, the domain is characterized as BEN.
+At position 80 to 278, the domain is characterized as SMP-LTD.
+At position 16 to 239, the domain is characterized as Radical SAM core.
+At position 135 to 226, the domain is characterized as PpiC.
+At position 2 to 30, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 31 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 52 to 170, the domain is characterized as CUB.
+At position 4 to 238, the domain is characterized as ABC transporter.
+At position 297 to 362, the domain is characterized as Mop.
+At position 4 to 91, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 235 to 420, the domain is characterized as FAD-binding PCMH-type.
+At position 28 to 76, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 120 to 155, the domain is characterized as Tify.
+At position 96 to 330, the domain is characterized as Radical SAM core.
+At position 1 to 143, the domain is characterized as ABC transporter 1.
+At position 179 to 416, the domain is characterized as ABC transporter 2.
+At position 177 to 350, the domain is characterized as EngA-type G 2.
+At position 25 to 88, the domain is characterized as LCN-type CS-alpha/beta.
+At position 178 to 224, the domain is characterized as F-box.
+At position 434 to 548, the domain is characterized as Toprim.
+At position 45 to 365, the domain is characterized as AB hydrolase-1.
+At position 42 to 100, the domain is characterized as Ig-like 1.
+At position 137 to 192, the domain is characterized as Ig-like 2.
+At position 26 to 107, the domain is characterized as IGFBP N-terminal.
+At position 173 to 251, the domain is characterized as Thyroglobulin type-1.
+At position 29 to 158, the domain is characterized as AB hydrolase-1.
+At position 59 to 252, the domain is characterized as HD.
+At position 20 to 104, the domain is characterized as SCAN box.
+At position 59 to 158, the domain is characterized as PH.
+At position 5 to 107, the domain is characterized as Glutaredoxin.
+At position 90 to 193, the domain is characterized as Glutaredoxin.
+At position 263 to 377, the domain is characterized as GST C-terminal.
+At position 194 to 382, the domain is characterized as GMPS ATP-PPase.
+At position 109 to 174, the domain is characterized as HTH luxR-type.
+At position 36 to 117, the domain is characterized as RRM.
+At position 162 to 187, the domain is characterized as DAZ.
+At position 13 to 123, the domain is characterized as MTTase N-terminal.
+At position 140 to 377, the domain is characterized as Radical SAM core.
+At position 380 to 445, the domain is characterized as TRAM.
+At position 4 to 383, the domain is characterized as Trm1 methyltransferase.
+At position 24 to 158, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 202 to 271, the domain is characterized as SH3b 1.
+At position 298 to 367, the domain is characterized as SH3b 2.
+At position 39 to 106, the domain is characterized as BTB.
+At position 695 to 976, the domain is characterized as Autotransporter.
+At position 1 to 91, the domain is characterized as B12-binding N-terminal.
+At position 93 to 217, the domain is characterized as B12-binding.
+At position 108 to 314, the domain is characterized as ATP-grasp.
+At position 218 to 370, the domain is characterized as TrmE-type G.
+At position 391 to 560, the domain is characterized as tr-type G.
+At position 241 to 353, the domain is characterized as CUB 1.
+At position 352 to 411, the domain is characterized as Sushi 1.
+At position 413 to 524, the domain is characterized as CUB 2.
+At position 527 to 588, the domain is characterized as Sushi 2.
+At position 590 to 701, the domain is characterized as CUB 3.
+At position 705 to 764, the domain is characterized as Sushi 3.
+At position 766 to 829, the domain is characterized as Sushi 4.
+At position 833 to 894, the domain is characterized as Sushi 5.
+At position 222 to 381, the domain is characterized as TrmE-type G.
+At position 469 to 664, the domain is characterized as N-acetyltransferase.
+At position 8 to 125, the domain is characterized as MSP.
+At position 25 to 234, the domain is characterized as GH16.
+At position 184 to 255, the domain is characterized as RST.
+At position 25 to 72, the domain is characterized as G-patch.
+At position 4 to 134, the domain is characterized as RNase III.
+At position 209 to 437, the domain is characterized as NR LBD.
+At position 3 to 180, the domain is characterized as Guanylate kinase-like.
+At position 190 to 310, the domain is characterized as AB hydrolase-1.
+At position 130 to 224, the domain is characterized as Rhodanese.
+At position 44 to 149, the domain is characterized as Cadherin 1.
+At position 150 to 256, the domain is characterized as Cadherin 2.
+At position 257 to 371, the domain is characterized as Cadherin 3.
+At position 372 to 478, the domain is characterized as Cadherin 4.
+At position 478 to 585, the domain is characterized as Cadherin 5.
+At position 28 to 135, the domain is characterized as Cadherin 1.
+At position 136 to 244, the domain is characterized as Cadherin 2.
+At position 245 to 352, the domain is characterized as Cadherin 3.
+At position 355 to 460, the domain is characterized as Cadherin 4.
+At position 461 to 565, the domain is characterized as Cadherin 5.
+At position 600 to 711, the domain is characterized as Cadherin 6.
+At position 10 to 145, the domain is characterized as UBC core.
+At position 658 to 722, the domain is characterized as CBS 1.
+At position 755 to 812, the domain is characterized as CBS 2.
+At position 684 to 878, the domain is characterized as DDHD.
+At position 553 to 612, the domain is characterized as KH.
+At position 622 to 715, the domain is characterized as S1 motif.
+At position 46 to 132, the domain is characterized as Phosphagen kinase N-terminal.
+At position 159 to 401, the domain is characterized as Phosphagen kinase C-terminal.
+At position 8 to 272, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 125, the domain is characterized as C2.
+At position 326 to 364, the domain is characterized as PLD phosphodiesterase 1.
+At position 654 to 681, the domain is characterized as PLD phosphodiesterase 2.
+At position 202 to 289, the domain is characterized as Ig-like C1-type.
+At position 8 to 123, the domain is characterized as MTTase N-terminal.
+At position 146 to 379, the domain is characterized as Radical SAM core.
+At position 382 to 449, the domain is characterized as TRAM.
+At position 46 to 245, the domain is characterized as TLC.
+At position 77 to 172, the domain is characterized as Toprim.
+At position 220 to 257, the domain is characterized as EGF-like 1.
+At position 258 to 293, the domain is characterized as EGF-like 2.
+At position 301 to 335, the domain is characterized as EGF-like 3.
+At position 1 to 56, the domain is characterized as ClpX-type ZB.
+At position 11 to 287, the domain is characterized as tr-type G.
+At position 71 to 366, the domain is characterized as FAE.
+At position 1 to 190, the domain is characterized as SMP-LTD.
+At position 680 to 733, the domain is characterized as PDZ.
+At position 4 to 185, the domain is characterized as tr-type G.
+At position 214 to 266, the domain is characterized as HAMP.
+At position 271 to 500, the domain is characterized as Methyl-accepting transducer.
+At position 26 to 57, the domain is characterized as LRRNT.
+At position 359 to 416, the domain is characterized as LRRCT.
+At position 27 to 216, the domain is characterized as RNase H type-2.
+At position 3 to 192, the domain is characterized as Glutamine amidotransferase type-1.
+At position 235 to 351, the domain is characterized as CobW C-terminal.
+At position 45 to 322, the domain is characterized as tr-type G.
+At position 128 to 222, the domain is characterized as Rhodanese.
+At position 265 to 359, the domain is characterized as Ras-associating.
+At position 361 to 408, the domain is characterized as SARAH.
+At position 67 to 283, the domain is characterized as Radical SAM core.
+At position 4 to 173, the domain is characterized as N-acetyltransferase.
+At position 5 to 205, the domain is characterized as PPIase cyclophilin-type.
+At position 352 to 503, the domain is characterized as PI-PLC X-box.
+At position 605 to 704, the domain is characterized as SH2 1.
+At position 715 to 804, the domain is characterized as SH2 2.
+At position 832 to 890, the domain is characterized as SH3.
+At position 855 to 960, the domain is characterized as PH.
+At position 982 to 1092, the domain is characterized as PI-PLC Y-box.
+At position 1099 to 1220, the domain is characterized as C2.
+At position 22 to 169, the domain is characterized as CENP-V/GFA.
+At position 53 to 145, the domain is characterized as PPIase FKBP-type.
+At position 27 to 73, the domain is characterized as F-box.
+At position 25 to 441, the domain is characterized as GH18.
+At position 95 to 177, the domain is characterized as PRC barrel.
+At position 5 to 238, the domain is characterized as ABC transporter.
+At position 1 to 65, the domain is characterized as L27.
+At position 555 to 641, the domain is characterized as PDZ 4.
+At position 688 to 774, the domain is characterized as PDZ 5.
+At position 1074 to 1166, the domain is characterized as PDZ 6.
+At position 1245 to 1328, the domain is characterized as PDZ 7.
+At position 1472 to 1555, the domain is characterized as PDZ 8.
+At position 1568 to 1650, the domain is characterized as PDZ 9.
+At position 1709 to 1795, the domain is characterized as PDZ 10.
+At position 221 to 380, the domain is characterized as TrmE-type G.
+At position 134 to 572, the domain is characterized as Urease.
+At position 1045 to 1297, the domain is characterized as Glutamine amidotransferase type-1.
+At position 484 to 669, the domain is characterized as DUF724.
+At position 25 to 71, the domain is characterized as G-patch.
+At position 44 to 160, the domain is characterized as RabBD.
+At position 392 to 514, the domain is characterized as C2 1.
+At position 550 to 683, the domain is characterized as C2 2.
+At position 109 to 435, the domain is characterized as Peptidase A1.
+At position 96 to 188, the domain is characterized as Olduvai 1.
+At position 189 to 277, the domain is characterized as Olduvai 2.
+At position 280 to 335, the domain is characterized as Olduvai 3.
+At position 336 to 427, the domain is characterized as Olduvai 4.
+At position 430 to 485, the domain is characterized as Olduvai 5.
+At position 486 to 577, the domain is characterized as Olduvai 6.
+At position 580 to 652, the domain is characterized as Olduvai 7.
+At position 655 to 710, the domain is characterized as Olduvai 8.
+At position 711 to 803, the domain is characterized as Olduvai 9.
+At position 804 to 902, the domain is characterized as Olduvai 10.
+At position 97 to 132, the domain is characterized as Tify.
+At position 20 to 195, the domain is characterized as Exonuclease.
+At position 27 to 80, the domain is characterized as LIM zinc-binding 1.
+At position 89 to 143, the domain is characterized as LIM zinc-binding 2.
+At position 302 to 557, the domain is characterized as Protein kinase.
+At position 3 to 233, the domain is characterized as Glutamine amidotransferase type-1.
+At position 52 to 182, the domain is characterized as SCP.
+At position 228 to 261, the domain is characterized as EGF-like.
+At position 306 to 442, the domain is characterized as C-type lectin.
+At position 2 to 159, the domain is characterized as Obg.
+At position 160 to 340, the domain is characterized as OBG-type G.
+At position 371 to 444, the domain is characterized as OCT.
+At position 182 to 226, the domain is characterized as DSL.
+At position 227 to 260, the domain is characterized as EGF-like 1.
+At position 261 to 291, the domain is characterized as EGF-like 2; atypical.
+At position 293 to 331, the domain is characterized as EGF-like 3.
+At position 333 to 369, the domain is characterized as EGF-like 4.
+At position 371 to 407, the domain is characterized as EGF-like 5; calcium-binding.
+At position 409 to 445, the domain is characterized as EGF-like 6; calcium-binding.
+At position 447 to 482, the domain is characterized as EGF-like 7; calcium-binding.
+At position 484 to 520, the domain is characterized as EGF-like 8; calcium-binding.
+At position 522 to 558, the domain is characterized as EGF-like 9.
+At position 592 to 624, the domain is characterized as EGF-like 10.
+At position 626 to 662, the domain is characterized as EGF-like 11; calcium-binding.
+At position 664 to 700, the domain is characterized as EGF-like 12; calcium-binding.
+At position 702 to 738, the domain is characterized as EGF-like 13.
+At position 746 to 777, the domain is characterized as EGF-like 14.
+At position 779 to 815, the domain is characterized as EGF-like 15; calcium-binding.
+At position 817 to 853, the domain is characterized as EGF-like 16; calcium-binding.
+At position 860 to 914, the domain is characterized as VWFC.
+At position 918 to 956, the domain is characterized as EGF-like 17.
+At position 9 to 147, the domain is characterized as N-acetyltransferase.
+At position 6 to 84, the domain is characterized as KRAB.
+At position 131 to 232, the domain is characterized as Fibronectin type-III.
+At position 140 to 374, the domain is characterized as ABC transporter.
+At position 57 to 232, the domain is characterized as VWFA 1.
+At position 238 to 278, the domain is characterized as EGF-like 1.
+At position 279 to 319, the domain is characterized as EGF-like 2.
+At position 320 to 360, the domain is characterized as EGF-like 3.
+At position 361 to 401, the domain is characterized as EGF-like 4.
+At position 402 to 442, the domain is characterized as EGF-like 5.
+At position 443 to 483, the domain is characterized as EGF-like 6.
+At position 484 to 524, the domain is characterized as EGF-like 7.
+At position 525 to 565, the domain is characterized as EGF-like 8.
+At position 566 to 606, the domain is characterized as EGF-like 9.
+At position 607 to 647, the domain is characterized as EGF-like 10.
+At position 655 to 830, the domain is characterized as VWFA 2.
+At position 276 to 360, the domain is characterized as PUA.
+At position 5 to 96, the domain is characterized as HIG1.
+At position 105 to 338, the domain is characterized as Radical SAM core.
+At position 82 to 146, the domain is characterized as J.
+At position 12 to 248, the domain is characterized as ABC transporter.
+At position 2 to 245, the domain is characterized as Protein kinase.
+At position 37 to 383, the domain is characterized as G-alpha.
+At position 49 to 109, the domain is characterized as Sushi 1.
+At position 110 to 171, the domain is characterized as Sushi 2.
+At position 172 to 236, the domain is characterized as Sushi 3.
+At position 237 to 296, the domain is characterized as Sushi 4.
+At position 297 to 364, the domain is characterized as Sushi 5.
+At position 365 to 427, the domain is characterized as Sushi 6.
+At position 428 to 485, the domain is characterized as Sushi 7.
+At position 486 to 543, the domain is characterized as Sushi 8.
+At position 24 to 106, the domain is characterized as GS beta-grasp.
+At position 404 to 576, the domain is characterized as CRAL-TRIO.
+At position 580 to 681, the domain is characterized as GOLD.
+At position 3 to 115, the domain is characterized as Response regulatory.
+At position 12 to 98, the domain is characterized as Acylphosphatase-like.
+At position 30 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 360, the domain is characterized as SPX.
+At position 18 to 210, the domain is characterized as Radical SAM core.
+At position 210 to 375, the domain is characterized as Hflx-type G.
+At position 1 to 251, the domain is characterized as Pterin-binding.
+At position 57 to 215, the domain is characterized as Cupin type-1 1.
+At position 259 to 445, the domain is characterized as Cupin type-1 2.
+At position 20 to 83, the domain is characterized as KRAB-related.
+At position 111 to 350, the domain is characterized as Radical SAM core.
+At position 3 to 172, the domain is characterized as N-acetyltransferase.
+At position 211 to 295, the domain is characterized as RCK C-terminal 1.
+At position 317 to 401, the domain is characterized as RCK C-terminal 2.
+At position 406 to 491, the domain is characterized as RCK C-terminal 3.
+At position 497 to 583, the domain is characterized as RCK C-terminal 4.
+At position 18 to 147, the domain is characterized as RNase III.
+At position 173 to 242, the domain is characterized as DRBM.
+At position 236 to 256, the domain is characterized as ELK.
+At position 32 to 126, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 129 to 269, the domain is characterized as FAD-binding FR-type.
+At position 88 to 351, the domain is characterized as ABC transporter.
+At position 433 to 643, the domain is characterized as ABC transmembrane type-2.
+At position 27 to 60, the domain is characterized as LRRNT.
+At position 1 to 117, the domain is characterized as C2.
+At position 408 to 665, the domain is characterized as Protein kinase.
+At position 666 to 737, the domain is characterized as AGC-kinase C-terminal.
+At position 33 to 280, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 4 to 60, the domain is characterized as HTH lysR-type.
+At position 36 to 308, the domain is characterized as CN hydrolase.
+At position 114 to 190, the domain is characterized as PRC barrel.
+At position 45 to 274, the domain is characterized as Radical SAM core.
+At position 1 to 130, the domain is characterized as C-type lysozyme.
+At position 8 to 174, the domain is characterized as N-acetyltransferase 1.
+At position 176 to 339, the domain is characterized as N-acetyltransferase 2.
+At position 456 to 570, the domain is characterized as Toprim.
+At position 90 to 153, the domain is characterized as S4 RNA-binding.
+At position 13 to 255, the domain is characterized as EAL.
+At position 49 to 174, the domain is characterized as EamA 1.
+At position 272 to 325, the domain is characterized as EamA 2.
+At position 586 to 667, the domain is characterized as BRCT.
+At position 1194 to 1452, the domain is characterized as Protein kinase.
+At position 726 to 801, the domain is characterized as Smr.
+At position 119 to 285, the domain is characterized as Helicase ATP-binding.
+At position 371 to 532, the domain is characterized as Helicase C-terminal.
+At position 29 to 149, the domain is characterized as PINc.
+At position 510 to 578, the domain is characterized as KH.
+At position 112 to 207, the domain is characterized as SRCR.
+At position 218 to 453, the domain is characterized as Peptidase S1.
+At position 12 to 96, the domain is characterized as YcgL.
+At position 58 to 204, the domain is characterized as Cupin type-1.
+At position 220 to 792, the domain is characterized as RINT1/TIP20.
+At position 33 to 249, the domain is characterized as TLC.
+At position 24 to 224, the domain is characterized as Pentraxin (PTX).
+At position 149 to 464, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 69 to 309, the domain is characterized as ABC transporter 1.
+At position 380 to 595, the domain is characterized as ABC transporter 2.
+At position 298 to 493, the domain is characterized as Histidine kinase.
+At position 33 to 102, the domain is characterized as DRBM 1.
+At position 118 to 185, the domain is characterized as DRBM 2.
+At position 41 to 213, the domain is characterized as Laminin G-like 1.
+At position 220 to 386, the domain is characterized as Laminin G-like 2.
+At position 218 to 470, the domain is characterized as Olfactomedin-like.
+At position 29 to 131, the domain is characterized as Gnk2-homologous 1.
+At position 137 to 237, the domain is characterized as Gnk2-homologous 2.
+At position 318 to 602, the domain is characterized as Protein kinase.
+At position 30 to 117, the domain is characterized as YebF/Cmi.
+At position 180 to 462, the domain is characterized as NB-ARC.
+At position 190 to 472, the domain is characterized as Peptidase S8.
+At position 207 to 284, the domain is characterized as KH type-2.
+At position 4 to 94, the domain is characterized as Toprim.
+At position 160 to 209, the domain is characterized as LRRCT.
+At position 210 to 300, the domain is characterized as Ig-like C2-type 1.
+At position 319 to 382, the domain is characterized as Ig-like C2-type 2.
+At position 540 to 812, the domain is characterized as Protein kinase.
+At position 34 to 147, the domain is characterized as Ig-like V-type.
+At position 153 to 248, the domain is characterized as Link 1.
+At position 254 to 350, the domain is characterized as Link 2.
+At position 478 to 573, the domain is characterized as Link 3.
+At position 579 to 675, the domain is characterized as Link 4.
+At position 2279 to 2314, the domain is characterized as EGF-like.
+At position 2327 to 2441, the domain is characterized as C-type lectin.
+At position 2445 to 2505, the domain is characterized as Sushi.
+At position 7 to 289, the domain is characterized as Protein kinase.
+At position 66 to 247, the domain is characterized as NodB homology.
+At position 132 to 190, the domain is characterized as HTH cro/C1-type.
+At position 107 to 303, the domain is characterized as ATP-grasp.
+At position 522 to 695, the domain is characterized as tr-type G.
+At position 97 to 325, the domain is characterized as Radical SAM core.
+At position 1 to 87, the domain is characterized as PWI.
+At position 138 to 333, the domain is characterized as ATP-grasp 1.
+At position 695 to 886, the domain is characterized as ATP-grasp 2.
+At position 968 to 1113, the domain is characterized as MGS-like.
+At position 6 to 151, the domain is characterized as MGS-like.
+At position 17 to 255, the domain is characterized as ABC transporter.
+At position 67 to 238, the domain is characterized as Helicase ATP-binding.
+At position 248 to 408, the domain is characterized as Helicase C-terminal.
+At position 109 to 183, the domain is characterized as S4 RNA-binding.
+At position 239 to 466, the domain is characterized as NR LBD.
+At position 163 to 393, the domain is characterized as Histidine kinase.
+At position 75 to 182, the domain is characterized as DM10 1.
+At position 226 to 367, the domain is characterized as DM10 2.
+At position 429 to 536, the domain is characterized as DM10 3.
+At position 557 to 592, the domain is characterized as EF-hand.
+At position 94 to 324, the domain is characterized as ATP-grasp.
+At position 164 to 237, the domain is characterized as HTH crp-type.
+At position 1 to 194, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 307, the domain is characterized as Dynamin-type G.
+At position 546 to 637, the domain is characterized as GED.
+At position 177 to 387, the domain is characterized as Histidine kinase.
+At position 727 to 1022, the domain is characterized as Protein kinase.
+At position 765 to 825, the domain is characterized as RAP.
+At position 31 to 362, the domain is characterized as BPP.
+At position 26 to 131, the domain is characterized as Bulb-type lectin 1.
+At position 145 to 252, the domain is characterized as Bulb-type lectin 2.
+At position 13 to 260, the domain is characterized as ABC transporter.
+At position 22 to 193, the domain is characterized as EngB-type G.
+At position 42 to 306, the domain is characterized as PPM-type phosphatase.
+At position 135 to 364, the domain is characterized as Histidine kinase.
+At position 49 to 167, the domain is characterized as THUMP.
+At position 22 to 254, the domain is characterized as AB hydrolase-1.
+At position 13 to 181, the domain is characterized as Era-type G.
+At position 204 to 288, the domain is characterized as KH type-2.
+At position 65 to 330, the domain is characterized as Protein kinase.
+At position 198 to 490, the domain is characterized as SF4 helicase.
+At position 29 to 86, the domain is characterized as MIR 1.
+At position 94 to 149, the domain is characterized as MIR 2.
+At position 151 to 206, the domain is characterized as MIR 3.
+At position 4 to 170, the domain is characterized as Era-type G.
+At position 136 to 348, the domain is characterized as Histidine kinase.
+At position 173 to 362, the domain is characterized as Helicase ATP-binding.
+At position 373 to 533, the domain is characterized as Helicase C-terminal.
+At position 472 to 614, the domain is characterized as B12-binding.
+At position 9 to 245, the domain is characterized as ABC transporter.
+At position 1183 to 1406, the domain is characterized as MIF4G.
+At position 1603 to 1727, the domain is characterized as MI.
+At position 1 to 196, the domain is characterized as RNase H type-2.
+At position 92 to 212, the domain is characterized as GST C-terminal.
+At position 8 to 119, the domain is characterized as Longin.
+At position 1742 to 1777, the domain is characterized as EF-hand.
+At position 197 to 231, the domain is characterized as SAP.
+At position 2 to 146, the domain is characterized as Jacalin-type lectin 1.
+At position 154 to 297, the domain is characterized as Jacalin-type lectin 2.
+At position 155 to 218, the domain is characterized as bZIP.
+At position 26 to 109, the domain is characterized as SWIB/MDM2.
+At position 6 to 84, the domain is characterized as Carrier.
+At position 3 to 134, the domain is characterized as ADF-H.
+At position 47 to 277, the domain is characterized as Radical SAM core.
+At position 148 to 213, the domain is characterized as HTH luxR-type.
+At position 35 to 265, the domain is characterized as GB1/RHD3-type G.
+At position 7 to 123, the domain is characterized as MTTase N-terminal.
+At position 147 to 377, the domain is characterized as Radical SAM core.
+At position 380 to 448, the domain is characterized as TRAM.
+At position 1 to 121, the domain is characterized as C-type lysozyme.
+At position 183 to 244, the domain is characterized as LIM zinc-binding 1.
+At position 245 to 302, the domain is characterized as LIM zinc-binding 2.
+At position 303 to 372, the domain is characterized as LIM zinc-binding 3.
+At position 471 to 694, the domain is characterized as Histidine kinase.
+At position 716 to 827, the domain is characterized as Response regulatory.
+At position 22 to 385, the domain is characterized as GH18.
+At position 92 to 156, the domain is characterized as S4 RNA-binding.
+At position 28 to 116, the domain is characterized as Ig-like 1.
+At position 121 to 207, the domain is characterized as Ig-like 2.
+At position 212 to 302, the domain is characterized as Ig-like 3.
+At position 312 to 451, the domain is characterized as FZ.
+At position 464 to 543, the domain is characterized as Kringle.
+At position 655 to 934, the domain is characterized as Protein kinase.
+At position 31 to 58, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 95 to 427, the domain is characterized as Rab-GAP TBC.
+At position 564 to 665, the domain is characterized as tRNA-binding.
+At position 112 to 173, the domain is characterized as F-box.
+At position 71 to 219, the domain is characterized as Cupin type-1.
+At position 423 to 619, the domain is characterized as FtsK.
+At position 22 to 58, the domain is characterized as Collagen-like.
+At position 64 to 191, the domain is characterized as C1q.
+At position 258 to 325, the domain is characterized as SAM.
+At position 6 to 70, the domain is characterized as HTH deoR-type.
+At position 83 to 139, the domain is characterized as CBS 1.
+At position 148 to 211, the domain is characterized as CBS 2.
+At position 1 to 145, the domain is characterized as Clp R.
+At position 364 to 405, the domain is characterized as HNH.
+At position 15 to 334, the domain is characterized as Protein kinase.
+At position 46 to 136, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 16 to 133, the domain is characterized as Response regulatory.
+At position 175 to 367, the domain is characterized as CheB-type methylesterase.
+At position 29 to 126, the domain is characterized as Plastocyanin-like.
+At position 64 to 138, the domain is characterized as RRM.
+At position 17 to 80, the domain is characterized as HTH dtxR-type.
+At position 223 to 301, the domain is characterized as Rho RNA-BD.
+At position 6 to 329, the domain is characterized as Kinesin motor.
+At position 161 to 208, the domain is characterized as SOCS box.
+At position 59 to 94, the domain is characterized as QLQ.
+At position 120 to 164, the domain is characterized as WRC.
+At position 239 to 289, the domain is characterized as DHHC.
+At position 99 to 175, the domain is characterized as RRM.
+At position 589 to 690, the domain is characterized as tRNA-binding.
+At position 12 to 147, the domain is characterized as UBC core.
+At position 5 to 201, the domain is characterized as CYTH.
+At position 652 to 906, the domain is characterized as Protein kinase.
+At position 3 to 53, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 163 to 284, the domain is characterized as MI 1.
+At position 326 to 449, the domain is characterized as MI 2.
+At position 28 to 139, the domain is characterized as Ig-like V-type.
+At position 281 to 474, the domain is characterized as B30.2/SPRY.
+At position 1211 to 1272, the domain is characterized as PAP-associated.
+At position 34 to 88, the domain is characterized as MIR 1.
+At position 96 to 151, the domain is characterized as MIR 2.
+At position 154 to 208, the domain is characterized as MIR 3.
+At position 17 to 294, the domain is characterized as Helicase ATP-binding.
+At position 517 to 698, the domain is characterized as Helicase C-terminal.
+At position 2 to 101, the domain is characterized as Sm.
+At position 186 to 253, the domain is characterized as SH3 1.
+At position 315 to 408, the domain is characterized as Fibronectin type-III 1.
+At position 411 to 493, the domain is characterized as Fibronectin type-III 2.
+At position 507 to 608, the domain is characterized as Fibronectin type-III 3.
+At position 1121 to 1189, the domain is characterized as SH3 2.
+At position 1225 to 1292, the domain is characterized as SH3 3.
+At position 9 to 277, the domain is characterized as Protein kinase.
+At position 28 to 96, the domain is characterized as GRAM.
+At position 162 to 537, the domain is characterized as Myotubularin phosphatase.
+At position 56 to 235, the domain is characterized as Macro.
+At position 371 to 528, the domain is characterized as CRAL-TRIO.
+At position 24 to 154, the domain is characterized as TsaA-like.
+At position 295 to 502, the domain is characterized as MCM.
+At position 2 to 131, the domain is characterized as RCK N-terminal 1.
+At position 143 to 227, the domain is characterized as RCK C-terminal 1.
+At position 234 to 356, the domain is characterized as RCK N-terminal 2.
+At position 368 to 453, the domain is characterized as RCK C-terminal 2.
+At position 47 to 171, the domain is characterized as C-type lectin.
+At position 220 to 416, the domain is characterized as Peptidase M12B.
+At position 424 to 505, the domain is characterized as Disintegrin.
+At position 52 to 115, the domain is characterized as S5 DRBM.
+At position 162 to 243, the domain is characterized as PPIase FKBP-type.
+At position 235 to 334, the domain is characterized as PH.
+At position 21 to 113, the domain is characterized as Ig-like.
+At position 24 to 225, the domain is characterized as HORMA.
+At position 61 to 288, the domain is characterized as Radical SAM core.
+At position 1297 to 1877, the domain is characterized as FAT.
+At position 2051 to 2369, the domain is characterized as PI3K/PI4K catalytic.
+At position 2433 to 2465, the domain is characterized as FATC.
+At position 480 to 543, the domain is characterized as SAM.
+At position 4 to 51, the domain is characterized as SpoVT-AbrB.
+At position 26 to 215, the domain is characterized as RNase H type-2.
+At position 394 to 601, the domain is characterized as MCM.
+At position 53 to 270, the domain is characterized as Radical SAM core.
+At position 183 to 388, the domain is characterized as PNPLA.
+At position 122 to 200, the domain is characterized as Cytochrome b5 heme-binding.
+At position 100 to 292, the domain is characterized as Rab-GAP TBC.
+At position 301 to 396, the domain is characterized as Rhodanese.
+At position 285 to 365, the domain is characterized as PB1.
+At position 369 to 428, the domain is characterized as SH3.
+At position 45 to 379, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 28 to 122, the domain is characterized as Ig-like V-type.
+At position 226 to 309, the domain is characterized as Ig-like C2-type 2.
+At position 32 to 519, the domain is characterized as Sema.
+At position 552 to 670, the domain is characterized as Ig-like C2-type.
+At position 232 to 477, the domain is characterized as CN hydrolase.
+At position 24 to 81, the domain is characterized as 4Fe-4S Wbl-type.
+At position 43 to 133, the domain is characterized as Inhibitor I9.
+At position 144 to 450, the domain is characterized as Peptidase S8.
+At position 1 to 85, the domain is characterized as DIX.
+At position 251 to 323, the domain is characterized as PDZ.
+At position 425 to 499, the domain is characterized as DEP.
+At position 6 to 155, the domain is characterized as RNase III.
+At position 198 to 267, the domain is characterized as DRBM 1.
+At position 285 to 355, the domain is characterized as DRBM 2.
+At position 11 to 26, the domain is characterized as Helicase ATP-binding.
+At position 41 to 82, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 88 to 128, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 129 to 171, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 3 to 195, the domain is characterized as DPCK.
+At position 450 to 518, the domain is characterized as PAS 1.
+At position 738 to 807, the domain is characterized as PAS 2.
+At position 1096 to 1354, the domain is characterized as Protein kinase.
+At position 94 to 218, the domain is characterized as B12-binding.
+At position 261 to 332, the domain is characterized as Fibronectin type-III 1.
+At position 446 to 565, the domain is characterized as Fibronectin type-III 2.
+At position 43 to 106, the domain is characterized as S4 RNA-binding.
+At position 20 to 216, the domain is characterized as Lon N-terminal.
+At position 606 to 787, the domain is characterized as Lon proteolytic.
+At position 12 to 206, the domain is characterized as YjeF N-terminal.
+At position 3 to 79, the domain is characterized as ZAD.
+At position 5 to 362, the domain is characterized as DZF.
+At position 386 to 452, the domain is characterized as DRBM 1.
+At position 509 to 575, the domain is characterized as DRBM 2.
+At position 29 to 279, the domain is characterized as AB hydrolase-1.
+At position 29 to 265, the domain is characterized as ABC transporter 1.
+At position 275 to 515, the domain is characterized as ABC transporter 2.
+At position 214 to 315, the domain is characterized as HTH araC/xylS-type.
+At position 23 to 59, the domain is characterized as Pacifastin 1.
+At position 85 to 121, the domain is characterized as Pacifastin 2.
+At position 147 to 184, the domain is characterized as Pacifastin 3.
+At position 22 to 82, the domain is characterized as v-SNARE coiled-coil homology.
+At position 31 to 88, the domain is characterized as FHA.
+At position 218 to 368, the domain is characterized as TrmE-type G.
+At position 1 to 68, the domain is characterized as YbbR-like.
+At position 13 to 228, the domain is characterized as tr-type G.
+At position 9 to 56, the domain is characterized as F-box.
+At position 179 to 280, the domain is characterized as PpiC 1.
+At position 290 to 388, the domain is characterized as PpiC 2.
+At position 6 to 93, the domain is characterized as Acylphosphatase-like.
+At position 262 to 457, the domain is characterized as PCI.
+At position 15 to 69, the domain is characterized as HTH cro/C1-type.
+At position 121 to 201, the domain is characterized as CBS 1.
+At position 205 to 261, the domain is characterized as CBS 2.
+At position 2 to 83, the domain is characterized as GST N-terminal.
+At position 89 to 219, the domain is characterized as GST C-terminal.
+At position 4 to 173, the domain is characterized as Era-type G.
+At position 204 to 280, the domain is characterized as KH type-2.
+At position 1 to 119, the domain is characterized as Calponin-homology (CH).
+At position 194 to 373, the domain is characterized as DH.
+At position 402 to 504, the domain is characterized as PH.
+At position 592 to 660, the domain is characterized as SH3 1.
+At position 671 to 765, the domain is characterized as SH2.
+At position 782 to 842, the domain is characterized as SH3 2.
+At position 180 to 222, the domain is characterized as CHCH.
+At position 103 to 155, the domain is characterized as bHLH.
+At position 414 to 564, the domain is characterized as SEFIR.
+At position 371 to 540, the domain is characterized as tr-type G.
+At position 104 to 301, the domain is characterized as ATP-grasp.
+At position 6 to 200, the domain is characterized as Lon N-terminal.
+At position 596 to 776, the domain is characterized as Lon proteolytic.
+At position 2 to 189, the domain is characterized as Glutamine amidotransferase type-1.
+At position 56 to 120, the domain is characterized as SH3.
+At position 142 to 402, the domain is characterized as Protein kinase.
+At position 92 to 351, the domain is characterized as PPM-type phosphatase.
+At position 56 to 102, the domain is characterized as F-box.
+At position 23 to 66, the domain is characterized as CUE.
+At position 21 to 43, the domain is characterized as Follistatin-like 1.
+At position 121 to 143, the domain is characterized as Follistatin-like 2.
+At position 151 to 173, the domain is characterized as Follistatin-like 3.
+At position 27 to 139, the domain is characterized as Cadherin 1.
+At position 140 to 249, the domain is characterized as Cadherin 2.
+At position 250 to 355, the domain is characterized as Cadherin 3.
+At position 362 to 466, the domain is characterized as Cadherin 4.
+At position 467 to 570, the domain is characterized as Cadherin 5.
+At position 571 to 673, the domain is characterized as Cadherin 6.
+At position 677 to 795, the domain is characterized as Cadherin 7.
+At position 1 to 257, the domain is characterized as F-BAR.
+At position 322 to 513, the domain is characterized as Rho-GAP.
+At position 8 to 202, the domain is characterized as Lon N-terminal.
+At position 590 to 770, the domain is characterized as Lon proteolytic.
+At position 6 to 144, the domain is characterized as DAC.
+At position 29 to 108, the domain is characterized as RRM 1.
+At position 118 to 195, the domain is characterized as RRM 2.
+At position 71 to 168, the domain is characterized as Plastocyanin-like.
+At position 369 to 605, the domain is characterized as TLDc.
+At position 20 to 96, the domain is characterized as PAN.
+At position 41 to 130, the domain is characterized as PPIase FKBP-type.
+At position 91 to 262, the domain is characterized as Helicase ATP-binding.
+At position 286 to 434, the domain is characterized as Helicase C-terminal.
+At position 36 to 135, the domain is characterized as Cadherin 1.
+At position 136 to 247, the domain is characterized as Cadherin 2.
+At position 248 to 354, the domain is characterized as Cadherin 3.
+At position 360 to 473, the domain is characterized as Cadherin 4.
+At position 474 to 577, the domain is characterized as Cadherin 5.
+At position 569 to 691, the domain is characterized as Cadherin 6.
+At position 333 to 382, the domain is characterized as bHLH.
+At position 91 to 165, the domain is characterized as PRC barrel.
+At position 92 to 354, the domain is characterized as Protein kinase.
+At position 357 to 425, the domain is characterized as AGC-kinase C-terminal.
+At position 497 to 573, the domain is characterized as REM-1.
+At position 979 to 1047, the domain is characterized as RhoBD.
+At position 1150 to 1349, the domain is characterized as PH.
+At position 462 to 577, the domain is characterized as HD.
+At position 701 to 778, the domain is characterized as ACT 1.
+At position 808 to 882, the domain is characterized as ACT 2.
+At position 1 to 92, the domain is characterized as HIG1.
+At position 14 to 106, the domain is characterized as GS beta-grasp.
+At position 113 to 446, the domain is characterized as GS catalytic.
+At position 64 to 114, the domain is characterized as S4 RNA-binding.
+At position 22 to 126, the domain is characterized as Ig-like V-type 1.
+At position 127 to 219, the domain is characterized as Ig-like V-type 2.
+At position 220 to 312, the domain is characterized as Ig-like V-type 3.
+At position 313 to 415, the domain is characterized as Ig-like V-type 4.
+At position 416 to 513, the domain is characterized as Ig-like V-type 5.
+At position 1258 to 1526, the domain is characterized as Autotransporter.
+At position 4 to 156, the domain is characterized as Thioredoxin.
+At position 35 to 91, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 190 to 375, the domain is characterized as Glutamine amidotransferase type-1.
+At position 22 to 89, the domain is characterized as POTRA 1.
+At position 90 to 170, the domain is characterized as POTRA 2.
+At position 173 to 259, the domain is characterized as POTRA 3.
+At position 262 to 341, the domain is characterized as POTRA 4.
+At position 344 to 418, the domain is characterized as POTRA 5.
+At position 224 to 244, the domain is characterized as ELK.
+At position 3 to 64, the domain is characterized as LIM zinc-binding 1.
+At position 122 to 183, the domain is characterized as LIM zinc-binding 2.
+At position 4 to 249, the domain is characterized as ABC transporter.
+At position 31 to 175, the domain is characterized as Nudix hydrolase.
+At position 10 to 94, the domain is characterized as Core-binding (CB).
+At position 115 to 294, the domain is characterized as Tyr recombinase.
+At position 93 to 128, the domain is characterized as Tify.
+At position 41 to 307, the domain is characterized as Septin-type G.
+At position 1 to 85, the domain is characterized as PTS EIIB type-2 1.
+At position 104 to 201, the domain is characterized as PTS EIIB type-2 2.
+At position 226 to 561, the domain is characterized as PTS EIIC type-2.
+At position 4 to 386, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 225 to 263, the domain is characterized as Myb-like 1.
+At position 268 to 333, the domain is characterized as HTH myb-type.
+At position 339 to 388, the domain is characterized as Myb-like 2.
+At position 92 to 180, the domain is characterized as PB1.
+At position 33 to 82, the domain is characterized as Myosin N-terminal SH3-like.
+At position 86 to 782, the domain is characterized as Myosin motor.
+At position 785 to 814, the domain is characterized as IQ.
+At position 235 to 461, the domain is characterized as tr-type G.
+At position 175 to 289, the domain is characterized as Fe2OG dioxygenase.
+At position 3 to 86, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 95 to 473, the domain is characterized as PRONE.
+At position 22 to 278, the domain is characterized as Protein kinase.
+At position 77 to 449, the domain is characterized as GRAS.
+At position 158 to 430, the domain is characterized as ABC transporter 1.
+At position 508 to 721, the domain is characterized as ABC transmembrane type-2 1.
+At position 843 to 1095, the domain is characterized as ABC transporter 2.
+At position 1168 to 1382, the domain is characterized as ABC transmembrane type-2 2.
+At position 7 to 99, the domain is characterized as HTH La-type RNA-binding.
+At position 111 to 187, the domain is characterized as RRM.
+At position 227 to 348, the domain is characterized as xRRM.
+At position 31 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 185 to 267, the domain is characterized as PDZ.
+At position 24 to 68, the domain is characterized as Fibronectin type-II 1.
+At position 69 to 117, the domain is characterized as Fibronectin type-II 2.
+At position 124 to 170, the domain is characterized as Fibronectin type-II 3.
+At position 177 to 223, the domain is characterized as Fibronectin type-II 4.
+At position 42 to 107, the domain is characterized as Ig-like C2-type 1.
+At position 142 to 205, the domain is characterized as Ig-like C2-type 2.
+At position 610 to 712, the domain is characterized as tRNA-binding.
+At position 95 to 153, the domain is characterized as CBS 1.
+At position 157 to 216, the domain is characterized as CBS 2.
+At position 28 to 122, the domain is characterized as HTH arsR-type.
+At position 73 to 215, the domain is characterized as HD.
+At position 3 to 193, the domain is characterized as Glutamine amidotransferase type-1.
+At position 20 to 119, the domain is characterized as CBM39.
+At position 152 to 490, the domain is characterized as GH16.
+At position 8 to 55, the domain is characterized as SpoVT-AbrB 1.
+At position 84 to 127, the domain is characterized as SpoVT-AbrB 2.
+At position 88 to 239, the domain is characterized as Nudix hydrolase.
+At position 1 to 383, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 412 to 631, the domain is characterized as VWFA.
+At position 186 to 386, the domain is characterized as Helicase ATP-binding.
+At position 422 to 571, the domain is characterized as Helicase C-terminal.
+At position 160 to 367, the domain is characterized as DAGKc.
+At position 14 to 83, the domain is characterized as HTH HARE-type.
+At position 28 to 318, the domain is characterized as Protein kinase.
+At position 107 to 147, the domain is characterized as UBA.
+At position 35 to 128, the domain is characterized as UPAR/Ly6 1.
+At position 142 to 224, the domain is characterized as UPAR/Ly6 2.
+At position 49 to 235, the domain is characterized as Helicase ATP-binding.
+At position 248 to 477, the domain is characterized as Helicase C-terminal.
+At position 1 to 169, the domain is characterized as PPIase cyclophilin-type.
+At position 246 to 324, the domain is characterized as RRM.
+At position 337 to 521, the domain is characterized as PCI.
+At position 3 to 65, the domain is characterized as LCN-type CS-alpha/beta.
+At position 21 to 55, the domain is characterized as EGF-like 1.
+At position 61 to 93, the domain is characterized as EGF-like 2.
+At position 12 to 133, the domain is characterized as MsrB.
+At position 94 to 170, the domain is characterized as PUA.
+At position 3 to 88, the domain is characterized as Core-binding (CB).
+At position 109 to 302, the domain is characterized as Tyr recombinase.
+At position 8 to 106, the domain is characterized as HTH araC/xylS-type.
+At position 66 to 270, the domain is characterized as ABC transmembrane type-1.
+At position 23 to 200, the domain is characterized as EngB-type G.
+At position 2 to 200, the domain is characterized as ABC transporter.
+At position 21 to 81, the domain is characterized as LCN-type CS-alpha/beta.
+At position 80 to 299, the domain is characterized as ABC transporter.
+At position 43 to 286, the domain is characterized as ABC transporter.
+At position 41 to 88, the domain is characterized as P-type 1.
+At position 904 to 950, the domain is characterized as P-type 2.
+At position 17 to 254, the domain is characterized as Radical SAM core.
+At position 44 to 74, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 20 to 60, the domain is characterized as Chitin-binding type-1.
+At position 33 to 77, the domain is characterized as EGF-like.
+At position 3 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 347 to 382, the domain is characterized as EF-hand 1.
+At position 2 to 71, the domain is characterized as Biotinyl-binding.
+At position 6 to 188, the domain is characterized as UmuC.
+At position 5 to 62, the domain is characterized as HTH lysR-type.
+At position 426 to 653, the domain is characterized as Histidine kinase.
+At position 669 to 784, the domain is characterized as Response regulatory 1.
+At position 1078 to 1200, the domain is characterized as Response regulatory 2.
+At position 71 to 262, the domain is characterized as RNase H type-2.
+At position 59 to 111, the domain is characterized as F-box.
+At position 23 to 412, the domain is characterized as Helicase ATP-binding.
+At position 429 to 588, the domain is characterized as Helicase C-terminal.
+At position 46 to 169, the domain is characterized as C-type lectin.
+At position 414 to 628, the domain is characterized as BURP.
+At position 9 to 131, the domain is characterized as RNase III.
+At position 158 to 228, the domain is characterized as DRBM.
+At position 48 to 158, the domain is characterized as Ig-like V-type 1.
+At position 159 to 243, the domain is characterized as Ig-like C2-type 1.
+At position 250 to 362, the domain is characterized as Ig-like V-type 2.
+At position 353 to 453, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 84, the domain is characterized as GRAM.
+At position 1 to 26, the domain is characterized as Chitin-binding type-1.
+At position 27 to 91, the domain is characterized as Barwin.
+At position 1026 to 1072, the domain is characterized as EGF-like.
+At position 1076 to 1114, the domain is characterized as LDL-receptor class A 1.
+At position 1115 to 1155, the domain is characterized as LDL-receptor class A 2.
+At position 1156 to 1194, the domain is characterized as LDL-receptor class A 3.
+At position 1198 to 1236, the domain is characterized as LDL-receptor class A 4.
+At position 1238 to 1272, the domain is characterized as LDL-receptor class A 5.
+At position 1273 to 1317, the domain is characterized as LDL-receptor class A 6.
+At position 1323 to 1361, the domain is characterized as LDL-receptor class A 7.
+At position 1366 to 1405, the domain is characterized as LDL-receptor class A 8.
+At position 1417 to 1455, the domain is characterized as LDL-receptor class A 9.
+At position 1469 to 1508, the domain is characterized as LDL-receptor class A 10.
+At position 1512 to 1551, the domain is characterized as LDL-receptor class A 11.
+At position 1557 to 1649, the domain is characterized as Fibronectin type-III 1.
+At position 1653 to 1745, the domain is characterized as Fibronectin type-III 2.
+At position 1747 to 1846, the domain is characterized as Fibronectin type-III 3.
+At position 1844 to 1928, the domain is characterized as Fibronectin type-III 4.
+At position 1935 to 2030, the domain is characterized as Fibronectin type-III 5.
+At position 2031 to 2119, the domain is characterized as Fibronectin type-III 6.
+At position 158 to 342, the domain is characterized as MIF4G.
+At position 454 to 570, the domain is characterized as MI.
+At position 2 to 52, the domain is characterized as HTH psq-type.
+At position 65 to 136, the domain is characterized as HTH CENPB-type.
+At position 87 to 285, the domain is characterized as Peptidase M12A.
+At position 287 to 399, the domain is characterized as CUB.
+At position 61 to 217, the domain is characterized as NHR 1.
+At position 292 to 447, the domain is characterized as NHR 2.
+At position 2 to 184, the domain is characterized as B30.2/SPRY.
+At position 19 to 125, the domain is characterized as CFEM.
+At position 30 to 251, the domain is characterized as ABC transmembrane type-2.
+At position 36 to 96, the domain is characterized as Sushi 1.
+At position 43 to 346, the domain is characterized as AB hydrolase-1.
+At position 46 to 275, the domain is characterized as Radical SAM core.
+At position 565 to 631, the domain is characterized as KH.
+At position 633 to 701, the domain is characterized as S1 motif.
+At position 18 to 61, the domain is characterized as CHCH.
+At position 676 to 870, the domain is characterized as ATP-grasp 2.
+At position 951 to 1095, the domain is characterized as MGS-like.
+At position 271 to 333, the domain is characterized as SAM.
+At position 219 to 378, the domain is characterized as TrmE-type G.
+At position 43 to 134, the domain is characterized as Inhibitor I9.
+At position 186 to 238, the domain is characterized as HAMP.
+At position 246 to 456, the domain is characterized as Histidine kinase.
+At position 33 to 224, the domain is characterized as ABC transmembrane type-1.
+At position 22 to 150, the domain is characterized as Ig-like C2-type.
+At position 590 to 723, the domain is characterized as N-terminal Ras-GEF.
+At position 752 to 985, the domain is characterized as Ras-GEF.
+At position 591 to 662, the domain is characterized as KHA.
+At position 9 to 245, the domain is characterized as ATP-grasp.
+At position 218 to 597, the domain is characterized as GRAS.
+At position 11 to 179, the domain is characterized as Era-type G.
+At position 210 to 287, the domain is characterized as KH type-2.
+At position 30 to 225, the domain is characterized as GH16.
+At position 2 to 56, the domain is characterized as HTH lacI-type.
+At position 632 to 691, the domain is characterized as PASTA 1.
+At position 692 to 750, the domain is characterized as PASTA 2.
+At position 28 to 150, the domain is characterized as MsrB.
+At position 706 to 741, the domain is characterized as EF-hand 1.
+At position 738 to 773, the domain is characterized as EF-hand 2.
+At position 1121 to 1183, the domain is characterized as FIP-RBD.
+At position 62 to 185, the domain is characterized as Rhodanese.
+At position 4 to 69, the domain is characterized as J.
+At position 18 to 103, the domain is characterized as GS beta-grasp.
+At position 110 to 446, the domain is characterized as GS catalytic.
+At position 28 to 105, the domain is characterized as GIY-YIG.
+At position 102 to 367, the domain is characterized as Protein kinase.
+At position 14 to 137, the domain is characterized as Rhodanese.
+At position 130 to 302, the domain is characterized as Helicase ATP-binding.
+At position 359 to 513, the domain is characterized as Helicase C-terminal.
+At position 82 to 117, the domain is characterized as EF-hand 3.
+At position 118 to 153, the domain is characterized as EF-hand 4.
+At position 539 to 630, the domain is characterized as BRCT.
+At position 30 to 219, the domain is characterized as RNase H type-2.
+At position 480 to 560, the domain is characterized as FH1.
+At position 585 to 1032, the domain is characterized as FH2.
+At position 84 to 186, the domain is characterized as FAR1.
+At position 284 to 380, the domain is characterized as MULE.
+At position 11 to 93, the domain is characterized as DIX.
+At position 267 to 339, the domain is characterized as PDZ.
+At position 433 to 507, the domain is characterized as DEP.
+At position 424 to 496, the domain is characterized as HSA.
+At position 777 to 942, the domain is characterized as Helicase ATP-binding.
+At position 1314 to 1464, the domain is characterized as Helicase C-terminal.
+At position 83 to 258, the domain is characterized as Helicase ATP-binding.
+At position 270 to 431, the domain is characterized as Helicase C-terminal.
+At position 344 to 467, the domain is characterized as PLAT.
+At position 619 to 725, the domain is characterized as tRNA-binding.
+At position 438 to 698, the domain is characterized as Protein kinase.
+At position 699 to 749, the domain is characterized as AGC-kinase C-terminal.
+At position 69 to 247, the domain is characterized as Helicase ATP-binding.
+At position 332 to 531, the domain is characterized as Helicase C-terminal.
+At position 2 to 216, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 68, the domain is characterized as HMA.
+At position 40 to 86, the domain is characterized as G-patch.
+At position 175 to 261, the domain is characterized as Toprim.
+At position 144 to 269, the domain is characterized as NEAT 1.
+At position 341 to 458, the domain is characterized as NEAT 2.
+At position 92 to 136, the domain is characterized as Fibronectin type-II 1.
+At position 137 to 183, the domain is characterized as Fibronectin type-II 2.
+At position 600 to 654, the domain is characterized as SAM.
+At position 20 to 170, the domain is characterized as GRAD2.
+At position 171 to 681, the domain is characterized as GRAD1.
+At position 97 to 264, the domain is characterized as TNase-like.
+At position 14 to 94, the domain is characterized as WWE 1.
+At position 95 to 171, the domain is characterized as WWE 2.
+At position 1 to 145, the domain is characterized as RNase H type-1.
+At position 20 to 356, the domain is characterized as F5/8 type A 1.
+At position 20 to 199, the domain is characterized as Plastocyanin-like 1.
+At position 208 to 356, the domain is characterized as Plastocyanin-like 2.
+At position 369 to 713, the domain is characterized as F5/8 type A 2.
+At position 369 to 555, the domain is characterized as Plastocyanin-like 3.
+At position 565 to 713, the domain is characterized as Plastocyanin-like 4.
+At position 725 to 1056, the domain is characterized as F5/8 type A 3.
+At position 725 to 895, the domain is characterized as Plastocyanin-like 5.
+At position 903 to 1056, the domain is characterized as Plastocyanin-like 6.
+At position 231 to 415, the domain is characterized as Reverse transcriptase.
+At position 810 to 967, the domain is characterized as Integrase catalytic.
+At position 11 to 231, the domain is characterized as Glutamine amidotransferase type-2.
+At position 99 to 134, the domain is characterized as EF-hand 3.
+At position 143 to 178, the domain is characterized as EF-hand 4.
+At position 187 to 222, the domain is characterized as EF-hand 5.
+At position 622 to 690, the domain is characterized as S1 motif.
+At position 377 to 582, the domain is characterized as Helicase ATP-binding.
+At position 593 to 756, the domain is characterized as Helicase C-terminal.
+At position 138 to 231, the domain is characterized as PpiC.
+At position 217 to 325, the domain is characterized as Guanylate cyclase.
+At position 44 to 155, the domain is characterized as THUMP.
+At position 42 to 107, the domain is characterized as SUZ.
+At position 111 to 152, the domain is characterized as SUZ-C.
+At position 454 to 623, the domain is characterized as tr-type G.
+At position 30 to 146, the domain is characterized as LRAT.
+At position 6 to 224, the domain is characterized as ABC transporter.
+At position 53 to 305, the domain is characterized as Protein kinase.
+At position 261 to 313, the domain is characterized as bHLH.
+At position 464 to 758, the domain is characterized as NACHT.
+At position 1 to 120, the domain is characterized as N-acetyltransferase.
+At position 2 to 79, the domain is characterized as GST N-terminal.
+At position 81 to 206, the domain is characterized as GST C-terminal.
+At position 11 to 305, the domain is characterized as Hcy-binding.
+At position 36 to 87, the domain is characterized as AWS.
+At position 84 to 206, the domain is characterized as SET.
+At position 213 to 229, the domain is characterized as Post-SET.
+At position 41 to 131, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 241 to 326, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 407, the domain is characterized as Ig-like C2-type 4.
+At position 413 to 500, the domain is characterized as Ig-like C2-type 5.
+At position 504 to 603, the domain is characterized as Ig-like C2-type 6.
+At position 608 to 706, the domain is characterized as Fibronectin type-III 1.
+At position 711 to 808, the domain is characterized as Fibronectin type-III 2.
+At position 813 to 908, the domain is characterized as Fibronectin type-III 3.
+At position 909 to 1002, the domain is characterized as Fibronectin type-III 4.
+At position 32 to 181, the domain is characterized as IRG-type G.
+At position 42 to 166, the domain is characterized as Nudix hydrolase.
+At position 75 to 144, the domain is characterized as HTH iclR-type.
+At position 6 to 56, the domain is characterized as F-box.
+At position 50 to 441, the domain is characterized as Rab-GAP TBC.
+At position 339 to 404, the domain is characterized as S4 RNA-binding.
+At position 80 to 206, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 11 to 89, the domain is characterized as RRM 1.
+At position 99 to 175, the domain is characterized as RRM 2.
+At position 191 to 268, the domain is characterized as RRM 3.
+At position 294 to 370, the domain is characterized as RRM 4.
+At position 539 to 616, the domain is characterized as PABC.
+At position 1 to 93, the domain is characterized as PE.
+At position 126 to 165, the domain is characterized as UBA.
+At position 233 to 308, the domain is characterized as MIT.
+At position 65 to 76, the domain is characterized as EF-hand 1.
+At position 86 to 121, the domain is characterized as EF-hand 2.
+At position 125 to 155, the domain is characterized as EF-hand 3.
+At position 157 to 192, the domain is characterized as EF-hand 4.
+At position 9 to 74, the domain is characterized as J.
+At position 120 to 183, the domain is characterized as bZIP.
+At position 6 to 76, the domain is characterized as TRAM.
+At position 30 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 496 to 613, the domain is characterized as HD.
+At position 737 to 818, the domain is characterized as ACT 1.
+At position 848 to 931, the domain is characterized as ACT 2.
+At position 1 to 141, the domain is characterized as N-acetyltransferase.
+At position 51 to 407, the domain is characterized as Peptidase A1.
+At position 97 to 326, the domain is characterized as Radical SAM core.
+At position 13 to 43, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 50 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 16 to 135, the domain is characterized as NTF2.
+At position 61 to 261, the domain is characterized as TLC.
+At position 159 to 362, the domain is characterized as OBG-type G.
+At position 489 to 746, the domain is characterized as Olfactomedin-like.
+At position 649 to 907, the domain is characterized as Protein kinase.
+At position 63 to 290, the domain is characterized as Radical SAM core.
+At position 724 to 800, the domain is characterized as Carrier.
+At position 31 to 205, the domain is characterized as PI-PLC X-box.
+At position 629 to 846, the domain is characterized as tr-type G.
+At position 80 to 179, the domain is characterized as Fe2OG dioxygenase.
+At position 215 to 266, the domain is characterized as HAMP.
+At position 274 to 480, the domain is characterized as Histidine kinase.
+At position 608 to 667, the domain is characterized as KH.
+At position 679 to 748, the domain is characterized as S1 motif.
+At position 9 to 41, the domain is characterized as LisH.
+At position 6 to 122, the domain is characterized as C2.
+At position 138 to 739, the domain is characterized as PLA2c.
+At position 9 to 77, the domain is characterized as HTH gntR-type.
+At position 59 to 237, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 175, the domain is characterized as Macro.
+At position 2 to 127, the domain is characterized as ApaG.
+At position 142 to 169, the domain is characterized as PLD phosphodiesterase.
+At position 10 to 142, the domain is characterized as ENTH.
+At position 226 to 245, the domain is characterized as UIM 1.
+At position 254 to 273, the domain is characterized as UIM 2.
+At position 8 to 62, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 1 to 141, the domain is characterized as KARI N-terminal Rossmann.
+At position 142 to 286, the domain is characterized as KARI C-terminal knotted 1.
+At position 287 to 346, the domain is characterized as KARI C-terminal knotted 2.
+At position 56 to 289, the domain is characterized as Peptidase S1.
+At position 11 to 70, the domain is characterized as Myb-like.
+At position 2 to 117, the domain is characterized as MTTase N-terminal.
+At position 140 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 437, the domain is characterized as TRAM.
+At position 158 to 258, the domain is characterized as Rhodanese.
+At position 267 to 348, the domain is characterized as ACT 1.
+At position 349 to 421, the domain is characterized as ACT 2.
+At position 111 to 235, the domain is characterized as Plastocyanin-like.
+At position 1139 to 1372, the domain is characterized as Fibrillar collagen NC1.
+At position 36 to 154, the domain is characterized as Plastocyanin-like 1.
+At position 167 to 311, the domain is characterized as Plastocyanin-like 2.
+At position 379 to 504, the domain is characterized as Plastocyanin-like 3.
+At position 35 to 139, the domain is characterized as Plastocyanin-like.
+At position 59 to 88, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 114 to 145, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 147 to 176, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 174 to 203, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 15 to 57, the domain is characterized as JmjN.
+At position 146 to 309, the domain is characterized as JmjC.
+At position 917 to 974, the domain is characterized as Tudor 1.
+At position 975 to 1031, the domain is characterized as Tudor 2.
+At position 227 to 258, the domain is characterized as EGF-like 1.
+At position 256 to 289, the domain is characterized as EGF-like 2.
+At position 291 to 329, the domain is characterized as EGF-like 3.
+At position 331 to 372, the domain is characterized as EGF-like 4.
+At position 374 to 416, the domain is characterized as EGF-like 5.
+At position 418 to 451, the domain is characterized as EGF-like 6.
+At position 453 to 489, the domain is characterized as EGF-like 7; calcium-binding.
+At position 491 to 527, the domain is characterized as EGF-like 8.
+At position 529 to 565, the domain is characterized as EGF-like 9; calcium-binding.
+At position 426 to 476, the domain is characterized as DHHC.
+At position 93 to 173, the domain is characterized as PRC barrel.
+At position 138 to 452, the domain is characterized as Kinesin motor.
+At position 930 to 1060, the domain is characterized as MGS-like.
+At position 592 to 651, the domain is characterized as KH.
+At position 663 to 732, the domain is characterized as S1 motif.
+At position 19 to 60, the domain is characterized as Chitin-binding type-1.
+At position 213 to 334, the domain is characterized as SET.
+At position 4 to 139, the domain is characterized as ADF-H.
+At position 302 to 332, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 351 to 380, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 87 to 320, the domain is characterized as ABC transmembrane type-1.
+At position 65 to 160, the domain is characterized as PA.
+At position 10 to 99, the domain is characterized as Chorein N-terminal.
+At position 206 to 291, the domain is characterized as RCK C-terminal 1.
+At position 293 to 376, the domain is characterized as RCK C-terminal 2.
+At position 123 to 434, the domain is characterized as IF rod.
+At position 46 to 124, the domain is characterized as RRM 1.
+At position 134 to 211, the domain is characterized as RRM 2.
+At position 225 to 302, the domain is characterized as RRM 3.
+At position 328 to 405, the domain is characterized as RRM 4.
+At position 558 to 635, the domain is characterized as PABC.
+At position 24 to 254, the domain is characterized as Phosphagen kinase C-terminal.
+At position 2 to 143, the domain is characterized as Jacalin-type lectin 1.
+At position 146 to 289, the domain is characterized as Jacalin-type lectin 2.
+At position 297 to 441, the domain is characterized as Jacalin-type lectin 3.
+At position 45 to 180, the domain is characterized as N-acetyltransferase.
+At position 10 to 366, the domain is characterized as YjeF C-terminal.
+At position 299 to 377, the domain is characterized as RRM.
+At position 57 to 317, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 13 to 97, the domain is characterized as GS beta-grasp.
+At position 105 to 469, the domain is characterized as GS catalytic.
+At position 38 to 69, the domain is characterized as EF-hand 2.
+At position 325 to 445, the domain is characterized as P/Homo B.
+At position 824 to 900, the domain is characterized as Carrier.
+At position 71 to 196, the domain is characterized as TBDR plug.
+At position 204 to 1067, the domain is characterized as TBDR beta-barrel.
+At position 54 to 281, the domain is characterized as Radical SAM core.
+At position 35 to 144, the domain is characterized as Ig-like V-type.
+At position 147 to 234, the domain is characterized as Ig-like C2-type 1.
+At position 240 to 327, the domain is characterized as Ig-like C2-type 2.
+At position 335 to 410, the domain is characterized as Ig-like C2-type 3.
+At position 1727 to 1762, the domain is characterized as EF-hand.
+At position 1 to 63, the domain is characterized as LCN-type CS-alpha/beta.
+At position 339 to 410, the domain is characterized as ACT.
+At position 36 to 279, the domain is characterized as ATP-grasp.
+At position 137 to 319, the domain is characterized as Guanylate kinase-like.
+At position 210 to 408, the domain is characterized as Peptidase M12B.
+At position 416 to 502, the domain is characterized as Disintegrin.
+At position 650 to 682, the domain is characterized as EGF-like.
+At position 237 to 257, the domain is characterized as ELK.
+At position 402 to 570, the domain is characterized as tr-type G.
+At position 3 to 126, the domain is characterized as MsrB.
+At position 17 to 101, the domain is characterized as GS beta-grasp.
+At position 109 to 472, the domain is characterized as GS catalytic.
+At position 11 to 126, the domain is characterized as C-type lectin.
+At position 27 to 245, the domain is characterized as Radical SAM core.
+At position 95 to 168, the domain is characterized as PRC barrel.
+At position 148 to 183, the domain is characterized as EF-hand 1.
+At position 193 to 228, the domain is characterized as EF-hand 2.
+At position 432 to 566, the domain is characterized as DAGKc.
+At position 153 to 333, the domain is characterized as CP-type G.
+At position 144 to 367, the domain is characterized as Collagen-like.
+At position 371 to 508, the domain is characterized as C1q.
+At position 31 to 130, the domain is characterized as Ig-like C2-type 1.
+At position 149 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 100 to 154, the domain is characterized as bHLH.
+At position 96 to 173, the domain is characterized as RRM.
+At position 345 to 485, the domain is characterized as KARI C-terminal knotted 2.
+At position 36 to 101, the domain is characterized as NAC-A/B.
+At position 16 to 162, the domain is characterized as Thioredoxin.
+At position 24 to 226, the domain is characterized as HORMA.
+At position 141 to 224, the domain is characterized as PDZ 1.
+At position 280 to 362, the domain is characterized as PDZ 2.
+At position 827 to 910, the domain is characterized as PDZ 3.
+At position 416 to 598, the domain is characterized as JmjC.
+At position 1 to 73, the domain is characterized as Ubiquitin-like.
+At position 188 to 278, the domain is characterized as ARID.
+At position 2 to 231, the domain is characterized as Glutamine amidotransferase type-2.
+At position 158 to 322, the domain is characterized as CheB-type methylesterase.
+At position 9 to 107, the domain is characterized as HTH araC/xylS-type.
+At position 1 to 99, the domain is characterized as FAD-binding FR-type.
+At position 45 to 99, the domain is characterized as EMI.
+At position 103 to 236, the domain is characterized as FAS1 1.
+At position 240 to 371, the domain is characterized as FAS1 2.
+At position 375 to 498, the domain is characterized as FAS1 3.
+At position 502 to 632, the domain is characterized as FAS1 4.
+At position 44 to 81, the domain is characterized as LDL-receptor class A.
+At position 9 to 239, the domain is characterized as ABC transporter.
+At position 192 to 277, the domain is characterized as PPIase FKBP-type.
+At position 27 to 131, the domain is characterized as Gnk2-homologous 1.
+At position 137 to 244, the domain is characterized as Gnk2-homologous 2.
+At position 335 to 612, the domain is characterized as Protein kinase.
+At position 58 to 190, the domain is characterized as RUN.
+At position 112 to 196, the domain is characterized as GST N-terminal.
+At position 205 to 354, the domain is characterized as GST C-terminal.
+At position 22 to 110, the domain is characterized as Ig-like.
+At position 10 to 127, the domain is characterized as PX.
+At position 14 to 49, the domain is characterized as EF-hand 1.
+At position 558 to 620, the domain is characterized as FIP-RBD.
+At position 37 to 165, the domain is characterized as SCP.
+At position 201 to 210, the domain is characterized as ShKT.
+At position 67 to 161, the domain is characterized as Toprim.
+At position 612 to 718, the domain is characterized as tRNA-binding.
+At position 88 to 246, the domain is characterized as CP-type G.
+At position 25 to 294, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 253 to 497, the domain is characterized as ABC transporter 2.
+At position 55 to 140, the domain is characterized as BTB.
+At position 72 to 246, the domain is characterized as Helicase ATP-binding.
+At position 278 to 437, the domain is characterized as Helicase C-terminal.
+At position 207 to 795, the domain is characterized as RINT1/TIP20.
+At position 230 to 349, the domain is characterized as PAZ.
+At position 518 to 820, the domain is characterized as Piwi.
+At position 284 to 351, the domain is characterized as SCA7.
+At position 110 to 267, the domain is characterized as Upf1 CH-rich.
+At position 547 to 611, the domain is characterized as FHA.
+At position 10 to 201, the domain is characterized as tr-type G.
+At position 5 to 130, the domain is characterized as ApaG.
+At position 49 to 263, the domain is characterized as Radical SAM core.
+At position 137 to 356, the domain is characterized as Radical SAM core.
+At position 28 to 316, the domain is characterized as Protein kinase.
+At position 319 to 502, the domain is characterized as PCI.
+At position 53 to 250, the domain is characterized as Peptidase M12A.
+At position 12 to 274, the domain is characterized as Protein kinase.
+At position 14 to 156, the domain is characterized as NAC.
+At position 48 to 236, the domain is characterized as BPL/LPL catalytic.
+At position 281 to 459, the domain is characterized as Helicase ATP-binding.
+At position 614 to 767, the domain is characterized as Helicase C-terminal.
+At position 8 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 358 to 383, the domain is characterized as WW.
+At position 12 to 167, the domain is characterized as N-acetyltransferase.
+At position 253 to 450, the domain is characterized as GATase cobBQ-type.
+At position 90 to 152, the domain is characterized as S4 RNA-binding.
+At position 362 to 481, the domain is characterized as LTD.
+At position 187 to 416, the domain is characterized as Sigma-54 factor interaction.
+At position 215 to 411, the domain is characterized as NR LBD.
+At position 25 to 178, the domain is characterized as Helicase ATP-binding.
+At position 433 to 607, the domain is characterized as Helicase C-terminal.
+At position 623 to 658, the domain is characterized as UVR.
+At position 392 to 560, the domain is characterized as N-acetyltransferase.
+At position 102 to 158, the domain is characterized as J.
+At position 27 to 69, the domain is characterized as CHCH.
+At position 255 to 441, the domain is characterized as GATase cobBQ-type.
+At position 76 to 184, the domain is characterized as FAD-binding FR-type.
+At position 30 to 140, the domain is characterized as GOLD.
+At position 26 to 86, the domain is characterized as HTH tetR-type.
+At position 420 to 457, the domain is characterized as EGF-like.
+At position 513 to 696, the domain is characterized as VWFA.
+At position 11 to 70, the domain is characterized as TRAM.
+At position 10 to 40, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 51 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 26 to 301, the domain is characterized as Protein kinase.
+At position 330 to 356, the domain is characterized as NAF.
+At position 26 to 254, the domain is characterized as Peptidase S1.
+At position 589 to 678, the domain is characterized as BRCT.
+At position 11 to 24, the domain is characterized as CRIB.
+At position 321 to 572, the domain is characterized as Protein kinase.
+At position 305 to 334, the domain is characterized as IQ.
+At position 14 to 76, the domain is characterized as J.
+At position 91 to 160, the domain is characterized as DPH-type MB.
+At position 316 to 534, the domain is characterized as Rap-GAP.
+At position 682 to 758, the domain is characterized as PDZ.
+At position 398 to 574, the domain is characterized as N-acetyltransferase.
+At position 24 to 314, the domain is characterized as FERM.
+At position 1 to 50, the domain is characterized as F-box.
+At position 5 to 274, the domain is characterized as OBG-type G.
+At position 1 to 186, the domain is characterized as N-acetyltransferase.
+At position 182 to 234, the domain is characterized as KH.
+At position 587 to 670, the domain is characterized as BRCT.
+At position 325 to 389, the domain is characterized as MIR 1.
+At position 396 to 454, the domain is characterized as MIR 2.
+At position 466 to 523, the domain is characterized as MIR 3.
+At position 48 to 337, the domain is characterized as ABC transmembrane type-1 1.
+At position 373 to 608, the domain is characterized as ABC transporter 1.
+At position 679 to 971, the domain is characterized as ABC transmembrane type-1 2.
+At position 1006 to 1242, the domain is characterized as ABC transporter 2.
+At position 40 to 96, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 2 to 64, the domain is characterized as LCN-type CS-alpha/beta.
+At position 4 to 241, the domain is characterized as ABC transporter 1.
+At position 258 to 499, the domain is characterized as ABC transporter 2.
+At position 1 to 173, the domain is characterized as tr-type G.
+At position 87 to 251, the domain is characterized as Helicase ATP-binding.
+At position 273 to 445, the domain is characterized as Helicase C-terminal.
+At position 240 to 371, the domain is characterized as GGDEF.
+At position 1398 to 1488, the domain is characterized as PDZ.
+At position 15 to 127, the domain is characterized as FAD-binding FR-type.
+At position 226 to 386, the domain is characterized as TrmE-type G.
+At position 217 to 493, the domain is characterized as Protein kinase.
+At position 2 to 128, the domain is characterized as RNase III.
+At position 152 to 220, the domain is characterized as DRBM.
+At position 7 to 38, the domain is characterized as LisH.
+At position 39 to 82, the domain is characterized as CHCH.
+At position 351 to 429, the domain is characterized as OCT.
+At position 456 to 543, the domain is characterized as Fibronectin type-III 1.
+At position 552 to 639, the domain is characterized as Fibronectin type-III 2.
+At position 638 to 747, the domain is characterized as CBM2.
+At position 29 to 352, the domain is characterized as GH10.
+At position 1 to 47, the domain is characterized as F-box.
+At position 340 to 388, the domain is characterized as FBD.
+At position 111 to 272, the domain is characterized as CP-type G.
+At position 43 to 75, the domain is characterized as ShKT.
+At position 39 to 184, the domain is characterized as N-acetyltransferase.
+At position 22 to 390, the domain is characterized as GH18.
+At position 424 to 473, the domain is characterized as Chitin-binding type-2.
+At position 228 to 415, the domain is characterized as Glutamine amidotransferase type-1.
+At position 371 to 413, the domain is characterized as EGF-like.
+At position 134 to 176, the domain is characterized as EGF-like 1.
+At position 288 to 329, the domain is characterized as EGF-like 2; calcium-binding.
+At position 5 to 242, the domain is characterized as ABC transporter 1.
+At position 259 to 505, the domain is characterized as ABC transporter 2.
+At position 346 to 408, the domain is characterized as S4 RNA-binding.
+At position 50 to 231, the domain is characterized as Rab-GAP TBC.
+At position 605 to 737, the domain is characterized as B12-binding.
+At position 105 to 299, the domain is characterized as Tyr recombinase.
+At position 33 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 26 to 139, the domain is characterized as Thioredoxin.
+At position 293 to 354, the domain is characterized as SH3.
+At position 5 to 149, the domain is characterized as RNase H type-1.
+At position 67 to 102, the domain is characterized as EF-hand 2.
+At position 104 to 139, the domain is characterized as EF-hand 3.
+At position 148 to 183, the domain is characterized as EF-hand 4.
+At position 3 to 104, the domain is characterized as FAD-binding FR-type.
+At position 296 to 537, the domain is characterized as Glutamine amidotransferase type-1.
+At position 93 to 264, the domain is characterized as Helicase ATP-binding.
+At position 299 to 448, the domain is characterized as Helicase C-terminal.
+At position 230 to 394, the domain is characterized as TrmE-type G.
+At position 249 to 341, the domain is characterized as ARID.
+At position 473 to 558, the domain is characterized as REKLES.
+At position 5 to 146, the domain is characterized as TIR.
+At position 170 to 421, the domain is characterized as NB-ARC.
+At position 158 to 372, the domain is characterized as NB-ARC.
+At position 2 to 152, the domain is characterized as F5/8 type C.
+At position 10 to 89, the domain is characterized as Ubiquitin-like.
+At position 2 to 160, the domain is characterized as Thioredoxin.
+At position 378 to 441, the domain is characterized as SAM.
+At position 529 to 799, the domain is characterized as Protein kinase.
+At position 23 to 203, the domain is characterized as Helicase ATP-binding.
+At position 368 to 531, the domain is characterized as Helicase C-terminal.
+At position 561 to 655, the domain is characterized as Dicer dsRNA-binding fold.
+At position 914 to 1052, the domain is characterized as RNase III 1.
+At position 1092 to 1275, the domain is characterized as RNase III 2.
+At position 707 to 793, the domain is characterized as Ubiquitin-like.
+At position 162 to 254, the domain is characterized as 5'-3' exonuclease.
+At position 1 to 122, the domain is characterized as C2 1.
+At position 130 to 248, the domain is characterized as C2 2.
+At position 289 to 507, the domain is characterized as VWFA.
+At position 51 to 236, the domain is characterized as BPL/LPL catalytic.
+At position 182 to 355, the domain is characterized as EngA-type G 2.
+At position 19 to 150, the domain is characterized as Galectin 1.
+At position 198 to 326, the domain is characterized as Galectin 2.
+At position 2 to 81, the domain is characterized as GST N-terminal.
+At position 83 to 204, the domain is characterized as GST C-terminal.
+At position 26 to 125, the domain is characterized as Ig-like V-type.
+At position 126 to 203, the domain is characterized as Ig-like C2-type 1.
+At position 204 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 318 to 374, the domain is characterized as Ig-like C2-type 3.
+At position 127 to 434, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 104 to 254, the domain is characterized as Flavodoxin-like.
+At position 307 to 554, the domain is characterized as FAD-binding FR-type.
+At position 2 to 76, the domain is characterized as Sm.
+At position 12 to 49, the domain is characterized as RIIa.
+At position 172 to 391, the domain is characterized as ATP-grasp.
+At position 10 to 262, the domain is characterized as Pyruvate carboxyltransferase.
+At position 146 to 241, the domain is characterized as PpiC.
+At position 10 to 285, the domain is characterized as Deacetylase sirtuin-type.
+At position 1 to 58, the domain is characterized as HTH myb-type.
+At position 59 to 104, the domain is characterized as Myb-like.
+At position 816 to 1096, the domain is characterized as Protein kinase.
+At position 452 to 594, the domain is characterized as SIS 2.
+At position 4 to 78, the domain is characterized as ACT.
+At position 21 to 375, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 30 to 294, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 299 to 694, the domain is characterized as GH16.
+At position 18 to 141, the domain is characterized as CUB 1.
+At position 142 to 190, the domain is characterized as EGF-like; calcium-binding.
+At position 193 to 305, the domain is characterized as CUB 2.
+At position 307 to 373, the domain is characterized as Sushi 1.
+At position 374 to 449, the domain is characterized as Sushi 2.
+At position 464 to 702, the domain is characterized as Peptidase S1.
+At position 13 to 249, the domain is characterized as ABC transporter 1.
+At position 260 to 503, the domain is characterized as ABC transporter 2.
+At position 37 to 155, the domain is characterized as SCP.
+At position 41 to 118, the domain is characterized as Sm.
+At position 620 to 698, the domain is characterized as BRCT.
+At position 19 to 129, the domain is characterized as MTTase N-terminal.
+At position 149 to 392, the domain is characterized as Radical SAM core.
+At position 395 to 468, the domain is characterized as TRAM.
+At position 23 to 106, the domain is characterized as Ig-like C2-type.
+At position 233 to 324, the domain is characterized as Fibronectin type-III.
+At position 8 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 379 to 548, the domain is characterized as tr-type G.
+At position 401 to 559, the domain is characterized as SSD.
+At position 29 to 298, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 2 to 184, the domain is characterized as Glutamine amidotransferase type-2.
+At position 285 to 601, the domain is characterized as Asparagine synthetase.
+At position 78 to 179, the domain is characterized as Fe2OG dioxygenase.
+At position 86 to 777, the domain is characterized as Myosin motor.
+At position 780 to 809, the domain is characterized as IQ.
+At position 4 to 47, the domain is characterized as JmjN.
+At position 381 to 549, the domain is characterized as JmjC.
+At position 13 to 222, the domain is characterized as Lon N-terminal.
+At position 655 to 841, the domain is characterized as Lon proteolytic.
+At position 18 to 114, the domain is characterized as Ig-like V-type.
+At position 118 to 210, the domain is characterized as Ig-like C2-type.
+At position 31 to 271, the domain is characterized as Helicase ATP-binding.
+At position 35 to 355, the domain is characterized as FERM.
+At position 422 to 680, the domain is characterized as Protein kinase.
+At position 26 to 115, the domain is characterized as SUEL-type lectin.
+At position 704 to 751, the domain is characterized as GPS.
+At position 1 to 95, the domain is characterized as FAD-binding FR-type.
+At position 22 to 212, the domain is characterized as RNase H type-2.
+At position 24 to 447, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 914 to 1198, the domain is characterized as PKS/mFAS DH.
+At position 2040 to 2126, the domain is characterized as Carrier.
+At position 17 to 195, the domain is characterized as Guanylate kinase-like.
+At position 160 to 331, the domain is characterized as OBG-type G.
+At position 33 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 224, the domain is characterized as Ig-like C2-type 2.
+At position 232 to 314, the domain is characterized as Ig-like C2-type 3.
+At position 321 to 411, the domain is characterized as Fibronectin type-III 1.
+At position 416 to 510, the domain is characterized as Fibronectin type-III 2.
+At position 514 to 603, the domain is characterized as Fibronectin type-III 3.
+At position 608 to 705, the domain is characterized as Fibronectin type-III 4.
+At position 710 to 809, the domain is characterized as Fibronectin type-III 5.
+At position 810 to 906, the domain is characterized as Fibronectin type-III 6.
+At position 907 to 1008, the domain is characterized as Fibronectin type-III 7.
+At position 1011 to 1095, the domain is characterized as Fibronectin type-III 8.
+At position 1352 to 1607, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1639 to 1898, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 76 to 145, the domain is characterized as POTRA.
+At position 118 to 380, the domain is characterized as Deacetylase sirtuin-type.
+At position 16 to 49, the domain is characterized as WW 1.
+At position 57 to 90, the domain is characterized as WW 2.
+At position 102 to 270, the domain is characterized as Helicase ATP-binding.
+At position 281 to 459, the domain is characterized as Helicase C-terminal.
+At position 14 to 126, the domain is characterized as PX.
+At position 88 to 481, the domain is characterized as Protein kinase.
+At position 549 to 568, the domain is characterized as WH2.
+At position 4 to 121, the domain is characterized as Response regulatory.
+At position 161 to 356, the domain is characterized as CheB-type methylesterase.
+At position 33 to 196, the domain is characterized as Helicase ATP-binding.
+At position 229 to 435, the domain is characterized as Helicase C-terminal.
+At position 337 to 408, the domain is characterized as Ubiquitin-like.
+At position 18 to 87, the domain is characterized as S4 RNA-binding.
+At position 27 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 90 to 236, the domain is characterized as Nudix hydrolase.
+At position 270 to 346, the domain is characterized as B5.
+At position 1 to 309, the domain is characterized as Hcy-binding.
+At position 340 to 599, the domain is characterized as Pterin-binding.
+At position 629 to 722, the domain is characterized as B12-binding N-terminal.
+At position 724 to 859, the domain is characterized as B12-binding.
+At position 896 to 1195, the domain is characterized as AdoMet activation.
+At position 313 to 363, the domain is characterized as DHHC.
+At position 2 to 49, the domain is characterized as F-box.
+At position 356 to 444, the domain is characterized as Ig-like C2-type 1.
+At position 498 to 586, the domain is characterized as Ig-like C2-type 2.
+At position 594 to 686, the domain is characterized as Fibronectin type-III.
+At position 725 to 980, the domain is characterized as Protein kinase.
+At position 1069 to 1158, the domain is characterized as Ig-like C2-type 3.
+At position 55 to 135, the domain is characterized as GS beta-grasp.
+At position 142 to 403, the domain is characterized as GS catalytic.
+At position 794 to 948, the domain is characterized as JmjC.
+At position 428 to 481, the domain is characterized as PAP-associated.
+At position 173 to 259, the domain is characterized as RRM 1.
+At position 262 to 341, the domain is characterized as RRM 2.
+At position 96 to 158, the domain is characterized as S4 RNA-binding.
+At position 154 to 367, the domain is characterized as Histidine kinase.
+At position 69 to 281, the domain is characterized as Rab-GAP TBC.
+At position 77 to 112, the domain is characterized as EF-hand 1.
+At position 113 to 148, the domain is characterized as EF-hand 2.
+At position 1 to 173, the domain is characterized as Macro.
+At position 51 to 253, the domain is characterized as ABC transmembrane type-1.
+At position 106 to 234, the domain is characterized as Nudix hydrolase.
+At position 518 to 819, the domain is characterized as Piwi.
+At position 367 to 556, the domain is characterized as PID.
+At position 569 to 654, the domain is characterized as PDZ 1.
+At position 660 to 736, the domain is characterized as PDZ 2.
+At position 45 to 75, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 91 to 120, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 4 to 99, the domain is characterized as Rieske.
+At position 649 to 718, the domain is characterized as S1 motif.
+At position 21 to 116, the domain is characterized as Ig-like.
+At position 98 to 160, the domain is characterized as S4 RNA-binding.
+At position 44 to 139, the domain is characterized as CTCK.
+At position 222 to 295, the domain is characterized as RRM.
+At position 33 to 288, the domain is characterized as GB1/RHD3-type G.
+At position 4 to 205, the domain is characterized as ABC transporter.
+At position 161 to 212, the domain is characterized as bHLH.
+At position 120 to 339, the domain is characterized as Radical SAM core.
+At position 303 to 343, the domain is characterized as UBA.
+At position 45 to 156, the domain is characterized as THUMP.
+At position 175 to 219, the domain is characterized as LysM.
+At position 241 to 378, the domain is characterized as Peptidase C51.
+At position 46 to 109, the domain is characterized as BTB.
+At position 4 to 164, the domain is characterized as Thioredoxin.
+At position 17 to 130, the domain is characterized as Pru.
+At position 278 to 390, the domain is characterized as DEUBAD.
+At position 290 to 542, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 132, the domain is characterized as CMP/dCMP-type deaminase.
+At position 141 to 424, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 11 to 73, the domain is characterized as LIM zinc-binding 1.
+At position 75 to 137, the domain is characterized as LIM zinc-binding 2.
+At position 96 to 227, the domain is characterized as Fe2OG dioxygenase.
+At position 3 to 239, the domain is characterized as ABC transporter 1.
+At position 238 to 492, the domain is characterized as ABC transporter 2.
+At position 88 to 181, the domain is characterized as Rieske.
+At position 126 to 375, the domain is characterized as Radical SAM core.
+At position 432 to 594, the domain is characterized as Helicase C-terminal.
+At position 624 to 659, the domain is characterized as UVR.
+At position 3 to 263, the domain is characterized as Protein kinase.
+At position 289 to 515, the domain is characterized as TLDc.
+At position 322 to 385, the domain is characterized as bZIP.
+At position 19 to 207, the domain is characterized as RNase H type-2.
+At position 151 to 250, the domain is characterized as PB1.
+At position 35 to 107, the domain is characterized as KRAB.
+At position 4 to 173, the domain is characterized as Thioredoxin.
+At position 166 to 245, the domain is characterized as PPIase FKBP-type.
+At position 47 to 167, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 186 to 296, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 53 to 282, the domain is characterized as Radical SAM core.
+At position 16 to 172, the domain is characterized as CheW-like.
+At position 193 to 313, the domain is characterized as Response regulatory.
+At position 29 to 149, the domain is characterized as MTTase N-terminal.
+At position 172 to 401, the domain is characterized as Radical SAM core.
+At position 404 to 474, the domain is characterized as TRAM.
+At position 73 to 248, the domain is characterized as FAD-binding PCMH-type.
+At position 136 to 197, the domain is characterized as HTH luxR-type.
+At position 25 to 114, the domain is characterized as Ig-like C1-type.
+At position 1 to 103, the domain is characterized as C2.
+At position 1 to 109, the domain is characterized as C2.
+At position 236 to 269, the domain is characterized as WW 1.
+At position 306 to 339, the domain is characterized as WW 2.
+At position 364 to 397, the domain is characterized as WW 3.
+At position 453 to 786, the domain is characterized as HECT.
+At position 120 to 294, the domain is characterized as CRAL-TRIO.
+At position 51 to 133, the domain is characterized as SCAN box.
+At position 43 to 209, the domain is characterized as Protein kinase.
+At position 12 to 127, the domain is characterized as Response regulatory.
+At position 195 to 254, the domain is characterized as HTH myb-type.
+At position 39 to 220, the domain is characterized as tr-type G.
+At position 52 to 308, the domain is characterized as Protein kinase.
+At position 10 to 114, the domain is characterized as Longin.
+At position 130 to 190, the domain is characterized as v-SNARE coiled-coil homology.
+At position 105 to 301, the domain is characterized as ATP-grasp.
+At position 224 to 371, the domain is characterized as TrmE-type G.
+At position 930 to 1070, the domain is characterized as MGS-like.
+At position 389 to 662, the domain is characterized as Protein kinase.
+At position 663 to 734, the domain is characterized as AGC-kinase C-terminal.
+At position 966 to 1054, the domain is characterized as PDZ.
+At position 57 to 189, the domain is characterized as RUN.
+At position 111 to 287, the domain is characterized as Helicase ATP-binding.
+At position 318 to 467, the domain is characterized as Helicase C-terminal.
+At position 221 to 408, the domain is characterized as FAD-binding PCMH-type.
+At position 518 to 725, the domain is characterized as MCM.
+At position 364 to 468, the domain is characterized as tRNA-binding.
+At position 695 to 971, the domain is characterized as Protein kinase.
+At position 450 to 621, the domain is characterized as tr-type G.
+At position 18 to 248, the domain is characterized as ABC transporter.
+At position 4 to 61, the domain is characterized as HTH lysR-type.
+At position 272 to 299, the domain is characterized as PLD phosphodiesterase 1.
+At position 492 to 518, the domain is characterized as PLD phosphodiesterase 2.
+At position 453 to 525, the domain is characterized as ACT.
+At position 118 to 256, the domain is characterized as DDE Tnp4.
+At position 10 to 61, the domain is characterized as LIM zinc-binding 1.
+At position 120 to 171, the domain is characterized as LIM zinc-binding 2.
+At position 208 to 271, the domain is characterized as KH.
+At position 334 to 427, the domain is characterized as HD.
+At position 32 to 187, the domain is characterized as Helicase ATP-binding.
+At position 29 to 170, the domain is characterized as GAF.
+At position 203 to 432, the domain is characterized as Sigma-54 factor interaction.
+At position 182 to 368, the domain is characterized as Glutamine amidotransferase type-1.
+At position 171 to 347, the domain is characterized as Helicase ATP-binding.
+At position 361 to 531, the domain is characterized as Helicase C-terminal.
+At position 3 to 49, the domain is characterized as F-box.
+At position 321 to 383, the domain is characterized as t-SNARE coiled-coil homology.
+At position 22 to 96, the domain is characterized as S1-like.
+At position 240 to 463, the domain is characterized as Helicase ATP-binding.
+At position 510 to 666, the domain is characterized as Helicase C-terminal.
+At position 91 to 154, the domain is characterized as S4 RNA-binding.
+At position 1 to 104, the domain is characterized as PTS EIIB type-2.
+At position 3 to 200, the domain is characterized as DPCK.
+At position 42 to 86, the domain is characterized as Gla.
+At position 87 to 123, the domain is characterized as EGF-like 1; calcium-binding.
+At position 128 to 169, the domain is characterized as EGF-like 2.
+At position 194 to 433, the domain is characterized as Peptidase S1.
+At position 26 to 89, the domain is characterized as BTB.
+At position 5 to 64, the domain is characterized as CHORD 1.
+At position 157 to 216, the domain is characterized as CHORD 2.
+At position 227 to 316, the domain is characterized as CS.
+At position 87 to 130, the domain is characterized as JmjN.
+At position 223 to 388, the domain is characterized as JmjC.
+At position 8 to 629, the domain is characterized as PFL.
+At position 645 to 774, the domain is characterized as Glycine radical.
+At position 17 to 231, the domain is characterized as UmuC.
+At position 44 to 246, the domain is characterized as TLC.
+At position 1 to 50, the domain is characterized as ClpX-type ZB.
+At position 1 to 60, the domain is characterized as HTH myb-type 1.
+At position 63 to 110, the domain is characterized as HTH myb-type 2.
+At position 216 to 339, the domain is characterized as OTU.
+At position 446 to 491, the domain is characterized as UBA.
+At position 17 to 198, the domain is characterized as tr-type G.
+At position 33 to 257, the domain is characterized as Peptidase S1.
+At position 5 to 222, the domain is characterized as Radical SAM core.
+At position 330 to 536, the domain is characterized as PCI.
+At position 10 to 190, the domain is characterized as Guanylate kinase-like.
+At position 29 to 66, the domain is characterized as Chitin-binding type-1.
+At position 83 to 302, the domain is characterized as Radical SAM core.
+At position 191 to 697, the domain is characterized as Peptidase S8.
+At position 17 to 241, the domain is characterized as AB hydrolase-1.
+At position 4 to 181, the domain is characterized as Guanylate kinase-like.
+At position 2 to 131, the domain is characterized as HTH rrf2-type.
+At position 137 to 239, the domain is characterized as HTH LytTR-type.
+At position 4 to 454, the domain is characterized as Hexokinase.
+At position 836 to 902, the domain is characterized as SAM 1.
+At position 951 to 1015, the domain is characterized as SAM 2.
+At position 1039 to 1108, the domain is characterized as SAM 3.
+At position 173 to 360, the domain is characterized as Glutamine amidotransferase type-1.
+At position 14 to 89, the domain is characterized as RRM 1.
+At position 111 to 187, the domain is characterized as RRM 2.
+At position 27 to 95, the domain is characterized as Bromo 1.
+At position 255 to 325, the domain is characterized as Bromo 2.
+At position 368 to 486, the domain is characterized as BAH.
+At position 382 to 551, the domain is characterized as tr-type G.
+At position 351 to 488, the domain is characterized as NYN.
+At position 788 to 867, the domain is characterized as RRM.
+At position 872 to 946, the domain is characterized as HTH OST-type 1.
+At position 1000 to 1076, the domain is characterized as HTH OST-type 2.
+At position 1096 to 1170, the domain is characterized as HTH OST-type 3.
+At position 1172 to 1248, the domain is characterized as HTH OST-type 4.
+At position 1256 to 1331, the domain is characterized as HTH OST-type 5.
+At position 1332 to 1407, the domain is characterized as HTH OST-type 6.
+At position 1408 to 1482, the domain is characterized as HTH OST-type 7.
+At position 1483 to 1557, the domain is characterized as HTH OST-type 8.
+At position 293 to 499, the domain is characterized as Peptidase M12B.
+At position 509 to 587, the domain is characterized as Disintegrin.
+At position 588 to 643, the domain is characterized as TSP type-1 1.
+At position 878 to 936, the domain is characterized as TSP type-1 2.
+At position 939 to 997, the domain is characterized as TSP type-1 3.
+At position 998 to 1049, the domain is characterized as TSP type-1 4.
+At position 1052 to 1109, the domain is characterized as TSP type-1 5.
+At position 1110 to 1166, the domain is characterized as TSP type-1 6.
+At position 1182 to 1240, the domain is characterized as TSP type-1 7.
+At position 1241 to 1296, the domain is characterized as TSP type-1 8.
+At position 1328 to 1379, the domain is characterized as TSP type-1 9.
+At position 1382 to 1440, the domain is characterized as TSP type-1 10.
+At position 1441 to 1494, the domain is characterized as TSP type-1 11.
+At position 1497 to 1555, the domain is characterized as TSP type-1 12.
+At position 1556 to 1611, the domain is characterized as TSP type-1 13.
+At position 1612 to 1676, the domain is characterized as TSP type-1 14.
+At position 1677 to 1734, the domain is characterized as TSP type-1 15.
+At position 1735 to 1935, the domain is characterized as GON.
+At position 268 to 359, the domain is characterized as PDZ 1.
+At position 365 to 457, the domain is characterized as PDZ 2.
+At position 54 to 174, the domain is characterized as DOMON.
+At position 559 to 618, the domain is characterized as KH.
+At position 628 to 702, the domain is characterized as S1 motif.
+At position 42 to 241, the domain is characterized as BPL/LPL catalytic.
+At position 29 to 106, the domain is characterized as Inhibitor I9.
+At position 111 to 556, the domain is characterized as Peptidase S8.
+At position 350 to 411, the domain is characterized as PA.
+At position 1257 to 1354, the domain is characterized as SH2.
+At position 11 to 250, the domain is characterized as ABC transporter.
+At position 59 to 165, the domain is characterized as Thioredoxin.
+At position 6 to 150, the domain is characterized as PTS EIIA type-2.
+At position 9 to 237, the domain is characterized as ATP-grasp.
+At position 31 to 109, the domain is characterized as Collagen-like.
+At position 110 to 245, the domain is characterized as C1q.
+At position 76 to 123, the domain is characterized as F-box.
+At position 25 to 169, the domain is characterized as VOC 1.
+At position 201 to 359, the domain is characterized as VOC 2.
+At position 1042 to 1295, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 80, the domain is characterized as HTH OST-type 1.
+At position 122 to 197, the domain is characterized as HTH OST-type 2.
+At position 291 to 365, the domain is characterized as HTH OST-type 3.
+At position 533 to 592, the domain is characterized as Tudor.
+At position 162 to 388, the domain is characterized as NB-ARC.
+At position 1 to 103, the domain is characterized as Core-binding (CB).
+At position 124 to 306, the domain is characterized as Tyr recombinase.
+At position 25 to 279, the domain is characterized as Protein kinase.
+At position 321 to 383, the domain is characterized as NAF.
+At position 29 to 146, the domain is characterized as NERD.
+At position 127 to 375, the domain is characterized as Radical SAM core.
+At position 368 to 537, the domain is characterized as tr-type G.
+At position 122 to 218, the domain is characterized as Rhodanese.
+At position 200 to 400, the domain is characterized as Peptidase M12B.
+At position 408 to 494, the domain is characterized as Disintegrin.
+At position 609 to 641, the domain is characterized as EGF-like.
+At position 266 to 342, the domain is characterized as Peptidase A2.
+At position 436 to 615, the domain is characterized as Reverse transcriptase.
+At position 979 to 1138, the domain is characterized as Integrase catalytic.
+At position 223 to 487, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 109 to 316, the domain is characterized as ATP-grasp.
+At position 55 to 302, the domain is characterized as Radical SAM core.
+At position 88 to 175, the domain is characterized as WGR.
+At position 28 to 359, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 86 to 203, the domain is characterized as SEA.
+At position 214 to 334, the domain is characterized as CUB 1.
+At position 340 to 447, the domain is characterized as CUB 2.
+At position 452 to 487, the domain is characterized as LDL-receptor class A 1.
+At position 487 to 524, the domain is characterized as LDL-receptor class A 2.
+At position 524 to 560, the domain is characterized as LDL-receptor class A 3.
+At position 566 to 603, the domain is characterized as LDL-receptor class A 4.
+At position 615 to 854, the domain is characterized as Peptidase S1.
+At position 222 to 296, the domain is characterized as CVC.
+At position 4 to 108, the domain is characterized as SSB.
+At position 107 to 181, the domain is characterized as S4 RNA-binding.
+At position 336 to 371, the domain is characterized as UVR.
+At position 159 to 330, the domain is characterized as OBG-type G.
+At position 344 to 422, the domain is characterized as OCT.
+At position 9 to 156, the domain is characterized as MGS-like.
+At position 30 to 193, the domain is characterized as Laminin G-like 1.
+At position 203 to 381, the domain is characterized as Laminin G-like 2.
+At position 227 to 385, the domain is characterized as TrmE-type G.
+At position 8 to 82, the domain is characterized as J.
+At position 2 to 118, the domain is characterized as MTTase N-terminal.
+At position 120 to 351, the domain is characterized as Radical SAM core.
+At position 346 to 414, the domain is characterized as TRAM.
+At position 4 to 86, the domain is characterized as Sm.
+At position 122 to 180, the domain is characterized as HTH luxR-type.
+At position 343 to 512, the domain is characterized as tr-type G.
+At position 568 to 628, the domain is characterized as KH.
+At position 638 to 710, the domain is characterized as S1 motif.
+At position 18 to 249, the domain is characterized as BAR.
+At position 290 to 349, the domain is characterized as SH3.
+At position 12 to 205, the domain is characterized as RNase H type-2.
+At position 28 to 137, the domain is characterized as Cadherin 1.
+At position 247 to 354, the domain is characterized as Cadherin 3.
+At position 361 to 465, the domain is characterized as Cadherin 4.
+At position 466 to 576, the domain is characterized as Cadherin 5.
+At position 582 to 697, the domain is characterized as Cadherin 6.
+At position 156 to 378, the domain is characterized as MIF4G.
+At position 3 to 204, the domain is characterized as DPCK.
+At position 53 to 199, the domain is characterized as 6-Cys 1.
+At position 210 to 351, the domain is characterized as 6-Cys 2.
+At position 213 to 351, the domain is characterized as TrmE-type G.
+At position 490 to 606, the domain is characterized as HD.
+At position 730 to 811, the domain is characterized as ACT 1.
+At position 841 to 920, the domain is characterized as ACT 2.
+At position 1 to 154, the domain is characterized as UBC core.
+At position 732 to 908, the domain is characterized as DH.
+At position 920 to 1027, the domain is characterized as PH.
+At position 7 to 146, the domain is characterized as N-acetyltransferase.
+At position 234 to 304, the domain is characterized as S1 motif.
+At position 550 to 713, the domain is characterized as Helicase ATP-binding.
+At position 738 to 911, the domain is characterized as Helicase C-terminal.
+At position 478 to 631, the domain is characterized as FtsK.
+At position 73 to 146, the domain is characterized as U-box.
+At position 53 to 272, the domain is characterized as Radical SAM core.
+At position 4 to 81, the domain is characterized as GST N-terminal.
+At position 83 to 200, the domain is characterized as GST C-terminal.
+At position 19 to 116, the domain is characterized as Yippee.
+At position 23 to 105, the domain is characterized as Toprim.
+At position 377 to 500, the domain is characterized as CMP/dCMP-type deaminase.
+At position 140 to 436, the domain is characterized as ABC transmembrane type-1.
+At position 472 to 706, the domain is characterized as ABC transporter.
+At position 1 to 71, the domain is characterized as SLD.
+At position 223 to 491, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 31 to 105, the domain is characterized as EamA.
+At position 10 to 130, the domain is characterized as C2.
+At position 197 to 230, the domain is characterized as WW 1.
+At position 369 to 402, the domain is characterized as WW 2.
+At position 481 to 514, the domain is characterized as WW 3.
+At position 532 to 565, the domain is characterized as WW 4.
+At position 624 to 958, the domain is characterized as HECT.
+At position 226 to 478, the domain is characterized as Olfactomedin-like.
+At position 697 to 1016, the domain is characterized as Autotransporter.
+At position 105 to 325, the domain is characterized as Radical SAM core.
+At position 234 to 287, the domain is characterized as bHLH.
+At position 563 to 622, the domain is characterized as KH.
+At position 632 to 700, the domain is characterized as S1 motif.
+At position 369 to 405, the domain is characterized as CBM1.
+At position 8 to 70, the domain is characterized as LCN-type CS-alpha/beta.
+At position 16 to 138, the domain is characterized as Ig-like V-type.
+At position 144 to 227, the domain is characterized as Ig-like C2-type 1.
+At position 234 to 326, the domain is characterized as Ig-like C2-type 2.
+At position 73 to 330, the domain is characterized as Protein kinase 1.
+At position 331 to 400, the domain is characterized as AGC-kinase C-terminal.
+At position 426 to 683, the domain is characterized as Protein kinase 2.
+At position 207 to 273, the domain is characterized as KH.
+At position 333 to 426, the domain is characterized as HD.
+At position 34 to 71, the domain is characterized as Myb-like.
+At position 44 to 219, the domain is characterized as PCI.
+At position 817 to 902, the domain is characterized as Fibronectin type-III.
+At position 1183 to 1289, the domain is characterized as CBM20.
+At position 126 to 494, the domain is characterized as Protein kinase.
+At position 2 to 96, the domain is characterized as FAD-binding FR-type.
+At position 43 to 131, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 174 to 204, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 57 to 92, the domain is characterized as EF-hand 2.
+At position 93 to 128, the domain is characterized as EF-hand 3.
+At position 136 to 172, the domain is characterized as EF-hand 4.
+At position 149 to 250, the domain is characterized as tRNA-binding.
+At position 339 to 405, the domain is characterized as S4 RNA-binding.
+At position 27 to 128, the domain is characterized as Ig-like V-type.
+At position 297 to 597, the domain is characterized as ABC transmembrane type-1 1.
+At position 665 to 912, the domain is characterized as ABC transporter 1.
+At position 994 to 1274, the domain is characterized as ABC transmembrane type-1 2.
+At position 1312 to 1546, the domain is characterized as ABC transporter 2.
+At position 31 to 312, the domain is characterized as Pyruvate carboxyltransferase.
+At position 45 to 420, the domain is characterized as GBD/FH3.
+At position 528 to 599, the domain is characterized as FH1.
+At position 600 to 1009, the domain is characterized as FH2.
+At position 1027 to 1058, the domain is characterized as DAD.
+At position 13 to 300, the domain is characterized as Protein kinase.
+At position 394 to 429, the domain is characterized as EF-hand 1.
+At position 430 to 465, the domain is characterized as EF-hand 2.
+At position 472 to 507, the domain is characterized as EF-hand 3.
+At position 9 to 232, the domain is characterized as BAR.
+At position 220 to 397, the domain is characterized as TrmE-type G.
+At position 31 to 189, the domain is characterized as Helicase ATP-binding.
+At position 437 to 599, the domain is characterized as Helicase C-terminal.
+At position 634 to 669, the domain is characterized as UVR.
+At position 28 to 132, the domain is characterized as Calponin-homology (CH).
+At position 33 to 68, the domain is characterized as EF-hand 1.
+At position 69 to 104, the domain is characterized as EF-hand 2.
+At position 299 to 487, the domain is characterized as Helicase ATP-binding.
+At position 631 to 790, the domain is characterized as Helicase C-terminal.
+At position 14 to 226, the domain is characterized as Radical SAM core.
+At position 6 to 202, the domain is characterized as DPCK.
+At position 160 to 330, the domain is characterized as OBG-type G.
+At position 131 to 380, the domain is characterized as Radical SAM core.
+At position 23 to 186, the domain is characterized as GAF 1.
+At position 461 to 598, the domain is characterized as GGDEF 1.
+At position 607 to 861, the domain is characterized as EAL.
+At position 939 to 1080, the domain is characterized as GAF 2.
+At position 1130 to 1266, the domain is characterized as GGDEF 2.
+At position 15 to 122, the domain is characterized as Bro-N.
+At position 223 to 419, the domain is characterized as E2.
+At position 158 to 210, the domain is characterized as HAMP.
+At position 218 to 425, the domain is characterized as Histidine kinase.
+At position 130 to 417, the domain is characterized as Tyr recombinase Flp-type.
+At position 67 to 171, the domain is characterized as AB hydrolase-1.
+At position 21 to 83, the domain is characterized as LCN-type CS-alpha/beta.
+At position 95 to 158, the domain is characterized as S5 DRBM.
+At position 184 to 217, the domain is characterized as WW 1.
+At position 225 to 258, the domain is characterized as WW 2.
+At position 404 to 458, the domain is characterized as FF 1.
+At position 471 to 526, the domain is characterized as FF 2.
+At position 532 to 593, the domain is characterized as FF 3.
+At position 611 to 674, the domain is characterized as FF 4.
+At position 679 to 734, the domain is characterized as FF 5.
+At position 736 to 801, the domain is characterized as FF 6.
+At position 350 to 627, the domain is characterized as Protein kinase.
+At position 96 to 163, the domain is characterized as GRAM.
+At position 372 to 543, the domain is characterized as VASt.
+At position 9 to 52, the domain is characterized as CHCH 1.
+At position 55 to 97, the domain is characterized as CHCH 2.
+At position 1 to 103, the domain is characterized as SSB.
+At position 12 to 253, the domain is characterized as ABC transporter.
+At position 33 to 251, the domain is characterized as Radical SAM core.
+At position 132 to 291, the domain is characterized as Upf1 CH-rich.
+At position 497 to 629, the domain is characterized as Helicase ATP-binding.
+At position 126 to 261, the domain is characterized as BFN.
+At position 291 to 326, the domain is characterized as UVR.
+At position 1 to 163, the domain is characterized as SPX.
+At position 26 to 295, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 82 to 316, the domain is characterized as Ferric oxidoreductase.
+At position 317 to 418, the domain is characterized as FAD-binding FR-type.
+At position 30 to 143, the domain is characterized as Ig-like V-type.
+At position 96 to 168, the domain is characterized as PRC barrel.
+At position 135 to 205, the domain is characterized as PAS.
+At position 203 to 262, the domain is characterized as PAC.
+At position 282 to 497, the domain is characterized as Histidine kinase.
+At position 296 to 566, the domain is characterized as F-BAR.
+At position 788 to 1001, the domain is characterized as Rho-GAP.
+At position 299 to 543, the domain is characterized as Glutamine amidotransferase type-1.
+At position 122 to 228, the domain is characterized as C-type lectin.
+At position 92 to 127, the domain is characterized as EF-hand 1.
+At position 131 to 166, the domain is characterized as EF-hand 2.
+At position 227 to 262, the domain is characterized as EF-hand 3.
+At position 272 to 307, the domain is characterized as EF-hand 4.
+At position 308 to 343, the domain is characterized as EF-hand 5.
+At position 3 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 181 to 233, the domain is characterized as KH.
+At position 39 to 308, the domain is characterized as Protein kinase 1.
+At position 309 to 377, the domain is characterized as AGC-kinase C-terminal.
+At position 416 to 677, the domain is characterized as Protein kinase 2.
+At position 321 to 627, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 232 to 355, the domain is characterized as HD.
+At position 3 to 250, the domain is characterized as F-BAR.
+At position 541 to 808, the domain is characterized as MHD.
+At position 38 to 384, the domain is characterized as G-alpha.
+At position 1096 to 1319, the domain is characterized as MIF4G.
+At position 1539 to 1663, the domain is characterized as MI.
+At position 319 to 453, the domain is characterized as Nudix hydrolase.
+At position 18 to 151, the domain is characterized as MARVEL.
+At position 269 to 351, the domain is characterized as Toprim.
+At position 3 to 75, the domain is characterized as J.
+At position 14 to 60, the domain is characterized as F-box.
+At position 23 to 392, the domain is characterized as GH18.
+At position 448 to 504, the domain is characterized as Chitin-binding type-2.
+At position 335 to 617, the domain is characterized as Protein kinase.
+At position 19 to 147, the domain is characterized as C-type lysozyme.
+At position 329 to 513, the domain is characterized as Helicase ATP-binding.
+At position 549 to 698, the domain is characterized as Helicase C-terminal.
+At position 421 to 644, the domain is characterized as Peptidase S1.
+At position 20 to 133, the domain is characterized as Thioredoxin 1.
+At position 151 to 287, the domain is characterized as Thioredoxin 2.
+At position 1272 to 1436, the domain is characterized as PNPLA.
+At position 847 to 927, the domain is characterized as Carrier.
+At position 35 to 108, the domain is characterized as KRAB.
+At position 7 to 130, the domain is characterized as HIG1.
+At position 44 to 147, the domain is characterized as HTH LytTR-type.
+At position 34 to 100, the domain is characterized as BTB.
+At position 560 to 623, the domain is characterized as bZIP.
+At position 111 to 308, the domain is characterized as ATP-grasp.
+At position 281 to 301, the domain is characterized as ELK.
+At position 34 to 155, the domain is characterized as C-type lectin.
+At position 129 to 366, the domain is characterized as ABC transmembrane type-2.
+At position 605 to 662, the domain is characterized as CBS 1.
+At position 807 to 868, the domain is characterized as CBS 2.
+At position 42 to 367, the domain is characterized as RHD.
+At position 805 to 892, the domain is characterized as Death.
+At position 33 to 100, the domain is characterized as BTB.
+At position 10 to 116, the domain is characterized as Thioredoxin.
+At position 205 to 271, the domain is characterized as J.
+At position 53 to 314, the domain is characterized as Protein kinase.
+At position 212 to 391, the domain is characterized as GAF.
+At position 606 to 677, the domain is characterized as PAS 1.
+At position 740 to 811, the domain is characterized as PAS 2.
+At position 887 to 1110, the domain is characterized as Histidine kinase.
+At position 1 to 239, the domain is characterized as IF rod.
+At position 272 to 389, the domain is characterized as LTD.
+At position 25 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 109 to 199, the domain is characterized as Ig-like C2-type 2.
+At position 251 to 365, the domain is characterized as Ig-like C2-type 3.
+At position 368 to 463, the domain is characterized as Ig-like C2-type 4.
+At position 468 to 558, the domain is characterized as Ig-like C2-type 5.
+At position 692 to 1028, the domain is characterized as Protein kinase; inactive.
+At position 62 to 212, the domain is characterized as Cupin type-1.
+At position 19 to 160, the domain is characterized as Tyrosine-protein phosphatase.
+At position 150 to 371, the domain is characterized as TRUD.
+At position 90 to 303, the domain is characterized as TLC.
+At position 12 to 194, the domain is characterized as Ku.
+At position 18 to 239, the domain is characterized as Peptidase S1.
+At position 24 to 311, the domain is characterized as Protein kinase.
+At position 457 to 518, the domain is characterized as LIM zinc-binding 1.
+At position 522 to 582, the domain is characterized as LIM zinc-binding 2.
+At position 583 to 651, the domain is characterized as LIM zinc-binding 3.
+At position 17 to 206, the domain is characterized as RNase H type-2.
+At position 207 to 271, the domain is characterized as KH.
+At position 251 to 444, the domain is characterized as GATase cobBQ-type.
+At position 155 to 230, the domain is characterized as Sm.
+At position 13 to 100, the domain is characterized as Core-binding (CB).
+At position 122 to 319, the domain is characterized as Tyr recombinase.
+At position 29 to 265, the domain is characterized as ABC transporter.
+At position 280 to 339, the domain is characterized as CBS 1.
+At position 343 to 400, the domain is characterized as CBS 2.
+At position 33 to 68, the domain is characterized as Tify.
+At position 95 to 137, the domain is characterized as CCT.
+At position 334 to 585, the domain is characterized as Protein kinase.
+At position 24 to 95, the domain is characterized as S1 motif.
+At position 1 to 87, the domain is characterized as GST N-terminal.
+At position 89 to 207, the domain is characterized as GST C-terminal.
+At position 133 to 571, the domain is characterized as Urease.
+At position 118 to 279, the domain is characterized as CRAL-TRIO.
+At position 129 to 255, the domain is characterized as MRH.
+At position 117 to 313, the domain is characterized as ATP-grasp.
+At position 302 to 582, the domain is characterized as ABC transmembrane type-1 1.
+At position 614 to 838, the domain is characterized as ABC transporter 1.
+At position 921 to 1205, the domain is characterized as ABC transmembrane type-1 2.
+At position 1242 to 1476, the domain is characterized as ABC transporter 2.
+At position 6 to 112, the domain is characterized as Nudix hydrolase.
+At position 260 to 539, the domain is characterized as Tyrosine-protein phosphatase.
+At position 178 to 346, the domain is characterized as tr-type G.
+At position 1 to 172, the domain is characterized as PRELI/MSF1.
+At position 7 to 316, the domain is characterized as Helicase ATP-binding.
+At position 645 to 741, the domain is characterized as Zinc-hook.
+At position 151 to 215, the domain is characterized as COMM.
+At position 708 to 783, the domain is characterized as Smr.
+At position 8 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 79 to 177, the domain is characterized as Mis18.
+At position 694 to 1064, the domain is characterized as DZF.
+At position 35 to 292, the domain is characterized as Protein kinase.
+At position 293 to 367, the domain is characterized as AGC-kinase C-terminal.
+At position 25 to 197, the domain is characterized as EngB-type G.
+At position 96 to 170, the domain is characterized as PRC barrel.
+At position 3 to 40, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 29 to 154, the domain is characterized as EamA.
+At position 74 to 216, the domain is characterized as MPN.
+At position 180 to 339, the domain is characterized as PCI.
+At position 97 to 405, the domain is characterized as IF rod.
+At position 95 to 157, the domain is characterized as S4 RNA-binding.
+At position 54 to 343, the domain is characterized as ABC transmembrane type-1 1.
+At position 380 to 622, the domain is characterized as ABC transporter 1.
+At position 713 to 996, the domain is characterized as ABC transmembrane type-1 2.
+At position 1043 to 1281, the domain is characterized as ABC transporter 2.
+At position 39 to 263, the domain is characterized as SET.
+At position 7 to 331, the domain is characterized as Protein kinase.
+At position 248 to 364, the domain is characterized as RGS.
+At position 1 to 65, the domain is characterized as RRM.
+At position 278 to 354, the domain is characterized as B5.
+At position 577 to 735, the domain is characterized as JmjC.
+At position 290 to 543, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 71, the domain is characterized as J.
+At position 127 to 221, the domain is characterized as Rhodanese.
+At position 63 to 215, the domain is characterized as Cupin type-1.
+At position 212 to 272, the domain is characterized as KH.
+At position 338 to 431, the domain is characterized as HD.
+At position 12 to 167, the domain is characterized as TIR.
+At position 185 to 406, the domain is characterized as NB-ARC.
+At position 3 to 163, the domain is characterized as UBC core.
+At position 40 to 70, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 101 to 132, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 133 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 70 to 285, the domain is characterized as ABC transmembrane type-1 1.
+At position 413 to 623, the domain is characterized as ABC transmembrane type-1 2.
+At position 171 to 225, the domain is characterized as bHLH.
+At position 16 to 62, the domain is characterized as F-box.
+At position 4 to 244, the domain is characterized as ABC transporter.
+At position 435 to 778, the domain is characterized as PUM-HD.
+At position 573 to 644, the domain is characterized as S1 motif.
+At position 98 to 159, the domain is characterized as S4 RNA-binding.
+At position 45 to 107, the domain is characterized as SH3.
+At position 142 to 377, the domain is characterized as Radical SAM core.
+At position 378 to 444, the domain is characterized as TRAM.
+At position 12 to 69, the domain is characterized as PWWP.
+At position 100 to 390, the domain is characterized as Radical SAM core.
+At position 414 to 565, the domain is characterized as N-acetyltransferase.
+At position 191 to 253, the domain is characterized as t-SNARE coiled-coil homology.
+At position 6 to 86, the domain is characterized as Sm.
+At position 1 to 233, the domain is characterized as ABC transporter.
+At position 714 to 883, the domain is characterized as Helicase C-terminal.
+At position 26 to 294, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 19 to 134, the domain is characterized as DUSP.
+At position 303 to 894, the domain is characterized as USP.
+At position 65 to 99, the domain is characterized as EF-hand 2.
+At position 101 to 136, the domain is characterized as EF-hand 3.
+At position 137 to 172, the domain is characterized as EF-hand 4.
+At position 742 to 821, the domain is characterized as BRCT.
+At position 47 to 163, the domain is characterized as FZ.
+At position 180 to 300, the domain is characterized as NTR.
+At position 65 to 245, the domain is characterized as tr-type G.
+At position 60 to 248, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 358, the domain is characterized as FAE.
+At position 109 to 304, the domain is characterized as ATP-grasp.
+At position 24 to 136, the domain is characterized as Calponin-homology (CH).
+At position 19 to 212, the domain is characterized as Lon N-terminal.
+At position 601 to 782, the domain is characterized as Lon proteolytic.
+At position 58 to 158, the domain is characterized as C-type lectin.
+At position 159 to 195, the domain is characterized as EGF-like.
+At position 198 to 259, the domain is characterized as Sushi 1.
+At position 260 to 321, the domain is characterized as Sushi 2.
+At position 322 to 383, the domain is characterized as Sushi 3.
+At position 384 to 445, the domain is characterized as Sushi 4.
+At position 446 to 507, the domain is characterized as Sushi 5.
+At position 508 to 569, the domain is characterized as Sushi 6.
+At position 578 to 639, the domain is characterized as Sushi 7.
+At position 640 to 701, the domain is characterized as Sushi 8.
+At position 29 to 78, the domain is characterized as FHA 1.
+At position 230 to 279, the domain is characterized as FHA 2.
+At position 319 to 552, the domain is characterized as ABC transporter.
+At position 596 to 810, the domain is characterized as ABC transmembrane type-2.
+At position 100 to 147, the domain is characterized as Fibronectin type-II.
+At position 157 to 195, the domain is characterized as EGF-like 1.
+At position 197 to 237, the domain is characterized as Fibronectin type-I.
+At position 238 to 276, the domain is characterized as EGF-like 2.
+At position 283 to 364, the domain is characterized as Kringle.
+At position 406 to 644, the domain is characterized as Peptidase S1.
+At position 29 to 135, the domain is characterized as Rieske.
+At position 167 to 312, the domain is characterized as MRH.
+At position 231 to 447, the domain is characterized as Helicase ATP-binding.
+At position 487 to 655, the domain is characterized as Helicase C-terminal.
+At position 13 to 259, the domain is characterized as CN hydrolase.
+At position 6 to 226, the domain is characterized as ABC transporter.
+At position 1 to 74, the domain is characterized as TGS.
+At position 159 to 296, the domain is characterized as ADD.
+At position 1581 to 1768, the domain is characterized as Helicase ATP-binding.
+At position 2025 to 2205, the domain is characterized as Helicase C-terminal.
+At position 6 to 186, the domain is characterized as KARI N-terminal Rossmann.
+At position 187 to 332, the domain is characterized as KARI C-terminal knotted.
+At position 366 to 508, the domain is characterized as DOD-type homing endonuclease.
+At position 437 to 609, the domain is characterized as tr-type G.
+At position 50 to 284, the domain is characterized as Radical SAM core.
+At position 423 to 537, the domain is characterized as Toprim.
+At position 50 to 243, the domain is characterized as GH16.
+At position 181 to 339, the domain is characterized as VOC 2.
+At position 13 to 110, the domain is characterized as SWIRM.
+At position 223 to 274, the domain is characterized as SANT.
+At position 10 to 95, the domain is characterized as Acylphosphatase-like.
+At position 251 to 438, the domain is characterized as GATase cobBQ-type.
+At position 109 to 249, the domain is characterized as PA14.
+At position 1 to 299, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 279 to 590, the domain is characterized as UvrD-like helicase C-terminal.
+At position 66 to 246, the domain is characterized as tr-type G.
+At position 1 to 52, the domain is characterized as PCI.
+At position 1 to 60, the domain is characterized as HTH lysR-type.
+At position 1 to 187, the domain is characterized as RNase H type-2.
+At position 205 to 282, the domain is characterized as KH type-2.
+At position 15 to 138, the domain is characterized as Rhodanese.
+At position 158 to 431, the domain is characterized as ABC transporter 1.
+At position 509 to 721, the domain is characterized as ABC transmembrane type-2 1.
+At position 852 to 1104, the domain is characterized as ABC transporter 2.
+At position 1177 to 1391, the domain is characterized as ABC transmembrane type-2 2.
+At position 156 to 331, the domain is characterized as Helicase ATP-binding.
+At position 343 to 508, the domain is characterized as Helicase C-terminal.
+At position 302 to 418, the domain is characterized as PX.
+At position 135 to 311, the domain is characterized as Helicase ATP-binding.
+At position 325 to 495, the domain is characterized as Helicase C-terminal.
+At position 829 to 1171, the domain is characterized as PUM-HD.
+At position 1 to 104, the domain is characterized as Thioredoxin.
+At position 5 to 166, the domain is characterized as UBC core.
+At position 455 to 599, the domain is characterized as SET.
+At position 491 to 617, the domain is characterized as Guanylate cyclase.
+At position 20 to 140, the domain is characterized as Ig-like V-type.
+At position 146 to 229, the domain is characterized as Ig-like C2-type 1.
+At position 236 to 336, the domain is characterized as Ig-like C2-type 2.
+At position 193 to 389, the domain is characterized as Peptidase M12B.
+At position 397 to 478, the domain is characterized as Disintegrin.
+At position 98 to 775, the domain is characterized as Peptidase M13.
+At position 1787 to 1822, the domain is characterized as EF-hand.
+At position 19 to 83, the domain is characterized as KRAB-related.
+At position 6 to 340, the domain is characterized as Kinesin motor.
+At position 26 to 88, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 148 to 210, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 174 to 239, the domain is characterized as HTH luxR-type.
+At position 118 to 169, the domain is characterized as LIM zinc-binding 2.
+At position 181 to 350, the domain is characterized as Helicase ATP-binding.
+At position 94 to 149, the domain is characterized as J.
+At position 22 to 174, the domain is characterized as VOC 1.
+At position 205 to 363, the domain is characterized as VOC 2.
+At position 90 to 165, the domain is characterized as PRC barrel.
+At position 147 to 313, the domain is characterized as Helicase ATP-binding.
+At position 338 to 518, the domain is characterized as Helicase C-terminal.
+At position 142 to 244, the domain is characterized as PpiC.
+At position 2 to 246, the domain is characterized as ABC transporter.
+At position 1108 to 1230, the domain is characterized as CMP/dCMP-type deaminase.
+At position 120 to 356, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 43 to 92, the domain is characterized as HTH crp-type.
+At position 1 to 178, the domain is characterized as Brix.
+At position 31 to 62, the domain is characterized as LRRNT 1.
+At position 310 to 359, the domain is characterized as LRRCT 1.
+At position 387 to 425, the domain is characterized as LRRNT 2.
+At position 675 to 724, the domain is characterized as LRRCT 2.
+At position 50 to 186, the domain is characterized as FAD-binding FR-type.
+At position 161 to 359, the domain is characterized as CP-type G.
+At position 95 to 176, the domain is characterized as S4 RNA-binding.
+At position 256 to 472, the domain is characterized as Histidine kinase.
+At position 23 to 84, the domain is characterized as TRAM.
+At position 108 to 225, the domain is characterized as G.
+At position 14 to 233, the domain is characterized as ABC transporter.
+At position 126 to 396, the domain is characterized as Protein kinase.
+At position 36 to 715, the domain is characterized as Myosin motor.
+At position 719 to 739, the domain is characterized as IQ 1.
+At position 740 to 767, the domain is characterized as IQ 2.
+At position 773 to 963, the domain is characterized as TH1.
+At position 1116 to 1178, the domain is characterized as SH3.
+At position 2 to 62, the domain is characterized as LCN-type CS-alpha/beta.
+At position 80 to 237, the domain is characterized as CP-type G.
+At position 334 to 401, the domain is characterized as SCA7.
+At position 39 to 587, the domain is characterized as PLA2c.
+At position 17 to 348, the domain is characterized as tr-type G.
+At position 10 to 131, the domain is characterized as RGS.
+At position 505 to 586, the domain is characterized as DIX.
+At position 11 to 93, the domain is characterized as HTH IS408-type.
+At position 128 to 317, the domain is characterized as Integrase catalytic.
+At position 311 to 591, the domain is characterized as Radical SAM core.
+At position 19 to 82, the domain is characterized as S5 DRBM.
+At position 81 to 167, the domain is characterized as Toprim.
+At position 6 to 153, the domain is characterized as UBC core.
+At position 2 to 71, the domain is characterized as HTH merR-type.
+At position 66 to 347, the domain is characterized as tr-type G.
+At position 175 to 348, the domain is characterized as EngA-type G 2.
+At position 349 to 433, the domain is characterized as KH-like.
+At position 299 to 425, the domain is characterized as SSD.
+At position 64 to 205, the domain is characterized as Tyrosine-protein phosphatase.
+At position 18 to 58, the domain is characterized as Saposin A-type.
+At position 58 to 140, the domain is characterized as Saposin B-type 1.
+At position 184 to 261, the domain is characterized as Saposin B-type 2.
+At position 277 to 352, the domain is characterized as Saposin B-type 3.
+At position 131 to 353, the domain is characterized as Ras-GAP.
+At position 1273 to 1413, the domain is characterized as VPS9.
+At position 179 to 367, the domain is characterized as CRAL-TRIO.
+At position 2 to 140, the domain is characterized as N-acetyltransferase.
+At position 23 to 220, the domain is characterized as GH16.
+At position 33 to 193, the domain is characterized as PID.
+At position 1 to 118, the domain is characterized as C2.
+At position 355 to 614, the domain is characterized as Protein kinase.
+At position 615 to 683, the domain is characterized as AGC-kinase C-terminal.
+At position 170 to 621, the domain is characterized as PPM-type phosphatase.
+At position 19 to 99, the domain is characterized as GS beta-grasp.
+At position 106 to 357, the domain is characterized as GS catalytic.
+At position 194 to 309, the domain is characterized as SET.
+At position 5 to 200, the domain is characterized as ABC transporter 1.
+At position 292 to 504, the domain is characterized as ABC transporter 2.
+At position 138 to 240, the domain is characterized as Fe2OG dioxygenase.
+At position 295 to 413, the domain is characterized as RGS.
+At position 209 to 353, the domain is characterized as KARI C-terminal knotted 1.
+At position 354 to 486, the domain is characterized as KARI C-terminal knotted 2.
+At position 402 to 424, the domain is characterized as Follistatin-like.
+At position 420 to 481, the domain is characterized as Kazal-like.
+At position 592 to 627, the domain is characterized as EF-hand.
+At position 129 to 250, the domain is characterized as C-type lectin 1.
+At position 264 to 377, the domain is characterized as C-type lectin 2.
+At position 6 to 407, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 69 to 392, the domain is characterized as Peptidase A1.
+At position 7 to 91, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 33 to 69, the domain is characterized as EF-hand 1.
+At position 385 to 554, the domain is characterized as tr-type G.
+At position 194 to 352, the domain is characterized as Tyrosine-protein phosphatase.
+At position 239 to 374, the domain is characterized as TFIIS central.
+At position 36 to 152, the domain is characterized as Plastocyanin-like 1.
+At position 161 to 315, the domain is characterized as Plastocyanin-like 2.
+At position 424 to 566, the domain is characterized as Plastocyanin-like 3.
+At position 13 to 189, the domain is characterized as EngB-type G.
+At position 2 to 61, the domain is characterized as SH3 1.
+At position 106 to 165, the domain is characterized as SH3 2.
+At position 190 to 252, the domain is characterized as SH3 3.
+At position 282 to 376, the domain is characterized as SH2.
+At position 33 to 127, the domain is characterized as Ig-like V-type.
+At position 150 to 225, the domain is characterized as Ig-like C2-type.
+At position 35 to 175, the domain is characterized as Thioredoxin.
+At position 3 to 224, the domain is characterized as Glutamine amidotransferase type-1.
+At position 452 to 769, the domain is characterized as PDEase.
+At position 4 to 286, the domain is characterized as Protein kinase.
+At position 4 to 99, the domain is characterized as SSB.
+At position 31 to 300, the domain is characterized as Dynamin-type G.
+At position 518 to 610, the domain is characterized as GED.
+At position 577 to 652, the domain is characterized as BRCT.
+At position 930 to 1061, the domain is characterized as MGS-like.
+At position 1 to 190, the domain is characterized as N-acetyltransferase.
+At position 528 to 781, the domain is characterized as Ras-GEF.
+At position 1373 to 1521, the domain is characterized as PI-PLC X-box.
+At position 1710 to 1826, the domain is characterized as PI-PLC Y-box.
+At position 1831 to 1956, the domain is characterized as C2.
+At position 1992 to 2094, the domain is characterized as Ras-associating 1.
+At position 2115 to 2218, the domain is characterized as Ras-associating 2.
+At position 172 to 346, the domain is characterized as Helicase ATP-binding.
+At position 503 to 660, the domain is characterized as Helicase C-terminal.
+At position 140 to 245, the domain is characterized as HTH LytTR-type.
+At position 82 to 400, the domain is characterized as Peptidase A1.
+At position 124 to 330, the domain is characterized as ATP-grasp.
+At position 165 to 272, the domain is characterized as Cadherin 1.
+At position 273 to 387, the domain is characterized as Cadherin 2.
+At position 388 to 502, the domain is characterized as Cadherin 3.
+At position 503 to 609, the domain is characterized as Cadherin 4.
+At position 610 to 720, the domain is characterized as Cadherin 5.
+At position 120 to 177, the domain is characterized as L27 1.
+At position 179 to 235, the domain is characterized as L27 2.
+At position 256 to 336, the domain is characterized as PDZ.
+At position 345 to 417, the domain is characterized as SH3.
+At position 479 to 660, the domain is characterized as Guanylate kinase-like.
+At position 223 to 364, the domain is characterized as TrmE-type G.
+At position 65 to 270, the domain is characterized as Laminin G-like.
+At position 316 to 373, the domain is characterized as VWFC.
+At position 379 to 429, the domain is characterized as TSP type-1 1.
+At position 435 to 490, the domain is characterized as TSP type-1 2.
+At position 492 to 547, the domain is characterized as TSP type-1 3.
+At position 547 to 587, the domain is characterized as EGF-like 1.
+At position 646 to 690, the domain is characterized as EGF-like 2.
+At position 958 to 1170, the domain is characterized as TSP C-terminal.
+At position 133 to 168, the domain is characterized as EF-hand 1.
+At position 187 to 204, the domain is characterized as EF-hand 2.
+At position 210 to 245, the domain is characterized as EF-hand 3.
+At position 247 to 279, the domain is characterized as EF-hand 4.
+At position 199 to 299, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 102, the domain is characterized as PTS EIIA type-3.
+At position 80 to 248, the domain is characterized as Helicase ATP-binding.
+At position 416 to 582, the domain is characterized as Helicase C-terminal.
+At position 119 to 254, the domain is characterized as N-acetyltransferase.
+At position 171 to 272, the domain is characterized as PpiC 1.
+At position 282 to 382, the domain is characterized as PpiC 2.
+At position 209 to 269, the domain is characterized as KH.
+At position 63 to 253, the domain is characterized as Brix.
+At position 403 to 661, the domain is characterized as ABC transmembrane type-2.
+At position 14 to 91, the domain is characterized as GIY-YIG.
+At position 196 to 231, the domain is characterized as UVR.
+At position 125 to 311, the domain is characterized as ATP-grasp.
+At position 31 to 73, the domain is characterized as CAP-Gly.
+At position 1 to 58, the domain is characterized as SH3.
+At position 9 to 100, the domain is characterized as HIG1.
+At position 33 to 154, the domain is characterized as FZ.
+At position 232 to 479, the domain is characterized as CN hydrolase.
+At position 176 to 238, the domain is characterized as HAMP.
+At position 253 to 466, the domain is characterized as Histidine kinase.
+At position 429 to 516, the domain is characterized as Rieske.
+At position 190 to 224, the domain is characterized as EF-hand 1.
+At position 226 to 261, the domain is characterized as EF-hand 2.
+At position 10 to 154, the domain is characterized as Nudix hydrolase.
+At position 35 to 291, the domain is characterized as Protein kinase.
+At position 617 to 769, the domain is characterized as Collagen-like.
+At position 56 to 171, the domain is characterized as RGS.
+At position 4 to 36, the domain is characterized as LisH.
+At position 34 to 92, the domain is characterized as CTLH.
+At position 411 to 477, the domain is characterized as Dockerin.
+At position 2 to 184, the domain is characterized as GMPS ATP-PPase.
+At position 242 to 424, the domain is characterized as GATase cobBQ-type.
+At position 125 to 191, the domain is characterized as PQ-loop 1.
+At position 266 to 327, the domain is characterized as PQ-loop 2.
+At position 124 to 191, the domain is characterized as Mop 1.
+At position 196 to 260, the domain is characterized as Mop 2.
+At position 74 to 378, the domain is characterized as Peptidase A1.
+At position 181 to 341, the domain is characterized as Helicase ATP-binding.
+At position 410 to 561, the domain is characterized as Helicase C-terminal.
+At position 19 to 78, the domain is characterized as KH; atypical.
+At position 71 to 296, the domain is characterized as Radical SAM core.
+At position 21 to 136, the domain is characterized as Thioredoxin 1.
+At position 343 to 470, the domain is characterized as Thioredoxin 2.
+At position 147 to 199, the domain is characterized as HAMP.
+At position 243 to 472, the domain is characterized as Methyl-accepting transducer.
+At position 6 to 114, the domain is characterized as HIT.
+At position 1 to 130, the domain is characterized as DAGKc.
+At position 21 to 176, the domain is characterized as PID.
+At position 4 to 105, the domain is characterized as LOB.
+At position 181 to 233, the domain is characterized as HAMP.
+At position 241 to 451, the domain is characterized as Histidine kinase.
+At position 552 to 615, the domain is characterized as KH.
+At position 393 to 473, the domain is characterized as ACT-like 1.
+At position 495 to 566, the domain is characterized as ACT-like 2.
+At position 84 to 342, the domain is characterized as ABC transporter 1.
+At position 411 to 626, the domain is characterized as ABC transporter 2.
+At position 9 to 193, the domain is characterized as Phosphatase tensin-type.
+At position 199 to 337, the domain is characterized as C2 tensin-type.
+At position 829 to 1226, the domain is characterized as FH2.
+At position 90 to 200, the domain is characterized as tRNA-binding.
+At position 296 to 417, the domain is characterized as C2 1.
+At position 428 to 562, the domain is characterized as C2 2.
+At position 109 to 298, the domain is characterized as Tyr recombinase.
+At position 15 to 67, the domain is characterized as HTH myb-type 1.
+At position 68 to 122, the domain is characterized as HTH myb-type 2.
+At position 1 to 53, the domain is characterized as Rubredoxin-like.
+At position 1 to 387, the domain is characterized as SMP-LTD.
+At position 69 to 130, the domain is characterized as LIM zinc-binding 1.
+At position 131 to 193, the domain is characterized as LIM zinc-binding 2.
+At position 184 to 379, the domain is characterized as Peptidase M12B.
+At position 37 to 192, the domain is characterized as SIS.
+At position 32 to 171, the domain is characterized as Nudix hydrolase.
+At position 11 to 62, the domain is characterized as Rubredoxin-like.
+At position 2 to 214, the domain is characterized as Glutamine amidotransferase type-1.
+At position 11 to 108, the domain is characterized as Fibronectin type-III.
+At position 652 to 846, the domain is characterized as FtsK 1.
+At position 997 to 1183, the domain is characterized as FtsK 2.
+At position 498 to 555, the domain is characterized as Kazal-like.
+At position 13 to 110, the domain is characterized as Yippee.
+At position 343 to 954, the domain is characterized as USP.
+At position 707 to 726, the domain is characterized as UIM 1.
+At position 809 to 828, the domain is characterized as UIM 2.
+At position 831 to 850, the domain is characterized as UIM 3.
+At position 674 to 866, the domain is characterized as ATP-grasp 2.
+At position 934 to 1028, the domain is characterized as MGS-like.
+At position 1 to 112, the domain is characterized as Ig-like.
+At position 1 to 42, the domain is characterized as PAS.
+At position 191 to 402, the domain is characterized as PPM-type phosphatase.
+At position 15 to 99, the domain is characterized as GST N-terminal.
+At position 105 to 230, the domain is characterized as GST C-terminal.
+At position 252 to 439, the domain is characterized as GATase cobBQ-type.
+At position 451 to 486, the domain is characterized as EF-hand 1.
+At position 487 to 522, the domain is characterized as EF-hand 2.
+At position 523 to 558, the domain is characterized as EF-hand 3.
+At position 561 to 592, the domain is characterized as EF-hand 4.
+At position 342 to 403, the domain is characterized as S4 RNA-binding.
+At position 91 to 419, the domain is characterized as Asparaginase/glutaminase.
+At position 219 to 382, the domain is characterized as TrmE-type G.
+At position 116 to 166, the domain is characterized as DHHC.
+At position 116 to 275, the domain is characterized as CP-type G.
+At position 333 to 411, the domain is characterized as WWE.
+At position 449 to 657, the domain is characterized as PARP catalytic.
+At position 22 to 72, the domain is characterized as bZIP.
+At position 30 to 221, the domain is characterized as RNase H type-2.
+At position 60 to 335, the domain is characterized as Pyruvate carboxyltransferase.
+At position 148 to 206, the domain is characterized as TCP.
+At position 287 to 304, the domain is characterized as R.
+At position 3 to 108, the domain is characterized as PTS EIIB type-3.
+At position 1 to 127, the domain is characterized as PINc.
+At position 430 to 596, the domain is characterized as Helicase C-terminal.
+At position 44 to 126, the domain is characterized as SCAN box.
+At position 9 to 73, the domain is characterized as LCN-type CS-alpha/beta.
+At position 190 to 294, the domain is characterized as Fe2OG dioxygenase.
+At position 389 to 558, the domain is characterized as tr-type G.
+At position 2 to 238, the domain is characterized as ABC transporter.
+At position 8 to 112, the domain is characterized as PH.
+At position 132 to 237, the domain is characterized as IRS-type PTB.
+At position 511 to 592, the domain is characterized as PB1.
+At position 217 to 531, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 124 to 307, the domain is characterized as MIF4G.
+At position 411 to 527, the domain is characterized as MI.
+At position 1 to 34, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 35 to 77, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 83 to 123, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 124 to 166, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 94 to 251, the domain is characterized as Upf1 CH-rich.
+At position 2 to 262, the domain is characterized as CN hydrolase.
+At position 69 to 147, the domain is characterized as GIY-YIG.
+At position 257 to 292, the domain is characterized as UVR.
+At position 648 to 812, the domain is characterized as MOSC.
+At position 32 to 94, the domain is characterized as BTB.
+At position 4 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 4 to 119, the domain is characterized as Response regulatory.
+At position 35 to 99, the domain is characterized as KH 1.
+At position 138 to 210, the domain is characterized as KH 2.
+At position 311 to 380, the domain is characterized as KH 3.
+At position 394 to 455, the domain is characterized as KH 4.
+At position 535 to 599, the domain is characterized as KH 5.
+At position 59 to 409, the domain is characterized as SAM-dependent MTase C5-type.
+At position 3 to 184, the domain is characterized as KARI N-terminal Rossmann.
+At position 185 to 329, the domain is characterized as KARI C-terminal knotted.
+At position 15 to 75, the domain is characterized as HTH tetR-type.
+At position 373 to 435, the domain is characterized as TRAM.
+At position 58 to 228, the domain is characterized as Helicase ATP-binding.
+At position 239 to 394, the domain is characterized as Helicase C-terminal.
+At position 19 to 256, the domain is characterized as Peptidase S1.
+At position 577 to 671, the domain is characterized as RWP-RK.
+At position 847 to 929, the domain is characterized as PB1.
+At position 1 to 66, the domain is characterized as HMA.
+At position 154 to 223, the domain is characterized as DRBM.
+At position 177 to 353, the domain is characterized as EngA-type G 2.
+At position 162 to 213, the domain is characterized as bHLH.
+At position 61 to 255, the domain is characterized as Helicase ATP-binding.
+At position 314 to 491, the domain is characterized as Helicase C-terminal.
+At position 127 to 175, the domain is characterized as LRRCT.
+At position 175 to 262, the domain is characterized as Ig-like C2-type 1.
+At position 281 to 347, the domain is characterized as Ig-like C2-type 2.
+At position 493 to 763, the domain is characterized as Protein kinase.
+At position 36 to 131, the domain is characterized as CTCK.
+At position 289 to 351, the domain is characterized as Mop.
+At position 6 to 165, the domain is characterized as UBC core.
+At position 190 to 359, the domain is characterized as tr-type G.
+At position 134 to 239, the domain is characterized as Core-binding (CB).
+At position 268 to 445, the domain is characterized as Tyr recombinase.
+At position 30 to 75, the domain is characterized as F-box.
+At position 98 to 213, the domain is characterized as C-type lectin.
+At position 34 to 154, the domain is characterized as Bulb-type lectin.
+At position 293 to 329, the domain is characterized as EGF-like; atypical.
+At position 348 to 428, the domain is characterized as PAN.
+At position 524 to 802, the domain is characterized as Protein kinase.
+At position 587 to 660, the domain is characterized as MIB/HERC2.
+At position 22 to 49, the domain is characterized as LRRNT.
+At position 572 to 621, the domain is characterized as LRRCT.
+At position 48 to 303, the domain is characterized as Obg.
+At position 304 to 476, the domain is characterized as OBG-type G.
+At position 1 to 195, the domain is characterized as RNase H type-2.
+At position 131 to 196, the domain is characterized as HTH luxR-type.
+At position 482 to 577, the domain is characterized as BRCT 1.
+At position 598 to 713, the domain is characterized as BRCT 2.
+At position 2 to 44, the domain is characterized as Helicase C-terminal.
+At position 161 to 258, the domain is characterized as HTH araC/xylS-type.
+At position 36 to 115, the domain is characterized as Inhibitor I9.
+At position 126 to 394, the domain is characterized as Peptidase S8.
+At position 510 to 783, the domain is characterized as Protein kinase.
+At position 196 to 258, the domain is characterized as t-SNARE coiled-coil homology.
+At position 27 to 259, the domain is characterized as Peptidase S1.
+At position 36 to 118, the domain is characterized as Inhibitor I9.
+At position 129 to 400, the domain is characterized as Peptidase S8.
+At position 32 to 74, the domain is characterized as LRRNT.
+At position 536 to 605, the domain is characterized as LRRCT.
+At position 51 to 136, the domain is characterized as PNT.
+At position 356 to 413, the domain is characterized as S4 RNA-binding.
+At position 13 to 200, the domain is characterized as FHA; atypical.
+At position 150 to 178, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 179 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 24 to 512, the domain is characterized as Sema.
+At position 560 to 619, the domain is characterized as KH.
+At position 629 to 698, the domain is characterized as S1 motif.
+At position 131 to 160, the domain is characterized as IQ.
+At position 614 to 690, the domain is characterized as BRCT.
+At position 27 to 209, the domain is characterized as tr-type G.
+At position 250 to 539, the domain is characterized as ABC transmembrane type-1 1.
+At position 575 to 804, the domain is characterized as ABC transporter 1.
+At position 903 to 1189, the domain is characterized as ABC transmembrane type-1 2.
+At position 1226 to 1460, the domain is characterized as ABC transporter 2.
+At position 148 to 192, the domain is characterized as P-type.
+At position 197 to 471, the domain is characterized as ZP.
+At position 334 to 484, the domain is characterized as N-acetyltransferase.
+At position 79 to 253, the domain is characterized as Helicase ATP-binding.
+At position 267 to 439, the domain is characterized as Helicase C-terminal.
+At position 3 to 37, the domain is characterized as SAP.
+At position 191 to 388, the domain is characterized as B30.2/SPRY.
+At position 30 to 84, the domain is characterized as Kazal-like.
+At position 1 to 72, the domain is characterized as MBD.
+At position 2 to 42, the domain is characterized as UBA.
+At position 211 to 293, the domain is characterized as UBX.
+At position 20 to 151, the domain is characterized as VHS.
+At position 260 to 279, the domain is characterized as UIM 1.
+At position 304 to 323, the domain is characterized as UIM 2.
+At position 98 to 171, the domain is characterized as POTRA.
+At position 335 to 526, the domain is characterized as PCI.
+At position 3 to 118, the domain is characterized as Response regulatory.
+At position 153 to 250, the domain is characterized as HTH araC/xylS-type.
+At position 32 to 239, the domain is characterized as MCM.
+At position 4 to 260, the domain is characterized as Protein kinase.
+At position 296 to 502, the domain is characterized as PCI.
+At position 5 to 107, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 125 to 379, the domain is characterized as Protein kinase.
+At position 425 to 460, the domain is characterized as EF-hand 1.
+At position 462 to 495, the domain is characterized as EF-hand 2.
+At position 496 to 531, the domain is characterized as EF-hand 3.
+At position 534 to 568, the domain is characterized as EF-hand 4.
+At position 40 to 230, the domain is characterized as GH11.
+At position 368 to 445, the domain is characterized as ACT.
+At position 62 to 125, the domain is characterized as bZIP.
+At position 224 to 383, the domain is characterized as TrmE-type G.
+At position 97 to 158, the domain is characterized as S4 RNA-binding.
+At position 36 to 494, the domain is characterized as Sema.
+At position 496 to 547, the domain is characterized as PSI.
+At position 572 to 630, the domain is characterized as Ig-like C2-type.
+At position 72 to 139, the domain is characterized as ACT 1.
+At position 262 to 322, the domain is characterized as ACT 2.
+At position 487 to 582, the domain is characterized as Link 3.
+At position 588 to 684, the domain is characterized as Link 4.
+At position 1918 to 2044, the domain is characterized as C-type lectin.
+At position 2047 to 2107, the domain is characterized as Sushi.
+At position 2 to 107, the domain is characterized as Thioredoxin.
+At position 309 to 384, the domain is characterized as PB1.
+At position 573 to 604, the domain is characterized as WW.
+At position 16 to 99, the domain is characterized as RRM 1.
+At position 108 to 188, the domain is characterized as RRM 2.
+At position 405 to 483, the domain is characterized as RRM 3.
+At position 131 to 362, the domain is characterized as Radical SAM core.
+At position 440 to 554, the domain is characterized as Toprim.
+At position 1 to 49, the domain is characterized as F-box.
+At position 32 to 124, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 127 to 267, the domain is characterized as FAD-binding FR-type.
+At position 96 to 148, the domain is characterized as bHLH.
+At position 28 to 137, the domain is characterized as Ig-like V-type.
+At position 1 to 139, the domain is characterized as CID.
+At position 569 to 643, the domain is characterized as RRM.
+At position 225 to 343, the domain is characterized as OmpA-like.
+At position 16 to 81, the domain is characterized as Chitin-binding type R&R.
+At position 6 to 198, the domain is characterized as RNase H type-2.
+At position 519 to 764, the domain is characterized as ABC transporter.
+At position 152 to 254, the domain is characterized as BACK.
+At position 199 to 395, the domain is characterized as Peptidase M12B.
+At position 403 to 488, the domain is characterized as Disintegrin.
+At position 297 to 539, the domain is characterized as Glutamine amidotransferase type-1.
+At position 228 to 498, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 319 to 442, the domain is characterized as GGDEF.
+At position 39 to 144, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 236, the domain is characterized as Ig-like C2-type 2.
+At position 252 to 341, the domain is characterized as Ig-like C2-type 3.
+At position 470 to 578, the domain is characterized as Fibronectin type-III 1.
+At position 4 to 87, the domain is characterized as Plastocyanin-like 1.
+At position 100 to 238, the domain is characterized as Plastocyanin-like 2.
+At position 12 to 217, the domain is characterized as ABC transporter.
+At position 14 to 272, the domain is characterized as Protein kinase.
+At position 77 to 149, the domain is characterized as BTB.
+At position 184 to 286, the domain is characterized as BACK.
+At position 468 to 613, the domain is characterized as Thioredoxin.
+At position 40 to 269, the domain is characterized as Radical SAM core.
+At position 18 to 263, the domain is characterized as Protein kinase.
+At position 36 to 120, the domain is characterized as Inhibitor I9.
+At position 130 to 403, the domain is characterized as Peptidase S8.
+At position 1 to 233, the domain is characterized as Radical SAM core.
+At position 145 to 391, the domain is characterized as ABC transporter.
+At position 484 to 691, the domain is characterized as ABC transmembrane type-2.
+At position 87 to 382, the domain is characterized as HAP1 N-terminal.
+At position 1 to 281, the domain is characterized as Deacetylase sirtuin-type.
+At position 64 to 169, the domain is characterized as CMP/dCMP-type deaminase.
+At position 596 to 674, the domain is characterized as BRCT.
+At position 13 to 157, the domain is characterized as HTH marR-type.
+At position 493 to 529, the domain is characterized as CBM1.
+At position 4 to 94, the domain is characterized as PE.
+At position 1 to 287, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 294 to 542, the domain is characterized as UvrD-like helicase C-terminal.
+At position 378 to 518, the domain is characterized as RanBD1.
+At position 21 to 120, the domain is characterized as Ig-like.
+At position 36 to 204, the domain is characterized as BUB1 N-terminal.
+At position 718 to 1044, the domain is characterized as Protein kinase.
+At position 33 to 106, the domain is characterized as EMI.
+At position 114 to 158, the domain is characterized as WAP.
+At position 264 to 313, the domain is characterized as EGF-like 1; calcium-binding.
+At position 314 to 398, the domain is characterized as Fibronectin type-III 1.
+At position 396 to 510, the domain is characterized as SEA 1.
+At position 507 to 552, the domain is characterized as EGF-like 2; calcium-binding.
+At position 702 to 791, the domain is characterized as Fibronectin type-III 2.
+At position 788 to 900, the domain is characterized as SEA 2.
+At position 897 to 938, the domain is characterized as EGF-like 3; calcium-binding.
+At position 992 to 1235, the domain is characterized as ZP.
+At position 126 to 332, the domain is characterized as Histidine kinase.
+At position 4 to 207, the domain is characterized as ABC transporter.
+At position 276 to 501, the domain is characterized as tr-type G.
+At position 14 to 85, the domain is characterized as PAS 1.
+At position 88 to 140, the domain is characterized as PAC 1.
+At position 141 to 208, the domain is characterized as PAS 2.
+At position 209 to 268, the domain is characterized as PAC 2.
+At position 288 to 503, the domain is characterized as Histidine kinase.
+At position 18 to 92, the domain is characterized as Sm.
+At position 21 to 108, the domain is characterized as UPAR/Ly6.
+At position 102 to 255, the domain is characterized as PID.
+At position 4 to 157, the domain is characterized as UBC core.
+At position 159 to 479, the domain is characterized as Protein kinase.
+At position 122 to 253, the domain is characterized as RCK N-terminal.
+At position 266 to 348, the domain is characterized as RCK C-terminal.
+At position 5 to 284, the domain is characterized as Deacetylase sirtuin-type.
+At position 67 to 106, the domain is characterized as Pentapeptide repeat 1.
+At position 107 to 146, the domain is characterized as Pentapeptide repeat 2.
+At position 162 to 201, the domain is characterized as Pentapeptide repeat 3.
+At position 207 to 246, the domain is characterized as Pentapeptide repeat 4.
+At position 247 to 286, the domain is characterized as Pentapeptide repeat 5.
+At position 62 to 140, the domain is characterized as GIY-YIG.
+At position 250 to 285, the domain is characterized as UVR.
+At position 30 to 96, the domain is characterized as Importin N-terminal.
+At position 26 to 160, the domain is characterized as HTH marR-type.
+At position 280 to 612, the domain is characterized as USP.
+At position 201 to 331, the domain is characterized as CBM21.
+At position 313 to 453, the domain is characterized as C-CAP/cofactor C-like.
+At position 8 to 61, the domain is characterized as HTH cro/C1-type.
+At position 79 to 681, the domain is characterized as Protein kinase.
+At position 120 to 315, the domain is characterized as ATP-grasp.
+At position 639 to 719, the domain is characterized as S1 motif.
+At position 278 to 320, the domain is characterized as CCT.
+At position 85 to 281, the domain is characterized as ABC transmembrane type-1.
+At position 36 to 117, the domain is characterized as Inhibitor I9.
+At position 128 to 395, the domain is characterized as Peptidase S8.
+At position 176 to 369, the domain is characterized as CheB-type methylesterase.
+At position 508 to 773, the domain is characterized as Protein kinase.
+At position 394 to 542, the domain is characterized as Thioredoxin.
+At position 1075 to 1126, the domain is characterized as SANT 1.
+At position 1360 to 1411, the domain is characterized as SANT 2.
+At position 5 to 231, the domain is characterized as Radical SAM core.
+At position 37 to 119, the domain is characterized as RRM 1.
+At position 186 to 274, the domain is characterized as RRM 2.
+At position 6 to 198, the domain is characterized as Thioredoxin.
+At position 36 to 322, the domain is characterized as Protein kinase.
+At position 23 to 318, the domain is characterized as Protein kinase.
+At position 63 to 151, the domain is characterized as PPIase FKBP-type 1.
+At position 175 to 263, the domain is characterized as PPIase FKBP-type 2.
+At position 287 to 375, the domain is characterized as PPIase FKBP-type 3.
+At position 400 to 487, the domain is characterized as PPIase FKBP-type 4.
+At position 498 to 533, the domain is characterized as EF-hand 1.
+At position 543 to 578, the domain is characterized as EF-hand 2.
+At position 1 to 177, the domain is characterized as N-acetyltransferase.
+At position 93 to 167, the domain is characterized as PRC barrel.
+At position 453 to 816, the domain is characterized as USP.
+At position 865 to 1043, the domain is characterized as Exonuclease.
+At position 448 to 506, the domain is characterized as COS.
+At position 513 to 607, the domain is characterized as Fibronectin type-III.
+At position 589 to 780, the domain is characterized as B30.2/SPRY.
+At position 6 to 192, the domain is characterized as Guanylate kinase-like.
+At position 1 to 63, the domain is characterized as L27.
+At position 137 to 224, the domain is characterized as PDZ 1.
+At position 257 to 337, the domain is characterized as PDZ 2.
+At position 377 to 463, the domain is characterized as PDZ 3.
+At position 553 to 634, the domain is characterized as PDZ 4.
+At position 700 to 786, the domain is characterized as PDZ 5.
+At position 1008 to 1089, the domain is characterized as PDZ 6.
+At position 1151 to 1243, the domain is characterized as PDZ 7.
+At position 1350 to 1433, the domain is characterized as PDZ 8.
+At position 1483 to 1564, the domain is characterized as PDZ 9.
+At position 1629 to 1712, the domain is characterized as PDZ 10.
+At position 1725 to 1807, the domain is characterized as PDZ 11.
+At position 1862 to 1948, the domain is characterized as PDZ 12.
+At position 1987 to 2070, the domain is characterized as PDZ 13.
+At position 201 to 309, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 105, the domain is characterized as Rieske.
+At position 72 to 115, the domain is characterized as CWF21.
+At position 478 to 592, the domain is characterized as N-terminal Ras-GEF.
+At position 597 to 679, the domain is characterized as PDZ.
+At position 782 to 869, the domain is characterized as Ras-associating.
+At position 894 to 1124, the domain is characterized as Ras-GEF.
+At position 296 to 597, the domain is characterized as Helicase ATP-binding.
+At position 887 to 1042, the domain is characterized as Helicase C-terminal.
+At position 102 to 342, the domain is characterized as Radical SAM core.
+At position 34 to 134, the domain is characterized as Fibronectin type-III 1.
+At position 139 to 235, the domain is characterized as Fibronectin type-III 2.
+At position 240 to 333, the domain is characterized as Fibronectin type-III 3.
+At position 1 to 134, the domain is characterized as C-type lectin.
+At position 465 to 508, the domain is characterized as CUE.
+At position 93 to 149, the domain is characterized as CBS 1.
+At position 153 to 214, the domain is characterized as CBS 2.
+At position 24 to 87, the domain is characterized as S5 DRBM.
+At position 37 to 214, the domain is characterized as EngB-type G.
+At position 47 to 128, the domain is characterized as RRM.
+At position 172 to 198, the domain is characterized as DAZ.
+At position 80 to 255, the domain is characterized as Helicase ATP-binding.
+At position 267 to 428, the domain is characterized as Helicase C-terminal.
+At position 15 to 458, the domain is characterized as SAM-dependent MTase C5-type.
+At position 134 to 192, the domain is characterized as HTH cro/C1-type.
+At position 271 to 329, the domain is characterized as COS.
+At position 32 to 138, the domain is characterized as Ig-like V-type.
+At position 150 to 248, the domain is characterized as Ig-like C1-type 1.
+At position 255 to 349, the domain is characterized as Ig-like C1-type 2.
+At position 23 to 117, the domain is characterized as PH.
+At position 389 to 618, the domain is characterized as START.
+At position 71 to 218, the domain is characterized as MPN.
+At position 3 to 81, the domain is characterized as DED.
+At position 97 to 181, the domain is characterized as Death.
+At position 516 to 588, the domain is characterized as ACT.
+At position 123 to 154, the domain is characterized as EF-hand 4.
+At position 37 to 99, the domain is characterized as S4 RNA-binding.
+At position 1 to 100, the domain is characterized as WH1.
+At position 137 to 458, the domain is characterized as PDEase.
+At position 145 to 242, the domain is characterized as HTH araC/xylS-type.
+At position 93 to 169, the domain is characterized as WWE.
+At position 67 to 211, the domain is characterized as SCP.
+At position 329 to 375, the domain is characterized as F-box.
+At position 143 to 334, the domain is characterized as Rho-GAP.
+At position 594 to 673, the domain is characterized as BRCT.
+At position 4 to 54, the domain is characterized as LIM zinc-binding 1.
+At position 63 to 117, the domain is characterized as LIM zinc-binding 2.
+At position 172 to 249, the domain is characterized as RRM.
+At position 2 to 184, the domain is characterized as Tyr recombinase.
+At position 4 to 88, the domain is characterized as YcgL.
+At position 353 to 406, the domain is characterized as HAMP 1.
+At position 434 to 486, the domain is characterized as HAMP 2.
+At position 491 to 720, the domain is characterized as Methyl-accepting transducer.
+At position 3 to 347, the domain is characterized as Kinesin motor.
+At position 1460 to 1558, the domain is characterized as PH.
+At position 86 to 207, the domain is characterized as GST C-terminal.
+At position 47 to 125, the domain is characterized as RRM 1.
+At position 135 to 211, the domain is characterized as RRM 2.
+At position 227 to 304, the domain is characterized as RRM 3.
+At position 330 to 407, the domain is characterized as RRM 4.
+At position 555 to 632, the domain is characterized as PABC.
+At position 16 to 74, the domain is characterized as HTH lysR-type.
+At position 67 to 280, the domain is characterized as ABC transmembrane type-1.
+At position 45 to 107, the domain is characterized as t-SNARE coiled-coil homology.
+At position 414 to 473, the domain is characterized as SH3.
+At position 371 to 549, the domain is characterized as Helicase ATP-binding.
+At position 560 to 721, the domain is characterized as Helicase C-terminal.
+At position 11 to 126, the domain is characterized as MTTase N-terminal.
+At position 147 to 388, the domain is characterized as Radical SAM core.
+At position 391 to 463, the domain is characterized as TRAM.
+At position 59 to 159, the domain is characterized as RRM.
+At position 300 to 353, the domain is characterized as TSP type-1 1.
+At position 355 to 408, the domain is characterized as TSP type-1 2.
+At position 410 to 463, the domain is characterized as TSP type-1 3.
+At position 466 to 519, the domain is characterized as TSP type-1 4.
+At position 865 to 917, the domain is characterized as GPS.
+At position 15 to 193, the domain is characterized as RNase H type-2.
+At position 276 to 318, the domain is characterized as CCT.
+At position 51 to 80, the domain is characterized as HhH.
+At position 100 to 314, the domain is characterized as FtsK.
+At position 2 to 114, the domain is characterized as PLAT.
+At position 114 to 662, the domain is characterized as Lipoxygenase.
+At position 339 to 429, the domain is characterized as FDX-ACB.
+At position 7 to 222, the domain is characterized as Radical SAM core.
+At position 379 to 431, the domain is characterized as bHLH.
+At position 101 to 222, the domain is characterized as MPN.
+At position 24 to 153, the domain is characterized as VHS.
+At position 253 to 272, the domain is characterized as UIM 1.
+At position 294 to 313, the domain is characterized as UIM 2.
+At position 47 to 105, the domain is characterized as Chromo.
+At position 189 to 247, the domain is characterized as Pre-SET.
+At position 250 to 373, the domain is characterized as SET.
+At position 394 to 410, the domain is characterized as Post-SET.
+At position 44 to 146, the domain is characterized as RRM.
+At position 27 to 210, the domain is characterized as BPL/LPL catalytic.
+At position 89 to 157, the domain is characterized as S4 RNA-binding.
+At position 20 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 200 to 325, the domain is characterized as Ig-like C2-type 2.
+At position 565 to 666, the domain is characterized as Ig-like C2-type 3.
+At position 673 to 758, the domain is characterized as Ig-like C2-type 4.
+At position 847 to 1175, the domain is characterized as Protein kinase.
+At position 36 to 319, the domain is characterized as AB hydrolase-1.
+At position 472 to 641, the domain is characterized as tr-type G.
+At position 33 to 159, the domain is characterized as NlpC/P60 1.
+At position 163 to 287, the domain is characterized as NlpC/P60 2.
+At position 291 to 413, the domain is characterized as NlpC/P60 3.
+At position 45 to 294, the domain is characterized as PPM-type phosphatase.
+At position 15 to 124, the domain is characterized as Thioredoxin 1.
+At position 334 to 455, the domain is characterized as Thioredoxin 2.
+At position 90 to 162, the domain is characterized as Bromo 1.
+At position 363 to 435, the domain is characterized as Bromo 2.
+At position 630 to 712, the domain is characterized as NET.
+At position 345 to 387, the domain is characterized as CCT.
+At position 1 to 176, the domain is characterized as SPX.
+At position 441 to 642, the domain is characterized as EXS.
+At position 25 to 133, the domain is characterized as Thioredoxin 1.
+At position 343 to 485, the domain is characterized as Thioredoxin 2.
+At position 37 to 279, the domain is characterized as ABC transporter.
+At position 381 to 644, the domain is characterized as ABC transmembrane type-2.
+At position 74 to 358, the domain is characterized as Protein kinase.
+At position 148 to 222, the domain is characterized as HMA.
+At position 15 to 92, the domain is characterized as GIY-YIG.
+At position 8 to 74, the domain is characterized as TGS.
+At position 29 to 89, the domain is characterized as HTH tetR-type.
+At position 22 to 57, the domain is characterized as EF-hand 1.
+At position 58 to 86, the domain is characterized as EF-hand 2.
+At position 91 to 126, the domain is characterized as EF-hand 3.
+At position 127 to 162, the domain is characterized as EF-hand 4.
+At position 108 to 227, the domain is characterized as C2 1.
+At position 239 to 372, the domain is characterized as C2 2.
+At position 32 to 289, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 336 to 375, the domain is characterized as LIM interaction domain (LID).
+At position 4 to 152, the domain is characterized as UBC core.
+At position 165 to 273, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 145, the domain is characterized as MPN.
+At position 165 to 426, the domain is characterized as CP-type G.
+At position 34 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 10 to 147, the domain is characterized as CheW-like.
+At position 283 to 442, the domain is characterized as FCP1 homology.
+At position 104 to 168, the domain is characterized as S4 RNA-binding.
+At position 479 to 601, the domain is characterized as HD.
+At position 720 to 801, the domain is characterized as ACT 1.
+At position 827 to 904, the domain is characterized as ACT 2.
+At position 393 to 562, the domain is characterized as tr-type G.
+At position 16 to 66, the domain is characterized as CHCH.
+At position 59 to 128, the domain is characterized as S1 motif.
+At position 136 to 194, the domain is characterized as KH.
+At position 44 to 160, the domain is characterized as Cadherin 1.
+At position 161 to 280, the domain is characterized as Cadherin 2.
+At position 5 to 122, the domain is characterized as MTTase N-terminal.
+At position 145 to 378, the domain is characterized as Radical SAM core.
+At position 380 to 442, the domain is characterized as TRAM.
+At position 434 to 612, the domain is characterized as Helicase ATP-binding.
+At position 639 to 790, the domain is characterized as Helicase C-terminal.
+At position 34 to 461, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 945 to 1020, the domain is characterized as Carrier.
+At position 46 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 207, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 320, the domain is characterized as Ig-like C2-type 3.
+At position 328 to 414, the domain is characterized as Ig-like C2-type 4.
+At position 421 to 540, the domain is characterized as Ig-like C2-type 5.
+At position 547 to 654, the domain is characterized as Ig-like C2-type 6.
+At position 663 to 749, the domain is characterized as Ig-like C2-type 7.
+At position 830 to 1158, the domain is characterized as Protein kinase.
+At position 1 to 116, the domain is characterized as Tyrosine-protein phosphatase.
+At position 101 to 189, the domain is characterized as BRCT 1.
+At position 195 to 284, the domain is characterized as BRCT 2.
+At position 353 to 443, the domain is characterized as BRCT 3.
+At position 551 to 636, the domain is characterized as BRCT 4.
+At position 644 to 741, the domain is characterized as BRCT 5.
+At position 902 to 993, the domain is characterized as BRCT 6.
+At position 1255 to 1347, the domain is characterized as BRCT 7.
+At position 175 to 355, the domain is characterized as CNNM transmembrane.
+At position 374 to 435, the domain is characterized as CBS 1.
+At position 442 to 508, the domain is characterized as CBS 2.
+At position 1 to 276, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 273 to 586, the domain is characterized as UvrD-like helicase C-terminal.
+At position 114 to 352, the domain is characterized as Radical SAM core.
+At position 8 to 488, the domain is characterized as Protein kinase.
+At position 81 to 207, the domain is characterized as GST C-terminal.
+At position 822 to 963, the domain is characterized as Peptidase S59.
+At position 234 to 286, the domain is characterized as PAC.
+At position 287 to 358, the domain is characterized as PAS.
+At position 556 to 908, the domain is characterized as Histidine kinase.
+At position 1551 to 1674, the domain is characterized as Response regulatory.
+At position 41 to 123, the domain is characterized as SCAN box.
+At position 217 to 289, the domain is characterized as KRAB.
+At position 36 to 220, the domain is characterized as SIS.
+At position 5 to 192, the domain is characterized as Josephin.
+At position 231 to 465, the domain is characterized as PABS.
+At position 304 to 443, the domain is characterized as C-CAP/cofactor C-like.
+At position 12 to 275, the domain is characterized as Protein kinase.
+At position 361 to 428, the domain is characterized as PASTA 1.
+At position 430 to 502, the domain is characterized as PASTA 2.
+At position 503 to 574, the domain is characterized as PASTA 3.
+At position 404 to 482, the domain is characterized as RRM 3.
+At position 211 to 298, the domain is characterized as Doublecortin 1.
+At position 340 to 423, the domain is characterized as Doublecortin 2.
+At position 482 to 743, the domain is characterized as Protein kinase.
+At position 35 to 161, the domain is characterized as VIT.
+At position 295 to 478, the domain is characterized as VWFA.
+At position 1 to 248, the domain is characterized as KaiC 1.
+At position 262 to 521, the domain is characterized as KaiC 2.
+At position 989 to 1061, the domain is characterized as Bromo.
+At position 532 to 639, the domain is characterized as CBM20.
+At position 524 to 696, the domain is characterized as tr-type G.
+At position 41 to 86, the domain is characterized as F-box-like.
+At position 2 to 106, the domain is characterized as Thioredoxin.
+At position 28 to 106, the domain is characterized as Ig-like V-type.
+At position 151 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 239 to 322, the domain is characterized as Ig-like C2-type 2.
+At position 325 to 407, the domain is characterized as Ig-like C2-type 3.
+At position 414 to 495, the domain is characterized as Ig-like C2-type 4.
+At position 36 to 195, the domain is characterized as SIS.
+At position 7 to 95, the domain is characterized as GST N-terminal.
+At position 104 to 226, the domain is characterized as GST C-terminal.
+At position 24 to 157, the domain is characterized as ENTH.
+At position 20 to 63, the domain is characterized as SMB 1.
+At position 85 to 128, the domain is characterized as SMB 2.
+At position 138 to 411, the domain is characterized as EndoU.
+At position 213 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 39 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 316 to 503, the domain is characterized as DH.
+At position 500 to 536, the domain is characterized as CBM1.
+At position 53 to 139, the domain is characterized as Phosphagen kinase N-terminal 1.
+At position 166 to 408, the domain is characterized as Phosphagen kinase C-terminal 1.
+At position 426 to 512, the domain is characterized as Phosphagen kinase N-terminal 2.
+At position 539 to 781, the domain is characterized as Phosphagen kinase C-terminal 2.
+At position 800 to 886, the domain is characterized as Phosphagen kinase N-terminal 3.
+At position 913 to 1155, the domain is characterized as Phosphagen kinase C-terminal 3.
+At position 6 to 89, the domain is characterized as PTS EIIA type-2.
+At position 1 to 120, the domain is characterized as OCIA.
+At position 170 to 435, the domain is characterized as MHD.
+At position 95 to 202, the domain is characterized as Calponin-homology (CH) 1.
+At position 262 to 369, the domain is characterized as Calponin-homology (CH) 2.
+At position 1 to 60, the domain is characterized as HTH myb-type.
+At position 113 to 181, the domain is characterized as H15.
+At position 42 to 130, the domain is characterized as PPIase FKBP-type 1.
+At position 157 to 243, the domain is characterized as PPIase FKBP-type 2.
+At position 55 to 107, the domain is characterized as HAMP 1.
+At position 142 to 195, the domain is characterized as HAMP 2.
+At position 214 to 455, the domain is characterized as Methyl-accepting transducer.
+At position 1 to 220, the domain is characterized as Peptidase C83.
+At position 33 to 294, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 10 to 19, the domain is characterized as Peptidase M12B.
+At position 5 to 92, the domain is characterized as GST N-terminal.
+At position 94 to 212, the domain is characterized as GST C-terminal.
+At position 6 to 70, the domain is characterized as S4 RNA-binding.
+At position 23 to 69, the domain is characterized as F-box.
+At position 30 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 814 to 868, the domain is characterized as FHA.
+At position 58 to 307, the domain is characterized as Radical SAM core.
+At position 227 to 383, the domain is characterized as TrmE-type G.
+At position 107 to 300, the domain is characterized as ATP-grasp.
+At position 21 to 105, the domain is characterized as UPAR/Ly6.
+At position 404 to 483, the domain is characterized as Rhodanese.
+At position 4 to 242, the domain is characterized as ABC transporter.
+At position 8 to 152, the domain is characterized as PTS EIIA type-2.
+At position 288 to 357, the domain is characterized as Plastocyanin-like.
+At position 6 to 99, the domain is characterized as Ig-like.
+At position 1 to 158, the domain is characterized as Thioredoxin 1.
+At position 171 to 315, the domain is characterized as Thioredoxin 2.
+At position 321 to 488, the domain is characterized as Thioredoxin 3.
+At position 187 to 296, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 30 to 93, the domain is characterized as S5 DRBM.
+At position 88 to 193, the domain is characterized as Bulb-type lectin.
+At position 276 to 354, the domain is characterized as RRM 3.
+At position 32 to 268, the domain is characterized as Peptidase S1.
+At position 22 to 86, the domain is characterized as Sushi 1.
+At position 87 to 146, the domain is characterized as Sushi 2.
+At position 149 to 206, the domain is characterized as Sushi 3.
+At position 254 to 452, the domain is characterized as VWFA.
+At position 464 to 744, the domain is characterized as Peptidase S1.
+At position 627 to 800, the domain is characterized as SSD.
+At position 169 to 231, the domain is characterized as t-SNARE coiled-coil homology.
+At position 92 to 179, the domain is characterized as PB1.
+At position 79 to 243, the domain is characterized as CP-type G.
+At position 86 to 181, the domain is characterized as Toprim.
+At position 4 to 168, the domain is characterized as EngA-type G 1.
+At position 18 to 55, the domain is characterized as EGF-like.
+At position 4 to 283, the domain is characterized as Protein kinase.
+At position 308 to 589, the domain is characterized as ABC transporter 1.
+At position 609 to 937, the domain is characterized as ABC transporter 2.
+At position 26 to 268, the domain is characterized as ABC transporter.
+At position 153 to 244, the domain is characterized as TonB C-terminal.
+At position 109 to 294, the domain is characterized as Tyr recombinase.
+At position 76 to 156, the domain is characterized as GS beta-grasp.
+At position 160 to 429, the domain is characterized as GS catalytic.
+At position 208 to 326, the domain is characterized as SET.
+At position 49 to 185, the domain is characterized as Tyrosine-protein phosphatase.
+At position 21 to 83, the domain is characterized as HTH iclR-type.
+At position 98 to 267, the domain is characterized as IclR-ED.
+At position 305 to 541, the domain is characterized as NR LBD.
+At position 7 to 122, the domain is characterized as VOC 1.
+At position 150 to 269, the domain is characterized as VOC 2.
+At position 35 to 415, the domain is characterized as PTS EIIC type-2.
+At position 298 to 551, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 127, the domain is characterized as Toprim.
+At position 7 to 95, the domain is characterized as MtN3/slv 1.
+At position 133 to 215, the domain is characterized as MtN3/slv 2.
+At position 624 to 726, the domain is characterized as PH.
+At position 770 to 1026, the domain is characterized as Protein kinase.
+At position 25 to 250, the domain is characterized as Peptidase S1.
+At position 16 to 158, the domain is characterized as PID.
+At position 211 to 307, the domain is characterized as SH2.
+At position 41 to 268, the domain is characterized as Radical SAM core.
+At position 22 to 258, the domain is characterized as ABC transporter 1.
+At position 263 to 512, the domain is characterized as ABC transporter 2.
+At position 584 to 777, the domain is characterized as Fibrinogen C-terminal.
+At position 778 to 943, the domain is characterized as Laminin G-like 3.
+At position 944 to 982, the domain is characterized as EGF-like 2.
+At position 987 to 1185, the domain is characterized as Laminin G-like 4.
+At position 73 to 151, the domain is characterized as RRM.
+At position 20 to 83, the domain is characterized as S5 DRBM.
+At position 14 to 269, the domain is characterized as Protein kinase.
+At position 307 to 331, the domain is characterized as NAF.
+At position 19 to 51, the domain is characterized as LisH.
+At position 9 to 99, the domain is characterized as Acylphosphatase-like.
+At position 66 to 116, the domain is characterized as FHA 1.
+At position 198 to 466, the domain is characterized as Protein kinase.
+At position 601 to 664, the domain is characterized as FHA 2.
+At position 1497 to 1588, the domain is characterized as Olduvai.
+At position 152 to 227, the domain is characterized as Ubiquitin-like.
+At position 4 to 166, the domain is characterized as Flavodoxin-like.
+At position 4 to 67, the domain is characterized as J.
+At position 82 to 150, the domain is characterized as DPH-type MB.
+At position 258 to 334, the domain is characterized as RRM.
+At position 976 to 1163, the domain is characterized as Reticulon.
+At position 287 to 427, the domain is characterized as SIS 1.
+At position 460 to 601, the domain is characterized as SIS 2.
+At position 209 to 397, the domain is characterized as Glutamine amidotransferase type-1.
+At position 159 to 283, the domain is characterized as Rhodanese.
+At position 446 to 804, the domain is characterized as USP.
+At position 17 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 109 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 208 to 291, the domain is characterized as Ig-like C2-type 3.
+At position 114 to 224, the domain is characterized as PH.
+At position 399 to 543, the domain is characterized as PI-PLC X-box.
+At position 586 to 702, the domain is characterized as PI-PLC Y-box.
+At position 702 to 831, the domain is characterized as C2.
+At position 40 to 126, the domain is characterized as RRM.
+At position 398 to 565, the domain is characterized as tr-type G.
+At position 127 to 251, the domain is characterized as Nudix hydrolase.
+At position 45 to 411, the domain is characterized as AB hydrolase-1.
+At position 21 to 289, the domain is characterized as GH16.
+At position 40 to 293, the domain is characterized as Protein kinase.
+At position 343 to 418, the domain is characterized as ACT.
+At position 140 to 345, the domain is characterized as ATP-grasp.
+At position 36 to 63, the domain is characterized as LRRNT.
+At position 310 to 362, the domain is characterized as LRRCT.
+At position 1 to 133, the domain is characterized as C2 1.
+At position 142 to 265, the domain is characterized as C2 2.
+At position 309 to 510, the domain is characterized as VWFA.
+At position 102 to 497, the domain is characterized as AB hydrolase-1.
+At position 272 to 350, the domain is characterized as PUA.
+At position 67 to 228, the domain is characterized as BUB1 N-terminal.
+At position 37 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 83 to 114, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 116 to 145, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 7 to 430, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1042 to 1116, the domain is characterized as Carrier.
+At position 5 to 52, the domain is characterized as F-box.
+At position 5 to 93, the domain is characterized as Acylphosphatase-like.
+At position 162 to 319, the domain is characterized as Plastocyanin-like 2.
+At position 436 to 563, the domain is characterized as Plastocyanin-like 3.
+At position 170 to 296, the domain is characterized as Fatty acid hydroxylase.
+At position 159 to 327, the domain is characterized as OBG-type G.
+At position 10 to 284, the domain is characterized as tr-type G.
+At position 2 to 82, the domain is characterized as IGFBP N-terminal.
+At position 150 to 228, the domain is characterized as Thyroglobulin type-1.
+At position 142 to 457, the domain is characterized as IF rod.
+At position 138 to 316, the domain is characterized as Era-type G.
+At position 347 to 423, the domain is characterized as KH type-2.
+At position 115 to 300, the domain is characterized as ATP-grasp.
+At position 6 to 185, the domain is characterized as Guanylate kinase-like.
+At position 1 to 53, the domain is characterized as ClpX-type ZB.
+At position 5 to 125, the domain is characterized as MTTase N-terminal.
+At position 152 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 449, the domain is characterized as TRAM.
+At position 183 to 330, the domain is characterized as KARI C-terminal knotted.
+At position 503 to 583, the domain is characterized as HRDC.
+At position 79 to 303, the domain is characterized as BPL/LPL catalytic.
+At position 5 to 82, the domain is characterized as TFIIS N-terminal.
+At position 187 to 303, the domain is characterized as TFIIS central.
+At position 190 to 377, the domain is characterized as Glutamine amidotransferase type-1.
+At position 17 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 145 to 174, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 338 to 507, the domain is characterized as tr-type G.
+At position 3 to 53, the domain is characterized as Kazal-like.
+At position 1 to 90, the domain is characterized as Core-binding (CB).
+At position 111 to 298, the domain is characterized as Tyr recombinase.
+At position 24 to 216, the domain is characterized as Velvet.
+At position 203 to 263, the domain is characterized as KH.
+At position 329 to 422, the domain is characterized as HD.
+At position 105 to 780, the domain is characterized as Myosin motor.
+At position 134 to 239, the domain is characterized as Fe2OG dioxygenase.
+At position 38 to 247, the domain is characterized as tr-type G.
+At position 693 to 884, the domain is characterized as ATP-grasp 2.
+At position 966 to 1113, the domain is characterized as MGS-like.
+At position 370 to 537, the domain is characterized as tr-type G.
+At position 232 to 499, the domain is characterized as CN hydrolase.
+At position 7 to 107, the domain is characterized as HTH araC/xylS-type.
+At position 96 to 134, the domain is characterized as LRRCT.
+At position 429 to 646, the domain is characterized as ABC transporter 1.
+At position 672 to 998, the domain is characterized as ABC transporter 2.
+At position 74 to 192, the domain is characterized as C-type lectin.
+At position 229 to 331, the domain is characterized as HD.
+At position 437 to 487, the domain is characterized as DHHC.
+At position 471 to 640, the domain is characterized as tr-type G.
+At position 277 to 440, the domain is characterized as YrdC-like.
+At position 246 to 412, the domain is characterized as Helicase ATP-binding.
+At position 463 to 703, the domain is characterized as Helicase C-terminal.
+At position 1 to 177, the domain is characterized as SPX.
+At position 439 to 643, the domain is characterized as EXS.
+At position 7 to 66, the domain is characterized as CSD.
+At position 207 to 297, the domain is characterized as SWIRM.
+At position 657 to 836, the domain is characterized as MOSC.
+At position 22 to 141, the domain is characterized as EamA 1.
+At position 160 to 280, the domain is characterized as EamA 2.
+At position 61 to 166, the domain is characterized as THUMP.
+At position 61 to 89, the domain is characterized as ITAM 1.
+At position 99 to 127, the domain is characterized as ITAM 2.
+At position 132 to 160, the domain is characterized as ITAM 3.
+At position 35 to 151, the domain is characterized as MTTase N-terminal.
+At position 175 to 419, the domain is characterized as Radical SAM core.
+At position 422 to 485, the domain is characterized as TRAM.
+At position 2 to 138, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 857 to 993, the domain is characterized as Peptidase S59.
+At position 48 to 390, the domain is characterized as Kinesin motor.
+At position 1 to 59, the domain is characterized as HTH tetR-type.
+At position 170 to 277, the domain is characterized as Cadherin 1.
+At position 278 to 392, the domain is characterized as Cadherin 2.
+At position 393 to 507, the domain is characterized as Cadherin 3.
+At position 508 to 613, the domain is characterized as Cadherin 4.
+At position 614 to 724, the domain is characterized as Cadherin 5.
+At position 468 to 666, the domain is characterized as MAGE.
+At position 2 to 78, the domain is characterized as PUA.
+At position 39 to 132, the domain is characterized as CTCK.
+At position 1 to 104, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 1 to 424, the domain is characterized as Hexokinase.
+At position 20 to 136, the domain is characterized as Ig-like V-type.
+At position 153 to 235, the domain is characterized as Ig-like C2-type 1.
+At position 239 to 321, the domain is characterized as Ig-like C2-type 2.
+At position 326 to 406, the domain is characterized as Ig-like C2-type 3.
+At position 416 to 508, the domain is characterized as Ig-like C2-type 4.
+At position 509 to 594, the domain is characterized as Ig-like C2-type 5.
+At position 602 to 701, the domain is characterized as Ig-like C2-type 6.
+At position 704 to 781, the domain is characterized as Ig-like C2-type 7.
+At position 795 to 890, the domain is characterized as Ig-like C2-type 8.
+At position 894 to 973, the domain is characterized as Ig-like C2-type 9.
+At position 980 to 1079, the domain is characterized as Ig-like C2-type 10.
+At position 1081 to 1161, the domain is characterized as Ig-like C2-type 11.
+At position 1172 to 1264, the domain is characterized as Ig-like C2-type 12.
+At position 1245 to 1337, the domain is characterized as Ig-like C2-type 13.
+At position 1342 to 1439, the domain is characterized as Ig-like C2-type 14.
+At position 1442 to 1520, the domain is characterized as Ig-like C2-type 15.
+At position 1534 to 1627, the domain is characterized as Ig-like C2-type 16.
+At position 58 to 129, the domain is characterized as SAM.
+At position 586 to 734, the domain is characterized as HD.
+At position 3 to 245, the domain is characterized as ABC transporter.
+At position 10 to 95, the domain is characterized as SCD.
+At position 1 to 240, the domain is characterized as F-BAR.
+At position 371 to 426, the domain is characterized as SH3.
+At position 3 to 136, the domain is characterized as Toprim.
+At position 16 to 275, the domain is characterized as Protein kinase.
+At position 12 to 218, the domain is characterized as YjeF N-terminal.
+At position 557 to 616, the domain is characterized as KH.
+At position 626 to 694, the domain is characterized as S1 motif.
+At position 9 to 55, the domain is characterized as F-box.
+At position 372 to 424, the domain is characterized as FBD.
+At position 90 to 180, the domain is characterized as K-box.
+At position 121 to 153, the domain is characterized as LisH.
+At position 159 to 254, the domain is characterized as CTLH.
+At position 285 to 561, the domain is characterized as Dynamin-type G.
+At position 25 to 193, the domain is characterized as Era-type G.
+At position 216 to 302, the domain is characterized as KH type-2.
+At position 2 to 472, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 492 to 783, the domain is characterized as UvrD-like helicase C-terminal.
+At position 370 to 580, the domain is characterized as TRUD.
+At position 5 to 255, the domain is characterized as ABC transporter 1.
+At position 350 to 600, the domain is characterized as ABC transporter 2.
+At position 17 to 240, the domain is characterized as AB hydrolase-1.
+At position 425 to 457, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 471 to 500, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 514 to 743, the domain is characterized as AIG1-type G.
+At position 1 to 51, the domain is characterized as ClpX-type ZB.
+At position 99 to 221, the domain is characterized as MPN.
+At position 7 to 95, the domain is characterized as ATP-cone.
+At position 84 to 188, the domain is characterized as C-type lectin.
+At position 260 to 351, the domain is characterized as PDZ 1.
+At position 357 to 463, the domain is characterized as PDZ 2.
+At position 118 to 303, the domain is characterized as CP-type G.
+At position 6 to 256, the domain is characterized as ABC transporter 1.
+At position 322 to 552, the domain is characterized as ABC transporter 2.
+At position 500 to 578, the domain is characterized as GRAM.
+At position 590 to 679, the domain is characterized as BRCT.
+At position 112 to 345, the domain is characterized as Peptidase S1.
+At position 23 to 98, the domain is characterized as Ig-like 1.
+At position 115 to 195, the domain is characterized as Ig-like 2.
+At position 6 to 332, the domain is characterized as Transferrin-like 1.
+At position 346 to 672, the domain is characterized as Transferrin-like 2.
+At position 47 to 594, the domain is characterized as PLA2c.
+At position 393 to 452, the domain is characterized as SH3.
+At position 32 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 218 to 299, the domain is characterized as HTH OST-type.
+At position 325 to 411, the domain is characterized as RRM.
+At position 130 to 189, the domain is characterized as Collagen-like 1.
+At position 217 to 276, the domain is characterized as Collagen-like 2.
+At position 283 to 342, the domain is characterized as Collagen-like 3.
+At position 343 to 478, the domain is characterized as C1q.
+At position 248 to 441, the domain is characterized as GATase cobBQ-type.
+At position 27 to 196, the domain is characterized as Helicase ATP-binding.
+At position 216 to 367, the domain is characterized as Helicase C-terminal.
+At position 513 to 591, the domain is characterized as HRDC.
+At position 104 to 200, the domain is characterized as RRM 1.
+At position 191 to 262, the domain is characterized as RRM 2.
+At position 31 to 94, the domain is characterized as S5 DRBM.
+At position 4 to 280, the domain is characterized as Protein kinase.
+At position 167 to 412, the domain is characterized as ABC transporter 1.
+At position 509 to 738, the domain is characterized as ABC transmembrane type-2 1.
+At position 837 to 1085, the domain is characterized as ABC transporter 2.
+At position 1249 to 1479, the domain is characterized as ABC transmembrane type-2 2.
+At position 28 to 210, the domain is characterized as Eph LBD.
+At position 333 to 446, the domain is characterized as Fibronectin type-III 1.
+At position 448 to 539, the domain is characterized as Fibronectin type-III 2.
+At position 625 to 885, the domain is characterized as Protein kinase.
+At position 914 to 977, the domain is characterized as SAM.
+At position 62 to 113, the domain is characterized as HTH myb-type 1.
+At position 114 to 169, the domain is characterized as HTH myb-type 2.
+At position 170 to 220, the domain is characterized as HTH myb-type 3.
+At position 1 to 99, the domain is characterized as PTS EIIB type-2 1.
+At position 120 to 215, the domain is characterized as PTS EIIB type-2 2.
+At position 243 to 580, the domain is characterized as PTS EIIC type-2.
+At position 8 to 117, the domain is characterized as FAD-binding FR-type.
+At position 264 to 353, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 4 to 220, the domain is characterized as Radical SAM core.
+At position 29 to 309, the domain is characterized as ABC transmembrane type-1.
+At position 342 to 577, the domain is characterized as ABC transporter.
+At position 3 to 81, the domain is characterized as RRM.
+At position 149 to 195, the domain is characterized as G-patch.
+At position 404 to 460, the domain is characterized as MIR 1.
+At position 473 to 529, the domain is characterized as MIR 2.
+At position 534 to 591, the domain is characterized as MIR 3.
+At position 3 to 92, the domain is characterized as Acylphosphatase-like.
+At position 515 to 723, the domain is characterized as SEC7.
+At position 774 to 887, the domain is characterized as PH.
+At position 15 to 83, the domain is characterized as BTB.
+At position 13 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 403, the domain is characterized as GMPS ATP-PPase.
+At position 12 to 197, the domain is characterized as RNase H type-2.
+At position 100 to 301, the domain is characterized as AIG1-type G.
+At position 23 to 69, the domain is characterized as LRRNT.
+At position 368 to 421, the domain is characterized as LRRCT.
+At position 421 to 514, the domain is characterized as Ig-like C2-type.
+At position 523 to 614, the domain is characterized as Fibronectin type-III.
+At position 29 to 164, the domain is characterized as Thioredoxin.
+At position 290 to 392, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 28 to 237, the domain is characterized as GH16.
+At position 357 to 425, the domain is characterized as PAS.
+At position 476 to 692, the domain is characterized as Histidine kinase.
+At position 705 to 805, the domain is characterized as ABL.
+At position 826 to 940, the domain is characterized as Response regulatory.
+At position 26 to 181, the domain is characterized as Helicase ATP-binding.
+At position 430 to 592, the domain is characterized as Helicase C-terminal.
+At position 7 to 257, the domain is characterized as Pyruvate carboxyltransferase.
+At position 480 to 516, the domain is characterized as CBM1.
+At position 10 to 158, the domain is characterized as EXPERA.
+At position 6 to 225, the domain is characterized as ABC transporter.
+At position 1 to 62, the domain is characterized as LCN-type CS-alpha/beta.
+At position 131 to 569, the domain is characterized as Urease.
+At position 134 to 212, the domain is characterized as RRM 1.
+At position 231 to 309, the domain is characterized as RRM 2.
+At position 467 to 554, the domain is characterized as RRM 3; atypical.
+At position 335 to 713, the domain is characterized as GRAS.
+At position 83 to 135, the domain is characterized as Kazal-like.
+At position 175 to 210, the domain is characterized as EF-hand 1.
+At position 211 to 246, the domain is characterized as EF-hand 2.
+At position 250 to 337, the domain is characterized as Ig-like 1.
+At position 341 to 426, the domain is characterized as Ig-like 2.
+At position 83 to 324, the domain is characterized as ABC transporter.
+At position 185 to 239, the domain is characterized as PQ-loop 2.
+At position 432 to 487, the domain is characterized as Kazal-like.
+At position 376 to 442, the domain is characterized as TRAM.
+At position 178 to 366, the domain is characterized as Glutamine amidotransferase type-1.
+At position 169 to 247, the domain is characterized as Toprim.
+At position 586 to 649, the domain is characterized as bZIP.
+At position 72 to 134, the domain is characterized as S4 RNA-binding.
+At position 25 to 107, the domain is characterized as BTB.
+At position 131 to 325, the domain is characterized as ATP-grasp 1.
+At position 673 to 863, the domain is characterized as ATP-grasp 2.
+At position 930 to 1051, the domain is characterized as MGS-like.
+At position 97 to 252, the domain is characterized as CP-type G.
+At position 107 to 456, the domain is characterized as PTS EIIC type-1.
+At position 106 to 305, the domain is characterized as ATP-grasp.
+At position 471 to 542, the domain is characterized as PAS.
+At position 78 to 249, the domain is characterized as Helicase ATP-binding.
+At position 260 to 469, the domain is characterized as Helicase C-terminal.
+At position 640 to 719, the domain is characterized as BRCT.
+At position 10 to 168, the domain is characterized as Thioredoxin.
+At position 4 to 185, the domain is characterized as DHFR.
+At position 38 to 195, the domain is characterized as PPIase cyclophilin-type.
+At position 47 to 135, the domain is characterized as PPIase FKBP-type.
+At position 7 to 79, the domain is characterized as Sm.
+At position 43 to 160, the domain is characterized as PLAT 1.
+At position 172 to 287, the domain is characterized as PLAT 2.
+At position 296 to 412, the domain is characterized as PLAT 3.
+At position 425 to 540, the domain is characterized as PLAT 4.
+At position 553 to 673, the domain is characterized as PLAT 5.
+At position 684 to 803, the domain is characterized as PLAT 6.
+At position 814 to 934, the domain is characterized as PLAT 7.
+At position 970 to 1088, the domain is characterized as PLAT 8.
+At position 1101 to 1226, the domain is characterized as PLAT 9.
+At position 1255 to 1373, the domain is characterized as PLAT 10.
+At position 1422 to 1540, the domain is characterized as PLAT 11.
+At position 1553 to 1668, the domain is characterized as PLAT 12.
+At position 1680 to 1798, the domain is characterized as PLAT 13.
+At position 1811 to 1932, the domain is characterized as PLAT 14.
+At position 1949 to 2065, the domain is characterized as PLAT 15.
+At position 142 to 181, the domain is characterized as STI1 1.
+At position 521 to 560, the domain is characterized as STI1 2.
+At position 150 to 190, the domain is characterized as LRRCT.
+At position 208 to 396, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 403, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 520 to 623, the domain is characterized as SMC hinge.
+At position 1 to 52, the domain is characterized as ClpX-type ZB.
+At position 421 to 581, the domain is characterized as tr-type G.
+At position 444 to 794, the domain is characterized as Protein kinase.
+At position 17 to 193, the domain is characterized as Phosphatase tensin-type.
+At position 199 to 338, the domain is characterized as C2 tensin-type.
+At position 735 to 1135, the domain is characterized as FH2.
+At position 476 to 593, the domain is characterized as Toprim.
+At position 29 to 143, the domain is characterized as Response regulatory.
+At position 167 to 265, the domain is characterized as HTH araC/xylS-type.
+At position 177 to 229, the domain is characterized as BSD.
+At position 748 to 1003, the domain is characterized as Protein kinase.
+At position 208 to 355, the domain is characterized as YDG.
+At position 430 to 491, the domain is characterized as Pre-SET.
+At position 494 to 638, the domain is characterized as SET.
+At position 653 to 669, the domain is characterized as Post-SET.
+At position 3 to 178, the domain is characterized as EngA-type G 1.
+At position 190 to 363, the domain is characterized as EngA-type G 2.
+At position 48 to 318, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 25 to 295, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 34 to 356, the domain is characterized as Kinesin motor.
+At position 44 to 163, the domain is characterized as FZ.
+At position 490 to 664, the domain is characterized as Helicase C-terminal.
+At position 763 to 827, the domain is characterized as SAM.
+At position 149 to 289, the domain is characterized as CID.
+At position 850 to 900, the domain is characterized as G-patch.
+At position 3 to 199, the domain is characterized as DPCK.
+At position 64 to 229, the domain is characterized as CP-type G.
+At position 226 to 495, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 210 to 435, the domain is characterized as MIF4G.
+At position 621 to 743, the domain is characterized as MI.
+At position 133 to 314, the domain is characterized as Helicase ATP-binding.
+At position 459 to 618, the domain is characterized as Helicase C-terminal.
+At position 651 to 741, the domain is characterized as Dicer dsRNA-binding fold.
+At position 891 to 1019, the domain is characterized as PAZ.
+At position 1043 to 1202, the domain is characterized as RNase III 1.
+At position 1253 to 1405, the domain is characterized as RNase III 2.
+At position 1439 to 1507, the domain is characterized as DRBM.
+At position 299 to 554, the domain is characterized as Protein kinase.
+At position 54 to 368, the domain is characterized as AB hydrolase-1.
+At position 49 to 180, the domain is characterized as WIF.
+At position 317 to 577, the domain is characterized as Protein kinase.
+At position 123 to 437, the domain is characterized as Peptidase S8.
+At position 446 to 580, the domain is characterized as P/Homo B.
+At position 23 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 25 to 100, the domain is characterized as EMI.
+At position 99 to 129, the domain is characterized as EGF-like 1.
+At position 137 to 172, the domain is characterized as EGF-like 2.
+At position 180 to 215, the domain is characterized as EGF-like 3.
+At position 223 to 258, the domain is characterized as EGF-like 4.
+At position 266 to 301, the domain is characterized as EGF-like 5.
+At position 309 to 344, the domain is characterized as EGF-like 6.
+At position 398 to 433, the domain is characterized as EGF-like 7.
+At position 484 to 519, the domain is characterized as EGF-like 8.
+At position 572 to 607, the domain is characterized as EGF-like 9.
+At position 660 to 695, the domain is characterized as EGF-like 10.
+At position 33 to 211, the domain is characterized as Eph LBD.
+At position 330 to 440, the domain is characterized as Fibronectin type-III 1.
+At position 441 to 536, the domain is characterized as Fibronectin type-III 2.
+At position 630 to 943, the domain is characterized as Protein kinase.
+At position 960 to 1024, the domain is characterized as SAM.
+At position 39 to 316, the domain is characterized as tr-type G.
+At position 165 to 343, the domain is characterized as CP-type G.
+At position 47 to 216, the domain is characterized as VWFA.
+At position 233 to 479, the domain is characterized as ZP.
+At position 19 to 248, the domain is characterized as Chitin-binding type-4.
+At position 278 to 385, the domain is characterized as CBM20.
+At position 171 to 190, the domain is characterized as UIM.
+At position 415 to 493, the domain is characterized as UBX.
+At position 158 to 307, the domain is characterized as GAF.
+At position 350 to 587, the domain is characterized as Histidine kinase.
+At position 1 to 42, the domain is characterized as UBA.
+At position 208 to 287, the domain is characterized as UBX.
+At position 131 to 325, the domain is characterized as ATP-grasp.
+At position 18 to 69, the domain is characterized as FHA.
+At position 270 to 372, the domain is characterized as ERCC4.
+At position 24 to 89, the domain is characterized as BTB.
+At position 10 to 120, the domain is characterized as MTTase N-terminal.
+At position 377 to 443, the domain is characterized as TRAM.
+At position 5 to 191, the domain is characterized as DHFR.
+At position 27 to 289, the domain is characterized as Alpha-carbonic anhydrase.
+At position 20 to 83, the domain is characterized as LCN-type CS-alpha/beta.
+At position 208 to 381, the domain is characterized as EngA-type G 2.
+At position 118 to 231, the domain is characterized as C-type lectin.
+At position 4 to 185, the domain is characterized as YrdC-like.
+At position 78 to 128, the domain is characterized as DHHC.
+At position 125 to 180, the domain is characterized as HTH cro/C1-type.
+At position 523 to 598, the domain is characterized as Carrier 1.
+At position 616 to 1039, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 2002 to 2077, the domain is characterized as Carrier 2.
+At position 453 to 711, the domain is characterized as Protein kinase.
+At position 712 to 762, the domain is characterized as AGC-kinase C-terminal.
+At position 565 to 594, the domain is characterized as IQ.
+At position 614 to 690, the domain is characterized as Carrier 1.
+At position 1699 to 1775, the domain is characterized as Carrier 2.
+At position 711 to 978, the domain is characterized as Protein kinase.
+At position 160 to 336, the domain is characterized as OBG-type G.
+At position 34 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 15 to 93, the domain is characterized as GIY-YIG.
+At position 28 to 109, the domain is characterized as IGFBP N-terminal.
+At position 177 to 255, the domain is characterized as Thyroglobulin type-1.
+At position 154 to 401, the domain is characterized as NR LBD.
+At position 1 to 105, the domain is characterized as Thioredoxin.
+At position 326 to 515, the domain is characterized as Protein kinase.
+At position 485 to 924, the domain is characterized as USP.
+At position 975 to 1147, the domain is characterized as Exonuclease.
+At position 3 to 36, the domain is characterized as WW 1.
+At position 89 to 122, the domain is characterized as WW 2.
+At position 239 to 293, the domain is characterized as FF.
+At position 930 to 1064, the domain is characterized as MGS-like.
+At position 165 to 250, the domain is characterized as PPIase FKBP-type.
+At position 277 to 520, the domain is characterized as GT92.
+At position 23 to 246, the domain is characterized as Alpha-carbonic anhydrase.
+At position 166 to 278, the domain is characterized as PINc.
+At position 292 to 353, the domain is characterized as TRAM.
+At position 228 to 490, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 34 to 94, the domain is characterized as HTH myb-type.
+At position 93 to 182, the domain is characterized as VPS37 C-terminal.
+At position 34 to 301, the domain is characterized as Protein kinase.
+At position 106 to 329, the domain is characterized as Radical SAM core.
+At position 62 to 135, the domain is characterized as RRM 1.
+At position 141 to 226, the domain is characterized as RRM 2.
+At position 302 to 538, the domain is characterized as NR LBD.
+At position 80 to 161, the domain is characterized as Inhibitor I9.
+At position 169 to 451, the domain is characterized as Peptidase S8.
+At position 35 to 86, the domain is characterized as LysM.
+At position 61 to 350, the domain is characterized as YjeF C-terminal.
+At position 138 to 375, the domain is characterized as Radical SAM core.
+At position 106 to 211, the domain is characterized as PH.
+At position 266 to 523, the domain is characterized as Protein kinase.
+At position 524 to 597, the domain is characterized as AGC-kinase C-terminal.
+At position 296 to 380, the domain is characterized as RCK C-terminal.
+At position 465 to 644, the domain is characterized as Reverse transcriptase.
+At position 844 to 997, the domain is characterized as Integrase catalytic.
+At position 116 to 427, the domain is characterized as IF rod.
+At position 56 to 242, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 88, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 219 to 400, the domain is characterized as FAD-binding PCMH-type.
+At position 55 to 189, the domain is characterized as Thioredoxin 1.
+At position 403 to 545, the domain is characterized as Thioredoxin 2.
+At position 1 to 280, the domain is characterized as CheR-type methyltransferase.
+At position 8 to 99, the domain is characterized as CARD.
+At position 130 to 369, the domain is characterized as Radical SAM core.
+At position 160 to 328, the domain is characterized as OBG-type G.
+At position 333 to 404, the domain is characterized as ACT-like 1.
+At position 427 to 498, the domain is characterized as ACT-like 2.
+At position 133 to 246, the domain is characterized as CENP-V/GFA.
+At position 16 to 48, the domain is characterized as LisH.
+At position 25 to 172, the domain is characterized as PX.
+At position 202 to 404, the domain is characterized as BAR.
+At position 87 to 153, the domain is characterized as KH.
+At position 24 to 353, the domain is characterized as FERM.
+At position 372 to 472, the domain is characterized as SH2; atypical.
+At position 517 to 777, the domain is characterized as Protein kinase 1.
+At position 818 to 1100, the domain is characterized as Protein kinase 2.
+At position 2 to 240, the domain is characterized as ABC transporter.
+At position 10 to 199, the domain is characterized as RNase H type-2.
+At position 392 to 518, the domain is characterized as DOD-type homing endonuclease.
+At position 428 to 554, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 49 to 136, the domain is characterized as ATP-cone.
+At position 222 to 399, the domain is characterized as PCI.
+At position 66 to 206, the domain is characterized as SCP.
+At position 302 to 397, the domain is characterized as LCCL 1.
+At position 403 to 505, the domain is characterized as LCCL 2.
+At position 67 to 115, the domain is characterized as Collagen-like.
+At position 125 to 258, the domain is characterized as C1q.
+At position 4 to 108, the domain is characterized as HIT.
+At position 226 to 329, the domain is characterized as HD.
+At position 61 to 117, the domain is characterized as EF-hand 1; degenerate.
+At position 120 to 155, the domain is characterized as EF-hand 2.
+At position 156 to 191, the domain is characterized as EF-hand 3.
+At position 204 to 239, the domain is characterized as EF-hand 4.
+At position 7 to 170, the domain is characterized as PPIase cyclophilin-type.
+At position 71 to 272, the domain is characterized as Laminin G-like.
+At position 15 to 86, the domain is characterized as KRAB.
+At position 97 to 288, the domain is characterized as ABC transmembrane type-1.
+At position 443 to 733, the domain is characterized as Protein kinase.
+At position 174 to 223, the domain is characterized as bHLH.
+At position 4 to 236, the domain is characterized as ABC transporter.
+At position 100 to 275, the domain is characterized as Helicase ATP-binding.
+At position 299 to 451, the domain is characterized as Helicase C-terminal.
+At position 60 to 247, the domain is characterized as PID.
+At position 53 to 147, the domain is characterized as PA.
+At position 31 to 91, the domain is characterized as v-SNARE coiled-coil homology.
+At position 20 to 55, the domain is characterized as EF-hand 1.
+At position 88 to 123, the domain is characterized as EF-hand 2.
+At position 49 to 127, the domain is characterized as Kringle 1.
+At position 163 to 241, the domain is characterized as Kringle 2.
+At position 277 to 355, the domain is characterized as Kringle 3.
+At position 391 to 469, the domain is characterized as Kringle 4.
+At position 505 to 583, the domain is characterized as Kringle 5.
+At position 619 to 697, the domain is characterized as Kringle 6.
+At position 725 to 803, the domain is characterized as Kringle 7.
+At position 839 to 917, the domain is characterized as Kringle 8.
+At position 953 to 1031, the domain is characterized as Kringle 9.
+At position 1067 to 1145, the domain is characterized as Kringle 10.
+At position 1191 to 1418, the domain is characterized as Peptidase S1.
+At position 709 to 969, the domain is characterized as Tyrosine-protein phosphatase.
+At position 49 to 279, the domain is characterized as Radical SAM core.
+At position 25 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 97 to 213, the domain is characterized as Ferric oxidoreductase.
+At position 187 to 363, the domain is characterized as FAD-binding FR-type.
+At position 535 to 636, the domain is characterized as tRNA-binding.
+At position 928 to 1420, the domain is characterized as FAT.
+At position 1494 to 1793, the domain is characterized as PI3K/PI4K catalytic.
+At position 1773 to 1805, the domain is characterized as FATC.
+At position 89 to 152, the domain is characterized as S4 RNA-binding.
+At position 27 to 115, the domain is characterized as UPAR/Ly6.
+At position 39 to 264, the domain is characterized as Radical SAM core.
+At position 67 to 217, the domain is characterized as Cupin type-1.
+At position 32 to 96, the domain is characterized as BTB.
+At position 142 to 509, the domain is characterized as PUM-HD.
+At position 26 to 131, the domain is characterized as Ig-like V-type.
+At position 6 to 60, the domain is characterized as HTH lacI-type.
+At position 102 to 413, the domain is characterized as IF rod.
+At position 8 to 283, the domain is characterized as tr-type G.
+At position 2 to 82, the domain is characterized as Carrier.
+At position 289 to 562, the domain is characterized as Radical SAM core.
+At position 9 to 442, the domain is characterized as Helicase ATP-binding.
+At position 321 to 482, the domain is characterized as 3'-5' exonuclease.
+At position 305 to 368, the domain is characterized as bZIP.
+At position 39 to 141, the domain is characterized as Gnk2-homologous 1.
+At position 147 to 259, the domain is characterized as Gnk2-homologous 2.
+At position 5 to 183, the domain is characterized as Guanylate kinase-like.
+At position 58 to 200, the domain is characterized as PID.
+At position 150 to 275, the domain is characterized as Plus3.
+At position 497 to 551, the domain is characterized as GYF.
+At position 71 to 256, the domain is characterized as TR mART core.
+At position 16 to 130, the domain is characterized as Arf-GAP.
+At position 5 to 245, the domain is characterized as PABS.
+At position 36 to 272, the domain is characterized as Radical SAM core.
+At position 3 to 233, the domain is characterized as ABC transporter.
+At position 331 to 508, the domain is characterized as Helicase C-terminal.
+At position 2 to 70, the domain is characterized as J.
+At position 8 to 104, the domain is characterized as SH2.
+At position 24 to 195, the domain is characterized as EngB-type G.
+At position 1 to 108, the domain is characterized as VPS28 N-terminal.
+At position 112 to 208, the domain is characterized as VPS28 C-terminal.
+At position 38 to 204, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 153, the domain is characterized as C-type lectin.
+At position 215 to 462, the domain is characterized as CN hydrolase.
+At position 49 to 282, the domain is characterized as Radical SAM core.
+At position 209 to 287, the domain is characterized as RRM.
+At position 85 to 504, the domain is characterized as USP.
+At position 564 to 628, the domain is characterized as SAM 1.
+At position 636 to 699, the domain is characterized as SAM 2.
+At position 724 to 789, the domain is characterized as SAM 3.
+At position 742 to 874, the domain is characterized as BAH 1.
+At position 910 to 1049, the domain is characterized as BAH 2.
+At position 1092 to 1526, the domain is characterized as SAM-dependent MTase C5-type.
+At position 455 to 596, the domain is characterized as SIS 2.
+At position 159 to 328, the domain is characterized as OBG-type G.
+At position 343 to 426, the domain is characterized as OCT.
+At position 207 to 254, the domain is characterized as F-box.
+At position 174 to 272, the domain is characterized as ELM2.
+At position 277 to 329, the domain is characterized as SANT.
+At position 34 to 323, the domain is characterized as Deacetylase sirtuin-type.
+At position 9 to 116, the domain is characterized as C-type lectin.
+At position 2 to 125, the domain is characterized as MsrB.
+At position 4 to 199, the domain is characterized as Flavodoxin-like.
+At position 47 to 263, the domain is characterized as Radical SAM core.
+At position 84 to 266, the domain is characterized as Brix.
+At position 99 to 184, the domain is characterized as FAR1.
+At position 297 to 392, the domain is characterized as MULE.
+At position 34 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 18 to 142, the domain is characterized as EamA 1.
+At position 164 to 297, the domain is characterized as EamA 2.
+At position 96 to 169, the domain is characterized as PRC barrel.
+At position 463 to 580, the domain is characterized as Toprim.
+At position 278 to 356, the domain is characterized as PUA.
+At position 1 to 132, the domain is characterized as DAGKc.
+At position 50 to 158, the domain is characterized as Cadherin 1.
+At position 159 to 270, the domain is characterized as Cadherin 2.
+At position 271 to 385, the domain is characterized as Cadherin 3.
+At position 386 to 496, the domain is characterized as Cadherin 4.
+At position 66 to 164, the domain is characterized as Flavodoxin-like.
+At position 138 to 443, the domain is characterized as Velvet.
+At position 5 to 70, the domain is characterized as HMA 1.
+At position 72 to 138, the domain is characterized as HMA 2.
+At position 51 to 110, the domain is characterized as VWFC 1.
+At position 114 to 172, the domain is characterized as VWFC 2.
+At position 2 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 48 to 162, the domain is characterized as Ig-like V-type.
+At position 151 to 232, the domain is characterized as Ig-like C2-type.
+At position 151 to 210, the domain is characterized as SH3.
+At position 244 to 428, the domain is characterized as DH.
+At position 459 to 565, the domain is characterized as PH.
+At position 7 to 93, the domain is characterized as ASCH.
+At position 136 to 193, the domain is characterized as VWFC 1.
+At position 194 to 253, the domain is characterized as VWFC 2.
+At position 253 to 312, the domain is characterized as VWFC 3.
+At position 312 to 370, the domain is characterized as VWFC 4.
+At position 426 to 485, the domain is characterized as VWFC 5.
+At position 485 to 544, the domain is characterized as VWFC 6.
+At position 544 to 602, the domain is characterized as VWFC 7.
+At position 602 to 661, the domain is characterized as VWFC 8.
+At position 667 to 725, the domain is characterized as VWFC 9.
+At position 725 to 782, the domain is characterized as VWFC 10.
+At position 782 to 841, the domain is characterized as VWFC 11.
+At position 900 to 959, the domain is characterized as VWFC 12.
+At position 959 to 1017, the domain is characterized as VWFC 13.
+At position 1017 to 1085, the domain is characterized as VWFC 14.
+At position 1082 to 1145, the domain is characterized as VWFC 15.
+At position 1149 to 1209, the domain is characterized as VWFC 16.
+At position 1213 to 1389, the domain is characterized as VWFD.
+At position 1483 to 1543, the domain is characterized as TIL.
+At position 1 to 46, the domain is characterized as Rubredoxin-like.
+At position 207 to 298, the domain is characterized as Ig-like C1-type.
+At position 4 to 288, the domain is characterized as Protein kinase.
+At position 78 to 109, the domain is characterized as EF-hand 2.
+At position 24 to 207, the domain is characterized as EngB-type G.
+At position 162 to 425, the domain is characterized as Lon N-terminal.
+At position 854 to 1040, the domain is characterized as Lon proteolytic.
+At position 7 to 296, the domain is characterized as Helicase ATP-binding.
+At position 422 to 578, the domain is characterized as Exonuclease.
+At position 1 to 167, the domain is characterized as TCTP.
+At position 38 to 318, the domain is characterized as tr-type G.
+At position 131 to 444, the domain is characterized as IF rod.
+At position 29 to 144, the domain is characterized as Plastocyanin-like 1.
+At position 154 to 277, the domain is characterized as Plastocyanin-like 2.
+At position 364 to 491, the domain is characterized as Plastocyanin-like 3.
+At position 32 to 205, the domain is characterized as EngB-type G.
+At position 4 to 139, the domain is characterized as B12-binding.
+At position 671 to 847, the domain is characterized as PCI.
+At position 166 to 251, the domain is characterized as PPIase FKBP-type.
+At position 191 to 270, the domain is characterized as RRM.
+At position 755 to 869, the domain is characterized as WWE.
+At position 1918 to 2025, the domain is characterized as HECT.
+At position 1 to 116, the domain is characterized as C2.
+At position 167 to 200, the domain is characterized as WW 1.
+At position 513 to 546, the domain is characterized as WW 2.
+At position 561 to 594, the domain is characterized as WW 3.
+At position 723 to 1061, the domain is characterized as HECT.
+At position 26 to 146, the domain is characterized as MTTase N-terminal.
+At position 173 to 405, the domain is characterized as Radical SAM core.
+At position 408 to 470, the domain is characterized as TRAM.
+At position 568 to 650, the domain is characterized as S1 motif.
+At position 275 to 360, the domain is characterized as SCD.
+At position 25 to 156, the domain is characterized as ENTH.
+At position 412 to 712, the domain is characterized as Protein kinase.
+At position 71 to 104, the domain is characterized as EF-hand 1.
+At position 105 to 140, the domain is characterized as EF-hand 2.
+At position 142 to 175, the domain is characterized as EF-hand 3.
+At position 176 to 211, the domain is characterized as EF-hand 4.
+At position 17 to 215, the domain is characterized as ABC transmembrane type-1.
+At position 192 to 502, the domain is characterized as USP.
+At position 589 to 686, the domain is characterized as SH2.
+At position 376 to 472, the domain is characterized as Fibronectin type-III 1.
+At position 473 to 568, the domain is characterized as Fibronectin type-III 2.
+At position 642 to 901, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 933 to 1216, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 183 to 329, the domain is characterized as KARI C-terminal knotted.
+At position 24 to 264, the domain is characterized as Laminin N-terminal.
+At position 265 to 331, the domain is characterized as Laminin EGF-like 1.
+At position 395 to 454, the domain is characterized as Laminin EGF-like 3.
+At position 455 to 505, the domain is characterized as Laminin EGF-like 4.
+At position 506 to 552, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 545 to 763, the domain is characterized as Laminin IV type B.
+At position 769 to 816, the domain is characterized as Laminin EGF-like 6.
+At position 817 to 862, the domain is characterized as Laminin EGF-like 7.
+At position 863 to 910, the domain is characterized as Laminin EGF-like 8.
+At position 911 to 969, the domain is characterized as Laminin EGF-like 9.
+At position 970 to 1021, the domain is characterized as Laminin EGF-like 10.
+At position 1022 to 1079, the domain is characterized as Laminin EGF-like 11.
+At position 1080 to 1127, the domain is characterized as Laminin EGF-like 12.
+At position 1128 to 1174, the domain is characterized as Laminin EGF-like 13.
+At position 5 to 129, the domain is characterized as VOC.
+At position 199 to 375, the domain is characterized as DH.
+At position 380 to 499, the domain is characterized as PH.
+At position 28 to 147, the domain is characterized as CUB 1.
+At position 162 to 272, the domain is characterized as CUB 2.
+At position 286 to 417, the domain is characterized as CUB 3.
+At position 435 to 554, the domain is characterized as CUB 4.
+At position 67 to 322, the domain is characterized as Radical SAM core.
+At position 193 to 269, the domain is characterized as UBX.
+At position 90 to 430, the domain is characterized as Peptidase A1.
+At position 19 to 54, the domain is characterized as EF-hand 1.
+At position 55 to 88, the domain is characterized as EF-hand 2.
+At position 86 to 121, the domain is characterized as EF-hand 3.
+At position 122 to 157, the domain is characterized as EF-hand 4.
+At position 363 to 516, the domain is characterized as CBM3 1.
+At position 566 to 719, the domain is characterized as CBM3 2.
+At position 1 to 442, the domain is characterized as SMP-LTD.
+At position 222 to 273, the domain is characterized as Kazal-like.
+At position 468 to 503, the domain is characterized as EF-hand 1.
+At position 508 to 535, the domain is characterized as EF-hand 2.
+At position 533 to 594, the domain is characterized as Thyroglobulin type-1.
+At position 1 to 274, the domain is characterized as Protein kinase.
+At position 397 to 594, the domain is characterized as Helicase ATP-binding.
+At position 730 to 890, the domain is characterized as Helicase C-terminal.
+At position 13 to 154, the domain is characterized as Nudix hydrolase.
+At position 585 to 614, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 616 to 645, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 117 to 445, the domain is characterized as PI3K/PI4K catalytic.
+At position 379 to 559, the domain is characterized as VWFA.
+At position 497 to 803, the domain is characterized as Calpain catalytic.
+At position 1 to 48, the domain is characterized as Disintegrin.
+At position 26 to 694, the domain is characterized as PFL.
+At position 701 to 824, the domain is characterized as Glycine radical.
+At position 1 to 78, the domain is characterized as GST N-terminal.
+At position 80 to 201, the domain is characterized as GST C-terminal.
+At position 137 to 199, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 4 to 224, the domain is characterized as Lon N-terminal.
+At position 649 to 832, the domain is characterized as Lon proteolytic.
+At position 286 to 510, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 46, the domain is characterized as F-box.
+At position 92 to 149, the domain is characterized as bHLH.
+At position 389 to 822, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1318 to 1628, the domain is characterized as PKS/mFAS DH.
+At position 1717 to 1794, the domain is characterized as Carrier.
+At position 40 to 222, the domain is characterized as NodB homology.
+At position 62 to 103, the domain is characterized as CWF21.
+At position 6 to 66, the domain is characterized as Kazal-like 1.
+At position 67 to 115, the domain is characterized as Kazal-like 2.
+At position 7 to 62, the domain is characterized as HTH cro/C1-type.
+At position 1 to 58, the domain is characterized as SH3 1.
+At position 98 to 157, the domain is characterized as SH3 2.
+At position 311 to 372, the domain is characterized as SH3 3.
+At position 6 to 124, the domain is characterized as VOC.
+At position 854 to 909, the domain is characterized as WAPL.
+At position 47 to 356, the domain is characterized as AB hydrolase-1.
+At position 377 to 434, the domain is characterized as CBS 1.
+At position 438 to 493, the domain is characterized as CBS 2.
+At position 102 to 173, the domain is characterized as SUI1.
+At position 14 to 77, the domain is characterized as Histone-fold.
+At position 629 to 697, the domain is characterized as S1 motif.
+At position 507 to 622, the domain is characterized as Ricin B-type lectin.
+At position 104 to 222, the domain is characterized as MRH.
+At position 23 to 212, the domain is characterized as Rho-GAP.
+At position 197 to 232, the domain is characterized as UVR.
+At position 1 to 242, the domain is characterized as Deacetylase sirtuin-type.
+At position 500 to 783, the domain is characterized as UvrD-like helicase C-terminal.
+At position 81 to 516, the domain is characterized as Protein kinase.
+At position 292 to 528, the domain is characterized as NR LBD.
+At position 364 to 444, the domain is characterized as OCT.
+At position 196 to 295, the domain is characterized as Fe2OG dioxygenase.
+At position 231 to 490, the domain is characterized as Olfactomedin-like.
+At position 39 to 111, the domain is characterized as KH type-2.
+At position 23 to 167, the domain is characterized as Flavodoxin-like.
+At position 235 to 485, the domain is characterized as FAD-binding FR-type.
+At position 5 to 152, the domain is characterized as N-acetyltransferase.
+At position 197 to 343, the domain is characterized as TrmE-type G.
+At position 30 to 80, the domain is characterized as PSI.
+At position 144 to 382, the domain is characterized as VWFA.
+At position 444 to 506, the domain is characterized as EGF-like 1.
+At position 507 to 559, the domain is characterized as EGF-like 2.
+At position 560 to 596, the domain is characterized as EGF-like 3.
+At position 597 to 640, the domain is characterized as EGF-like 4.
+At position 592 to 670, the domain is characterized as BRCT.
+At position 117 to 303, the domain is characterized as FAD-binding PCMH-type.
+At position 133 to 348, the domain is characterized as ABC transmembrane type-1.
+At position 225 to 273, the domain is characterized as Fibronectin type-II 1.
+At position 283 to 331, the domain is characterized as Fibronectin type-II 2.
+At position 342 to 390, the domain is characterized as Fibronectin type-II 3.
+At position 495 to 517, the domain is characterized as GoLoco 1.
+At position 548 to 570, the domain is characterized as GoLoco 2.
+At position 596 to 618, the domain is characterized as GoLoco 3.
+At position 630 to 652, the domain is characterized as GoLoco 4.
+At position 248 to 432, the domain is characterized as GATase cobBQ-type.
+At position 13 to 148, the domain is characterized as Obg.
+At position 149 to 344, the domain is characterized as OBG-type G.
+At position 68 to 205, the domain is characterized as DAGKc.
+At position 65 to 137, the domain is characterized as S1 motif.
+At position 147 to 205, the domain is characterized as KH.
+At position 146 to 320, the domain is characterized as CRAL-TRIO.
+At position 278 to 362, the domain is characterized as PDZ 1.
+At position 385 to 467, the domain is characterized as PDZ 2.
+At position 508 to 593, the domain is characterized as PDZ 3.
+At position 638 to 723, the domain is characterized as PDZ 4.
+At position 180 to 327, the domain is characterized as JmjC.
+At position 107 to 166, the domain is characterized as Chromo 1.
+At position 348 to 412, the domain is characterized as Chromo 2; shadow subtype.
+At position 341 to 417, the domain is characterized as HTH rpiR-type.
+At position 461 to 600, the domain is characterized as SIS.
+At position 1 to 83, the domain is characterized as GST N-terminal.
+At position 89 to 211, the domain is characterized as GST C-terminal.
+At position 46 to 325, the domain is characterized as GH10.
+At position 966 to 1112, the domain is characterized as MGS-like.
+At position 593 to 672, the domain is characterized as BRCT.
+At position 35 to 114, the domain is characterized as Importin N-terminal.
+At position 36 to 73, the domain is characterized as VM.
+At position 6 to 202, the domain is characterized as Peptidase M12B.
+At position 5 to 226, the domain is characterized as Radical SAM core.
+At position 13 to 61, the domain is characterized as F-box.
+At position 346 to 396, the domain is characterized as FBD.
+At position 100 to 389, the domain is characterized as FAE.
+At position 571 to 611, the domain is characterized as UBA.
+At position 22 to 324, the domain is characterized as F-BAR.
+At position 1 to 152, the domain is characterized as Jacalin-type lectin.
+At position 1 to 59, the domain is characterized as TRAM.
+At position 10 to 198, the domain is characterized as RNase H type-2.
+At position 22 to 84, the domain is characterized as Sushi 1.
+At position 123 to 186, the domain is characterized as Sushi 2.
+At position 93 to 382, the domain is characterized as FAE.
+At position 53 to 121, the domain is characterized as POTRA.
+At position 233 to 420, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 124 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 40 to 267, the domain is characterized as Radical SAM core.
+At position 30 to 281, the domain is characterized as Protein kinase.
+At position 433 to 480, the domain is characterized as SARAH.
+At position 391 to 806, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1291 to 1603, the domain is characterized as PKS/mFAS DH.
+At position 1661 to 1738, the domain is characterized as Carrier.
+At position 85 to 291, the domain is characterized as ABC transmembrane type-1.
+At position 22 to 154, the domain is characterized as MPN.
+At position 636 to 954, the domain is characterized as Protein kinase.
+At position 6 to 205, the domain is characterized as tr-type G.
+At position 158 to 275, the domain is characterized as C2.
+At position 342 to 600, the domain is characterized as Protein kinase.
+At position 601 to 671, the domain is characterized as AGC-kinase C-terminal.
+At position 95 to 250, the domain is characterized as Protein kinase.
+At position 275 to 350, the domain is characterized as B5.
+At position 2 to 469, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 497 to 784, the domain is characterized as UvrD-like helicase C-terminal.
+At position 297 to 513, the domain is characterized as Histidine kinase.
+At position 34 to 206, the domain is characterized as Tyrosine-protein phosphatase.
+At position 138 to 575, the domain is characterized as Urease.
+At position 207 to 439, the domain is characterized as CN hydrolase.
+At position 1 to 58, the domain is characterized as IBB.
+At position 200 to 310, the domain is characterized as Fe2OG dioxygenase.
+At position 35 to 113, the domain is characterized as RRM 1.
+At position 123 to 200, the domain is characterized as RRM 2.
+At position 216 to 293, the domain is characterized as RRM 3.
+At position 319 to 396, the domain is characterized as RRM 4.
+At position 487 to 566, the domain is characterized as PABC.
+At position 68 to 90, the domain is characterized as Follistatin-like.
+At position 86 to 148, the domain is characterized as Kazal-like.
+At position 258 to 293, the domain is characterized as EF-hand.
+At position 1 to 172, the domain is characterized as TCTP.
+At position 26 to 143, the domain is characterized as DOMON.
+At position 199 to 372, the domain is characterized as EngA-type G 2.
+At position 373 to 457, the domain is characterized as KH-like.
+At position 25 to 141, the domain is characterized as MTTase N-terminal.
+At position 164 to 400, the domain is characterized as Radical SAM core.
+At position 403 to 471, the domain is characterized as TRAM.
+At position 608 to 698, the domain is characterized as BRCT.
+At position 114 to 305, the domain is characterized as ATP-grasp.
+At position 16 to 101, the domain is characterized as Sm.
+At position 65 to 216, the domain is characterized as Cupin type-1.
+At position 6 to 115, the domain is characterized as HIT.
+At position 7 to 57, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 12 to 272, the domain is characterized as Protein kinase.
+At position 302 to 408, the domain is characterized as BEN.
+At position 179 to 271, the domain is characterized as PH.
+At position 102 to 254, the domain is characterized as Nudix hydrolase.
+At position 165 to 262, the domain is characterized as HTH araC/xylS-type.
+At position 47 to 97, the domain is characterized as Myosin N-terminal SH3-like.
+At position 101 to 804, the domain is characterized as Myosin motor.
+At position 807 to 836, the domain is characterized as IQ.
+At position 300 to 483, the domain is characterized as B30.2/SPRY.
+At position 93 to 272, the domain is characterized as DH.
+At position 296 to 394, the domain is characterized as PH.
+At position 5 to 230, the domain is characterized as tr-type G.
+At position 1232 to 1329, the domain is characterized as SH2.
+At position 56 to 219, the domain is characterized as SIS.
+At position 408 to 585, the domain is characterized as Helicase ATP-binding.
+At position 611 to 831, the domain is characterized as Helicase C-terminal.
+At position 5 to 122, the domain is characterized as Response regulatory.
+At position 152 to 344, the domain is characterized as CheB-type methylesterase.
+At position 8 to 85, the domain is characterized as RRM.
+At position 4 to 76, the domain is characterized as RRM 1.
+At position 295 to 373, the domain is characterized as RRM 2.
+At position 478 to 550, the domain is characterized as RRM 3.
+At position 592 to 675, the domain is characterized as RRM 4.
+At position 697 to 774, the domain is characterized as RRM 5.
+At position 24 to 65, the domain is characterized as CHCH.
+At position 33 to 247, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 178, the domain is characterized as FAD-binding PCMH-type.
+At position 452 to 693, the domain is characterized as ABC transporter.
+At position 1 to 35, the domain is characterized as Rubredoxin-like.
+At position 52 to 181, the domain is characterized as Ferritin-like diiron.
+At position 317 to 540, the domain is characterized as TLDc.
+At position 4 to 254, the domain is characterized as Pyruvate carboxyltransferase.
+At position 146 to 388, the domain is characterized as Protein kinase.
+At position 127 to 249, the domain is characterized as MPN.
+At position 166 to 286, the domain is characterized as Fe2OG dioxygenase.
+At position 1203 to 1327, the domain is characterized as C2 1.
+At position 1637 to 1780, the domain is characterized as MHD1.
+At position 1886 to 2028, the domain is characterized as MHD2.
+At position 2044 to 2169, the domain is characterized as C2 2.
+At position 94 to 129, the domain is characterized as EF-hand 2.
+At position 130 to 165, the domain is characterized as EF-hand 3.
+At position 285 to 454, the domain is characterized as tr-type G.
+At position 10 to 68, the domain is characterized as CBS 1.
+At position 88 to 148, the domain is characterized as CBS 2.
+At position 152 to 207, the domain is characterized as CBS 3.
+At position 226 to 284, the domain is characterized as CBS 4.
+At position 1 to 68, the domain is characterized as S4 RNA-binding.
+At position 8 to 170, the domain is characterized as Tyrosine-protein phosphatase.
+At position 293 to 357, the domain is characterized as Mop.
+At position 13 to 205, the domain is characterized as Lon N-terminal.
+At position 603 to 803, the domain is characterized as Lon proteolytic.
+At position 93 to 377, the domain is characterized as ABC transmembrane type-1 1.
+At position 410 to 633, the domain is characterized as ABC transporter 1.
+At position 714 to 1005, the domain is characterized as ABC transmembrane type-1 2.
+At position 1041 to 1274, the domain is characterized as ABC transporter 2.
+At position 22 to 64, the domain is characterized as Chitin-binding type-1.
+At position 72 to 193, the domain is characterized as Barwin.
+At position 82 to 197, the domain is characterized as Expansin-like EG45.
+At position 207 to 287, the domain is characterized as Expansin-like CBD.
+At position 47 to 349, the domain is characterized as AB hydrolase-1.
+At position 120 to 415, the domain is characterized as Protein kinase.
+At position 344 to 534, the domain is characterized as Integrase catalytic.
+At position 2 to 80, the domain is characterized as DED 1.
+At position 100 to 177, the domain is characterized as DED 2.
+At position 7 to 287, the domain is characterized as tr-type G.
+At position 2 to 186, the domain is characterized as Glutamine amidotransferase type-2.
+At position 37 to 226, the domain is characterized as Exonuclease.
+At position 9 to 228, the domain is characterized as ABC transporter.
+At position 206 to 493, the domain is characterized as GT23.
+At position 502 to 563, the domain is characterized as SH3.
+At position 22 to 101, the domain is characterized as Importin N-terminal.
+At position 92 to 262, the domain is characterized as HD.
+At position 432 to 607, the domain is characterized as Rab-GAP TBC.
+At position 217 to 273, the domain is characterized as J.
+At position 46 to 163, the domain is characterized as CUB.
+At position 1 to 283, the domain is characterized as 5'-3' exonuclease.
+At position 70 to 137, the domain is characterized as POTRA 1.
+At position 138 to 214, the domain is characterized as POTRA 2.
+At position 219 to 309, the domain is characterized as POTRA 3.
+At position 312 to 391, the domain is characterized as POTRA 4.
+At position 394 to 466, the domain is characterized as POTRA 5.
+At position 422 to 529, the domain is characterized as Fe2OG dioxygenase.
+At position 60 to 336, the domain is characterized as GH84.
+At position 65 to 479, the domain is characterized as Peptidase A1.
+At position 927 to 1093, the domain is characterized as PNPLA.
+At position 231 to 404, the domain is characterized as TrmE-type G.
+At position 29 to 219, the domain is characterized as RNase H type-2.
+At position 61 to 137, the domain is characterized as J.
+At position 9 to 91, the domain is characterized as Phosphagen kinase N-terminal.
+At position 119 to 356, the domain is characterized as Phosphagen kinase C-terminal.
+At position 18 to 105, the domain is characterized as RRM.
+At position 23 to 114, the domain is characterized as Ig-like C1-type.
+At position 41 to 147, the domain is characterized as Expansin-like EG45.
+At position 161 to 244, the domain is characterized as Expansin-like CBD.
+At position 635 to 1179, the domain is characterized as WAPL.
+At position 8 to 299, the domain is characterized as YjeF C-terminal.
+At position 18 to 171, the domain is characterized as Nudix hydrolase.
+At position 112 to 345, the domain is characterized as Radical SAM core.
+At position 238 to 265, the domain is characterized as PLD phosphodiesterase 1.
+At position 422 to 449, the domain is characterized as PLD phosphodiesterase 2.
+At position 6 to 89, the domain is characterized as Phosphagen kinase N-terminal.
+At position 115 to 358, the domain is characterized as Phosphagen kinase C-terminal.
+At position 4 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 54 to 228, the domain is characterized as FAD-binding PCMH-type.
+At position 49 to 184, the domain is characterized as HTH marR-type.
+At position 284 to 359, the domain is characterized as B5.
+At position 321 to 404, the domain is characterized as Toprim.
+At position 31 to 133, the domain is characterized as Cadherin 1.
+At position 243 to 347, the domain is characterized as Cadherin 3.
+At position 348 to 452, the domain is characterized as Cadherin 4.
+At position 453 to 562, the domain is characterized as Cadherin 5.
+At position 570 to 675, the domain is characterized as Cadherin 6.
+At position 520 to 793, the domain is characterized as Protein kinase.
+At position 72 to 139, the domain is characterized as BTB.
+At position 174 to 276, the domain is characterized as BACK.
+At position 4 to 87, the domain is characterized as Toprim.
+At position 10 to 128, the domain is characterized as Arf-GAP.
+At position 1 to 156, the domain is characterized as Obg.
+At position 157 to 334, the domain is characterized as OBG-type G.
+At position 342 to 419, the domain is characterized as OCT.
+At position 49 to 183, the domain is characterized as Thioredoxin.
+At position 76 to 360, the domain is characterized as Protein kinase.
+At position 7 to 203, the domain is characterized as tr-type G.
+At position 27 to 153, the domain is characterized as Arf-GAP.
+At position 9 to 410, the domain is characterized as PTS EIIC type-3.
+At position 467 to 570, the domain is characterized as PTS EIIB type-3.
+At position 16 to 208, the domain is characterized as Lon N-terminal.
+At position 597 to 778, the domain is characterized as Lon proteolytic.
+At position 438 to 563, the domain is characterized as DBINO.
+At position 684 to 856, the domain is characterized as Helicase ATP-binding.
+At position 1240 to 1387, the domain is characterized as Helicase C-terminal.
+At position 38 to 138, the domain is characterized as Ig-like V-type.
+At position 185 to 213, the domain is characterized as ITAM.
+At position 4 to 139, the domain is characterized as ADF-H 1.
+At position 177 to 313, the domain is characterized as ADF-H 2.
+At position 217 to 244, the domain is characterized as PLD phosphodiesterase 1.
+At position 395 to 422, the domain is characterized as PLD phosphodiesterase 2.
+At position 531 to 606, the domain is characterized as Cytochrome b5 heme-binding.
+At position 647 to 759, the domain is characterized as FAD-binding FR-type.
+At position 283 to 403, the domain is characterized as Nop.
+At position 247 to 321, the domain is characterized as POU-specific.
+At position 30 to 110, the domain is characterized as ACT 1.
+At position 120 to 207, the domain is characterized as ACT 2.
+At position 250 to 326, the domain is characterized as ACT 3.
+At position 328 to 402, the domain is characterized as ACT 4.
+At position 6 to 259, the domain is characterized as ABC transporter.
+At position 284 to 442, the domain is characterized as SSD.
+At position 143 to 338, the domain is characterized as ATP-grasp 1.
+At position 689 to 880, the domain is characterized as ATP-grasp 2.
+At position 953 to 1093, the domain is characterized as MGS-like.
+At position 171 to 381, the domain is characterized as ATP-grasp.
+At position 13 to 182, the domain is characterized as N-acetyltransferase.
+At position 15 to 231, the domain is characterized as ABC transporter.
+At position 17 to 179, the domain is characterized as UBC core.
+At position 194 to 368, the domain is characterized as EngA-type G 2.
+At position 369 to 453, the domain is characterized as KH-like.
+At position 339 to 400, the domain is characterized as S4 RNA-binding.
+At position 350 to 585, the domain is characterized as Histidine kinase.
+At position 611 to 729, the domain is characterized as Response regulatory.
+At position 19 to 117, the domain is characterized as HTH araC/xylS-type.
+At position 32 to 86, the domain is characterized as Kazal-like.
+At position 8 to 190, the domain is characterized as YrdC-like.
+At position 6 to 74, the domain is characterized as MIB/HERC2 1.
+At position 143 to 221, the domain is characterized as MIB/HERC2 2.
+At position 108 to 341, the domain is characterized as Radical SAM core.
+At position 4 to 278, the domain is characterized as EndoU.
+At position 451 to 521, the domain is characterized as Bromo.
+At position 92 to 163, the domain is characterized as PRC barrel.
+At position 558 to 658, the domain is characterized as tRNA-binding.
+At position 25 to 83, the domain is characterized as Chitin-binding type-2 1.
+At position 86 to 143, the domain is characterized as Chitin-binding type-2 2.
+At position 153 to 210, the domain is characterized as Chitin-binding type-2 3.
+At position 224 to 292, the domain is characterized as Chitin-binding type-2 4.
+At position 294 to 360, the domain is characterized as Chitin-binding type-2 5.
+At position 57 to 117, the domain is characterized as Sushi 1.
+At position 118 to 176, the domain is characterized as Sushi 2.
+At position 177 to 259, the domain is characterized as HYR.
+At position 260 to 319, the domain is characterized as Sushi 3.
+At position 21 to 98, the domain is characterized as Toprim.
+At position 187 to 911, the domain is characterized as TBDR beta-barrel.
+At position 20 to 301, the domain is characterized as Deacetylase sirtuin-type.
+At position 30 to 157, the domain is characterized as NtA.
+At position 191 to 244, the domain is characterized as Kazal-like 1.
+At position 264 to 319, the domain is characterized as Kazal-like 2.
+At position 337 to 391, the domain is characterized as Kazal-like 3.
+At position 408 to 463, the domain is characterized as Kazal-like 4.
+At position 484 to 536, the domain is characterized as Kazal-like 5.
+At position 540 to 601, the domain is characterized as Kazal-like 6.
+At position 607 to 666, the domain is characterized as Kazal-like 7.
+At position 699 to 752, the domain is characterized as Kazal-like 8.
+At position 793 to 846, the domain is characterized as Laminin EGF-like 1.
+At position 847 to 893, the domain is characterized as Laminin EGF-like 2.
+At position 917 to 971, the domain is characterized as Kazal-like 9.
+At position 1130 to 1252, the domain is characterized as SEA.
+At position 1329 to 1367, the domain is characterized as EGF-like 1.
+At position 1372 to 1548, the domain is characterized as Laminin G-like 1.
+At position 1549 to 1586, the domain is characterized as EGF-like 2.
+At position 1588 to 1625, the domain is characterized as EGF-like 3.
+At position 1635 to 1822, the domain is characterized as Laminin G-like 2.
+At position 1818 to 1857, the domain is characterized as EGF-like 4.
+At position 1868 to 2065, the domain is characterized as Laminin G-like 3.
+At position 635 to 738, the domain is characterized as tRNA-binding.
+At position 70 to 135, the domain is characterized as NAC-A/B.
+At position 177 to 217, the domain is characterized as UBA.
+At position 21 to 467, the domain is characterized as Hexokinase.
+At position 18 to 90, the domain is characterized as PAS.
+At position 93 to 145, the domain is characterized as PAC.
+At position 67 to 295, the domain is characterized as Radical SAM core.
+At position 7 to 79, the domain is characterized as J.
+At position 2 to 128, the domain is characterized as PINc.
+At position 28 to 294, the domain is characterized as Dynamin-type G.
+At position 519 to 625, the domain is characterized as PH.
+At position 659 to 750, the domain is characterized as GED.
+At position 15 to 96, the domain is characterized as PB1.
+At position 170 to 429, the domain is characterized as Protein kinase.
+At position 518 to 564, the domain is characterized as F-box.
+At position 28 to 131, the domain is characterized as Cystatin kininogen-type 1.
+At position 150 to 253, the domain is characterized as Cystatin kininogen-type 2.
+At position 272 to 375, the domain is characterized as Cystatin kininogen-type 3.
+At position 6 to 203, the domain is characterized as tr-type G.
+At position 492 to 686, the domain is characterized as Helicase C-terminal.
+At position 72 to 213, the domain is characterized as Helicase ATP-binding.
+At position 214 to 388, the domain is characterized as Helicase C-terminal.
+At position 17 to 144, the domain is characterized as Nudix hydrolase.
+At position 19 to 89, the domain is characterized as LCN-type CS-alpha/beta.
+At position 186 to 271, the domain is characterized as PDZ.
+At position 71 to 263, the domain is characterized as ABC transmembrane type-1.
+At position 3 to 110, the domain is characterized as PH.
+At position 180 to 392, the domain is characterized as START.
+At position 22 to 59, the domain is characterized as Pacifastin 1.
+At position 62 to 97, the domain is characterized as Pacifastin 2.
+At position 1 to 179, the domain is characterized as CheB-type methylesterase.
+At position 45 to 149, the domain is characterized as FAD-binding FR-type.
+At position 624 to 801, the domain is characterized as Helicase ATP-binding.
+At position 901 to 1076, the domain is characterized as Helicase C-terminal.
+At position 387 to 554, the domain is characterized as tr-type G.
+At position 10 to 206, the domain is characterized as Peptidase M12B.
+At position 214 to 300, the domain is characterized as Disintegrin.
+At position 11 to 322, the domain is characterized as IF rod.
+At position 17 to 70, the domain is characterized as LIM zinc-binding 1.
+At position 79 to 133, the domain is characterized as LIM zinc-binding 2.
+At position 6 to 116, the domain is characterized as MTTase N-terminal.
+At position 135 to 373, the domain is characterized as Radical SAM core.
+At position 376 to 440, the domain is characterized as TRAM.
+At position 208 to 286, the domain is characterized as RRM.
+At position 1 to 65, the domain is characterized as S4 RNA-binding.
+At position 29 to 76, the domain is characterized as KH.
+At position 20 to 122, the domain is characterized as Rieske.
+At position 488 to 598, the domain is characterized as OCEL.
+At position 185 to 277, the domain is characterized as CS.
+At position 582 to 688, the domain is characterized as Cadherin 6.
+At position 405 to 617, the domain is characterized as N-acetyltransferase.
+At position 79 to 127, the domain is characterized as F-box.
+At position 138 to 330, the domain is characterized as B30.2/SPRY.
+At position 133 to 161, the domain is characterized as KOW.
+At position 210 to 273, the domain is characterized as bZIP.
+At position 29 to 133, the domain is characterized as Cadherin 1.
+At position 570 to 682, the domain is characterized as Cadherin 6.
+At position 90 to 401, the domain is characterized as IF rod.
+At position 1 to 106, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 35 to 269, the domain is characterized as AB hydrolase-1.
+At position 18 to 141, the domain is characterized as RNase III.
+At position 6 to 92, the domain is characterized as MtN3/slv 1.
+At position 129 to 212, the domain is characterized as MtN3/slv 2.
+At position 55 to 163, the domain is characterized as sHSP.
+At position 1 to 113, the domain is characterized as BMC circularly permuted 1.
+At position 114 to 215, the domain is characterized as BMC circularly permuted 2.
+At position 37 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 216, the domain is characterized as Ig-like C2-type 2.
+At position 220 to 314, the domain is characterized as Ig-like C2-type 3.
+At position 25 to 272, the domain is characterized as Protein kinase.
+At position 167 to 217, the domain is characterized as DHHC.
+At position 2 to 190, the domain is characterized as ABC transporter.
+At position 6 to 192, the domain is characterized as DOC.
+At position 401 to 582, the domain is characterized as RHD.
+At position 586 to 683, the domain is characterized as IPT/TIG.
+At position 1 to 52, the domain is characterized as Rubredoxin-like.
+At position 126 to 398, the domain is characterized as Peptidase S8.
+At position 32 to 126, the domain is characterized as PpiC.
+At position 31 to 166, the domain is characterized as MPN.
+At position 20 to 172, the domain is characterized as NAC.
+At position 13 to 166, the domain is characterized as Tyrosine-protein phosphatase.
+At position 48 to 218, the domain is characterized as PCI.
+At position 109 to 180, the domain is characterized as S4 RNA-binding.
+At position 2 to 62, the domain is characterized as HTH tetR-type.
+At position 287 to 461, the domain is characterized as Helicase ATP-binding.
+At position 491 to 635, the domain is characterized as Helicase C-terminal.
+At position 278 to 362, the domain is characterized as Ig-like C2-type 1.
+At position 412 to 503, the domain is characterized as Ig-like C2-type 2.
+At position 511 to 601, the domain is characterized as Ig-like C2-type 3.
+At position 3 to 35, the domain is characterized as LisH.
+At position 1 to 108, the domain is characterized as Thioredoxin.
+At position 125 to 227, the domain is characterized as Glutaredoxin 1.
+At position 227 to 326, the domain is characterized as Glutaredoxin 2.
+At position 60 to 210, the domain is characterized as Cupin type-1.
+At position 559 to 619, the domain is characterized as KH.
+At position 629 to 696, the domain is characterized as S1 motif.
+At position 1 to 167, the domain is characterized as FeoB-type G.
+At position 142 to 192, the domain is characterized as bHLH.
+At position 4 to 145, the domain is characterized as Flavodoxin-like.
+At position 1 to 81, the domain is characterized as Glutaredoxin.
+At position 131 to 361, the domain is characterized as Radical SAM core.
+At position 364 to 430, the domain is characterized as TRAM.
+At position 91 to 127, the domain is characterized as LRRNT.
+At position 2 to 417, the domain is characterized as SAM-dependent MTase C5-type.
+At position 49 to 272, the domain is characterized as Radical SAM core.
+At position 348 to 430, the domain is characterized as OCT.
+At position 98 to 326, the domain is characterized as Radical SAM core.
+At position 280 to 494, the domain is characterized as B30.2/SPRY.
+At position 1 to 102, the domain is characterized as KaiA C-terminal.
+At position 1 to 92, the domain is characterized as PE.
+At position 151 to 259, the domain is characterized as Gnk2-homologous 2.
+At position 353 to 419, the domain is characterized as S4 RNA-binding.
+At position 70 to 217, the domain is characterized as Thioredoxin.
+At position 45 to 126, the domain is characterized as RRM 1.
+At position 134 to 214, the domain is characterized as RRM 2.
+At position 400 to 478, the domain is characterized as RRM 3.
+At position 30 to 115, the domain is characterized as Ig-like 1.
+At position 139 to 226, the domain is characterized as Ig-like 2.
+At position 228 to 320, the domain is characterized as Ig-like 3.
+At position 324 to 415, the domain is characterized as Ig-like 4.
+At position 420 to 504, the domain is characterized as Ig-like 5.
+At position 512 to 604, the domain is characterized as Fibronectin type-III 1.
+At position 614 to 708, the domain is characterized as Fibronectin type-III 2.
+At position 108 to 310, the domain is characterized as ATP-grasp.
+At position 1 to 102, the domain is characterized as C2 1.
+At position 249 to 421, the domain is characterized as VASt 1.
+At position 517 to 635, the domain is characterized as C2 2.
+At position 689 to 752, the domain is characterized as GRAM.
+At position 848 to 1010, the domain is characterized as VASt 2.
+At position 71 to 181, the domain is characterized as Thioredoxin.
+At position 86 to 784, the domain is characterized as Myosin motor.
+At position 787 to 816, the domain is characterized as IQ.
+At position 3 to 86, the domain is characterized as RRM 1.
+At position 96 to 175, the domain is characterized as RRM 2.
+At position 18 to 89, the domain is characterized as Sm.
+At position 155 to 424, the domain is characterized as NR LBD.
+At position 2 to 218, the domain is characterized as Peptidase S1.
+At position 493 to 515, the domain is characterized as GoLoco 1.
+At position 546 to 568, the domain is characterized as GoLoco 2.
+At position 594 to 616, the domain is characterized as GoLoco 3.
+At position 628 to 650, the domain is characterized as GoLoco 4.
+At position 379 to 488, the domain is characterized as Rhodanese.
+At position 244 to 333, the domain is characterized as EH 1.
+At position 277 to 312, the domain is characterized as EF-hand 1.
+At position 513 to 602, the domain is characterized as EH 2.
+At position 546 to 581, the domain is characterized as EF-hand 2.
+At position 1500 to 1517, the domain is characterized as WH2.
+At position 190 to 245, the domain is characterized as bHLH.
+At position 131 to 343, the domain is characterized as ATP-grasp 1.
+At position 947 to 1042, the domain is characterized as MGS-like.
+At position 27 to 80, the domain is characterized as bHLH.
+At position 120 to 173, the domain is characterized as PAS 1.
+At position 281 to 336, the domain is characterized as PAS 2.
+At position 346 to 384, the domain is characterized as PAC.
+At position 21 to 250, the domain is characterized as Peptidase S1.
+At position 15 to 136, the domain is characterized as FAD-binding FR-type.
+At position 5 to 77, the domain is characterized as J.
+At position 348 to 561, the domain is characterized as TLDc.
+At position 32 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 7 to 248, the domain is characterized as ABC transporter.
+At position 9 to 192, the domain is characterized as tr-type G.
+At position 6 to 87, the domain is characterized as NAB.
+At position 127 to 358, the domain is characterized as Radical SAM core.
+At position 361 to 430, the domain is characterized as TRAM.
+At position 18 to 248, the domain is characterized as BAR.
+At position 305 to 364, the domain is characterized as SH3.
+At position 5 to 127, the domain is characterized as RNase III.
+At position 154 to 224, the domain is characterized as DRBM.
+At position 14 to 285, the domain is characterized as F-BAR.
+At position 374 to 560, the domain is characterized as Rho-GAP.
+At position 111 to 255, the domain is characterized as VPS9.
+At position 3 to 247, the domain is characterized as KaiC.
+At position 19 to 337, the domain is characterized as Protein kinase.
+At position 39 to 275, the domain is characterized as Radical SAM core.
+At position 21 to 138, the domain is characterized as MTTase N-terminal.
+At position 161 to 395, the domain is characterized as Radical SAM core.
+At position 397 to 460, the domain is characterized as TRAM.
+At position 27 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 205, the domain is characterized as Ig-like C2-type 2.
+At position 212 to 308, the domain is characterized as Ig-like C2-type 3.
+At position 317 to 410, the domain is characterized as Ig-like C2-type 4.
+At position 413 to 507, the domain is characterized as Ig-like C2-type 5.
+At position 585 to 933, the domain is characterized as Protein kinase.
+At position 135 to 200, the domain is characterized as HTH luxR-type.
+At position 57 to 87, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 154 to 428, the domain is characterized as ABC transporter 1.
+At position 505 to 718, the domain is characterized as ABC transmembrane type-2 1.
+At position 838 to 1090, the domain is characterized as ABC transporter 2.
+At position 1163 to 1380, the domain is characterized as ABC transmembrane type-2 2.
+At position 30 to 209, the domain is characterized as Eph LBD.
+At position 328 to 439, the domain is characterized as Fibronectin type-III 1.
+At position 440 to 537, the domain is characterized as Fibronectin type-III 2.
+At position 621 to 882, the domain is characterized as Protein kinase.
+At position 911 to 975, the domain is characterized as SAM.
+At position 5 to 103, the domain is characterized as BMC circularly permuted.
+At position 41 to 86, the domain is characterized as Gla.
+At position 125 to 165, the domain is characterized as EGF-like 2.
+At position 239 to 470, the domain is characterized as Peptidase S1.
+At position 283 to 488, the domain is characterized as B30.2/SPRY.
+At position 58 to 93, the domain is characterized as EF-hand 2.
+At position 105 to 140, the domain is characterized as EF-hand 3.
+At position 149 to 184, the domain is characterized as EF-hand 4.
+At position 197 to 232, the domain is characterized as EF-hand 5.
+At position 240 to 276, the domain is characterized as EF-hand 6.
+At position 5 to 136, the domain is characterized as RNase III.
+At position 163 to 232, the domain is characterized as DRBM.
+At position 223 to 433, the domain is characterized as Helicase ATP-binding.
+At position 485 to 635, the domain is characterized as Helicase C-terminal.
+At position 2 to 221, the domain is characterized as Glutamine amidotransferase type-2.
+At position 286 to 426, the domain is characterized as SIS 1.
+At position 10 to 139, the domain is characterized as MH1.
+At position 197 to 393, the domain is characterized as MH2.
+At position 14 to 61, the domain is characterized as Death.
+At position 38 to 112, the domain is characterized as H15.
+At position 401 to 479, the domain is characterized as ACT 1.
+At position 481 to 544, the domain is characterized as ACT 2.
+At position 11 to 78, the domain is characterized as HTH gntR-type.
+At position 69 to 224, the domain is characterized as BUB1 N-terminal.
+At position 28 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 451 to 540, the domain is characterized as EH.
+At position 12 to 219, the domain is characterized as Cytochrome b561.
+At position 29 to 230, the domain is characterized as ABC transmembrane type-1.
+At position 72 to 210, the domain is characterized as Flavodoxin-like.
+At position 244 to 458, the domain is characterized as FAD-binding FR-type.
+At position 52 to 305, the domain is characterized as Protein kinase.
+At position 211 to 283, the domain is characterized as KRAB.
+At position 560 to 677, the domain is characterized as Toprim.
+At position 15 to 132, the domain is characterized as Response regulatory.
+At position 172 to 367, the domain is characterized as CheB-type methylesterase.
+At position 418 to 512, the domain is characterized as PH 2.
+At position 614 to 851, the domain is characterized as ABC transporter.
+At position 216 to 394, the domain is characterized as VWFA.
+At position 10 to 90, the domain is characterized as Sm.
+At position 463 to 632, the domain is characterized as tr-type G.
+At position 66 to 259, the domain is characterized as HD.
+At position 6 to 247, the domain is characterized as ABC transporter.
+At position 246 to 439, the domain is characterized as GATase cobBQ-type.
+At position 31 to 207, the domain is characterized as BPL/LPL catalytic.
+At position 287 to 512, the domain is characterized as tr-type G.
+At position 56 to 138, the domain is characterized as Lipoyl-binding.
+At position 1 to 235, the domain is characterized as Deacetylase sirtuin-type.
+At position 35 to 192, the domain is characterized as Helicase ATP-binding.
+At position 439 to 605, the domain is characterized as Helicase C-terminal.
+At position 10 to 176, the domain is characterized as N-acetyltransferase.
+At position 306 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 165 to 334, the domain is characterized as PCI.
+At position 48 to 83, the domain is characterized as EF-hand 2.
+At position 88 to 123, the domain is characterized as EF-hand 3.
+At position 124 to 159, the domain is characterized as EF-hand 4.
+At position 2 to 67, the domain is characterized as J.
+At position 8 to 243, the domain is characterized as ABC transporter.
+At position 143 to 208, the domain is characterized as HTH luxR-type.
+At position 40 to 110, the domain is characterized as KH type-2.
+At position 90 to 169, the domain is characterized as PRC barrel.
+At position 258 to 535, the domain is characterized as ABC transmembrane type-1 1.
+At position 607 to 835, the domain is characterized as ABC transporter 1.
+At position 932 to 1193, the domain is characterized as ABC transmembrane type-1 2.
+At position 1230 to 1461, the domain is characterized as ABC transporter 2.
+At position 208 to 252, the domain is characterized as TSP type-1.
+At position 279 to 442, the domain is characterized as AMOP.
+At position 103 to 167, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 12 to 155, the domain is characterized as RNase H type-1.
+At position 1557 to 1956, the domain is characterized as USP.
+At position 108 to 194, the domain is characterized as PDZ.
+At position 1 to 107, the domain is characterized as C2.
+At position 380 to 634, the domain is characterized as Protein kinase.
+At position 635 to 706, the domain is characterized as AGC-kinase C-terminal.
+At position 83 to 135, the domain is characterized as bHLH.
+At position 16 to 93, the domain is characterized as Ubiquitin-like.
+At position 159 to 278, the domain is characterized as C2 1.
+At position 292 to 425, the domain is characterized as C2 2.
+At position 170 to 357, the domain is characterized as Glutamine amidotransferase type-1.
+At position 105 to 476, the domain is characterized as PTS EIIC type-1.
+At position 506 to 610, the domain is characterized as PTS EIIA type-1.
+At position 36 to 104, the domain is characterized as BTB.
+At position 142 to 240, the domain is characterized as BACK.
+At position 22 to 110, the domain is characterized as WSC.
+At position 288 to 560, the domain is characterized as Radical SAM core.
+At position 340 to 510, the domain is characterized as tr-type G.
+At position 6 to 458, the domain is characterized as Helicase ATP-binding.
+At position 209 to 345, the domain is characterized as KARI C-terminal knotted 1.
+At position 346 to 486, the domain is characterized as KARI C-terminal knotted 2.
+At position 35 to 127, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 130 to 269, the domain is characterized as FAD-binding FR-type.
+At position 318 to 398, the domain is characterized as PDZ.
+At position 99 to 179, the domain is characterized as PRC barrel.
+At position 422 to 550, the domain is characterized as RCK N-terminal.
+At position 1167 to 1460, the domain is characterized as Autotransporter.
+At position 36 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 221, the domain is characterized as Ig-like C2-type 2.
+At position 236 to 322, the domain is characterized as Ig-like C2-type 3.
+At position 418 to 506, the domain is characterized as Ig-like C2-type 5.
+At position 510 to 597, the domain is characterized as Ig-like C2-type 6.
+At position 603 to 698, the domain is characterized as Fibronectin type-III 1.
+At position 700 to 804, the domain is characterized as Fibronectin type-III 2.
+At position 809 to 930, the domain is characterized as Fibronectin type-III 3.
+At position 934 to 1021, the domain is characterized as Fibronectin type-III 4.
+At position 1022 to 1118, the domain is characterized as Fibronectin type-III 5.
+At position 432 to 599, the domain is characterized as tr-type G.
+At position 20 to 132, the domain is characterized as HotDog ACOT-type.
+At position 4 to 286, the domain is characterized as DegV.
+At position 38 to 142, the domain is characterized as Calponin-homology (CH) 1.
+At position 151 to 257, the domain is characterized as Calponin-homology (CH) 2.
+At position 753 to 788, the domain is characterized as EF-hand 1.
+At position 789 to 824, the domain is characterized as EF-hand 2.
+At position 245 to 500, the domain is characterized as Protein kinase.
+At position 502 to 573, the domain is characterized as AGC-kinase C-terminal.
+At position 74 to 405, the domain is characterized as Asparaginase/glutaminase.
+At position 246 to 466, the domain is characterized as Histidine kinase.
+At position 150 to 322, the domain is characterized as FAD-binding PCMH-type.
+At position 277 to 332, the domain is characterized as F-box.
+At position 119 to 217, the domain is characterized as SH2.
+At position 17 to 116, the domain is characterized as CBM39.
+At position 188 to 495, the domain is characterized as GH16.
+At position 17 to 70, the domain is characterized as bHLH.
+At position 85 to 157, the domain is characterized as PAS 1.
+At position 229 to 300, the domain is characterized as PAS 2.
+At position 303 to 346, the domain is characterized as PAC.
+At position 4 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 54 to 278, the domain is characterized as Radical SAM core.
+At position 5 to 286, the domain is characterized as CN hydrolase.
+At position 138 to 368, the domain is characterized as Histidine kinase.
+At position 56 to 128, the domain is characterized as RRM.
+At position 491 to 549, the domain is characterized as PAP-associated.
+At position 6 to 239, the domain is characterized as ABC transporter.
+At position 62 to 255, the domain is characterized as HD.
+At position 4 to 126, the domain is characterized as C2.
+At position 193 to 226, the domain is characterized as WW 1.
+At position 385 to 418, the domain is characterized as WW 2.
+At position 497 to 530, the domain is characterized as WW 3.
+At position 548 to 581, the domain is characterized as WW 4.
+At position 640 to 974, the domain is characterized as HECT.
+At position 58 to 236, the domain is characterized as Helicase ATP-binding.
+At position 247 to 489, the domain is characterized as Helicase C-terminal.
+At position 5 to 241, the domain is characterized as ABC transporter 1.
+At position 251 to 498, the domain is characterized as ABC transporter 2.
+At position 153 to 256, the domain is characterized as FAD-binding FR-type.
+At position 1 to 110, the domain is characterized as OCIA.
+At position 164 to 338, the domain is characterized as VWFA.
+At position 30 to 81, the domain is characterized as HTH myb-type 1.
+At position 82 to 137, the domain is characterized as HTH myb-type 2.
+At position 138 to 188, the domain is characterized as HTH myb-type 3.
+At position 18 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 3 to 420, the domain is characterized as F-BAR.
+At position 213 to 296, the domain is characterized as DEP.
+At position 454 to 650, the domain is characterized as Rho-GAP.
+At position 53 to 303, the domain is characterized as Protein kinase.
+At position 41 to 192, the domain is characterized as PI-PLC X-box.
+At position 41 to 232, the domain is characterized as RGSL.
+At position 416 to 605, the domain is characterized as DH.
+At position 647 to 760, the domain is characterized as PH.
+At position 124 to 218, the domain is characterized as Rhodanese.
+At position 421 to 554, the domain is characterized as Guanylate cyclase.
+At position 21 to 104, the domain is characterized as RRM 1.
+At position 152 to 235, the domain is characterized as RRM 2.
+At position 231 to 454, the domain is characterized as Fibrinogen C-terminal.
+At position 71 to 310, the domain is characterized as AB hydrolase-1.
+At position 53 to 104, the domain is characterized as bHLH.
+At position 1 to 116, the domain is characterized as MTTase N-terminal.
+At position 134 to 365, the domain is characterized as Radical SAM core.
+At position 367 to 430, the domain is characterized as TRAM.
+At position 28 to 349, the domain is characterized as Kinesin motor.
+At position 6 to 233, the domain is characterized as ABC transporter.
+At position 7 to 58, the domain is characterized as F-box.
+At position 48 to 112, the domain is characterized as Disintegrin.
+At position 24 to 71, the domain is characterized as TSP type-1 1.
+At position 236 to 292, the domain is characterized as TSP type-1 2.
+At position 294 to 510, the domain is characterized as TSP type-1 3.
+At position 512 to 572, the domain is characterized as TSP type-1 4.
+At position 576 to 635, the domain is characterized as TSP type-1 5.
+At position 637 to 732, the domain is characterized as Ig-like C2-type.
+At position 811 to 873, the domain is characterized as TSP type-1 6.
+At position 932 to 990, the domain is characterized as TSP type-1 7.
+At position 1004 to 1041, the domain is characterized as PLAC.
+At position 5 to 48, the domain is characterized as SpoVT-AbrB 1.
+At position 1 to 20, the domain is characterized as Peptidase S1.
+At position 37 to 258, the domain is characterized as ABC transmembrane type-2.
+At position 5 to 79, the domain is characterized as ACT.
+At position 108 to 420, the domain is characterized as IF rod.
+At position 25 to 121, the domain is characterized as PH.
+At position 179 to 273, the domain is characterized as SH2.
+At position 34 to 112, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 112 to 151, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 251 to 307, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 3 to 61, the domain is characterized as LIM zinc-binding 1.
+At position 62 to 125, the domain is characterized as LIM zinc-binding 2.
+At position 1 to 90, the domain is characterized as PE.
+At position 105 to 305, the domain is characterized as ATP-grasp.
+At position 101 to 120, the domain is characterized as SAP 1.
+At position 250 to 264, the domain is characterized as SAP 2.
+At position 181 to 213, the domain is characterized as EGF-like 1.
+At position 391 to 423, the domain is characterized as EGF-like 2.
+At position 549 to 601, the domain is characterized as TB 1.
+At position 618 to 658, the domain is characterized as EGF-like 3; calcium-binding.
+At position 669 to 721, the domain is characterized as TB 2.
+At position 865 to 906, the domain is characterized as EGF-like 4; calcium-binding.
+At position 907 to 948, the domain is characterized as EGF-like 5; calcium-binding.
+At position 949 to 989, the domain is characterized as EGF-like 6; calcium-binding.
+At position 990 to 1029, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1030 to 1070, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1071 to 1111, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1112 to 1152, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1153 to 1193, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1194 to 1235, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1236 to 1277, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1278 to 1320, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1338 to 1392, the domain is characterized as TB 3.
+At position 1415 to 1457, the domain is characterized as EGF-like 15; calcium-binding.
+At position 1458 to 1498, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1515 to 1568, the domain is characterized as TB 4.
+At position 1612 to 1652, the domain is characterized as EGF-like 17.
+At position 1653 to 1697, the domain is characterized as EGF-like 18; calcium-binding.
+At position 59 to 103, the domain is characterized as LysM.
+At position 111 to 344, the domain is characterized as Radical SAM core.
+At position 137 to 175, the domain is characterized as LRRCT.
+At position 142 to 223, the domain is characterized as UPAR/Ly6.
+At position 381 to 456, the domain is characterized as Ubiquitin-like 6.
+At position 148 to 258, the domain is characterized as ELM2.
+At position 265 to 317, the domain is characterized as SANT.
+At position 102 to 200, the domain is characterized as HTH araC/xylS-type.
+At position 2 to 103, the domain is characterized as Glutaredoxin.
+At position 1 to 45, the domain is characterized as CSD.
+At position 8 to 306, the domain is characterized as YjeF C-terminal.
+At position 93 to 310, the domain is characterized as RNase H type-2.
+At position 574 to 670, the domain is characterized as BTB 1.
+At position 801 to 870, the domain is characterized as BTB 2.
+At position 172 to 257, the domain is characterized as PPIase FKBP-type.
+At position 7 to 97, the domain is characterized as GIY-YIG.
+At position 21 to 288, the domain is characterized as Protein kinase.
+At position 778 to 1070, the domain is characterized as CNH.
+At position 400 to 1143, the domain is characterized as Myosin motor.
+At position 1145 to 1174, the domain is characterized as IQ.
+At position 62 to 180, the domain is characterized as sHSP.
+At position 52 to 110, the domain is characterized as TCP.
+At position 70 to 83, the domain is characterized as CRIB.
+At position 268 to 519, the domain is characterized as Protein kinase.
+At position 25 to 158, the domain is characterized as MPN.
+At position 81 to 142, the domain is characterized as SH3.
+At position 148 to 245, the domain is characterized as SH2.
+At position 270 to 523, the domain is characterized as Protein kinase.
+At position 176 to 417, the domain is characterized as MHD.
+At position 62 to 129, the domain is characterized as CSD.
+At position 32 to 304, the domain is characterized as Septin-type G.
+At position 58 to 289, the domain is characterized as Dynamin-type G.
+At position 447 to 535, the domain is characterized as EH.
+At position 479 to 514, the domain is characterized as EF-hand.
+At position 200 to 467, the domain is characterized as SF4 helicase.
+At position 1014 to 1321, the domain is characterized as Calpain catalytic.
+At position 192 to 485, the domain is characterized as Protein kinase.
+At position 1 to 156, the domain is characterized as N-acetyltransferase 1.
+At position 149 to 299, the domain is characterized as N-acetyltransferase 2.
+At position 590 to 751, the domain is characterized as Helicase ATP-binding.
+At position 867 to 1021, the domain is characterized as Helicase C-terminal.
+At position 71 to 281, the domain is characterized as ABC transmembrane type-1.
+At position 405 to 504, the domain is characterized as Fibronectin type-III.
+At position 2 to 66, the domain is characterized as LCN-type CS-alpha/beta.
+At position 222 to 384, the domain is characterized as TrmE-type G.
+At position 11 to 155, the domain is characterized as Nudix hydrolase.
+At position 21 to 418, the domain is characterized as Protein kinase.
+At position 719 to 769, the domain is characterized as bHLH.
+At position 92 to 318, the domain is characterized as Radical SAM core.
+At position 178 to 207, the domain is characterized as GS.
+At position 208 to 502, the domain is characterized as Protein kinase.
+At position 92 to 166, the domain is characterized as PRC barrel.
+At position 388 to 401, the domain is characterized as CRIB.
+At position 844 to 1095, the domain is characterized as Protein kinase.
+At position 899 to 1125, the domain is characterized as Grh/CP2 DB.
+At position 53 to 117, the domain is characterized as UPAR/Ly6 1.
+At position 143 to 218, the domain is characterized as UPAR/Ly6 2.
+At position 416 to 488, the domain is characterized as HSA.
+At position 835 to 1000, the domain is characterized as Helicase ATP-binding.
+At position 1367 to 1520, the domain is characterized as Helicase C-terminal.
+At position 22 to 65, the domain is characterized as FAR1.
+At position 66 to 150, the domain is characterized as MULE.
+At position 109 to 340, the domain is characterized as Radical SAM core.
+At position 1 to 136, the domain is characterized as VWFD.
+At position 4 to 147, the domain is characterized as MGS-like.
+At position 6 to 147, the domain is characterized as SprT-like.
+At position 106 to 355, the domain is characterized as GS catalytic.
+At position 1 to 247, the domain is characterized as tr-type G.
+At position 81 to 210, the domain is characterized as GST C-terminal.
+At position 5 to 173, the domain is characterized as Era-type G.
+At position 12 to 75, the domain is characterized as Histone-fold.
+At position 28 to 105, the domain is characterized as EMI.
+At position 104 to 136, the domain is characterized as EGF-like 1.
+At position 138 to 178, the domain is characterized as EGF-like 2; calcium-binding.
+At position 2 to 217, the domain is characterized as tr-type G.
+At position 443 to 565, the domain is characterized as HD.
+At position 682 to 761, the domain is characterized as ACT 1.
+At position 790 to 858, the domain is characterized as ACT 2.
+At position 23 to 90, the domain is characterized as LCN-type CS-alpha/beta.
+At position 68 to 287, the domain is characterized as Radical SAM core.
+At position 32 to 214, the domain is characterized as Radical SAM core.
+At position 28 to 63, the domain is characterized as Chitin-binding type-1.
+At position 1 to 124, the domain is characterized as C2.
+At position 138 to 740, the domain is characterized as PLA2c.
+At position 139 to 340, the domain is characterized as ATP-grasp.
+At position 54 to 226, the domain is characterized as Helicase ATP-binding.
+At position 237 to 398, the domain is characterized as Helicase C-terminal.
+At position 14 to 259, the domain is characterized as CN hydrolase.
+At position 23 to 295, the domain is characterized as PPM-type phosphatase.
+At position 33 to 155, the domain is characterized as C-type lectin.
+At position 253 to 432, the domain is characterized as GATase cobBQ-type.
+At position 3 to 142, the domain is characterized as PINc.
+At position 29 to 276, the domain is characterized as NodB homology.
+At position 22 to 215, the domain is characterized as Radical SAM core.
+At position 96 to 161, the domain is characterized as S4 RNA-binding.
+At position 106 to 356, the domain is characterized as GS catalytic.
+At position 5 to 114, the domain is characterized as HIT.
+At position 11 to 82, the domain is characterized as KRAB.
+At position 714 to 801, the domain is characterized as PDZ 1.
+At position 848 to 936, the domain is characterized as PDZ 2.
+At position 990 to 1079, the domain is characterized as PDZ 3.
+At position 1086 to 1180, the domain is characterized as PDZ 4.
+At position 108 to 230, the domain is characterized as MRH.
+At position 108 to 230, the domain is characterized as MPN.
+At position 1 to 98, the domain is characterized as BRCT.
+At position 61 to 165, the domain is characterized as Cadherin 1.
+At position 166 to 274, the domain is characterized as Cadherin 2.
+At position 275 to 391, the domain is characterized as Cadherin 3.
+At position 392 to 495, the domain is characterized as Cadherin 4.
+At position 496 to 613, the domain is characterized as Cadherin 5.
+At position 141 to 366, the domain is characterized as Ras-GAP.
+At position 1635 to 1774, the domain is characterized as VPS9.
+At position 828 to 1168, the domain is characterized as PUM-HD.
+At position 163 to 332, the domain is characterized as Helicase ATP-binding.
+At position 491 to 655, the domain is characterized as Helicase C-terminal.
+At position 24 to 196, the domain is characterized as EngB-type G.
+At position 6 to 44, the domain is characterized as UBA-like.
+At position 62 to 268, the domain is characterized as DCUN1.
+At position 73 to 222, the domain is characterized as Integrase catalytic.
+At position 34 to 154, the domain is characterized as FZ.
+At position 171 to 294, the domain is characterized as NTR.
+At position 5 to 33, the domain is characterized as EF-hand 1.
+At position 33 to 68, the domain is characterized as EF-hand 2.
+At position 55 to 85, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 13 to 66, the domain is characterized as HTH cro/C1-type.
+At position 38 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 732 to 927, the domain is characterized as ATP-grasp.
+At position 14 to 89, the domain is characterized as KRAB.
+At position 291 to 338, the domain is characterized as F-box.
+At position 220 to 317, the domain is characterized as GST C-terminal.
+At position 24 to 101, the domain is characterized as Death.
+At position 147 to 281, the domain is characterized as TIR.
+At position 4 to 144, the domain is characterized as Clp R.
+At position 83 to 269, the domain is characterized as RNase H type-2.
+At position 1 to 146, the domain is characterized as RNase H type-1.
+At position 2 to 200, the domain is characterized as Protein kinase.
+At position 70 to 117, the domain is characterized as LIM zinc-binding.
+At position 1 to 69, the domain is characterized as Peptidase M12B.
+At position 135 to 438, the domain is characterized as NB-ARC.
+At position 12 to 139, the domain is characterized as RNase III.
+At position 165 to 236, the domain is characterized as DRBM.
+At position 87 to 178, the domain is characterized as K-box.
+At position 1 to 42, the domain is characterized as TGS.
+At position 35 to 360, the domain is characterized as GP-PDE.
+At position 379 to 518, the domain is characterized as JmjC.
+At position 5 to 59, the domain is characterized as HTH cro/C1-type.
+At position 77 to 236, the domain is characterized as CP-type G.
+At position 23 to 83, the domain is characterized as LIM zinc-binding 1.
+At position 87 to 147, the domain is characterized as LIM zinc-binding 2.
+At position 475 to 644, the domain is characterized as tr-type G.
+At position 6 to 186, the domain is characterized as Guanylate kinase-like.
+At position 33 to 80, the domain is characterized as KH.
+At position 16 to 205, the domain is characterized as RNase H type-2.
+At position 1 to 118, the domain is characterized as B12-binding.
+At position 148 to 377, the domain is characterized as Radical SAM core.
+At position 217 to 388, the domain is characterized as PCI.
+At position 83 to 162, the domain is characterized as Cytochrome b5 heme-binding.
+At position 478 to 713, the domain is characterized as ABC transporter 1.
+At position 1290 to 1533, the domain is characterized as ABC transporter 2.
+At position 8 to 159, the domain is characterized as Nudix hydrolase.
+At position 466 to 580, the domain is characterized as STAS.
+At position 6 to 155, the domain is characterized as N-acetyltransferase.
+At position 57 to 230, the domain is characterized as Helicase ATP-binding.
+At position 241 to 401, the domain is characterized as Helicase C-terminal.
+At position 12 to 266, the domain is characterized as Protein kinase.
+At position 309 to 333, the domain is characterized as NAF.
+At position 40 to 221, the domain is characterized as Macro.
+At position 329 to 486, the domain is characterized as CRAL-TRIO.
+At position 460 to 669, the domain is characterized as MCM.
+At position 12 to 143, the domain is characterized as SIS.
+At position 21 to 81, the domain is characterized as HTH tetR-type.
+At position 2 to 78, the domain is characterized as GST N-terminal.
+At position 80 to 198, the domain is characterized as GST C-terminal.
+At position 196 to 296, the domain is characterized as Fe2OG dioxygenase.
+At position 13 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 203 to 402, the domain is characterized as GMPS ATP-PPase.
+At position 88 to 215, the domain is characterized as GST C-terminal.
+At position 162 to 409, the domain is characterized as AB hydrolase-1.
+At position 6 to 91, the domain is characterized as Acylphosphatase-like.
+At position 4 to 41, the domain is characterized as Chitin-binding type-1.
+At position 118 to 192, the domain is characterized as MIT.
+At position 457 to 532, the domain is characterized as Ubiquitin-like 7.
+At position 12 to 240, the domain is characterized as ABC transporter 1.
+At position 240 to 503, the domain is characterized as ABC transporter 2.
+At position 45 to 338, the domain is characterized as MYST-type HAT.
+At position 755 to 983, the domain is characterized as MIF4G.
+At position 1221 to 1343, the domain is characterized as MI.
+At position 1416 to 1585, the domain is characterized as W2.
+At position 165 to 194, the domain is characterized as GS.
+At position 195 to 485, the domain is characterized as Protein kinase.
+At position 190 to 253, the domain is characterized as bZIP.
+At position 11 to 71, the domain is characterized as Tudor 1.
+At position 85 to 141, the domain is characterized as Tudor 2.
+At position 30 to 103, the domain is characterized as Histone-fold.
+At position 73 to 136, the domain is characterized as bZIP.
+At position 272 to 511, the domain is characterized as Peptidase M12B.
+At position 520 to 609, the domain is characterized as Disintegrin.
+At position 92 to 164, the domain is characterized as S4 RNA-binding.
+At position 72 to 255, the domain is characterized as RNase H type-2.
+At position 7 to 167, the domain is characterized as N-acetyltransferase.
+At position 66 to 306, the domain is characterized as Peptidase S1.
+At position 21 to 132, the domain is characterized as Thioredoxin 1.
+At position 339 to 470, the domain is characterized as Thioredoxin 2.
+At position 161 to 391, the domain is characterized as Histidine kinase.
+At position 193 to 271, the domain is characterized as RRM.
+At position 25 to 325, the domain is characterized as SAM-dependent MTase C5-type.
+At position 172 to 366, the domain is characterized as Helicase ATP-binding.
+At position 404 to 580, the domain is characterized as Helicase C-terminal.
+At position 7 to 124, the domain is characterized as Response regulatory.
+At position 36 to 139, the domain is characterized as Ig-like C2-type 1.
+At position 140 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 238 to 321, the domain is characterized as Ig-like C2-type 3.
+At position 329 to 416, the domain is characterized as Ig-like C2-type 4.
+At position 426 to 520, the domain is characterized as Fibronectin type-III 1.
+At position 523 to 618, the domain is characterized as Fibronectin type-III 2.
+At position 84 to 203, the domain is characterized as RGS.
+At position 730 to 812, the domain is characterized as DIX.
+At position 208 to 432, the domain is characterized as NR LBD.
+At position 861 to 909, the domain is characterized as GRIP.
+At position 29 to 95, the domain is characterized as Sushi 1.
+At position 97 to 158, the domain is characterized as Sushi 2.
+At position 644 to 725, the domain is characterized as S1 motif.
+At position 110 to 322, the domain is characterized as ATP-grasp.
+At position 225 to 285, the domain is characterized as KH.
+At position 351 to 444, the domain is characterized as HD.
+At position 49 to 492, the domain is characterized as Hexokinase.
+At position 4 to 165, the domain is characterized as Flavodoxin-like.
+At position 238 to 398, the domain is characterized as PID.
+At position 887 to 1081, the domain is characterized as Rab-GAP TBC.
+At position 23 to 174, the domain is characterized as F5/8 type C.
+At position 1017 to 1198, the domain is characterized as Laminin G-like 4.
+At position 81 to 368, the domain is characterized as Protein kinase.
+At position 24 to 101, the domain is characterized as Kringle.
+At position 61 to 242, the domain is characterized as PIK helical.
+At position 8 to 194, the domain is characterized as AMMECR1.
+At position 229 to 367, the domain is characterized as C2 1.
+At position 954 to 1082, the domain is characterized as C2 2.
+At position 1120 to 1246, the domain is characterized as C2 3.
+At position 1363 to 1484, the domain is characterized as C2 4.
+At position 1684 to 1831, the domain is characterized as C2 5.
+At position 73 to 417, the domain is characterized as Calpain catalytic.
+At position 644 to 719, the domain is characterized as Smr.
+At position 142 to 261, the domain is characterized as C2 1.
+At position 273 to 406, the domain is characterized as C2 2.
+At position 12 to 228, the domain is characterized as Radical SAM core.
+At position 555 to 618, the domain is characterized as bZIP.
+At position 93 to 158, the domain is characterized as S4 RNA-binding.
+At position 35 to 222, the domain is characterized as Exonuclease.
+At position 38 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 142 to 254, the domain is characterized as Gnk2-homologous 2.
+At position 223 to 274, the domain is characterized as bHLH.
+At position 450 to 794, the domain is characterized as Peptidase M60.
+At position 26 to 197, the domain is characterized as EngB-type G.
+At position 31 to 301, the domain is characterized as Alpha-carbonic anhydrase.
+At position 116 to 195, the domain is characterized as PDZ 1.
+At position 200 to 274, the domain is characterized as PDZ 2.
+At position 405 to 480, the domain is characterized as B5.
+At position 707 to 809, the domain is characterized as FDX-ACB.
+At position 287 to 465, the domain is characterized as TLDc.
+At position 421 to 590, the domain is characterized as tr-type G.
+At position 10 to 113, the domain is characterized as EH 1.
+At position 285 to 374, the domain is characterized as EH 2.
+At position 318 to 353, the domain is characterized as EF-hand.
+At position 432 to 474, the domain is characterized as CUE.
+At position 43 to 405, the domain is characterized as Peptidase A1.
+At position 250 to 468, the domain is characterized as Peptidase M12B.
+At position 495 to 557, the domain is characterized as Disintegrin.
+At position 558 to 613, the domain is characterized as TSP type-1 1.
+At position 840 to 900, the domain is characterized as TSP type-1 2.
+At position 902 to 960, the domain is characterized as TSP type-1 3.
+At position 962 to 1007, the domain is characterized as TSP type-1 4.
+At position 1018 to 1073, the domain is characterized as TSP type-1 5.
+At position 1079 to 1117, the domain is characterized as PLAC.
+At position 144 to 501, the domain is characterized as PDEase.
+At position 14 to 209, the domain is characterized as Lon N-terminal.
+At position 39 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 136 to 219, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 310, the domain is characterized as Ig-like C2-type 3.
+At position 36 to 106, the domain is characterized as BTB.
+At position 210 to 490, the domain is characterized as NPH3.
+At position 304 to 344, the domain is characterized as UBA.
+At position 409 to 683, the domain is characterized as Protein kinase.
+At position 336 to 666, the domain is characterized as NACHT.
+At position 164 to 251, the domain is characterized as PPIase FKBP-type.
+At position 10 to 191, the domain is characterized as YrdC-like.
+At position 617 to 695, the domain is characterized as BRCT.
+At position 495 to 569, the domain is characterized as PUA.
+At position 36 to 96, the domain is characterized as Kazal-like.
+At position 182 to 300, the domain is characterized as SET.
+At position 63 to 199, the domain is characterized as HD.
+At position 77 to 327, the domain is characterized as Protein kinase.
+At position 491 to 614, the domain is characterized as DOD-type homing endonuclease.
+At position 70 to 253, the domain is characterized as RNase H type-2.
+At position 1 to 263, the domain is characterized as F-BAR.
+At position 339 to 416, the domain is characterized as REM-1.
+At position 479 to 540, the domain is characterized as SH3.
+At position 72 to 139, the domain is characterized as GRAM.
+At position 35 to 839, the domain is characterized as Protein kinase.
+At position 840 to 883, the domain is characterized as AGC-kinase C-terminal.
+At position 90 to 154, the domain is characterized as S4 RNA-binding.
+At position 234 to 386, the domain is characterized as TrmE-type G.
+At position 1 to 61, the domain is characterized as HTH lysR-type.
+At position 216 to 365, the domain is characterized as TrmE-type G.
+At position 928 to 1094, the domain is characterized as PNPLA.
+At position 367 to 397, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 406 to 481, the domain is characterized as B5.
+At position 708 to 801, the domain is characterized as FDX-ACB.
+At position 13 to 76, the domain is characterized as S5 DRBM.
+At position 169 to 273, the domain is characterized as Fe2OG dioxygenase.
+At position 45 to 95, the domain is characterized as bHLH.
+At position 119 to 201, the domain is characterized as PDZ.
+At position 4 to 264, the domain is characterized as F-BAR.
+At position 716 to 791, the domain is characterized as Smr.
+At position 101 to 303, the domain is characterized as ATP-grasp.
+At position 1 to 259, the domain is characterized as Pterin-binding.
+At position 86 to 284, the domain is characterized as Laminin G-like.
+At position 109 to 271, the domain is characterized as N-acetyltransferase.
+At position 67 to 328, the domain is characterized as Protein kinase.
+At position 329 to 399, the domain is characterized as AGC-kinase C-terminal.
+At position 107 to 229, the domain is characterized as MPN.
+At position 73 to 200, the domain is characterized as ALOG.
+At position 17 to 211, the domain is characterized as RNase H type-2.
+At position 6 to 243, the domain is characterized as ABC transporter 1.
+At position 262 to 505, the domain is characterized as ABC transporter 2.
+At position 10 to 183, the domain is characterized as PCI.
+At position 29 to 110, the domain is characterized as Lipoyl-binding.
+At position 44 to 247, the domain is characterized as AH.
+At position 5 to 81, the domain is characterized as Cytochrome b5 heme-binding.
+At position 266 to 506, the domain is characterized as ABC transporter 2.
+At position 829 to 894, the domain is characterized as HTH luxR-type.
+At position 311 to 347, the domain is characterized as CBM1.
+At position 172 to 270, the domain is characterized as HTH araC/xylS-type.
+At position 19 to 191, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 430, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 922 to 1209, the domain is characterized as PKS/mFAS DH.
+At position 2414 to 2491, the domain is characterized as Carrier.
+At position 8 to 250, the domain is characterized as ABC transporter.
+At position 129 to 162, the domain is characterized as WW.
+At position 18 to 49, the domain is characterized as HNF-p1.
+At position 145 to 241, the domain is characterized as POU-specific atypical.
+At position 100 to 268, the domain is characterized as CP-type G.
+At position 347 to 376, the domain is characterized as IQ.
+At position 746 to 939, the domain is characterized as SEC7.
+At position 180 to 220, the domain is characterized as UBA.
+At position 554 to 721, the domain is characterized as Helicase ATP-binding.
+At position 830 to 1010, the domain is characterized as Helicase C-terminal.
+At position 1 to 61, the domain is characterized as SH3.
+At position 227 to 339, the domain is characterized as PX.
+At position 362 to 566, the domain is characterized as BAR.
+At position 177 to 335, the domain is characterized as Cupin type-1 1.
+At position 394 to 551, the domain is characterized as Cupin type-1 2.
+At position 303 to 345, the domain is characterized as CAP-Gly 1.
+At position 504 to 546, the domain is characterized as CAP-Gly 2.
+At position 643 to 685, the domain is characterized as CAP-Gly 3.
+At position 24 to 255, the domain is characterized as Phosphagen kinase C-terminal.
+At position 25 to 131, the domain is characterized as BTB.
+At position 1 to 197, the domain is characterized as CNNM transmembrane.
+At position 216 to 275, the domain is characterized as CBS 1.
+At position 282 to 343, the domain is characterized as CBS 2.
+At position 535 to 651, the domain is characterized as SMC hinge.
+At position 25 to 106, the domain is characterized as Importin N-terminal.
+At position 190 to 242, the domain is characterized as HAMP.
+At position 250 to 470, the domain is characterized as Histidine kinase.
+At position 31 to 159, the domain is characterized as Bulb-type lectin.
+At position 356 to 437, the domain is characterized as PAN.
+At position 44 to 90, the domain is characterized as G-patch.
+At position 184 to 413, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 197 to 362, the domain is characterized as PCI.
+At position 164 to 259, the domain is characterized as 5'-3' exonuclease.
+At position 5 to 30, the domain is characterized as LIM zinc-binding.
+At position 2 to 188, the domain is characterized as UmuC.
+At position 1 to 179, the domain is characterized as KARI N-terminal Rossmann.
+At position 180 to 325, the domain is characterized as KARI C-terminal knotted.
+At position 38 to 99, the domain is characterized as S4 RNA-binding; degenerate.
+At position 1 to 102, the domain is characterized as CMP/dCMP-type deaminase.
+At position 175 to 277, the domain is characterized as THUMP.
+At position 74 to 325, the domain is characterized as Protein kinase.
+At position 132 to 318, the domain is characterized as CNNM transmembrane.
+At position 333 to 396, the domain is characterized as CBS 1.
+At position 413 to 473, the domain is characterized as CBS 2.
+At position 55 to 280, the domain is characterized as Radical SAM core.
+At position 271 to 313, the domain is characterized as CCT.
+At position 2 to 216, the domain is characterized as Glutamine amidotransferase type-2.
+At position 282 to 421, the domain is characterized as SIS 1.
+At position 68 to 257, the domain is characterized as Reticulon.
+At position 1 to 124, the domain is characterized as RNase III.
+At position 153 to 223, the domain is characterized as DRBM.
+At position 135 to 178, the domain is characterized as CUE.
+At position 37 to 140, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 248 to 327, the domain is characterized as Ig-like C2-type 3.
+At position 332 to 420, the domain is characterized as Ig-like C2-type 4.
+At position 2 to 55, the domain is characterized as HTH lacI-type.
+At position 2 to 166, the domain is characterized as EngA-type G 1.
+At position 212 to 385, the domain is characterized as EngA-type G 2.
+At position 386 to 470, the domain is characterized as KH-like.
+At position 34 to 112, the domain is characterized as EMI.
+At position 111 to 143, the domain is characterized as EGF-like 1.
+At position 145 to 185, the domain is characterized as EGF-like 2; calcium-binding.
+At position 3 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 192 to 254, the domain is characterized as t-SNARE coiled-coil homology.
+At position 1 to 196, the domain is characterized as Brix.
+At position 58 to 171, the domain is characterized as Expansin-like EG45.
+At position 181 to 260, the domain is characterized as Expansin-like CBD.
+At position 69 to 353, the domain is characterized as Protein kinase.
+At position 29 to 115, the domain is characterized as Sm.
+At position 10 to 248, the domain is characterized as ABC transporter.
+At position 15 to 326, the domain is characterized as Kinesin motor.
+At position 5 to 136, the domain is characterized as HTH marR-type.
+At position 12 to 110, the domain is characterized as Rhodanese.
+At position 228 to 395, the domain is characterized as Helicase ATP-binding.
+At position 491 to 646, the domain is characterized as Helicase C-terminal.
+At position 33 to 66, the domain is characterized as WW.
+At position 78 to 155, the domain is characterized as PDZ.
+At position 204 to 519, the domain is characterized as FERM.
+At position 1 to 32, the domain is characterized as HNF-p1.
+At position 92 to 187, the domain is characterized as POU-specific atypical.
+At position 8 to 223, the domain is characterized as ABC transporter.
+At position 53 to 108, the domain is characterized as F-box.
+At position 1 to 92, the domain is characterized as Core-binding (CB).
+At position 113 to 298, the domain is characterized as Tyr recombinase.
+At position 98 to 197, the domain is characterized as Cytochrome b5 heme-binding.
+At position 250 to 435, the domain is characterized as GATase cobBQ-type.
+At position 15 to 178, the domain is characterized as UBC core.
+At position 111 to 304, the domain is characterized as ATP-grasp.
+At position 1 to 92, the domain is characterized as Chorismate mutase.
+At position 43 to 272, the domain is characterized as GB1/RHD3-type G.
+At position 142 to 184, the domain is characterized as LRRCT.
+At position 119 to 208, the domain is characterized as SH2.
+At position 209 to 450, the domain is characterized as Protein kinase.
+At position 304 to 380, the domain is characterized as SPOR.
+At position 141 to 263, the domain is characterized as MPN.
+At position 7 to 184, the domain is characterized as uDENN.
+At position 203 to 336, the domain is characterized as cDENN.
+At position 338 to 439, the domain is characterized as dDENN.
+At position 880 to 968, the domain is characterized as GRAM.
+At position 1120 to 1596, the domain is characterized as Myotubularin phosphatase.
+At position 1761 to 1865, the domain is characterized as PH.
+At position 31 to 177, the domain is characterized as F5/8 type C.
+At position 183 to 364, the domain is characterized as Laminin G-like 1.
+At position 370 to 545, the domain is characterized as Laminin G-like 2.
+At position 551 to 583, the domain is characterized as EGF-like 1.
+At position 584 to 792, the domain is characterized as Fibrinogen C-terminal.
+At position 793 to 958, the domain is characterized as Laminin G-like 3.
+At position 962 to 996, the domain is characterized as EGF-like 2.
+At position 1015 to 1203, the domain is characterized as Laminin G-like 4.
+At position 186 to 270, the domain is characterized as RCK C-terminal 1.
+At position 273 to 356, the domain is characterized as RCK C-terminal 2.
+At position 51 to 77, the domain is characterized as EF-hand 2.
+At position 403 to 649, the domain is characterized as Roc.
+At position 43 to 224, the domain is characterized as ABC transmembrane type-1.
+At position 23 to 136, the domain is characterized as FZ.
+At position 14 to 85, the domain is characterized as KRAB.
+At position 22 to 81, the domain is characterized as FHA.
+At position 101 to 191, the domain is characterized as BRCT.
+At position 24 to 51, the domain is characterized as LRRNT.
+At position 645 to 698, the domain is characterized as LRRCT.
+At position 754 to 897, the domain is characterized as TIR.
+At position 60 to 114, the domain is characterized as HTH myb-type.
+At position 10 to 78, the domain is characterized as HTH gntR-type.
+At position 5 to 97, the domain is characterized as Ig-like 1.
+At position 99 to 184, the domain is characterized as Ig-like 2.
+At position 201 to 301, the domain is characterized as Ig-like 3.
+At position 310 to 410, the domain is characterized as Ig-like 4.
+At position 62 to 266, the domain is characterized as ABC transmembrane type-1 1.
+At position 339 to 530, the domain is characterized as ABC transmembrane type-1 2.
+At position 1 to 28, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 29 to 56, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 20 to 293, the domain is characterized as Protein kinase.
+At position 525 to 579, the domain is characterized as LRRCT.
+At position 639 to 782, the domain is characterized as TIR.
+At position 80 to 330, the domain is characterized as Protein kinase.
+At position 38 to 290, the domain is characterized as GP-PDE.
+At position 220 to 358, the domain is characterized as PADR1 zinc-binding.
+At position 382 to 473, the domain is characterized as BRCT.
+At position 527 to 625, the domain is characterized as WGR.
+At position 647 to 764, the domain is characterized as PARP alpha-helical.
+At position 773 to 996, the domain is characterized as PARP catalytic.
+At position 223 to 391, the domain is characterized as SSD.
+At position 72 to 242, the domain is characterized as Helicase ATP-binding.
+At position 253 to 414, the domain is characterized as Helicase C-terminal.
+At position 40 to 75, the domain is characterized as EF-hand 1.
+At position 77 to 112, the domain is characterized as EF-hand 2.
+At position 394 to 652, the domain is characterized as Olfactomedin-like.
+At position 233 to 375, the domain is characterized as Tyrosine-protein phosphatase.
+At position 337 to 398, the domain is characterized as SH3.
+At position 16 to 79, the domain is characterized as S5 DRBM.
+At position 26 to 503, the domain is characterized as PPM-type phosphatase.
+At position 42 to 87, the domain is characterized as Gla.
+At position 96 to 131, the domain is characterized as EGF-like 1.
+At position 135 to 175, the domain is characterized as EGF-like 2.
+At position 214 to 448, the domain is characterized as Peptidase S1.
+At position 183 to 248, the domain is characterized as HTH luxR-type.
+At position 230 to 297, the domain is characterized as SCA7.
+At position 445 to 577, the domain is characterized as Ricin B-type lectin.
+At position 34 to 354, the domain is characterized as Kinesin motor.
+At position 603 to 712, the domain is characterized as Peptidase S72.
+At position 133 to 572, the domain is characterized as Urease.
+At position 10 to 127, the domain is characterized as Response regulatory.
+At position 173 to 362, the domain is characterized as CheB-type methylesterase.
+At position 148 to 502, the domain is characterized as PUM-HD.
+At position 4 to 172, the domain is characterized as Miro 1.
+At position 188 to 223, the domain is characterized as EF-hand 1.
+At position 455 to 624, the domain is characterized as Miro 2.
+At position 175 to 274, the domain is characterized as PDZ.
+At position 250 to 327, the domain is characterized as POU-specific.
+At position 233 to 292, the domain is characterized as SH3.
+At position 11 to 157, the domain is characterized as UBC core.
+At position 36 to 109, the domain is characterized as H15.
+At position 15 to 154, the domain is characterized as Clp R.
+At position 6 to 104, the domain is characterized as PTS EIIA type-3.
+At position 120 to 206, the domain is characterized as PNT.
+At position 52 to 277, the domain is characterized as Radical SAM core.
+At position 219 to 429, the domain is characterized as Peptidase M12B.
+At position 438 to 525, the domain is characterized as Disintegrin.
+At position 526 to 581, the domain is characterized as TSP type-1 1.
+At position 833 to 888, the domain is characterized as TSP type-1 2.
+At position 57 to 157, the domain is characterized as Glutaredoxin.
+At position 27 to 196, the domain is characterized as PNPLA.
+At position 24 to 222, the domain is characterized as GH16.
+At position 337 to 390, the domain is characterized as TSP type-1.
+At position 53 to 288, the domain is characterized as GB1/RHD3-type G.
+At position 29 to 123, the domain is characterized as Ig-like C2-type.
+At position 137 to 181, the domain is characterized as EGF-like.
+At position 46 to 349, the domain is characterized as Protein kinase.
+At position 92 to 173, the domain is characterized as bHLH.
+At position 123 to 320, the domain is characterized as Peptidase M12A.
+At position 320 to 355, the domain is characterized as EGF-like.
+At position 365 to 478, the domain is characterized as CUB.
+At position 503 to 552, the domain is characterized as TSP type-1.
+At position 5 to 109, the domain is characterized as SSB.
+At position 670 to 739, the domain is characterized as S1 motif.
+At position 14 to 267, the domain is characterized as Protein kinase.
+At position 379 to 496, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 497 to 600, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 658 to 737, the domain is characterized as POLO box.
+At position 23 to 285, the domain is characterized as Protein kinase.
+At position 19 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 239, the domain is characterized as Ig-like C2-type 2.
+At position 48 to 191, the domain is characterized as SIS.
+At position 217 to 273, the domain is characterized as CBS 1.
+At position 282 to 327, the domain is characterized as CBS 2.
+At position 451 to 512, the domain is characterized as SAM.
+At position 2 to 192, the domain is characterized as CNNM transmembrane.
+At position 208 to 270, the domain is characterized as CBS 1.
+At position 272 to 332, the domain is characterized as CBS 2.
+At position 212 to 441, the domain is characterized as START.
+At position 54 to 234, the domain is characterized as Helicase ATP-binding.
+At position 400 to 564, the domain is characterized as Helicase C-terminal.
+At position 591 to 684, the domain is characterized as Dicer dsRNA-binding fold.
+At position 956 to 1099, the domain is characterized as RNase III 1.
+At position 1141 to 1323, the domain is characterized as RNase III 2.
+At position 203 to 399, the domain is characterized as Peptidase M12B.
+At position 407 to 493, the domain is characterized as Disintegrin.
+At position 308 to 556, the domain is characterized as Glutamine amidotransferase type-1.
+At position 594 to 671, the domain is characterized as Carrier 1.
+At position 1677 to 1756, the domain is characterized as Carrier 2.
+At position 5 to 69, the domain is characterized as NAC-A/B.
+At position 731 to 818, the domain is characterized as PDZ 1.
+At position 929 to 1019, the domain is characterized as PDZ 2.
+At position 1239 to 1329, the domain is characterized as PDZ 3.
+At position 1336 to 1428, the domain is characterized as PDZ 4.
+At position 46 to 247, the domain is characterized as AIG1-type G 1.
+At position 282 to 472, the domain is characterized as AIG1-type G 2.
+At position 473 to 677, the domain is characterized as AIG1-type G 3.
+At position 7 to 114, the domain is characterized as RWD.
+At position 20 to 83, the domain is characterized as S4 RNA-binding.
+At position 39 to 163, the domain is characterized as C-type lectin.
+At position 307 to 343, the domain is characterized as CBM1.
+At position 4 to 70, the domain is characterized as J.
+At position 117 to 618, the domain is characterized as Biotin carboxylation.
+At position 275 to 466, the domain is characterized as ATP-grasp.
+At position 745 to 819, the domain is characterized as Biotinyl-binding.
+At position 1576 to 1914, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1918 to 2234, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 171 to 384, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 9 to 248, the domain is characterized as ATP-grasp.
+At position 2 to 67, the domain is characterized as LCN-type CS-alpha/beta.
+At position 12 to 94, the domain is characterized as GIY-YIG.
+At position 3 to 88, the domain is characterized as ACB.
+At position 45 to 282, the domain is characterized as PABS.
+At position 328 to 649, the domain is characterized as Protein kinase.
+At position 903 to 963, the domain is characterized as SH3.
+At position 99 to 173, the domain is characterized as PRC barrel.
+At position 47 to 88, the domain is characterized as Gla.
+At position 97 to 132, the domain is characterized as EGF-like 1.
+At position 136 to 176, the domain is characterized as EGF-like 2.
+At position 211 to 445, the domain is characterized as Peptidase S1.
+At position 191 to 384, the domain is characterized as Helicase ATP-binding.
+At position 395 to 556, the domain is characterized as Helicase C-terminal.
+At position 48 to 278, the domain is characterized as Radical SAM core.
+At position 9 to 353, the domain is characterized as Kinesin motor.
+At position 129 to 179, the domain is characterized as DHHC.
+At position 8 to 92, the domain is characterized as Acylphosphatase-like.
+At position 200 to 376, the domain is characterized as YrdC-like.
+At position 1 to 89, the domain is characterized as FAD-binding FR-type.
+At position 10 to 120, the domain is characterized as HIT.
+At position 2 to 83, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 83 to 122, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 221 to 277, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 5 to 74, the domain is characterized as Inhibitor I9.
+At position 33 to 217, the domain is characterized as EngB-type G.
+At position 20 to 129, the domain is characterized as Thioredoxin 1.
+At position 131 to 250, the domain is characterized as Thioredoxin 2.
+At position 40 to 294, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 72 to 147, the domain is characterized as S4 RNA-binding.
+At position 3 to 259, the domain is characterized as Alpha-carbonic anhydrase.
+At position 97 to 327, the domain is characterized as ABC transmembrane type-1.
+At position 39 to 156, the domain is characterized as sHSP.
+At position 18 to 658, the domain is characterized as Vitellogenin.
+At position 1564 to 1732, the domain is characterized as VWFD.
+At position 323 to 392, the domain is characterized as ACT 1.
+At position 409 to 473, the domain is characterized as ACT 2.
+At position 1 to 73, the domain is characterized as LCN-type CS-alpha/beta.
+At position 6 to 216, the domain is characterized as Radical SAM core.
+At position 195 to 292, the domain is characterized as HTH araC/xylS-type.
+At position 295 to 388, the domain is characterized as EH.
+At position 66 to 387, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 391 to 426, the domain is characterized as EF-hand 1.
+At position 428 to 463, the domain is characterized as EF-hand 2.
+At position 1 to 53, the domain is characterized as MADS-box.
+At position 12 to 100, the domain is characterized as Ig-like 1.
+At position 128 to 225, the domain is characterized as Ig-like 2.
+At position 243 to 330, the domain is characterized as Ig-like 3.
+At position 339 to 425, the domain is characterized as Ig-like 4.
+At position 517 to 615, the domain is characterized as Fibronectin type-III.
+At position 714 to 800, the domain is characterized as Ig-like 5.
+At position 804 to 893, the domain is characterized as Ig-like 6.
+At position 902 to 982, the domain is characterized as Ig-like 7.
+At position 986 to 1075, the domain is characterized as Ig-like 8.
+At position 1078 to 1172, the domain is characterized as Ig-like 9.
+At position 1174 to 1261, the domain is characterized as Ig-like 10.
+At position 1265 to 1357, the domain is characterized as Ig-like 11.
+At position 1357 to 1534, the domain is characterized as Ig-like 12.
+At position 1628 to 1720, the domain is characterized as Ig-like 13.
+At position 1794 to 1896, the domain is characterized as Ig-like 14.
+At position 1 to 77, the domain is characterized as HTH rpiR-type.
+At position 128 to 268, the domain is characterized as SIS.
+At position 41 to 127, the domain is characterized as KRAB.
+At position 23 to 135, the domain is characterized as Ig-like V-type.
+At position 139 to 227, the domain is characterized as Ig-like C2-type 1.
+At position 238 to 316, the domain is characterized as Ig-like C2-type 2.
+At position 317 to 405, the domain is characterized as Ig-like C2-type 3.
+At position 415 to 505, the domain is characterized as Ig-like C2-type 4.
+At position 511 to 593, the domain is characterized as Ig-like C2-type 5.
+At position 601 to 705, the domain is characterized as Ig-like C2-type 6.
+At position 708 to 790, the domain is characterized as Ig-like C2-type 7.
+At position 798 to 893, the domain is characterized as Ig-like C2-type 8.
+At position 897 to 976, the domain is characterized as Ig-like C2-type 9.
+At position 983 to 1082, the domain is characterized as Ig-like C2-type 10.
+At position 1083 to 1165, the domain is characterized as Ig-like C2-type 11.
+At position 1172 to 1257, the domain is characterized as Ig-like C2-type 12.
+At position 1259 to 1335, the domain is characterized as Ig-like C2-type 13.
+At position 1346 to 1442, the domain is characterized as Ig-like C2-type 14.
+At position 1443 to 1529, the domain is characterized as Ig-like C2-type 15.
+At position 1537 to 1630, the domain is characterized as Ig-like C2-type 16.
+At position 46 to 162, the domain is characterized as Cyclin N-terminal.
+At position 132 to 191, the domain is characterized as SH3 1.
+At position 194 to 257, the domain is characterized as SH3 2.
+At position 398 to 459, the domain is characterized as SH3 3.
+At position 767 to 826, the domain is characterized as SH3 4.
+At position 43 to 122, the domain is characterized as PB1.
+At position 356 to 616, the domain is characterized as Protein kinase.
+At position 232 to 317, the domain is characterized as PDZ 1.
+At position 338 to 421, the domain is characterized as PDZ 2.
+At position 465 to 551, the domain is characterized as PDZ 3.
+At position 597 to 685, the domain is characterized as PDZ 4.
+At position 4 to 25, the domain is characterized as Disintegrin.
+At position 36 to 239, the domain is characterized as Brix.
+At position 24 to 293, the domain is characterized as PPM-type phosphatase.
+At position 534 to 821, the domain is characterized as NB-ARC.
+At position 1217 to 1284, the domain is characterized as HMA.
+At position 35 to 196, the domain is characterized as N-acetyltransferase.
+At position 3 to 214, the domain is characterized as ABC transporter.
+At position 39 to 147, the domain is characterized as tRNA-binding.
+At position 400 to 476, the domain is characterized as B5.
+At position 698 to 791, the domain is characterized as FDX-ACB.
+At position 434 to 468, the domain is characterized as PLD phosphodiesterase.
+At position 295 to 442, the domain is characterized as N-acetyltransferase.
+At position 109 to 284, the domain is characterized as Helicase ATP-binding.
+At position 315 to 464, the domain is characterized as Helicase C-terminal.
+At position 4 to 254, the domain is characterized as ABC transporter.
+At position 2 to 95, the domain is characterized as ABM.
+At position 8 to 42, the domain is characterized as SAP.
+At position 136 to 201, the domain is characterized as HTH luxR-type.
+At position 430 to 464, the domain is characterized as PLD phosphodiesterase.
+At position 197 to 395, the domain is characterized as Peptidase M12B.
+At position 311 to 374, the domain is characterized as bZIP.
+At position 191 to 252, the domain is characterized as LIM zinc-binding 1.
+At position 256 to 315, the domain is characterized as LIM zinc-binding 2.
+At position 316 to 385, the domain is characterized as LIM zinc-binding 3.
+At position 34 to 111, the domain is characterized as Ubiquitin-like 1.
+At position 112 to 190, the domain is characterized as Ubiquitin-like 2.
+At position 234 to 532, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 57, the domain is characterized as IBB.
+At position 177 to 279, the domain is characterized as AB hydrolase-1.
+At position 54 to 151, the domain is characterized as SRCR.
+At position 163 to 405, the domain is characterized as Peptidase S1.
+At position 494 to 530, the domain is characterized as CBM1.
+At position 130 to 203, the domain is characterized as PDZ.
+At position 1302 to 1413, the domain is characterized as PH.
+At position 203 to 292, the domain is characterized as RCK C-terminal 1.
+At position 363 to 415, the domain is characterized as FBD.
+At position 376 to 716, the domain is characterized as PUM-HD.
+At position 26 to 266, the domain is characterized as Laminin N-terminal.
+At position 267 to 333, the domain is characterized as Laminin EGF-like 1.
+At position 334 to 396, the domain is characterized as Laminin EGF-like 2.
+At position 397 to 448, the domain is characterized as Laminin EGF-like 3.
+At position 449 to 500, the domain is characterized as Laminin EGF-like 4.
+At position 501 to 544, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 540 to 847, the domain is characterized as Laminin IV type B.
+At position 853 to 900, the domain is characterized as Laminin EGF-like 6.
+At position 901 to 946, the domain is characterized as Laminin EGF-like 7.
+At position 947 to 994, the domain is characterized as Laminin EGF-like 8.
+At position 995 to 1053, the domain is characterized as Laminin EGF-like 9.
+At position 1054 to 1105, the domain is characterized as Laminin EGF-like 10.
+At position 1106 to 1162, the domain is characterized as Laminin EGF-like 11.
+At position 1163 to 1210, the domain is characterized as Laminin EGF-like 12.
+At position 1211 to 1257, the domain is characterized as Laminin EGF-like 13.
+At position 22 to 141, the domain is characterized as Ig-like V-type 1.
+At position 146 to 257, the domain is characterized as Ig-like V-type 2.
+At position 5 to 125, the domain is characterized as RNase III.
+At position 6 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 197 to 386, the domain is characterized as GMPS ATP-PPase.
+At position 13 to 249, the domain is characterized as ABC transporter.
+At position 34 to 204, the domain is characterized as Helicase ATP-binding.
+At position 215 to 375, the domain is characterized as Helicase C-terminal.
+At position 258 to 357, the domain is characterized as CobW C-terminal.
+At position 85 to 203, the domain is characterized as GST C-terminal.
+At position 32 to 166, the domain is characterized as MARVEL.
+At position 468 to 635, the domain is characterized as tr-type G.
+At position 293 to 482, the domain is characterized as B30.2/SPRY.
+At position 32 to 136, the domain is characterized as Glutaredoxin.
+At position 375 to 648, the domain is characterized as Protein kinase.
+At position 61 to 270, the domain is characterized as YjeF N-terminal.
+At position 265 to 371, the domain is characterized as Rhodanese.
+At position 244 to 476, the domain is characterized as START.
+At position 6 to 237, the domain is characterized as Radical SAM core.
+At position 20 to 235, the domain is characterized as Radical SAM core.
+At position 103 to 144, the domain is characterized as JmjN.
+At position 250 to 420, the domain is characterized as JmjC.
+At position 112 to 239, the domain is characterized as HTH La-type RNA-binding.
+At position 247 to 335, the domain is characterized as RRM.
+At position 374 to 542, the domain is characterized as xRRM.
+At position 184 to 223, the domain is characterized as LRRCT.
+At position 38 to 100, the domain is characterized as S4 RNA-binding.
+At position 60 to 144, the domain is characterized as PA.
+At position 167 to 274, the domain is characterized as SPR.
+At position 25 to 256, the domain is characterized as Radical SAM core.
+At position 5 to 76, the domain is characterized as KRAB.
+At position 69 to 205, the domain is characterized as HD.
+At position 21 to 71, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 536 to 611, the domain is characterized as Cytochrome b5 heme-binding.
+At position 641 to 752, the domain is characterized as FAD-binding FR-type.
+At position 13 to 59, the domain is characterized as F-box.
+At position 169 to 413, the domain is characterized as NR LBD.
+At position 220 to 399, the domain is characterized as GAF.
+At position 613 to 684, the domain is characterized as PAS 1.
+At position 687 to 743, the domain is characterized as PAC.
+At position 747 to 818, the domain is characterized as PAS 2.
+At position 895 to 1116, the domain is characterized as Histidine kinase.
+At position 42 to 145, the domain is characterized as Glutaredoxin.
+At position 489 to 537, the domain is characterized as LysM.
+At position 137 to 232, the domain is characterized as Rhodanese.
+At position 41 to 74, the domain is characterized as LRRNT.
+At position 299 to 351, the domain is characterized as LRRCT.
+At position 352 to 441, the domain is characterized as Ig-like C2-type.
+At position 469 to 638, the domain is characterized as tr-type G.
+At position 23 to 115, the domain is characterized as Ig-like V-type.
+At position 123 to 220, the domain is characterized as Ig-like C2-type 1.
+At position 238 to 327, the domain is characterized as Ig-like C2-type 2.
+At position 109 to 144, the domain is characterized as EF-hand 3.
+At position 41 to 80, the domain is characterized as EGF-like 1.
+At position 81 to 205, the domain is characterized as SEA.
+At position 202 to 250, the domain is characterized as EGF-like 2; calcium-binding.
+At position 249 to 292, the domain is characterized as EGF-like 3.
+At position 173 to 225, the domain is characterized as KH.
+At position 204 to 391, the domain is characterized as Helicase ATP-binding.
+At position 424 to 575, the domain is characterized as Helicase C-terminal.
+At position 1 to 159, the domain is characterized as N-acetyltransferase.
+At position 7 to 233, the domain is characterized as ABC transporter.
+At position 172 to 359, the domain is characterized as Glutamine amidotransferase type-1.
+At position 25 to 328, the domain is characterized as Protein kinase.
+At position 11 to 293, the domain is characterized as Protein kinase.
+At position 32 to 161, the domain is characterized as Galectin.
+At position 38 to 101, the domain is characterized as S5 DRBM.
+At position 331 to 620, the domain is characterized as Protein kinase.
+At position 40 to 201, the domain is characterized as Helicase ATP-binding.
+At position 246 to 398, the domain is characterized as Helicase C-terminal.
+At position 21 to 483, the domain is characterized as Sema.
+At position 71 to 259, the domain is characterized as RNase H type-2.
+At position 44 to 145, the domain is characterized as LOB.
+At position 20 to 140, the domain is characterized as C-type lysozyme.
+At position 159 to 333, the domain is characterized as OBG-type G.
+At position 3 to 277, the domain is characterized as tr-type G.
+At position 53 to 257, the domain is characterized as ABC transmembrane type-1.
+At position 139 to 271, the domain is characterized as JmjC.
+At position 77 to 152, the domain is characterized as Rho RNA-BD.
+At position 194 to 295, the domain is characterized as HTH araC/xylS-type.
+At position 56 to 168, the domain is characterized as PA.
+At position 416 to 466, the domain is characterized as EGF-like 1.
+At position 469 to 516, the domain is characterized as EGF-like 2.
+At position 517 to 559, the domain is characterized as EGF-like 3; calcium-binding.
+At position 4 to 79, the domain is characterized as ACT.
+At position 37 to 103, the domain is characterized as BTB.
+At position 646 to 709, the domain is characterized as bZIP.
+At position 32 to 131, the domain is characterized as GOLD.
+At position 289 to 372, the domain is characterized as PDZ.
+At position 8 to 95, the domain is characterized as Acylphosphatase-like.
+At position 52 to 164, the domain is characterized as sHSP.
+At position 52 to 303, the domain is characterized as Radical SAM core.
+At position 349 to 416, the domain is characterized as S4 RNA-binding.
+At position 97 to 255, the domain is characterized as CP-type G.
+At position 129 to 372, the domain is characterized as Radical SAM core.
+At position 350 to 400, the domain is characterized as GPS.
+At position 153 to 223, the domain is characterized as PAS.
+At position 226 to 278, the domain is characterized as PAC.
+At position 289 to 507, the domain is characterized as Histidine kinase.
+At position 527 to 643, the domain is characterized as Response regulatory.
+At position 678 to 771, the domain is characterized as HPt.
+At position 6 to 60, the domain is characterized as HTH cro/C1-type.
+At position 140 to 196, the domain is characterized as CBS 1.
+At position 200 to 257, the domain is characterized as CBS 2.
+At position 24 to 102, the domain is characterized as Fibronectin type-III.
+At position 85 to 343, the domain is characterized as Protein kinase.
+At position 385 to 420, the domain is characterized as EF-hand 1.
+At position 421 to 456, the domain is characterized as EF-hand 2.
+At position 457 to 492, the domain is characterized as EF-hand 3.
+At position 497 to 527, the domain is characterized as EF-hand 4.
+At position 27 to 63, the domain is characterized as EGF-like.
+At position 70 to 151, the domain is characterized as Kringle.
+At position 179 to 424, the domain is characterized as Peptidase S1.
+At position 1 to 92, the domain is characterized as HTH arsR-type.
+At position 118 to 176, the domain is characterized as Chromo.
+At position 256 to 314, the domain is characterized as Pre-SET.
+At position 317 to 440, the domain is characterized as SET.
+At position 461 to 477, the domain is characterized as Post-SET.
+At position 19 to 86, the domain is characterized as HMA.
+At position 216 to 269, the domain is characterized as HAMP 1.
+At position 297 to 349, the domain is characterized as HAMP 2.
+At position 354 to 583, the domain is characterized as Methyl-accepting transducer.
+At position 22 to 357, the domain is characterized as PTS EIIC type-2.
+At position 392 to 481, the domain is characterized as PTS EIIB type-2.
+At position 31 to 173, the domain is characterized as C-type lectin.
+At position 257 to 298, the domain is characterized as EGF-like 1.
+At position 299 to 341, the domain is characterized as EGF-like 2.
+At position 342 to 381, the domain is characterized as EGF-like 3; calcium-binding.
+At position 382 to 423, the domain is characterized as EGF-like 4; calcium-binding.
+At position 424 to 462, the domain is characterized as EGF-like 5; calcium-binding.
+At position 22 to 86, the domain is characterized as 4Fe-4S Wbl-type.
+At position 119 to 227, the domain is characterized as CBM21.
+At position 65 to 196, the domain is characterized as HD.
+At position 1 to 73, the domain is characterized as Disintegrin.
+At position 20 to 110, the domain is characterized as RRM 1.
+At position 109 to 186, the domain is characterized as RRM 2.
+At position 370 to 482, the domain is characterized as Rhodanese.
+At position 226 to 280, the domain is characterized as bHLH.
+At position 4 to 261, the domain is characterized as Alpha-carbonic anhydrase.
+At position 105 to 160, the domain is characterized as EamA.
+At position 133 to 172, the domain is characterized as STI1 1.
+At position 32 to 263, the domain is characterized as BAR.
+At position 366 to 425, the domain is characterized as SH3.
+At position 92 to 239, the domain is characterized as C2 1.
+At position 557 to 675, the domain is characterized as MHD1.
+At position 786 to 893, the domain is characterized as MHD2.
+At position 908 to 1033, the domain is characterized as C2 2.
+At position 408 to 661, the domain is characterized as Tyrosine-protein phosphatase.
+At position 30 to 204, the domain is characterized as VWFA.
+At position 83 to 177, the domain is characterized as Toprim.
+At position 1 to 75, the domain is characterized as Carrier.
+At position 5 to 91, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 720 to 987, the domain is characterized as Protein kinase.
+At position 570 to 683, the domain is characterized as Cadherin 6.
+At position 52 to 134, the domain is characterized as SCAN box.
+At position 2 to 89, the domain is characterized as ATP-cone.
+At position 8 to 188, the domain is characterized as Guanylate kinase-like.
+At position 35 to 328, the domain is characterized as Protein kinase.
+At position 68 to 137, the domain is characterized as Apple 1.
+At position 141 to 214, the domain is characterized as Apple 2.
+At position 232 to 301, the domain is characterized as Apple 3.
+At position 305 to 375, the domain is characterized as Apple 4.
+At position 419 to 488, the domain is characterized as Apple 5.
+At position 492 to 565, the domain is characterized as Apple 6.
+At position 414 to 474, the domain is characterized as CBS.
+At position 83 to 364, the domain is characterized as Dynamin-type G.
+At position 90 to 161, the domain is characterized as GRAM.
+At position 226 to 601, the domain is characterized as Myotubularin phosphatase.
+At position 44 to 280, the domain is characterized as ABC transporter.
+At position 96 to 327, the domain is characterized as Radical SAM core.
+At position 40 to 149, the domain is characterized as tRNA-binding.
+At position 407 to 484, the domain is characterized as B5.
+At position 716 to 808, the domain is characterized as FDX-ACB.
+At position 1 to 146, the domain is characterized as MGS-like.
+At position 2 to 168, the domain is characterized as Miro 1.
+At position 184 to 219, the domain is characterized as EF-hand 1.
+At position 304 to 339, the domain is characterized as EF-hand 2.
+At position 416 to 578, the domain is characterized as Miro 2.
+At position 19 to 114, the domain is characterized as Rhodanese.
+At position 12 to 75, the domain is characterized as HMA.
+At position 72 to 244, the domain is characterized as Laminin G-like.
+At position 1609 to 1837, the domain is characterized as Fibrillar collagen NC1.
+At position 588 to 668, the domain is characterized as BRCT.
+At position 406 to 464, the domain is characterized as SOCS box.
+At position 1 to 243, the domain is characterized as KaiC 1.
+At position 257 to 509, the domain is characterized as KaiC 2.
+At position 23 to 88, the domain is characterized as J.
+At position 1 to 140, the domain is characterized as Nudix hydrolase.
+At position 463 to 577, the domain is characterized as Toprim.
+At position 307 to 544, the domain is characterized as Glutamine amidotransferase type-1.
+At position 19 to 73, the domain is characterized as HTH myb-type.
+At position 14 to 260, the domain is characterized as CN hydrolase.
+At position 29 to 210, the domain is characterized as Eph LBD.
+At position 328 to 441, the domain is characterized as Fibronectin type-III 1.
+At position 442 to 533, the domain is characterized as Fibronectin type-III 2.
+At position 626 to 887, the domain is characterized as Protein kinase.
+At position 910 to 974, the domain is characterized as SAM.
+At position 151 to 392, the domain is characterized as AB hydrolase-1.
+At position 8 to 74, the domain is characterized as HMA 1.
+At position 85 to 151, the domain is characterized as HMA 2.
+At position 171 to 237, the domain is characterized as HMA 3.
+At position 277 to 343, the domain is characterized as HMA 4.
+At position 377 to 443, the domain is characterized as HMA 5.
+At position 480 to 546, the domain is characterized as HMA 6.
+At position 556 to 622, the domain is characterized as HMA 7.
+At position 2 to 74, the domain is characterized as Sm.
+At position 1 to 57, the domain is characterized as TRAM.
+At position 44 to 259, the domain is characterized as Radical SAM core.
+At position 146 to 243, the domain is characterized as HD.
+At position 499 to 560, the domain is characterized as TGS.
+At position 763 to 837, the domain is characterized as ACT.
+At position 20 to 56, the domain is characterized as EGF-like 1.
+At position 57 to 106, the domain is characterized as EGF-like 2; calcium-binding.
+At position 107 to 156, the domain is characterized as EGF-like 3; calcium-binding.
+At position 414 to 466, the domain is characterized as GPS.
+At position 6 to 284, the domain is characterized as CN hydrolase.
+At position 1415 to 1937, the domain is characterized as FAT.
+At position 2044 to 2366, the domain is characterized as PI3K/PI4K catalytic.
+At position 2346 to 2378, the domain is characterized as FATC.
+At position 395 to 595, the domain is characterized as Helicase ATP-binding.
+At position 606 to 769, the domain is characterized as Helicase C-terminal.
+At position 24 to 198, the domain is characterized as Laminin G-like 1.
+At position 194 to 231, the domain is characterized as EGF-like 1.
+At position 258 to 455, the domain is characterized as Laminin G-like 2.
+At position 462 to 654, the domain is characterized as Laminin G-like 3.
+At position 658 to 695, the domain is characterized as EGF-like 2.
+At position 700 to 872, the domain is characterized as Laminin G-like 4.
+At position 886 to 1061, the domain is characterized as Laminin G-like 5.
+At position 1073 to 1110, the domain is characterized as EGF-like 3.
+At position 1114 to 1314, the domain is characterized as Laminin G-like 6.
+At position 63 to 282, the domain is characterized as ABC transporter.
+At position 93 to 168, the domain is characterized as Smr.
+At position 286 to 425, the domain is characterized as N-acetyltransferase.
+At position 14 to 239, the domain is characterized as Reverse transcriptase.
+At position 33 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 45 to 127, the domain is characterized as SCAN box.
+At position 492 to 774, the domain is characterized as Protein kinase.
+At position 8 to 138, the domain is characterized as MPN.
+At position 733 to 1013, the domain is characterized as Autotransporter.
+At position 40 to 62, the domain is characterized as Follistatin-like 1.
+At position 240 to 262, the domain is characterized as Follistatin-like 2.
+At position 62 to 159, the domain is characterized as Ig-like C2-type 1.
+At position 272 to 375, the domain is characterized as Ig-like C2-type 2.
+At position 86 to 261, the domain is characterized as Helicase ATP-binding.
+At position 273 to 434, the domain is characterized as Helicase C-terminal.
+At position 160 to 305, the domain is characterized as PX.
+At position 121 to 214, the domain is characterized as Rhodanese.
+At position 33 to 113, the domain is characterized as MANSC.
+At position 356 to 386, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 420 to 439, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 838 to 904, the domain is characterized as SAM 1.
+At position 953 to 1017, the domain is characterized as SAM 2.
+At position 1041 to 1110, the domain is characterized as SAM 3.
+At position 15 to 222, the domain is characterized as MARVEL.
+At position 28 to 146, the domain is characterized as PID.
+At position 296 to 392, the domain is characterized as SH2.
+At position 62 to 205, the domain is characterized as EXPERA.
+At position 289 to 576, the domain is characterized as Protein kinase.
+At position 2 to 167, the domain is characterized as EngA-type G 1.
+At position 1 to 27, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 46 to 273, the domain is characterized as Radical SAM core.
+At position 87 to 190, the domain is characterized as Glutaredoxin.
+At position 259 to 372, the domain is characterized as GST C-terminal.
+At position 159 to 233, the domain is characterized as PPIase FKBP-type.
+At position 64 to 168, the domain is characterized as Cadherin 1.
+At position 169 to 277, the domain is characterized as Cadherin 2.
+At position 278 to 394, the domain is characterized as Cadherin 3.
+At position 395 to 498, the domain is characterized as Cadherin 4.
+At position 499 to 616, the domain is characterized as Cadherin 5.
+At position 30 to 59, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 257 to 449, the domain is characterized as PPIase cyclophilin-type.
+At position 28 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 187 to 360, the domain is characterized as EngA-type G 2.
+At position 44 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 210 to 252, the domain is characterized as EGF-like 1.
+At position 254 to 299, the domain is characterized as EGF-like 2.
+At position 301 to 341, the domain is characterized as EGF-like 3.
+At position 350 to 440, the domain is characterized as Ig-like C2-type 2.
+At position 447 to 541, the domain is characterized as Fibronectin type-III 1.
+At position 545 to 637, the domain is characterized as Fibronectin type-III 2.
+At position 642 to 735, the domain is characterized as Fibronectin type-III 3.
+At position 825 to 1097, the domain is characterized as Protein kinase.
+At position 87 to 159, the domain is characterized as AB hydrolase-1.
+At position 54 to 234, the domain is characterized as Macro.
+At position 342 to 490, the domain is characterized as CRAL-TRIO.
+At position 20 to 132, the domain is characterized as Thioredoxin 1.
+At position 124 to 287, the domain is characterized as Thioredoxin 2.
+At position 11 to 93, the domain is characterized as GIY-YIG.
+At position 53 to 600, the domain is characterized as PLA2c.
+At position 32 to 352, the domain is characterized as G-alpha.
+At position 2 to 458, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 485 to 774, the domain is characterized as UvrD-like helicase C-terminal.
+At position 94 to 295, the domain is characterized as ABC transmembrane type-1.
+At position 325 to 505, the domain is characterized as PCI.
+At position 608 to 728, the domain is characterized as TFIIS central.
+At position 867 to 970, the domain is characterized as SPOC.
+At position 41 to 150, the domain is characterized as CUB.
+At position 152 to 248, the domain is characterized as LCCL.
+At position 248 to 412, the domain is characterized as F5/8 type C.
+At position 121 to 361, the domain is characterized as PABS.
+At position 1 to 66, the domain is characterized as LCN-type CS-alpha/beta.
+At position 406 to 484, the domain is characterized as Rhodanese.
+At position 10 to 304, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 305 to 560, the domain is characterized as UvrD-like helicase C-terminal.
+At position 633 to 713, the domain is characterized as HRDC.
+At position 23 to 281, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 9 to 100, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 6 to 134, the domain is characterized as MATH.
+At position 107 to 229, the domain is characterized as MSP.
+At position 9 to 75, the domain is characterized as HMA.
+At position 32 to 271, the domain is characterized as ABC transporter.
+At position 62 to 91, the domain is characterized as IQ.
+At position 126 to 282, the domain is characterized as ELMO.
+At position 90 to 130, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 131 to 173, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 31 to 109, the domain is characterized as Cystatin.
+At position 8 to 171, the domain is characterized as Clp R.
+At position 435 to 550, the domain is characterized as Toprim.
+At position 44 to 90, the domain is characterized as F-box.
+At position 4 to 195, the domain is characterized as DPCK.
+At position 72 to 346, the domain is characterized as Pyruvate carboxyltransferase.
+At position 318 to 411, the domain is characterized as BRCT.
+At position 1 to 56, the domain is characterized as HTH myb-type 1.
+At position 57 to 108, the domain is characterized as HTH myb-type 2.
+At position 43 to 106, the domain is characterized as S5 DRBM.
+At position 25 to 99, the domain is characterized as REM-1.
+At position 110 to 501, the domain is characterized as BRO1.
+At position 515 to 592, the domain is characterized as PDZ.
+At position 12 to 80, the domain is characterized as BTB.
+At position 20 to 221, the domain is characterized as Cytochrome b561.
+At position 679 to 870, the domain is characterized as ATP-grasp 2.
+At position 937 to 1077, the domain is characterized as MGS-like.
+At position 306 to 475, the domain is characterized as VWFA.
+At position 54 to 196, the domain is characterized as EXPERA.
+At position 122 to 223, the domain is characterized as Rhodanese.
+At position 13 to 192, the domain is characterized as Exonuclease.
+At position 202 to 355, the domain is characterized as ExoI SH3-like.
+At position 358 to 475, the domain is characterized as ExoI C-terminal.
+At position 2 to 95, the domain is characterized as Core-binding (CB).
+At position 116 to 304, the domain is characterized as Tyr recombinase.
+At position 25 to 182, the domain is characterized as Helicase ATP-binding.
+At position 5 to 50, the domain is characterized as SpoVT-AbrB 1.
+At position 93 to 136, the domain is characterized as SpoVT-AbrB 2.
+At position 263 to 378, the domain is characterized as C-type lectin.
+At position 3 to 71, the domain is characterized as DRBM 1.
+At position 180 to 252, the domain is characterized as DRBM 2.
+At position 398 to 564, the domain is characterized as Helicase ATP-binding.
+At position 636 to 809, the domain is characterized as Helicase C-terminal.
+At position 8 to 78, the domain is characterized as KRAB.
+At position 12 to 67, the domain is characterized as HTH cro/C1-type.
+At position 5 to 221, the domain is characterized as ABC transporter.
+At position 793 to 861, the domain is characterized as HP.
+At position 207 to 267, the domain is characterized as KH.
+At position 1851 to 1880, the domain is characterized as IQ.
+At position 428 to 769, the domain is characterized as Kinesin motor.
+At position 24 to 271, the domain is characterized as Protein kinase.
+At position 289 to 329, the domain is characterized as UBA.
+At position 415 to 582, the domain is characterized as tr-type G.
+At position 45 to 68, the domain is characterized as IQ.
+At position 805 to 914, the domain is characterized as MSP.
+At position 11 to 166, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 87, the domain is characterized as HPr.
+At position 214 to 360, the domain is characterized as TrmE-type G.
+At position 84 to 156, the domain is characterized as Chromo 1.
+At position 179 to 240, the domain is characterized as Chromo 2.
+At position 279 to 458, the domain is characterized as Helicase ATP-binding.
+At position 590 to 739, the domain is characterized as Helicase C-terminal.
+At position 25 to 132, the domain is characterized as Ig-like 1.
+At position 344 to 429, the domain is characterized as Ig-like 2.
+At position 178 to 373, the domain is characterized as EXS.
+At position 3 to 183, the domain is characterized as KARI N-terminal Rossmann.
+At position 8 to 63, the domain is characterized as HTH cro/C1-type.
+At position 61 to 177, the domain is characterized as CMP/dCMP-type deaminase.
+At position 5 to 145, the domain is characterized as N-acetyltransferase 1.
+At position 168 to 323, the domain is characterized as N-acetyltransferase 2.
+At position 99 to 304, the domain is characterized as ATP-grasp.
+At position 214 to 297, the domain is characterized as RRM 1.
+At position 334 to 412, the domain is characterized as RRM 2.
+At position 453 to 539, the domain is characterized as RRM 3.
+At position 64 to 283, the domain is characterized as Radical SAM core.
+At position 62 to 289, the domain is characterized as Radical SAM core.
+At position 514 to 686, the domain is characterized as tr-type G.
+At position 14 to 73, the domain is characterized as Sm.
+At position 327 to 497, the domain is characterized as tr-type G.
+At position 128 to 236, the domain is characterized as CUB.
+At position 235 to 272, the domain is characterized as EGF-like.
+At position 278 to 344, the domain is characterized as Sushi 1.
+At position 387 to 444, the domain is characterized as Sushi 2.
+At position 445 to 720, the domain is characterized as Peptidase S1.
+At position 39 to 129, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 175 to 205, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 49 to 153, the domain is characterized as Cadherin 1.
+At position 154 to 262, the domain is characterized as Cadherin 2.
+At position 263 to 377, the domain is characterized as Cadherin 3.
+At position 378 to 482, the domain is characterized as Cadherin 4.
+At position 482 to 599, the domain is characterized as Cadherin 5.
+At position 242 to 326, the domain is characterized as Ig-like C2-type 2.
+At position 679 to 913, the domain is characterized as NR LBD.
+At position 496 to 635, the domain is characterized as Flavodoxin-like.
+At position 674 to 907, the domain is characterized as FAD-binding FR-type.
+At position 229 to 397, the domain is characterized as PCI.
+At position 29 to 242, the domain is characterized as GH16.
+At position 29 to 120, the domain is characterized as Nudix hydrolase.
+At position 27 to 97, the domain is characterized as KRAB.
+At position 85 to 149, the domain is characterized as CSD.
+At position 81 to 199, the domain is characterized as GST C-terminal.
+At position 4 to 292, the domain is characterized as DegV.
+At position 164 to 210, the domain is characterized as G-patch.
+At position 231 to 258, the domain is characterized as KOW 1.
+At position 401 to 428, the domain is characterized as KOW 2.
+At position 4 to 97, the domain is characterized as Core-binding (CB).
+At position 118 to 309, the domain is characterized as Tyr recombinase.
+At position 455 to 485, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 501 to 530, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 4 to 229, the domain is characterized as tr-type G.
+At position 27 to 209, the domain is characterized as Eph LBD.
+At position 332 to 445, the domain is characterized as Fibronectin type-III 1.
+At position 447 to 538, the domain is characterized as Fibronectin type-III 2.
+At position 624 to 884, the domain is characterized as Protein kinase.
+At position 913 to 976, the domain is characterized as SAM.
+At position 44 to 141, the domain is characterized as RRM.
+At position 18 to 76, the domain is characterized as CpcD-like.
+At position 133 to 256, the domain is characterized as FAD-binding FR-type.
+At position 5 to 146, the domain is characterized as CBM-cenC 1.
+At position 183 to 313, the domain is characterized as CBM-cenC 2.
+At position 348 to 482, the domain is characterized as CBM-cenC 3.
+At position 517 to 662, the domain is characterized as CBM-cenC 4.
+At position 711 to 1006, the domain is characterized as GH10.
+At position 1 to 219, the domain is characterized as RNase H type-2.
+At position 1037 to 1173, the domain is characterized as RanBD1 1.
+At position 1334 to 1470, the domain is characterized as RanBD1 2.
+At position 1703 to 1753, the domain is characterized as GRIP.
+At position 285 to 424, the domain is characterized as SIS 1.
+At position 457 to 595, the domain is characterized as SIS 2.
+At position 223 to 319, the domain is characterized as BEN.
+At position 51 to 149, the domain is characterized as BTB.
+At position 8 to 40, the domain is characterized as LisH.
+At position 5 to 154, the domain is characterized as N-acetyltransferase.
+At position 1 to 225, the domain is characterized as BAR.
+At position 292 to 430, the domain is characterized as PH.
+At position 501 to 643, the domain is characterized as Arf-GAP.
+At position 327 to 371, the domain is characterized as TSP type-1.
+At position 396 to 559, the domain is characterized as AMOP.
+At position 263 to 372, the domain is characterized as CRC.
+At position 1 to 627, the domain is characterized as Peptidase M13.
+At position 63 to 428, the domain is characterized as Peptidase A1.
+At position 5 to 133, the domain is characterized as B12-binding.
+At position 570 to 629, the domain is characterized as KH.
+At position 639 to 713, the domain is characterized as S1 motif.
+At position 428 to 563, the domain is characterized as GGDEF.
+At position 9 to 120, the domain is characterized as HIT.
+At position 401 to 508, the domain is characterized as Rhodanese.
+At position 153 to 353, the domain is characterized as AH.
+At position 33 to 227, the domain is characterized as Lon N-terminal.
+At position 615 to 796, the domain is characterized as Lon proteolytic.
+At position 1 to 108, the domain is characterized as HSR.
+At position 358 to 439, the domain is characterized as SAND.
+At position 129 to 568, the domain is characterized as Urease.
+At position 34 to 285, the domain is characterized as Protein kinase.
+At position 152 to 262, the domain is characterized as FAD-binding FR-type.
+At position 93 to 188, the domain is characterized as POU-specific atypical.
+At position 416 to 580, the domain is characterized as Miro 2.
+At position 220 to 267, the domain is characterized as GRAM 1.
+At position 271 to 373, the domain is characterized as PH.
+At position 609 to 675, the domain is characterized as GRAM 2.
+At position 25 to 275, the domain is characterized as ABC transporter.
+At position 17 to 146, the domain is characterized as RNase III.
+At position 172 to 241, the domain is characterized as DRBM.
+At position 32 to 185, the domain is characterized as UBC core.
+At position 11 to 47, the domain is characterized as EF-hand 1.
+At position 102 to 137, the domain is characterized as EF-hand 2.
+At position 113 to 346, the domain is characterized as Radical SAM core.
+At position 56 to 132, the domain is characterized as Cytochrome b5 heme-binding.
+At position 42 to 273, the domain is characterized as SET.
+At position 4 to 222, the domain is characterized as Radical SAM core.
+At position 312 to 586, the domain is characterized as Protein kinase.
+At position 483 to 509, the domain is characterized as KASH.
+At position 132 to 375, the domain is characterized as Radical SAM core.
+At position 144 to 373, the domain is characterized as Radical SAM core.
+At position 376 to 444, the domain is characterized as TRAM.
+At position 19 to 126, the domain is characterized as Ig-like.
+At position 80 to 131, the domain is characterized as P-type.
+At position 37 to 291, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 125 to 440, the domain is characterized as RHD.
+At position 5 to 224, the domain is characterized as ABC transporter.
+At position 92 to 308, the domain is characterized as RNase H type-2.
+At position 25 to 156, the domain is characterized as AB hydrolase-1.
+At position 144 to 236, the domain is characterized as PpiC.
+At position 24 to 91, the domain is characterized as BTB.
+At position 1 to 130, the domain is characterized as MGS-like.
+At position 351 to 412, the domain is characterized as S4 RNA-binding.
+At position 54 to 180, the domain is characterized as C2.
+At position 246 to 279, the domain is characterized as WW 1.
+At position 402 to 435, the domain is characterized as WW 2.
+At position 459 to 492, the domain is characterized as WW 3.
+At position 551 to 887, the domain is characterized as HECT.
+At position 379 to 414, the domain is characterized as EF-hand.
+At position 76 to 188, the domain is characterized as DUF1279.
+At position 32 to 153, the domain is characterized as C-type lectin.
+At position 2 to 59, the domain is characterized as TGS.
+At position 110 to 490, the domain is characterized as GRAS.
+At position 22 to 315, the domain is characterized as Dynamin-type G.
+At position 657 to 748, the domain is characterized as GED.
+At position 80 to 286, the domain is characterized as Peptidase M12B.
+At position 287 to 383, the domain is characterized as Disintegrin.
+At position 384 to 439, the domain is characterized as TSP type-1 1.
+At position 682 to 730, the domain is characterized as TSP type-1 2.
+At position 742 to 805, the domain is characterized as TSP type-1 3.
+At position 808 to 859, the domain is characterized as TSP type-1 4.
+At position 896 to 950, the domain is characterized as TSP type-1 5.
+At position 951 to 1011, the domain is characterized as TSP type-1 6.
+At position 1012 to 1068, the domain is characterized as TSP type-1 7.
+At position 1072 to 1131, the domain is characterized as TSP type-1 8.
+At position 1192 to 1298, the domain is characterized as CUB 1.
+At position 1299 to 1427, the domain is characterized as CUB 2.
+At position 67 to 111, the domain is characterized as LysM.
+At position 36 to 108, the domain is characterized as FHA.
+At position 30 to 103, the domain is characterized as TB.
+At position 94 to 117, the domain is characterized as Follistatin-like 1.
+At position 112 to 166, the domain is characterized as Kazal-like 1.
+At position 167 to 190, the domain is characterized as Follistatin-like 2.
+At position 186 to 241, the domain is characterized as Kazal-like 2.
+At position 244 to 268, the domain is characterized as Follistatin-like 3.
+At position 264 to 318, the domain is characterized as Kazal-like 3.
+At position 63 to 102, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 110 to 193, the domain is characterized as MEIS N-terminal.
+At position 288 to 510, the domain is characterized as B30.2/SPRY.
+At position 196 to 386, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 68, the domain is characterized as Sm.
+At position 189 to 225, the domain is characterized as DFDF.
+At position 282 to 486, the domain is characterized as YjeF N-terminal.
+At position 65 to 253, the domain is characterized as ABC transmembrane type-1.
+At position 130 to 306, the domain is characterized as NodB homology.
+At position 152 to 383, the domain is characterized as Radical SAM core.
+At position 386 to 455, the domain is characterized as TRAM.
+At position 449 to 525, the domain is characterized as RRM 1.
+At position 549 to 630, the domain is characterized as RRM 2.
+At position 413 to 611, the domain is characterized as MAGE.
+At position 89 to 303, the domain is characterized as RNase H type-2.
+At position 2 to 310, the domain is characterized as Asparaginase/glutaminase.
+At position 99 to 171, the domain is characterized as PRC barrel.
+At position 816 to 1101, the domain is characterized as SMP-LTD.
+At position 26 to 160, the domain is characterized as Nudix hydrolase.
+At position 419 to 653, the domain is characterized as Histidine kinase.
+At position 32 to 478, the domain is characterized as Biotin carboxylation.
+At position 151 to 349, the domain is characterized as ATP-grasp.
+At position 653 to 729, the domain is characterized as Biotinyl-binding.
+At position 19 to 146, the domain is characterized as Response regulatory.
+At position 10 to 90, the domain is characterized as NAB.
+At position 506 to 716, the domain is characterized as Helicase ATP-binding.
+At position 988 to 1144, the domain is characterized as Helicase C-terminal.
+At position 178 to 375, the domain is characterized as Peptidase M12B.
+At position 384 to 473, the domain is characterized as Disintegrin.
+At position 612 to 645, the domain is characterized as EGF-like.
+At position 20 to 193, the domain is characterized as EngB-type G.
+At position 447 to 537, the domain is characterized as CARD.
+At position 202 to 265, the domain is characterized as KH.
+At position 328 to 421, the domain is characterized as HD.
+At position 442 to 579, the domain is characterized as YTH.
+At position 183 to 417, the domain is characterized as NR LBD.
+At position 41 to 58, the domain is characterized as EF-hand 1.
+At position 96 to 131, the domain is characterized as EF-hand 3.
+At position 144 to 179, the domain is characterized as EF-hand 4.
+At position 2 to 60, the domain is characterized as PTS EIIA type-2.
+At position 282 to 520, the domain is characterized as PIK helical.
+At position 5 to 167, the domain is characterized as EngA-type G 1.
+At position 174 to 349, the domain is characterized as EngA-type G 2.
+At position 350 to 433, the domain is characterized as KH-like.
+At position 65 to 161, the domain is characterized as Rieske.
+At position 252 to 441, the domain is characterized as GATase cobBQ-type.
+At position 4 to 499, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 526 to 853, the domain is characterized as UvrD-like helicase C-terminal.
+At position 5 to 100, the domain is characterized as PH.
+At position 120 to 374, the domain is characterized as Protein kinase.
+At position 375 to 444, the domain is characterized as AGC-kinase C-terminal.
+At position 267 to 460, the domain is characterized as B30.2/SPRY.
+At position 1 to 187, the domain is characterized as PTS EIIC type-5.
+At position 52 to 128, the domain is characterized as EMI.
+At position 199 to 267, the domain is characterized as Collagen-like 1.
+At position 302 to 334, the domain is characterized as Collagen-like 2.
+At position 240 to 286, the domain is characterized as G-patch.
+At position 13 to 137, the domain is characterized as C-type lectin.
+At position 99 to 397, the domain is characterized as Calpain catalytic.
+At position 658 to 693, the domain is characterized as EF-hand 1.
+At position 694 to 729, the domain is characterized as EF-hand 2.
+At position 1 to 231, the domain is characterized as Radical SAM core.
+At position 430 to 544, the domain is characterized as HD.
+At position 610 to 686, the domain is characterized as ACT 1.
+At position 730 to 805, the domain is characterized as ACT 2.
+At position 2 to 149, the domain is characterized as UBC core.
+At position 203 to 391, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1309 to 1887, the domain is characterized as FAT.
+At position 2065 to 2378, the domain is characterized as PI3K/PI4K catalytic.
+At position 2449 to 2481, the domain is characterized as FATC.
+At position 34 to 149, the domain is characterized as C-type lectin.
+At position 7 to 78, the domain is characterized as Sm.
+At position 56 to 70, the domain is characterized as PRAD.
+At position 232 to 540, the domain is characterized as Calpain catalytic.
+At position 276 to 351, the domain is characterized as B5.
+At position 149 to 234, the domain is characterized as Ig-like C2-type 1.
+At position 41 to 169, the domain is characterized as SCP.
+At position 205 to 237, the domain is characterized as ShKT.
+At position 44 to 129, the domain is characterized as ELM2.
+At position 130 to 181, the domain is characterized as SANT 1.
+At position 327 to 378, the domain is characterized as SANT 2.
+At position 120 to 473, the domain is characterized as PUM-HD.
+At position 18 to 221, the domain is characterized as YjeF N-terminal.
+At position 38 to 235, the domain is characterized as tr-type G.
+At position 10 to 279, the domain is characterized as tr-type G.
+At position 356 to 443, the domain is characterized as SWIRM.
+At position 303 to 562, the domain is characterized as Protein kinase.
+At position 44 to 262, the domain is characterized as Radical SAM core.
+At position 443 to 491, the domain is characterized as SANT.
+At position 518 to 619, the domain is characterized as CXC.
+At position 21 to 212, the domain is characterized as Velvet.
+At position 293 to 531, the domain is characterized as NR LBD.
+At position 68 to 285, the domain is characterized as Radical SAM core.
+At position 352 to 540, the domain is characterized as N-acetyltransferase.
+At position 62 to 200, the domain is characterized as Flavodoxin-like.
+At position 232 to 446, the domain is characterized as FAD-binding FR-type.
+At position 310 to 356, the domain is characterized as F-box.
+At position 18 to 142, the domain is characterized as MH1.
+At position 323 to 552, the domain is characterized as MH2.
+At position 40 to 148, the domain is characterized as tRNA-binding.
+At position 401 to 479, the domain is characterized as B5.
+At position 721 to 814, the domain is characterized as FDX-ACB.
+At position 7 to 124, the domain is characterized as MSP.
+At position 49 to 137, the domain is characterized as PPIase FKBP-type.
+At position 125 to 353, the domain is characterized as OTU.
+At position 592 to 650, the domain is characterized as RAP.
+At position 459 to 531, the domain is characterized as RRM.
+At position 1 to 162, the domain is characterized as NR LBD.
+At position 25 to 61, the domain is characterized as EGF-like.
+At position 20 to 216, the domain is characterized as ABC transmembrane type-1.
+At position 262 to 351, the domain is characterized as HTH La-type RNA-binding.
+At position 348 to 423, the domain is characterized as RRM.
+At position 7 to 308, the domain is characterized as Helicase ATP-binding.
+At position 45 to 159, the domain is characterized as CUB 1.
+At position 177 to 292, the domain is characterized as CUB 2.
+At position 296 to 332, the domain is characterized as LDL-receptor class A.
+At position 4 to 139, the domain is characterized as CID.
+At position 104 to 133, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 143 to 172, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 3 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 255 to 432, the domain is characterized as VWFA.
+At position 448 to 539, the domain is characterized as Cache.
+At position 3 to 97, the domain is characterized as Acylphosphatase-like.
+At position 31 to 199, the domain is characterized as Era-type G.
+At position 230 to 306, the domain is characterized as KH type-2.
+At position 131 to 323, the domain is characterized as ATP-grasp 1.
+At position 661 to 852, the domain is characterized as ATP-grasp 2.
+At position 918 to 1053, the domain is characterized as MGS-like.
+At position 102 to 300, the domain is characterized as ATP-grasp.
+At position 137 to 200, the domain is characterized as bZIP.
+At position 31 to 179, the domain is characterized as N-acetyltransferase.
+At position 121 to 315, the domain is characterized as ATP-grasp.
+At position 3 to 90, the domain is characterized as Acylphosphatase-like.
+At position 138 to 374, the domain is characterized as Alpha-carbonic anhydrase.
+At position 97 to 273, the domain is characterized as Protein kinase.
+At position 22 to 90, the domain is characterized as HTH gntR-type.
+At position 256 to 499, the domain is characterized as ABC transporter 2.
+At position 83 to 161, the domain is characterized as GIY-YIG.
+At position 271 to 306, the domain is characterized as UVR.
+At position 583 to 663, the domain is characterized as BRCT.
+At position 1 to 202, the domain is characterized as CNNM transmembrane.
+At position 221 to 280, the domain is characterized as CBS 1.
+At position 290 to 347, the domain is characterized as CBS 2.
+At position 20 to 146, the domain is characterized as C2.
+At position 174 to 209, the domain is characterized as EF-hand 1.
+At position 210 to 245, the domain is characterized as EF-hand 2.
+At position 6 to 220, the domain is characterized as ABC transporter.
+At position 18 to 210, the domain is characterized as RNase H type-2.
+At position 8 to 278, the domain is characterized as tr-type G.
+At position 84 to 179, the domain is characterized as Toprim.
+At position 39 to 160, the domain is characterized as SET.
+At position 65 to 126, the domain is characterized as SH3.
+At position 132 to 229, the domain is characterized as SH2.
+At position 251 to 504, the domain is characterized as Protein kinase.
+At position 116 to 312, the domain is characterized as GST C-terminal.
+At position 132 to 381, the domain is characterized as Radical SAM core.
+At position 106 to 183, the domain is characterized as RRM.
+At position 66 to 118, the domain is characterized as bHLH.
+At position 235 to 484, the domain is characterized as Ku.
+At position 118 to 244, the domain is characterized as SLD.
+At position 34 to 158, the domain is characterized as C-type lectin.
+At position 3 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 166 to 217, the domain is characterized as FAF.
+At position 40 to 120, the domain is characterized as IGFBP N-terminal.
+At position 105 to 164, the domain is characterized as Kazal-like.
+At position 372 to 474, the domain is characterized as PDZ.
+At position 53 to 171, the domain is characterized as RGS.
+At position 186 to 449, the domain is characterized as Protein kinase.
+At position 138 to 200, the domain is characterized as CBS 1.
+At position 202 to 258, the domain is characterized as CBS 2.
+At position 7 to 168, the domain is characterized as Exonuclease.
+At position 26 to 68, the domain is characterized as WAP 1.
+At position 69 to 114, the domain is characterized as WAP 2.
+At position 119 to 162, the domain is characterized as WAP 3.
+At position 163 to 207, the domain is characterized as WAP 4.
+At position 13 to 275, the domain is characterized as Protein kinase.
+At position 57 to 230, the domain is characterized as FAD-binding PCMH-type.
+At position 41 to 381, the domain is characterized as G-alpha.
+At position 107 to 170, the domain is characterized as bZIP.
+At position 226 to 451, the domain is characterized as Rho-GAP.
+At position 2 to 195, the domain is characterized as Glutamine amidotransferase type-1.
+At position 70 to 255, the domain is characterized as RNase H type-2.
+At position 1 to 29, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 30 to 57, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 67 to 96, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 97 to 127, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 138 to 166, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 168 to 197, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 207 to 236, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 238 to 266, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 276 to 305, the domain is characterized as 4Fe-4S ferredoxin-type 9.
+At position 314 to 345, the domain is characterized as 4Fe-4S ferredoxin-type 10.
+At position 357 to 386, the domain is characterized as 4Fe-4S ferredoxin-type 11.
+At position 385 to 412, the domain is characterized as 4Fe-4S ferredoxin-type 12.
+At position 62 to 166, the domain is characterized as PA.
+At position 114 to 149, the domain is characterized as EF-hand 1.
+At position 155 to 183, the domain is characterized as EF-hand 2.
+At position 181 to 216, the domain is characterized as EF-hand 3.
+At position 217 to 253, the domain is characterized as EF-hand 4.
+At position 254 to 283, the domain is characterized as EF-hand 5.
+At position 81 to 135, the domain is characterized as HTH cro/C1-type.
+At position 411 to 599, the domain is characterized as Helicase ATP-binding.
+At position 632 to 792, the domain is characterized as Helicase C-terminal.
+At position 20 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 212 to 413, the domain is characterized as GMPS ATP-PPase.
+At position 702 to 777, the domain is characterized as Smr.
+At position 75 to 349, the domain is characterized as Protein kinase.
+At position 261 to 398, the domain is characterized as YTH.
+At position 46 to 202, the domain is characterized as PID.
+At position 492 to 551, the domain is characterized as SH3.
+At position 109 to 306, the domain is characterized as ATP-grasp.
+At position 263 to 346, the domain is characterized as IPT/TIG.
+At position 19 to 107, the domain is characterized as Ig-like C1-type.
+At position 27 to 102, the domain is characterized as RRM 1.
+At position 419 to 502, the domain is characterized as RRM 2.
+At position 40 to 185, the domain is characterized as FAS1 1.
+At position 271 to 414, the domain is characterized as FAS1 2.
+At position 20 to 97, the domain is characterized as GIY-YIG.
+At position 5 to 221, the domain is characterized as tr-type G.
+At position 1 to 388, the domain is characterized as SMP-LTD.
+At position 254 to 416, the domain is characterized as PCI.
+At position 35 to 343, the domain is characterized as Cbl-PTB.
+At position 931 to 970, the domain is characterized as UBA.
+At position 266 to 355, the domain is characterized as PpiC.
+At position 8 to 123, the domain is characterized as HotDog ACOT-type.
+At position 23 to 110, the domain is characterized as PDZ 1.
+At position 185 to 263, the domain is characterized as PDZ 2.
+At position 420 to 501, the domain is characterized as PDZ 3.
+At position 515 to 583, the domain is characterized as SH3.
+At position 609 to 790, the domain is characterized as Guanylate kinase-like.
+At position 1635 to 1769, the domain is characterized as ZU5.
+At position 10 to 209, the domain is characterized as tr-type G.
+At position 45 to 308, the domain is characterized as ZP.
+At position 19 to 96, the domain is characterized as Cytochrome b5 heme-binding.
+At position 5 to 80, the domain is characterized as GIY-YIG.
+At position 305 to 477, the domain is characterized as Helicase ATP-binding.
+At position 525 to 717, the domain is characterized as Helicase C-terminal.
+At position 14 to 79, the domain is characterized as J.
+At position 186 to 448, the domain is characterized as Protein kinase.
+At position 449 to 514, the domain is characterized as AGC-kinase C-terminal.
+At position 5 to 157, the domain is characterized as N-acetyltransferase 1.
+At position 159 to 306, the domain is characterized as N-acetyltransferase 2.
+At position 81 to 244, the domain is characterized as EngA-type G 1.
+At position 254 to 427, the domain is characterized as EngA-type G 2.
+At position 428 to 510, the domain is characterized as KH-like.
+At position 400 to 587, the domain is characterized as B30.2/SPRY.
+At position 617 to 649, the domain is characterized as LisH.
+At position 655 to 712, the domain is characterized as CTLH.
+At position 142 to 375, the domain is characterized as Radical SAM core.
+At position 378 to 448, the domain is characterized as TRAM.
+At position 32 to 90, the domain is characterized as 4Fe-4S.
+At position 105 to 134, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 135 to 164, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 398 to 430, the domain is characterized as EGF-like 1.
+At position 433 to 471, the domain is characterized as EGF-like 2.
+At position 33 to 209, the domain is characterized as Helicase ATP-binding.
+At position 242 to 389, the domain is characterized as Helicase C-terminal.
+At position 27 to 77, the domain is characterized as bHLH.
+At position 34 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 38 to 186, the domain is characterized as PADR1 zinc-binding.
+At position 187 to 274, the domain is characterized as BRCT.
+At position 322 to 422, the domain is characterized as WGR.
+At position 449 to 568, the domain is characterized as PARP alpha-helical.
+At position 577 to 808, the domain is characterized as PARP catalytic.
+At position 347 to 414, the domain is characterized as S4 RNA-binding.
+At position 12 to 286, the domain is characterized as tr-type G.
+At position 64 to 141, the domain is characterized as RRM.
+At position 8 to 80, the domain is characterized as Tudor-knot.
+At position 128 to 308, the domain is characterized as MRG.
+At position 16 to 191, the domain is characterized as RNase H type-2.
+At position 376 to 560, the domain is characterized as DH.
+At position 592 to 704, the domain is characterized as PH.
+At position 715 to 776, the domain is characterized as SH3.
+At position 156 to 219, the domain is characterized as bZIP.
+At position 364 to 414, the domain is characterized as SOCS box.
+At position 395 to 494, the domain is characterized as Ras-associating.
+At position 584 to 721, the domain is characterized as DAGKc.
+At position 41 to 157, the domain is characterized as MTTase N-terminal.
+At position 180 to 416, the domain is characterized as Radical SAM core.
+At position 419 to 486, the domain is characterized as TRAM.
+At position 87 to 146, the domain is characterized as KID.
+At position 269 to 327, the domain is characterized as bZIP.
+At position 2 to 250, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 38 to 158, the domain is characterized as Plastocyanin-like 1.
+At position 168 to 320, the domain is characterized as Plastocyanin-like 2.
+At position 426 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 46 to 69, the domain is characterized as IQ.
+At position 356 to 472, the domain is characterized as Cadherin 3.
+At position 473 to 580, the domain is characterized as Cadherin 4.
+At position 581 to 691, the domain is characterized as Cadherin 5.
+At position 24 to 184, the domain is characterized as MAM.
+At position 186 to 271, the domain is characterized as Ig-like C2-type.
+At position 284 to 379, the domain is characterized as Fibronectin type-III 1.
+At position 382 to 483, the domain is characterized as Fibronectin type-III 2.
+At position 489 to 590, the domain is characterized as Fibronectin type-III 3.
+At position 597 to 677, the domain is characterized as Fibronectin type-III 4.
+At position 886 to 1142, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1174 to 1437, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 19 to 168, the domain is characterized as Thioredoxin.
+At position 10 to 71, the domain is characterized as Sm.
+At position 105 to 179, the domain is characterized as S4 RNA-binding.
+At position 2 to 236, the domain is characterized as Glutamine amidotransferase type-2.
+At position 7 to 108, the domain is characterized as Rieske.
+At position 420 to 535, the domain is characterized as Toprim.
+At position 5 to 237, the domain is characterized as ABC transporter 1.
+At position 249 to 492, the domain is characterized as ABC transporter 2.
+At position 416 to 838, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1368 to 1700, the domain is characterized as PKS/mFAS DH.
+At position 1795 to 1870, the domain is characterized as Carrier.
+At position 363 to 642, the domain is characterized as Radical SAM core.
+At position 2 to 132, the domain is characterized as HTH rrf2-type.
+At position 84 to 222, the domain is characterized as GST C-terminal.
+At position 5 to 231, the domain is characterized as ABC transporter.
+At position 3 to 267, the domain is characterized as F-BAR.
+At position 359 to 436, the domain is characterized as REM-1.
+At position 527 to 589, the domain is characterized as SH3.
+At position 92 to 422, the domain is characterized as Asparaginase/glutaminase.
+At position 273 to 354, the domain is characterized as RRM.
+At position 533 to 678, the domain is characterized as CID.
+At position 11 to 207, the domain is characterized as DPCK.
+At position 289 to 391, the domain is characterized as PDZ.
+At position 106 to 317, the domain is characterized as ATP-grasp.
+At position 4 to 402, the domain is characterized as SAM-dependent MTase C5-type.
+At position 1 to 70, the domain is characterized as HTH merR-type.
+At position 25 to 100, the domain is characterized as UPAR/Ly6.
+At position 6 to 88, the domain is characterized as PDZ.
+At position 39 to 124, the domain is characterized as ACB.
+At position 16 to 51, the domain is characterized as EF-hand 1.
+At position 92 to 127, the domain is characterized as EF-hand 3.
+At position 12 to 124, the domain is characterized as PX.
+At position 162 to 464, the domain is characterized as Protein kinase.
+At position 420 to 496, the domain is characterized as AGC-kinase C-terminal.
+At position 112 to 192, the domain is characterized as PDZ.
+At position 50 to 87, the domain is characterized as LDL-receptor class A 1.
+At position 127 to 164, the domain is characterized as LDL-receptor class A 2.
+At position 128 to 163, the domain is characterized as EF-hand 2.
+At position 103 to 182, the domain is characterized as PRC barrel.
+At position 211 to 313, the domain is characterized as Fe2OG dioxygenase.
+At position 28 to 140, the domain is characterized as HD.
+At position 24 to 244, the domain is characterized as Peptidase S1.
+At position 226 to 310, the domain is characterized as Death.
+At position 183 to 257, the domain is characterized as POU-specific.
+At position 24 to 248, the domain is characterized as Peptidase S1.
+At position 621 to 677, the domain is characterized as CBS 1.
+At position 699 to 763, the domain is characterized as CBS 2.
+At position 109 to 212, the domain is characterized as PH.
+At position 283 to 344, the domain is characterized as SH3.
+At position 8 to 143, the domain is characterized as MPN.
+At position 191 to 292, the domain is characterized as Fe2OG dioxygenase.
+At position 2 to 103, the domain is characterized as BRCT 1.
+At position 117 to 213, the domain is characterized as BRCT 2.
+At position 260 to 352, the domain is characterized as BRCT 3.
+At position 369 to 453, the domain is characterized as BRCT 4.
+At position 829 to 910, the domain is characterized as BRCT 5.
+At position 934 to 1049, the domain is characterized as BRCT 6.
+At position 271 to 475, the domain is characterized as B30.2/SPRY.
+At position 136 to 314, the domain is characterized as CNNM transmembrane.
+At position 324 to 385, the domain is characterized as CBS 1.
+At position 392 to 458, the domain is characterized as CBS 2.
+At position 366 to 478, the domain is characterized as PAZ.
+At position 644 to 935, the domain is characterized as Piwi.
+At position 51 to 375, the domain is characterized as Asparaginase/glutaminase.
+At position 2 to 55, the domain is characterized as ClpX-type ZB.
+At position 285 to 420, the domain is characterized as Fido.
+At position 407 to 435, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 445 to 474, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 33 to 524, the domain is characterized as Sema.
+At position 571 to 673, the domain is characterized as IPT/TIG 1.
+At position 686 to 769, the domain is characterized as IPT/TIG 2.
+At position 772 to 864, the domain is characterized as IPT/TIG 3.
+At position 1059 to 1322, the domain is characterized as Protein kinase.
+At position 350 to 719, the domain is characterized as Kinesin motor.
+At position 19 to 94, the domain is characterized as RRM 1.
+At position 108 to 179, the domain is characterized as RRM 2.
+At position 205 to 282, the domain is characterized as RRM 3.
+At position 2 to 185, the domain is characterized as Glutamine amidotransferase type-2.
+At position 193 to 516, the domain is characterized as Asparagine synthetase.
+At position 403 to 465, the domain is characterized as HTH myb-type 1.
+At position 466 to 517, the domain is characterized as HTH myb-type 2.
+At position 518 to 570, the domain is characterized as Myb-like.
+At position 358 to 596, the domain is characterized as TRUD.
+At position 359 to 528, the domain is characterized as tr-type G.
+At position 270 to 441, the domain is characterized as RanBD1.
+At position 245 to 400, the domain is characterized as RNase NYN.
+At position 7 to 188, the domain is characterized as Era-type G.
+At position 219 to 296, the domain is characterized as KH type-2.
+At position 246 to 431, the domain is characterized as GATase cobBQ-type.
+At position 40 to 199, the domain is characterized as CBM-cenC.
+At position 828 to 894, the domain is characterized as Dockerin.
+At position 45 to 275, the domain is characterized as ABC transporter.
+At position 17 to 97, the domain is characterized as GLUE N-terminal.
+At position 115 to 149, the domain is characterized as GLUE C-terminal.
+At position 1 to 78, the domain is characterized as Carrier.
+At position 4 to 248, the domain is characterized as ABC transporter.
+At position 14 to 345, the domain is characterized as Kinesin motor.
+At position 489 to 650, the domain is characterized as CBM3.
+At position 658 to 724, the domain is characterized as Dockerin.
+At position 133 to 223, the domain is characterized as PpiC.
+At position 699 to 766, the domain is characterized as GST N-terminal.
+At position 739 to 874, the domain is characterized as GST C-terminal.
+At position 279 to 330, the domain is characterized as HAMP.
+At position 362 to 486, the domain is characterized as Guanylate cyclase.
+At position 1305 to 1491, the domain is characterized as PIK helical.
+At position 1593 to 1861, the domain is characterized as PI3K/PI4K catalytic.
+At position 90 to 163, the domain is characterized as PRC barrel.
+At position 81 to 152, the domain is characterized as KRAB.
+At position 179 to 277, the domain is characterized as HTH araC/xylS-type.
+At position 1414 to 1489, the domain is characterized as DEP.
+At position 516 to 575, the domain is characterized as PDZ.
+At position 13 to 115, the domain is characterized as LOB.
+At position 6 to 110, the domain is characterized as FHA.
+At position 30 to 208, the domain is characterized as Guanylate kinase-like.
+At position 14 to 230, the domain is characterized as Radical SAM core.
+At position 521 to 634, the domain is characterized as CRC.
+At position 220 to 276, the domain is characterized as J.
+At position 127 to 346, the domain is characterized as Radical SAM core.
+At position 90 to 265, the domain is characterized as Helicase ATP-binding.
+At position 293 to 438, the domain is characterized as Helicase C-terminal.
+At position 270 to 490, the domain is characterized as Fibrinogen C-terminal.
+At position 155 to 383, the domain is characterized as NR LBD.
+At position 975 to 1099, the domain is characterized as PH.
+At position 125 to 162, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 553 to 662, the domain is characterized as Peptidase S74.
+At position 52 to 204, the domain is characterized as Nudix hydrolase.
+At position 37 to 81, the domain is characterized as LysM.
+At position 55 to 160, the domain is characterized as Cadherin 1.
+At position 161 to 269, the domain is characterized as Cadherin 2.
+At position 270 to 384, the domain is characterized as Cadherin 3.
+At position 385 to 487, the domain is characterized as Cadherin 4.
+At position 488 to 606, the domain is characterized as Cadherin 5.
+At position 103 to 192, the domain is characterized as SUEL-type lectin.
+At position 202 to 461, the domain is characterized as Olfactomedin-like.
+At position 883 to 934, the domain is characterized as GPS.
+At position 345 to 512, the domain is characterized as tr-type G.
+At position 69 to 117, the domain is characterized as LysM.
+At position 740 to 834, the domain is characterized as Big-1 1.
+At position 841 to 932, the domain is characterized as Big-1 2.
+At position 939 to 1036, the domain is characterized as Big-1 3.
+At position 1043 to 1140, the domain is characterized as Big-1 4.
+At position 1147 to 1240, the domain is characterized as Big-1 5.
+At position 1248 to 1350, the domain is characterized as Big-1 6.
+At position 1358 to 1451, the domain is characterized as Big-1 7.
+At position 1458 to 1554, the domain is characterized as Big-1 8.
+At position 1561 to 1658, the domain is characterized as Big-1 9.
+At position 1665 to 1749, the domain is characterized as Big-1 10.
+At position 1765 to 1856, the domain is characterized as Big-1 11.
+At position 1859 to 1953, the domain is characterized as Big-1 12.
+At position 1961 to 2053, the domain is characterized as Big-1 13.
+At position 185 to 410, the domain is characterized as SEC7.
+At position 548 to 696, the domain is characterized as PH.
+At position 34 to 258, the domain is characterized as AIG1-type G.
+At position 12 to 75, the domain is characterized as Sushi 1.
+At position 80 to 140, the domain is characterized as Sushi 2.
+At position 144 to 204, the domain is characterized as Sushi 3.
+At position 205 to 265, the domain is characterized as Sushi 4.
+At position 266 to 336, the domain is characterized as Sushi 5.
+At position 341 to 400, the domain is characterized as Sushi 6.
+At position 401 to 460, the domain is characterized as Sushi 7.
+At position 461 to 516, the domain is characterized as Sushi 8.
+At position 517 to 587, the domain is characterized as Sushi 9.
+At position 592 to 651, the domain is characterized as Sushi 10.
+At position 652 to 706, the domain is characterized as Sushi 11.
+At position 707 to 771, the domain is characterized as Sushi 12.
+At position 776 to 835, the domain is characterized as Sushi 13.
+At position 839 to 899, the domain is characterized as Sushi 14.
+At position 900 to 960, the domain is characterized as Sushi 15.
+At position 65 to 237, the domain is characterized as PCI.
+At position 5 to 90, the domain is characterized as Acylphosphatase-like.
+At position 574 to 909, the domain is characterized as HECT.
+At position 7 to 221, the domain is characterized as Radical SAM core.
+At position 32 to 81, the domain is characterized as Myosin N-terminal SH3-like.
+At position 85 to 778, the domain is characterized as Myosin motor.
+At position 781 to 810, the domain is characterized as IQ.
+At position 1 to 140, the domain is characterized as RNase H type-1.
+At position 41 to 386, the domain is characterized as Rab-GAP TBC.
+At position 8 to 145, the domain is characterized as N-acetyltransferase 1.
+At position 163 to 315, the domain is characterized as N-acetyltransferase 2.
+At position 1 to 326, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 283 to 584, the domain is characterized as UvrD-like helicase C-terminal.
+At position 182 to 323, the domain is characterized as KARI C-terminal knotted.
+At position 88 to 208, the domain is characterized as GST C-terminal.
+At position 202 to 220, the domain is characterized as UIM.
+At position 19 to 153, the domain is characterized as SIS.
+At position 80 to 173, the domain is characterized as Toprim.
+At position 372 to 435, the domain is characterized as bZIP.
+At position 139 to 245, the domain is characterized as Cadherin 1.
+At position 246 to 363, the domain is characterized as Cadherin 2.
+At position 364 to 477, the domain is characterized as Cadherin 3.
+At position 478 to 585, the domain is characterized as Cadherin 4.
+At position 584 to 694, the domain is characterized as Cadherin 5.
+At position 98 to 294, the domain is characterized as VWFA.
+At position 300 to 554, the domain is characterized as Glutamine amidotransferase type-1.
+At position 26 to 414, the domain is characterized as Helicase ATP-binding.
+At position 635 to 670, the domain is characterized as UVR.
+At position 27 to 115, the domain is characterized as Ig-like C2-type.
+At position 43 to 132, the domain is characterized as PPIase FKBP-type.
+At position 746 to 827, the domain is characterized as SUEL-type lectin.
+At position 34 to 132, the domain is characterized as Cadherin 1.
+At position 137 to 241, the domain is characterized as Cadherin 2.
+At position 246 to 345, the domain is characterized as Cadherin 3.
+At position 350 to 449, the domain is characterized as Cadherin 4.
+At position 454 to 559, the domain is characterized as Cadherin 5.
+At position 566 to 669, the domain is characterized as Cadherin 6.
+At position 1 to 189, the domain is characterized as Glutamine amidotransferase type-1.
+At position 190 to 378, the domain is characterized as GMPS ATP-PPase.
+At position 197 to 224, the domain is characterized as PLD phosphodiesterase 1.
+At position 374 to 401, the domain is characterized as PLD phosphodiesterase 2.
+At position 43 to 272, the domain is characterized as Radical SAM core.
+At position 22 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 145 to 238, the domain is characterized as Ig-like C2-type 2.
+At position 247 to 349, the domain is characterized as Ig-like C2-type 3.
+At position 466 to 756, the domain is characterized as Protein kinase.
+At position 315 to 373, the domain is characterized as G-patch.
+At position 1 to 171, the domain is characterized as KARI N-terminal Rossmann.
+At position 172 to 317, the domain is characterized as KARI C-terminal knotted.
+At position 37 to 102, the domain is characterized as NAC-A/B.
+At position 152 to 189, the domain is characterized as UBA.
+At position 11 to 329, the domain is characterized as Kinesin motor.
+At position 348 to 413, the domain is characterized as S4 RNA-binding.
+At position 48 to 189, the domain is characterized as RUN.
+At position 306 to 367, the domain is characterized as SH3.
+At position 709 to 840, the domain is characterized as SEC7.
+At position 15 to 254, the domain is characterized as ABC transporter.
+At position 472 to 599, the domain is characterized as Guanylate cyclase 1.
+At position 1075 to 1214, the domain is characterized as Guanylate cyclase 2.
+At position 2 to 84, the domain is characterized as GST C-terminal.
+At position 535 to 702, the domain is characterized as tr-type G.
+At position 38 to 88, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 133 to 183, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 177 to 369, the domain is characterized as CheB-type methylesterase.
+At position 31 to 109, the domain is characterized as RRM.
+At position 42 to 71, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 81 to 110, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 7 to 71, the domain is characterized as HMA.
+At position 65 to 338, the domain is characterized as Dynamin-type G.
+At position 571 to 659, the domain is characterized as GED.
+At position 37 to 264, the domain is characterized as Radical SAM core.
+At position 558 to 753, the domain is characterized as N-acetyltransferase.
+At position 70 to 254, the domain is characterized as RNase H type-2.
+At position 30 to 109, the domain is characterized as PDZ.
+At position 1 to 72, the domain is characterized as HTH asnC-type.
+At position 27 to 143, the domain is characterized as Plastocyanin-like 1.
+At position 153 to 305, the domain is characterized as Plastocyanin-like 2.
+At position 408 to 547, the domain is characterized as Plastocyanin-like 3.
+At position 47 to 84, the domain is characterized as EF-hand 1.
+At position 126 to 161, the domain is characterized as EF-hand 2.
+At position 24 to 250, the domain is characterized as Peptidase S1.
+At position 110 to 343, the domain is characterized as Radical SAM core.
+At position 250 to 309, the domain is characterized as SH3.
+At position 702 to 1072, the domain is characterized as DZF.
+At position 158 to 244, the domain is characterized as Doublecortin 1.
+At position 313 to 396, the domain is characterized as Doublecortin 2.
+At position 477 to 735, the domain is characterized as Protein kinase.
+At position 280 to 300, the domain is characterized as ELK.
+At position 181 to 275, the domain is characterized as 5'-3' exonuclease.
+At position 10 to 77, the domain is characterized as C-type lectin.
+At position 24 to 274, the domain is characterized as Protein kinase.
+At position 157 to 225, the domain is characterized as DRBM.
+At position 59 to 94, the domain is characterized as EF-hand 1.
+At position 161 to 196, the domain is characterized as EF-hand 3.
+At position 202 to 236, the domain is characterized as EF-hand 4.
+At position 90 to 214, the domain is characterized as GST C-terminal.
+At position 1725 to 1789, the domain is characterized as KH.
+At position 551 to 736, the domain is characterized as N-acetyltransferase.
+At position 575 to 676, the domain is characterized as tRNA-binding.
+At position 190 to 268, the domain is characterized as RRM.
+At position 101 to 611, the domain is characterized as USP.
+At position 613 to 706, the domain is characterized as DUSP 1.
+At position 715 to 818, the domain is characterized as DUSP 2.
+At position 132 to 169, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 1 to 55, the domain is characterized as ClpX-type ZB.
+At position 26 to 179, the domain is characterized as Helicase ATP-binding.
+At position 190 to 357, the domain is characterized as Helicase C-terminal.
+At position 159 to 222, the domain is characterized as bZIP.
+At position 2 to 117, the domain is characterized as VOC.
+At position 69 to 116, the domain is characterized as Oxidoreductase-like.
+At position 23 to 86, the domain is characterized as KRAB-related.
+At position 244 to 358, the domain is characterized as SET.
+At position 4 to 243, the domain is characterized as ABC transporter.
+At position 10 to 217, the domain is characterized as YjeF N-terminal.
+At position 155 to 242, the domain is characterized as PDZ 1.
+At position 250 to 337, the domain is characterized as PDZ 2.
+At position 424 to 505, the domain is characterized as PDZ 3.
+At position 539 to 609, the domain is characterized as SH3.
+At position 683 to 866, the domain is characterized as Guanylate kinase-like.
+At position 819 to 1100, the domain is characterized as Protein kinase.
+At position 4 to 83, the domain is characterized as GST N-terminal.
+At position 37 to 120, the domain is characterized as Ig-like.
+At position 138 to 219, the domain is characterized as Ig-like C2-type.
+At position 221 to 320, the domain is characterized as Ig-like V-type.
+At position 2 to 80, the domain is characterized as RRM 1.
+At position 90 to 167, the domain is characterized as RRM 2.
+At position 181 to 259, the domain is characterized as RRM 3.
+At position 285 to 362, the domain is characterized as RRM 4.
+At position 552 to 629, the domain is characterized as PABC.
+At position 13 to 70, the domain is characterized as bHLH.
+At position 84 to 116, the domain is characterized as Orange.
+At position 6 to 291, the domain is characterized as CN hydrolase.
+At position 8 to 36, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 89 to 271, the domain is characterized as Helicase ATP-binding.
+At position 283 to 444, the domain is characterized as Helicase C-terminal.
+At position 14 to 99, the domain is characterized as GS beta-grasp.
+At position 106 to 469, the domain is characterized as GS catalytic.
+At position 32 to 356, the domain is characterized as G-alpha.
+At position 232 to 333, the domain is characterized as HD.
+At position 89 to 220, the domain is characterized as GST C-terminal.
+At position 65 to 377, the domain is characterized as GH18.
+At position 504 to 592, the domain is characterized as IPT/TIG.
+At position 168 to 474, the domain is characterized as USP.
+At position 1 to 213, the domain is characterized as Peptidase S1.
+At position 126 to 412, the domain is characterized as Protein kinase.
+At position 7 to 157, the domain is characterized as Thioredoxin.
+At position 38 to 259, the domain is characterized as ABC transmembrane type-2.
+At position 21 to 59, the domain is characterized as CBM10.
+At position 306 to 514, the domain is characterized as PCI.
+At position 16 to 145, the domain is characterized as VHS.
+At position 162 to 181, the domain is characterized as UIM.
+At position 215 to 274, the domain is characterized as SH3.
+At position 84 to 184, the domain is characterized as SRCR 1.
+At position 232 to 332, the domain is characterized as SRCR 2.
+At position 380 to 480, the domain is characterized as SRCR 3.
+At position 517 to 628, the domain is characterized as CUB 1.
+At position 634 to 737, the domain is characterized as SRCR 4.
+At position 752 to 861, the domain is characterized as CUB 2.
+At position 870 to 1118, the domain is characterized as ZP.
+At position 605 to 683, the domain is characterized as BRCT.
+At position 10 to 72, the domain is characterized as SH3.
+At position 263 to 296, the domain is characterized as WW 1.
+At position 355 to 388, the domain is characterized as WW 2.
+At position 466 to 567, the domain is characterized as PH.
+At position 648 to 836, the domain is characterized as Rho-GAP.
+At position 16 to 68, the domain is characterized as F-box.
+At position 49 to 185, the domain is characterized as Thioredoxin.
+At position 146 to 352, the domain is characterized as ATP-grasp.
+At position 46 to 342, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 21 to 145, the domain is characterized as Plastocyanin-like 1.
+At position 157 to 304, the domain is characterized as Plastocyanin-like 2.
+At position 376 to 576, the domain is characterized as Plastocyanin-like 3.
+At position 47 to 355, the domain is characterized as PPM-type phosphatase.
+At position 43 to 174, the domain is characterized as Peptidase S1.
+At position 163 to 213, the domain is characterized as bZIP.
+At position 246 to 383, the domain is characterized as MPN.
+At position 1 to 113, the domain is characterized as CBM20.
+At position 318 to 618, the domain is characterized as GP-PDE.
+At position 30 to 118, the domain is characterized as GOLD.
+At position 13 to 191, the domain is characterized as Reticulon.
+At position 146 to 465, the domain is characterized as NACHT.
+At position 4 to 200, the domain is characterized as DPCK.
+At position 155 to 411, the domain is characterized as Olfactomedin-like.
+At position 32 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 101 to 332, the domain is characterized as NR LBD.
+At position 273 to 336, the domain is characterized as SAM.
+At position 373 to 441, the domain is characterized as TRAM.
+At position 127 to 302, the domain is characterized as JmjC.
+At position 138 to 233, the domain is characterized as SH2.
+At position 200 to 373, the domain is characterized as EngA-type G 2.
+At position 374 to 458, the domain is characterized as KH-like.
+At position 269 to 345, the domain is characterized as B5.
+At position 101 to 180, the domain is characterized as PRC barrel.
+At position 147 to 360, the domain is characterized as Histidine kinase.
+At position 674 to 1093, the domain is characterized as PDEase.
+At position 703 to 978, the domain is characterized as Protein kinase.
+At position 21 to 75, the domain is characterized as HTH cro/C1-type.
+At position 221 to 319, the domain is characterized as Ig-like V-type.
+At position 83 to 147, the domain is characterized as PWWP.
+At position 4 to 173, the domain is characterized as Flavodoxin-like.
+At position 422 to 645, the domain is characterized as ABC transporter 1.
+At position 379 to 803, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1287 to 1589, the domain is characterized as PKS/mFAS DH.
+At position 1634 to 1711, the domain is characterized as Carrier 1.
+At position 1742 to 1821, the domain is characterized as Carrier 2.
+At position 47 to 317, the domain is characterized as Protein kinase.
+At position 289 to 429, the domain is characterized as N-acetyltransferase.
+At position 5 to 253, the domain is characterized as ABC transporter.
+At position 35 to 96, the domain is characterized as Sushi 1.
+At position 28 to 152, the domain is characterized as Cyclin N-terminal.
+At position 5 to 113, the domain is characterized as SCP2.
+At position 953 to 1113, the domain is characterized as UBC core.
+At position 100 to 176, the domain is characterized as PRC barrel.
+At position 71 to 181, the domain is characterized as sHSP.
+At position 12 to 135, the domain is characterized as Rhodanese.
+At position 122 to 160, the domain is characterized as LRRCT.
+At position 222 to 335, the domain is characterized as Calponin-homology (CH).
+At position 1330 to 1464, the domain is characterized as CKK.
+At position 255 to 337, the domain is characterized as Toprim.
+At position 61 to 139, the domain is characterized as RRM 1.
+At position 149 to 226, the domain is characterized as RRM 2.
+At position 242 to 320, the domain is characterized as RRM 3.
+At position 346 to 470, the domain is characterized as RRM 4.
+At position 664 to 741, the domain is characterized as PABC.
+At position 1 to 301, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 1 to 285, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 279 to 586, the domain is characterized as UvrD-like helicase C-terminal.
+At position 227 to 516, the domain is characterized as ABC transmembrane type-1.
+At position 550 to 784, the domain is characterized as ABC transporter.
+At position 5 to 135, the domain is characterized as Galectin.
+At position 41 to 193, the domain is characterized as GOLD.
+At position 208 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 838 to 1082, the domain is characterized as CHASE.
+At position 1235 to 1317, the domain is characterized as PAS.
+At position 1321 to 1376, the domain is characterized as PAC.
+At position 1393 to 1620, the domain is characterized as Histidine kinase.
+At position 2026 to 2146, the domain is characterized as Response regulatory.
+At position 440 to 532, the domain is characterized as Ig-like 5.
+At position 539 to 631, the domain is characterized as Ig-like 6.
+At position 643 to 743, the domain is characterized as Fibronectin type-III.
+At position 751 to 918, the domain is characterized as MAM.
+At position 105 to 308, the domain is characterized as ATP-grasp.
+At position 141 to 173, the domain is characterized as LisH.
+At position 179 to 236, the domain is characterized as CTLH.
+At position 348 to 479, the domain is characterized as Plus3.
+At position 15 to 96, the domain is characterized as GS beta-grasp.
+At position 104 to 469, the domain is characterized as GS catalytic.
+At position 16 to 73, the domain is characterized as HTH lysR-type.
+At position 236 to 286, the domain is characterized as GRAM 1.
+At position 286 to 385, the domain is characterized as PH.
+At position 730 to 796, the domain is characterized as GRAM 2.
+At position 2 to 241, the domain is characterized as ABC transporter 1.
+At position 267 to 491, the domain is characterized as ABC transporter 2.
+At position 1061 to 1324, the domain is characterized as Protein kinase.
+At position 28 to 162, the domain is characterized as Nudix hydrolase.
+At position 9 to 109, the domain is characterized as Ig-like C2-type.
+At position 163 to 307, the domain is characterized as TIR.
+At position 154 to 255, the domain is characterized as SWIRM.
+At position 18 to 359, the domain is characterized as Kinesin motor.
+At position 5 to 244, the domain is characterized as ABC transporter.
+At position 27 to 112, the domain is characterized as PDZ GRASP-type 1.
+At position 118 to 207, the domain is characterized as PDZ GRASP-type 2.
+At position 203 to 280, the domain is characterized as KH type-2.
+At position 46 to 111, the domain is characterized as S4 RNA-binding.
+At position 9 to 173, the domain is characterized as TIR.
+At position 168 to 454, the domain is characterized as NB-ARC.
+At position 139 to 402, the domain is characterized as tr-type G.
+At position 139 to 248, the domain is characterized as sHSP.
+At position 41 to 197, the domain is characterized as SIS.
+At position 19 to 260, the domain is characterized as tr-type G.
+At position 38 to 103, the domain is characterized as NAC-A/B.
+At position 8 to 244, the domain is characterized as ABC transporter 1.
+At position 28 to 282, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 125 to 199, the domain is characterized as RRM 1.
+At position 215 to 293, the domain is characterized as RRM 2.
+At position 384 to 458, the domain is characterized as RRM 3.
+At position 276 to 463, the domain is characterized as DH.
+At position 3 to 256, the domain is characterized as OBG-type G.
+At position 278 to 361, the domain is characterized as TGS.
+At position 1 to 182, the domain is characterized as RNase H type-2.
+At position 524 to 758, the domain is characterized as NR LBD.
+At position 6 to 191, the domain is characterized as CNNM transmembrane.
+At position 210 to 270, the domain is characterized as CBS 1.
+At position 275 to 335, the domain is characterized as CBS 2.
+At position 604 to 947, the domain is characterized as TTL.
+At position 186 to 280, the domain is characterized as 5'-3' exonuclease.
+At position 320 to 497, the domain is characterized as 3'-5' exonuclease.
+At position 12 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 116 to 212, the domain is characterized as Rieske.
+At position 55 to 226, the domain is characterized as Helicase ATP-binding.
+At position 237 to 397, the domain is characterized as Helicase C-terminal.
+At position 109 to 420, the domain is characterized as IF rod.
+At position 270 to 304, the domain is characterized as SAP.
+At position 1 to 72, the domain is characterized as Core-binding (CB).
+At position 84 to 246, the domain is characterized as Tyr recombinase.
+At position 42 to 91, the domain is characterized as UBA 1.
+At position 150 to 194, the domain is characterized as UBA 2.
+At position 272 to 598, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 16 to 109, the domain is characterized as DMAP1-binding.
+At position 758 to 884, the domain is characterized as BAH 1.
+At position 976 to 1103, the domain is characterized as BAH 2.
+At position 1142 to 1601, the domain is characterized as SAM-dependent MTase C5-type.
+At position 330 to 504, the domain is characterized as Helicase ATP-binding.
+At position 531 to 678, the domain is characterized as Helicase C-terminal.
+At position 38 to 105, the domain is characterized as BTB.
+At position 48 to 83, the domain is characterized as EF-hand 1.
+At position 130 to 165, the domain is characterized as EF-hand 2.
+At position 167 to 202, the domain is characterized as EF-hand 3.
+At position 237 to 272, the domain is characterized as EF-hand 4.
+At position 319 to 354, the domain is characterized as EF-hand 5.
+At position 356 to 391, the domain is characterized as EF-hand 6.
+At position 29 to 204, the domain is characterized as TLC.
+At position 270 to 315, the domain is characterized as GRAM 1.
+At position 318 to 413, the domain is characterized as PH.
+At position 798 to 901, the domain is characterized as GRAM 2.
+At position 2 to 46, the domain is characterized as HTH gntR-type.
+At position 99 to 331, the domain is characterized as Radical SAM core.
+At position 224 to 479, the domain is characterized as GP-PDE.
+At position 31 to 118, the domain is characterized as YebF/Cmi.
+At position 25 to 54, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 51 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 71 to 101, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 117 to 146, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 483 to 757, the domain is characterized as Reverse transcriptase.
+At position 1 to 610, the domain is characterized as PFL.
+At position 617 to 740, the domain is characterized as Glycine radical.
+At position 29 to 42, the domain is characterized as CRIB.
+At position 90 to 370, the domain is characterized as Protein kinase.
+At position 30 to 93, the domain is characterized as Sushi.
+At position 2 to 75, the domain is characterized as Sm.
+At position 11 to 87, the domain is characterized as S4 RNA-binding.
+At position 53 to 164, the domain is characterized as THUMP.
+At position 651 to 764, the domain is characterized as SMC hinge.
+At position 1 to 126, the domain is characterized as Peptidase C39.
+At position 155 to 437, the domain is characterized as ABC transmembrane type-1.
+At position 469 to 704, the domain is characterized as ABC transporter.
+At position 19 to 85, the domain is characterized as LCN-type CS-alpha/beta.
+At position 36 to 214, the domain is characterized as Josephin.
+At position 12 to 359, the domain is characterized as Kinesin motor.
+At position 1 to 67, the domain is characterized as Peptidase M12B.
+At position 75 to 156, the domain is characterized as Disintegrin.
+At position 81 to 234, the domain is characterized as Ferritin-like diiron.
+At position 7 to 65, the domain is characterized as TRAM.
+At position 1 to 77, the domain is characterized as Ubiquitin-like.
+At position 395 to 434, the domain is characterized as UBA.
+At position 21 to 138, the domain is characterized as PX.
+At position 615 to 701, the domain is characterized as BRCT.
+At position 18 to 130, the domain is characterized as HD.
+At position 9 to 139, the domain is characterized as HTH marR-type.
+At position 8 to 51, the domain is characterized as CUE.
+At position 143 to 241, the domain is characterized as PpiC.
+At position 425 to 609, the domain is characterized as DH.
+At position 19 to 261, the domain is characterized as tr-type G.
+At position 435 to 549, the domain is characterized as Toprim.
+At position 245 to 469, the domain is characterized as PE-PPE.
+At position 42 to 268, the domain is characterized as Radical SAM core.
+At position 45 to 247, the domain is characterized as Helicase ATP-binding.
+At position 283 to 438, the domain is characterized as Helicase C-terminal.
+At position 81 to 143, the domain is characterized as Chromo 1.
+At position 267 to 328, the domain is characterized as Chromo 2.
+At position 218 to 472, the domain is characterized as CN hydrolase.
+At position 32 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 19 to 114, the domain is characterized as PB1.
+At position 120 to 227, the domain is characterized as Rieske.
+At position 106 to 289, the domain is characterized as Helicase ATP-binding.
+At position 428 to 589, the domain is characterized as Helicase C-terminal.
+At position 624 to 718, the domain is characterized as Dicer dsRNA-binding fold.
+At position 871 to 1006, the domain is characterized as PAZ.
+At position 1051 to 1197, the domain is characterized as RNase III 1.
+At position 1248 to 1411, the domain is characterized as RNase III 2.
+At position 1445 to 1518, the domain is characterized as DRBM.
+At position 73 to 265, the domain is characterized as ABC transmembrane type-1.
+At position 5 to 147, the domain is characterized as Nudix hydrolase.
+At position 3 to 86, the domain is characterized as Toprim.
+At position 49 to 95, the domain is characterized as Gla.
+At position 185 to 301, the domain is characterized as DOD-type homing endonuclease 1.
+At position 940 to 1098, the domain is characterized as DOD-type homing endonuclease 2.
+At position 1 to 101, the domain is characterized as C2 1.
+At position 183 to 300, the domain is characterized as C2 2.
+At position 339 to 475, the domain is characterized as C2 3.
+At position 1110 to 1238, the domain is characterized as C2 4.
+At position 1269 to 1397, the domain is characterized as C2 5.
+At position 1523 to 1641, the domain is characterized as C2 6.
+At position 1759 to 1907, the domain is characterized as C2 7.
+At position 6 to 153, the domain is characterized as PHTF.
+At position 18 to 142, the domain is characterized as Toprim.
+At position 372 to 438, the domain is characterized as TRAM.
+At position 184 to 239, the domain is characterized as HTH myb-type 1.
+At position 240 to 290, the domain is characterized as HTH myb-type 2.
+At position 1 to 143, the domain is characterized as RNase H type-1.
+At position 19 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 31 to 272, the domain is characterized as Peptidase S1.
+At position 181 to 400, the domain is characterized as CN hydrolase.
+At position 17 to 122, the domain is characterized as Ig-like V-type.
+At position 673 to 864, the domain is characterized as ATP-grasp 2.
+At position 22 to 409, the domain is characterized as Kinesin motor.
+At position 26 to 130, the domain is characterized as Calponin-homology (CH).
+At position 239 to 430, the domain is characterized as GATase cobBQ-type.
+At position 18 to 331, the domain is characterized as Calpain catalytic.
+At position 552 to 587, the domain is characterized as EF-hand.
+At position 53 to 352, the domain is characterized as PPM-type phosphatase.
+At position 9 to 275, the domain is characterized as tr-type G.
+At position 272 to 319, the domain is characterized as F-box.
+At position 167 to 234, the domain is characterized as SH3 1.
+At position 297 to 390, the domain is characterized as Fibronectin type-III 1.
+At position 393 to 475, the domain is characterized as Fibronectin type-III 2.
+At position 848 to 916, the domain is characterized as SH3 2.
+At position 952 to 1019, the domain is characterized as SH3 3.
+At position 1 to 180, the domain is characterized as ABC transmembrane type-1 1.
+At position 214 to 437, the domain is characterized as ABC transporter 1.
+At position 483 to 765, the domain is characterized as ABC transmembrane type-1 2.
+At position 804 to 1036, the domain is characterized as ABC transporter 2.
+At position 258 to 335, the domain is characterized as SWIB/MDM2.
+At position 14 to 347, the domain is characterized as PTS EIIC type-2.
+At position 381 to 476, the domain is characterized as PTS EIIB type-2.
+At position 42 to 90, the domain is characterized as Fibronectin type-II.
+At position 94 to 131, the domain is characterized as EGF-like 1.
+At position 133 to 173, the domain is characterized as Fibronectin type-I.
+At position 174 to 210, the domain is characterized as EGF-like 2.
+At position 216 to 295, the domain is characterized as Kringle.
+At position 372 to 615, the domain is characterized as Peptidase S1.
+At position 1 to 31, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 971 to 1046, the domain is characterized as Carrier.
+At position 213 to 341, the domain is characterized as OTU.
+At position 224 to 262, the domain is characterized as LRRCT.
+At position 280 to 467, the domain is characterized as NTF2.
+At position 546 to 599, the domain is characterized as TAP-C.
+At position 350 to 384, the domain is characterized as EGF-like 1.
+At position 419 to 456, the domain is characterized as EGF-like 2.
+At position 75 to 100, the domain is characterized as EF-hand 2.
+At position 102 to 137, the domain is characterized as EF-hand 3.
+At position 141 to 174, the domain is characterized as EF-hand 4.
+At position 9 to 174, the domain is characterized as PPIase cyclophilin-type.
+At position 31 to 60, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 6 to 206, the domain is characterized as DPCK.
+At position 1 to 152, the domain is characterized as TLDc.
+At position 99 to 162, the domain is characterized as S4 RNA-binding.
+At position 28 to 78, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 106 to 156, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 29 to 124, the domain is characterized as Cystatin.
+At position 18 to 134, the domain is characterized as MTTase N-terminal.
+At position 156 to 386, the domain is characterized as Radical SAM core.
+At position 389 to 451, the domain is characterized as TRAM.
+At position 2 to 28, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 51, the domain is characterized as F-box.
+At position 19 to 270, the domain is characterized as Protein kinase.
+At position 8 to 45, the domain is characterized as UBA-like.
+At position 60 to 248, the domain is characterized as DCUN1.
+At position 18 to 50, the domain is characterized as LisH.
+At position 63 to 170, the domain is characterized as sHSP.
+At position 121 to 401, the domain is characterized as Peptidase S1.
+At position 269 to 452, the domain is characterized as B30.2/SPRY.
+At position 9 to 190, the domain is characterized as Era-type G.
+At position 221 to 298, the domain is characterized as KH type-2.
+At position 395 to 492, the domain is characterized as Zinc-hook.
+At position 21 to 242, the domain is characterized as Phosphagen kinase C-terminal.
+At position 2 to 36, the domain is characterized as SAP 1.
+At position 91 to 125, the domain is characterized as SAP 2.
+At position 179 to 281, the domain is characterized as WGR.
+At position 308 to 426, the domain is characterized as PARP alpha-helical.
+At position 434 to 660, the domain is characterized as PARP catalytic.
+At position 116 to 239, the domain is characterized as MPN.
+At position 229 to 441, the domain is characterized as Helicase ATP-binding.
+At position 493 to 643, the domain is characterized as Helicase C-terminal.
+At position 59 to 239, the domain is characterized as tr-type G.
+At position 131 to 332, the domain is characterized as TLC.
+At position 36 to 520, the domain is characterized as Sema.
+At position 651 to 740, the domain is characterized as Ig-like C2-type.
+At position 87 to 133, the domain is characterized as G-patch.
+At position 231 to 450, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 752 to 786, the domain is characterized as WW.
+At position 56 to 97, the domain is characterized as JmjN.
+At position 121 to 218, the domain is characterized as ARID.
+At position 1217 to 1381, the domain is characterized as PNPLA.
+At position 91 to 247, the domain is characterized as Tyr recombinase.
+At position 381 to 550, the domain is characterized as tr-type G.
+At position 203 to 292, the domain is characterized as Ig-like C1-type.
+At position 6 to 60, the domain is characterized as L27 1.
+At position 61 to 118, the domain is characterized as L27 2.
+At position 137 to 218, the domain is characterized as PDZ.
+At position 226 to 296, the domain is characterized as SH3.
+At position 385 to 568, the domain is characterized as Guanylate kinase-like.
+At position 1019 to 1081, the domain is characterized as SH3.
+At position 89 to 306, the domain is characterized as Radical SAM core.
+At position 79 to 260, the domain is characterized as Brix.
+At position 600 to 713, the domain is characterized as CNA-B 1.
+At position 714 to 824, the domain is characterized as CNA-B 2.
+At position 36 to 300, the domain is characterized as Alpha-carbonic anhydrase.
+At position 314 to 413, the domain is characterized as Fibronectin type-III.
+At position 1718 to 1993, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 2024 to 2283, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 675 to 756, the domain is characterized as ACT 1.
+At position 789 to 858, the domain is characterized as ACT 2.
+At position 585 to 691, the domain is characterized as tRNA-binding.
+At position 29 to 268, the domain is characterized as Laminin N-terminal.
+At position 269 to 324, the domain is characterized as Laminin EGF-like 1.
+At position 325 to 380, the domain is characterized as Laminin EGF-like 2.
+At position 381 to 427, the domain is characterized as Laminin EGF-like 3.
+At position 428 to 477, the domain is characterized as Laminin EGF-like 4.
+At position 504 to 672, the domain is characterized as Laminin IV type A.
+At position 707 to 755, the domain is characterized as Laminin EGF-like 5.
+At position 756 to 810, the domain is characterized as Laminin EGF-like 6.
+At position 811 to 866, the domain is characterized as Laminin EGF-like 7.
+At position 867 to 917, the domain is characterized as Laminin EGF-like 8.
+At position 918 to 965, the domain is characterized as Laminin EGF-like 9.
+At position 966 to 1013, the domain is characterized as Laminin EGF-like 10.
+At position 194 to 268, the domain is characterized as POU-specific.
+At position 391 to 440, the domain is characterized as bHLH.
+At position 46 to 367, the domain is characterized as ABC transmembrane type-1 1.
+At position 402 to 638, the domain is characterized as ABC transporter 1.
+At position 735 to 1023, the domain is characterized as ABC transmembrane type-1 2.
+At position 1059 to 1297, the domain is characterized as ABC transporter 2.
+At position 388 to 420, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 435 to 465, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 92 to 290, the domain is characterized as KARI N-terminal Rossmann.
+At position 291 to 439, the domain is characterized as KARI C-terminal knotted 1.
+At position 440 to 576, the domain is characterized as KARI C-terminal knotted 2.
+At position 25 to 57, the domain is characterized as LisH.
+At position 63 to 120, the domain is characterized as CTLH.
+At position 54 to 105, the domain is characterized as FHA.
+At position 1892 to 1970, the domain is characterized as BRCT 1.
+At position 1991 to 2082, the domain is characterized as BRCT 2.
+At position 79 to 394, the domain is characterized as IF rod.
+At position 191 to 453, the domain is characterized as Protein kinase.
+At position 454 to 521, the domain is characterized as AGC-kinase C-terminal.
+At position 558 to 652, the domain is characterized as PH.
+At position 3 to 79, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 104 to 193, the domain is characterized as NID 1.
+At position 202 to 294, the domain is characterized as NID 2.
+At position 2 to 237, the domain is characterized as ABC transporter.
+At position 18 to 291, the domain is characterized as GH18.
+At position 10 to 114, the domain is characterized as RWD.
+At position 573 to 650, the domain is characterized as BRCT.
+At position 39 to 137, the domain is characterized as GOLD.
+At position 332 to 494, the domain is characterized as JmjC.
+At position 31 to 417, the domain is characterized as Helicase ATP-binding.
+At position 436 to 602, the domain is characterized as Helicase C-terminal.
+At position 23 to 246, the domain is characterized as Radical SAM core.
+At position 49 to 265, the domain is characterized as Radical SAM core.
+At position 69 to 196, the domain is characterized as MATH.
+At position 215 to 522, the domain is characterized as USP.
+At position 30 to 140, the domain is characterized as MTTase N-terminal.
+At position 157 to 395, the domain is characterized as Radical SAM core.
+At position 398 to 463, the domain is characterized as TRAM.
+At position 5 to 240, the domain is characterized as ABC transporter.
+At position 14 to 253, the domain is characterized as ABC transporter.
+At position 37 to 314, the domain is characterized as Deacetylase sirtuin-type.
+At position 45 to 349, the domain is characterized as Cbl-PTB.
+At position 863 to 902, the domain is characterized as UBA.
+At position 6 to 92, the domain is characterized as ASCH.
+At position 40 to 133, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 176 to 206, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 19 to 101, the domain is characterized as Lipoyl-binding.
+At position 709 to 784, the domain is characterized as ACT 1.
+At position 517 to 632, the domain is characterized as SH2.
+At position 147 to 206, the domain is characterized as KH.
+At position 9 to 129, the domain is characterized as MSP.
+At position 4 to 133, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 38 to 360, the domain is characterized as Kinesin motor.
+At position 23 to 144, the domain is characterized as Rhodanese.
+At position 172 to 313, the domain is characterized as Tyrosine-protein phosphatase.
+At position 159 to 334, the domain is characterized as OBG-type G.
+At position 6 to 102, the domain is characterized as SH2.
+At position 174 to 334, the domain is characterized as Helicase ATP-binding.
+At position 370 to 538, the domain is characterized as Helicase C-terminal.
+At position 198 to 371, the domain is characterized as EngA-type G 2.
+At position 372 to 456, the domain is characterized as KH-like.
+At position 242 to 402, the domain is characterized as Helicase C-terminal.
+At position 282 to 391, the domain is characterized as OmpA-like.
+At position 212 to 323, the domain is characterized as PAS.
+At position 346 to 538, the domain is characterized as Histidine kinase.
+At position 61 to 356, the domain is characterized as Protein kinase.
+At position 95 to 245, the domain is characterized as Flavodoxin-like.
+At position 303 to 551, the domain is characterized as FAD-binding FR-type.
+At position 150 to 222, the domain is characterized as ACT.
+At position 22 to 194, the domain is characterized as EngB-type G.
+At position 15 to 72, the domain is characterized as HTH lysR-type.
+At position 44 to 87, the domain is characterized as CHCH 1.
+At position 88 to 130, the domain is characterized as CHCH 2.
+At position 36 to 107, the domain is characterized as TB.
+At position 99 to 119, the domain is characterized as Follistatin-like 1.
+At position 113 to 169, the domain is characterized as Kazal-like 1.
+At position 170 to 193, the domain is characterized as Follistatin-like 2.
+At position 189 to 245, the domain is characterized as Kazal-like 2.
+At position 21 to 107, the domain is characterized as UPAR/Ly6.
+At position 223 to 324, the domain is characterized as PpiC 1.
+At position 364 to 463, the domain is characterized as PpiC 2.
+At position 519 to 637, the domain is characterized as SMC hinge.
+At position 2 to 112, the domain is characterized as Thioredoxin.
+At position 5 to 38, the domain is characterized as WW.
+At position 496 to 794, the domain is characterized as Protein kinase.
+At position 25 to 265, the domain is characterized as ABC transporter.
+At position 204 to 456, the domain is characterized as Lon N-terminal.
+At position 898 to 1084, the domain is characterized as Lon proteolytic.
+At position 83 to 259, the domain is characterized as FAD-binding PCMH-type.
+At position 39 to 117, the domain is characterized as RRM.
+At position 217 to 410, the domain is characterized as Helicase ATP-binding.
+At position 421 to 582, the domain is characterized as Helicase C-terminal.
+At position 3 to 144, the domain is characterized as Clp R.
+At position 417 to 452, the domain is characterized as UVR.
+At position 60 to 162, the domain is characterized as THUMP.
+At position 3 to 57, the domain is characterized as ClpX-type ZB.
+At position 376 to 444, the domain is characterized as HMA.
+At position 55 to 237, the domain is characterized as IRG-type G.
+At position 182 to 241, the domain is characterized as FYR N-terminal.
+At position 242 to 321, the domain is characterized as FYR C-terminal.
+At position 30 to 139, the domain is characterized as Ig-like V-type.
+At position 83 to 132, the domain is characterized as FHA.
+At position 35 to 152, the domain is characterized as C2.
+At position 229 to 272, the domain is characterized as CUE.
+At position 54 to 113, the domain is characterized as LIM zinc-binding 1.
+At position 114 to 175, the domain is characterized as LIM zinc-binding 2.
+At position 61 to 295, the domain is characterized as Radical SAM core.
+At position 6 to 261, the domain is characterized as Protein kinase.
+At position 3 to 76, the domain is characterized as HTH OST-type 1.
+At position 233 to 302, the domain is characterized as HTH OST-type 2.
+At position 337 to 406, the domain is characterized as HTH OST-type 3.
+At position 513 to 570, the domain is characterized as Tudor 1.
+At position 703 to 760, the domain is characterized as Tudor 2.
+At position 27 to 318, the domain is characterized as GH18.
+At position 89 to 274, the domain is characterized as Reticulon.
+At position 29 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 123 to 207, the domain is characterized as Ig-like C2-type 2.
+At position 214 to 311, the domain is characterized as Ig-like C2-type 3.
+At position 320 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 416 to 510, the domain is characterized as Ig-like C2-type 5.
+At position 592 to 940, the domain is characterized as Protein kinase.
+At position 204 to 281, the domain is characterized as RRM.
+At position 802 to 899, the domain is characterized as PWI.
+At position 1 to 224, the domain is characterized as Peptidase S1.
+At position 96 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 917 to 981, the domain is characterized as SAM.
+At position 26 to 283, the domain is characterized as Protein kinase.
+At position 89 to 142, the domain is characterized as bHLH.
+At position 161 to 235, the domain is characterized as PAS 1.
+At position 349 to 419, the domain is characterized as PAS 2.
+At position 424 to 467, the domain is characterized as PAC.
+At position 79 to 295, the domain is characterized as Radical SAM core.
+At position 130 to 386, the domain is characterized as Olfactomedin-like.
+At position 249 to 391, the domain is characterized as Ferric oxidoreductase.
+At position 204 to 270, the domain is characterized as J.
+At position 225 to 359, the domain is characterized as PADR1 zinc-binding.
+At position 385 to 476, the domain is characterized as BRCT.
+At position 542 to 638, the domain is characterized as WGR.
+At position 662 to 779, the domain is characterized as PARP alpha-helical.
+At position 788 to 1014, the domain is characterized as PARP catalytic.
+At position 44 to 146, the domain is characterized as Gnk2-homologous 1.
+At position 152 to 276, the domain is characterized as Gnk2-homologous 2.
+At position 20 to 204, the domain is characterized as Rho-GAP.
+At position 238 to 298, the domain is characterized as SH3.
+At position 59 to 245, the domain is characterized as Rab-GAP TBC.
+At position 147 to 327, the domain is characterized as Helicase ATP-binding.
+At position 359 to 510, the domain is characterized as Helicase C-terminal.
+At position 42 to 184, the domain is characterized as SIS.
+At position 210 to 268, the domain is characterized as CBS 1.
+At position 277 to 328, the domain is characterized as CBS 2.
+At position 228 to 263, the domain is characterized as DMA.
+At position 621 to 699, the domain is characterized as BRCT.
+At position 3 to 206, the domain is characterized as DPCK.
+At position 4 to 391, the domain is characterized as SAM-dependent MTase C5-type.
+At position 111 to 158, the domain is characterized as LysM 1.
+At position 175 to 219, the domain is characterized as LysM 2.
+At position 165 to 333, the domain is characterized as Helicase ATP-binding.
+At position 475 to 629, the domain is characterized as Helicase C-terminal.
+At position 182 to 345, the domain is characterized as Tyrosine-protein phosphatase.
+At position 302 to 433, the domain is characterized as C-CAP/cofactor C-like.
+At position 22 to 88, the domain is characterized as HMA.
+At position 667 to 787, the domain is characterized as TFIIS central.
+At position 914 to 1016, the domain is characterized as GAE.
+At position 3 to 183, the domain is characterized as Miro 1.
+At position 199 to 234, the domain is characterized as EF-hand 1.
+At position 328 to 363, the domain is characterized as EF-hand 2.
+At position 444 to 609, the domain is characterized as Miro 2.
+At position 22 to 84, the domain is characterized as LIM zinc-binding 1.
+At position 86 to 148, the domain is characterized as LIM zinc-binding 2.
+At position 218 to 317, the domain is characterized as Fe2OG dioxygenase.
+At position 40 to 103, the domain is characterized as bZIP.
+At position 323 to 442, the domain is characterized as Toprim.
+At position 1 to 189, the domain is characterized as tr-type G.
+At position 52 to 342, the domain is characterized as PPM-type phosphatase.
+At position 46 to 418, the domain is characterized as PIPK.
+At position 220 to 369, the domain is characterized as TrmE-type G.
+At position 92 to 255, the domain is characterized as Helicase ATP-binding.
+At position 635 to 809, the domain is characterized as Toprim.
+At position 26 to 93, the domain is characterized as Rho RNA-BD.
+At position 18 to 146, the domain is characterized as RNase III.
+At position 214 to 332, the domain is characterized as Nop.
+At position 8 to 169, the domain is characterized as EngA-type G 1.
+At position 318 to 428, the domain is characterized as PAZ.
+At position 594 to 924, the domain is characterized as Piwi.
+At position 25 to 192, the domain is characterized as Laminin G-like.
+At position 281 to 320, the domain is characterized as EGF-like 1.
+At position 321 to 358, the domain is characterized as EGF-like 2; calcium-binding.
+At position 374 to 415, the domain is characterized as EGF-like 3; calcium-binding.
+At position 418 to 459, the domain is characterized as EGF-like 4.
+At position 728 to 942, the domain is characterized as TSP C-terminal.
+At position 242 to 452, the domain is characterized as Peptidase M12B.
+At position 462 to 537, the domain is characterized as Disintegrin.
+At position 538 to 593, the domain is characterized as TSP type-1 1.
+At position 821 to 880, the domain is characterized as TSP type-1 2.
+At position 881 to 940, the domain is characterized as TSP type-1 3.
+At position 942 to 995, the domain is characterized as TSP type-1 4.
+At position 1411 to 1459, the domain is characterized as TSP type-1 5.
+At position 1462 to 1522, the domain is characterized as TSP type-1 6.
+At position 1523 to 1567, the domain is characterized as TSP type-1 7.
+At position 1569 to 1629, the domain is characterized as TSP type-1 8.
+At position 1632 to 1672, the domain is characterized as PLAC.
+At position 66 to 184, the domain is characterized as MTTase N-terminal.
+At position 207 to 437, the domain is characterized as Radical SAM core.
+At position 440 to 503, the domain is characterized as TRAM.
+At position 1382 to 1982, the domain is characterized as FAT.
+At position 2156 to 2469, the domain is characterized as PI3K/PI4K catalytic.
+At position 2517 to 2549, the domain is characterized as FATC.
+At position 8 to 93, the domain is characterized as ASCH.
+At position 66 to 133, the domain is characterized as J.
+At position 14 to 302, the domain is characterized as PKS/mFAS DH.
+At position 1 to 231, the domain is characterized as ABC transporter.
+At position 292 to 363, the domain is characterized as Mop.
+At position 242 to 428, the domain is characterized as GATase cobBQ-type.
+At position 26 to 87, the domain is characterized as HTH iclR-type.
+At position 102 to 271, the domain is characterized as IclR-ED.
+At position 20 to 94, the domain is characterized as S4 RNA-binding.
+At position 33 to 344, the domain is characterized as ABC transmembrane type-1.
+At position 378 to 611, the domain is characterized as ABC transporter.
+At position 330 to 365, the domain is characterized as EF-hand 1.
+At position 365 to 388, the domain is characterized as EF-hand 2.
+At position 455 to 569, the domain is characterized as Toprim.
+At position 22 to 63, the domain is characterized as EGF-like 1.
+At position 64 to 115, the domain is characterized as EGF-like 2; calcium-binding.
+At position 116 to 159, the domain is characterized as EGF-like 3; calcium-binding.
+At position 160 to 208, the domain is characterized as EGF-like 4; calcium-binding.
+At position 209 to 257, the domain is characterized as EGF-like 5; calcium-binding.
+At position 492 to 542, the domain is characterized as GPS.
+At position 229 to 261, the domain is characterized as LisH.
+At position 1 to 59, the domain is characterized as Ferritin-like diiron.
+At position 98 to 220, the domain is characterized as MPN.
+At position 46 to 81, the domain is characterized as EF-hand.
+At position 148 to 187, the domain is characterized as STI1 1.
+At position 530 to 569, the domain is characterized as STI1 2.
+At position 5 to 65, the domain is characterized as HTH tetR-type.
+At position 2 to 125, the domain is characterized as Response regulatory.
+At position 143 to 238, the domain is characterized as HTH LytTR-type.
+At position 353 to 418, the domain is characterized as S4 RNA-binding.
+At position 25 to 106, the domain is characterized as Lipoyl-binding.
+At position 251 to 448, the domain is characterized as GATase cobBQ-type.
+At position 206 to 284, the domain is characterized as RRM.
+At position 2 to 226, the domain is characterized as Glutamine amidotransferase type-1.
+At position 443 to 537, the domain is characterized as BTB 1.
+At position 667 to 736, the domain is characterized as BTB 2.
+At position 326 to 376, the domain is characterized as GPS.
+At position 28 to 353, the domain is characterized as Calpain catalytic.
+At position 502 to 625, the domain is characterized as C2.
+At position 5 to 186, the domain is characterized as YrdC-like.
+At position 648 to 716, the domain is characterized as GRAM.
+At position 851 to 1018, the domain is characterized as VASt 1.
+At position 1059 to 1225, the domain is characterized as VASt 2.
+At position 147 to 255, the domain is characterized as SEA.
+At position 529 to 576, the domain is characterized as GPS.
+At position 181 to 331, the domain is characterized as GAF.
+At position 374 to 612, the domain is characterized as Histidine kinase.
+At position 643 to 761, the domain is characterized as Response regulatory.
+At position 369 to 704, the domain is characterized as Protein kinase.
+At position 31 to 359, the domain is characterized as Kinesin motor.
+At position 94 to 293, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 35, the domain is characterized as SAP.
+At position 243 to 422, the domain is characterized as PBS-linker 1.
+At position 499 to 675, the domain is characterized as PBS-linker 2.
+At position 696 to 873, the domain is characterized as PBS-linker 3.
+At position 268 to 363, the domain is characterized as PH.
+At position 403 to 525, the domain is characterized as Arf-GAP.
+At position 222 to 376, the domain is characterized as TrmE-type G.
+At position 155 to 220, the domain is characterized as HTH luxR-type.
+At position 19 to 209, the domain is characterized as ABC transmembrane type-1.
+At position 5 to 119, the domain is characterized as Response regulatory.
+At position 158 to 333, the domain is characterized as Helicase ATP-binding.
+At position 358 to 508, the domain is characterized as Helicase C-terminal.
+At position 453 to 567, the domain is characterized as Toprim.
+At position 8 to 215, the domain is characterized as DPCK.
+At position 208 to 875, the domain is characterized as USP.
+At position 1 to 83, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 46 to 162, the domain is characterized as Cadherin 1.
+At position 163 to 282, the domain is characterized as Cadherin 2.
+At position 66 to 118, the domain is characterized as HAMP.
+At position 133 to 355, the domain is characterized as Histidine kinase.
+At position 25 to 171, the domain is characterized as Helicase ATP-binding.
+At position 431 to 594, the domain is characterized as Helicase C-terminal.
+At position 1 to 17, the domain is characterized as GoLoco.
+At position 181 to 397, the domain is characterized as Rap-GAP.
+At position 4 to 90, the domain is characterized as Acylphosphatase-like.
+At position 631 to 700, the domain is characterized as SAM.
+At position 4 to 219, the domain is characterized as ABC transporter.
+At position 41 to 368, the domain is characterized as Protein kinase.
+At position 128 to 349, the domain is characterized as Radical SAM core.
+At position 49 to 245, the domain is characterized as Lon N-terminal.
+At position 633 to 814, the domain is characterized as Lon proteolytic.
+At position 465 to 724, the domain is characterized as Pterin-binding.
+At position 11 to 314, the domain is characterized as Hcy-binding.
+At position 42 to 266, the domain is characterized as Peptidase S1.
+At position 33 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 161 to 249, the domain is characterized as Ig-like C2-type 2.
+At position 414 to 503, the domain is characterized as Ig-like C2-type 3.
+At position 514 to 599, the domain is characterized as Ig-like C2-type 4.
+At position 620 to 711, the domain is characterized as Ig-like C2-type 5.
+At position 721 to 821, the domain is characterized as Ig-like C2-type 6.
+At position 1098 to 1186, the domain is characterized as Ig-like C2-type 7.
+At position 1238 to 1326, the domain is characterized as Ig-like C2-type 8.
+At position 1334 to 1426, the domain is characterized as Fibronectin type-III.
+At position 1464 to 1719, the domain is characterized as Protein kinase.
+At position 1809 to 1898, the domain is characterized as Ig-like C2-type 9.
+At position 10 to 208, the domain is characterized as tr-type G.
+At position 27 to 252, the domain is characterized as Glutamine amidotransferase type-2.
+At position 7 to 80, the domain is characterized as Sm.
+At position 80 to 284, the domain is characterized as tr-type G.
+At position 167 to 241, the domain is characterized as BTB.
+At position 45 to 110, the domain is characterized as Collagen-like.
+At position 111 to 247, the domain is characterized as C1q.
+At position 46 to 243, the domain is characterized as HIN-200 1.
+At position 244 to 441, the domain is characterized as HIN-200 2.
+At position 136 to 385, the domain is characterized as ABC transporter 1.
+At position 490 to 717, the domain is characterized as ABC transmembrane type-2 1.
+At position 822 to 1066, the domain is characterized as ABC transporter 2.
+At position 1157 to 1389, the domain is characterized as ABC transmembrane type-2 2.
+At position 6 to 63, the domain is characterized as HTH lacI-type.
+At position 11 to 176, the domain is characterized as PPIase cyclophilin-type.
+At position 518 to 624, the domain is characterized as Calponin-homology (CH).
+At position 762 to 824, the domain is characterized as LIM zinc-binding.
+At position 1799 to 1948, the domain is characterized as bMERB.
+At position 35 to 108, the domain is characterized as U-box.
+At position 278 to 433, the domain is characterized as PPIase cyclophilin-type.
+At position 350 to 422, the domain is characterized as PAS.
+At position 149 to 239, the domain is characterized as RRM.
+At position 383 to 400, the domain is characterized as WH2 1.
+At position 410 to 427, the domain is characterized as WH2 2.
+At position 21 to 245, the domain is characterized as Peptidase S1.
+At position 6 to 235, the domain is characterized as ABC transporter.
+At position 58 to 505, the domain is characterized as Biotin carboxylation.
+At position 177 to 374, the domain is characterized as ATP-grasp.
+At position 645 to 724, the domain is characterized as Biotinyl-binding.
+At position 1156 to 1226, the domain is characterized as Bromo 1.
+At position 1315 to 1409, the domain is characterized as Bromo 2.
+At position 1 to 191, the domain is characterized as RNase H type-2.
+At position 45 to 495, the domain is characterized as Sema.
+At position 551 to 605, the domain is characterized as TSP type-1 1.
+At position 606 to 662, the domain is characterized as TSP type-1 2.
+At position 664 to 713, the domain is characterized as TSP type-1 3.
+At position 721 to 776, the domain is characterized as TSP type-1 4.
+At position 795 to 850, the domain is characterized as TSP type-1 5.
+At position 852 to 907, the domain is characterized as TSP type-1 6.
+At position 908 to 952, the domain is characterized as TSP type-1 7.
+At position 3 to 153, the domain is characterized as UBC core.
+At position 78 to 113, the domain is characterized as EF-hand 1.
+At position 114 to 149, the domain is characterized as EF-hand 2.
+At position 14 to 79, the domain is characterized as HTH HARE-type.
+At position 70 to 284, the domain is characterized as ABC transporter.
+At position 35 to 169, the domain is characterized as MATH.
+At position 205 to 271, the domain is characterized as BTB.
+At position 14 to 132, the domain is characterized as EamA 1.
+At position 153 to 287, the domain is characterized as EamA 2.
+At position 368 to 634, the domain is characterized as ZP.
+At position 302 to 437, the domain is characterized as Fido.
+At position 63 to 123, the domain is characterized as SH3.
+At position 129 to 226, the domain is characterized as SH2.
+At position 247 to 501, the domain is characterized as Protein kinase.
+At position 55 to 274, the domain is characterized as Radical SAM core.
+At position 140 to 740, the domain is characterized as PLA2c.
+At position 33 to 281, the domain is characterized as ABC transporter.
+At position 236 to 452, the domain is characterized as FAD-binding FR-type.
+At position 42 to 153, the domain is characterized as THUMP.
+At position 8 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 396, the domain is characterized as GMPS ATP-PPase.
+At position 2 to 111, the domain is characterized as ABC transporter.
+At position 222 to 324, the domain is characterized as ABC transmembrane type-1.
+At position 45 to 310, the domain is characterized as Protein kinase.
+At position 25 to 58, the domain is characterized as WW 1.
+At position 63 to 97, the domain is characterized as WW 2.
+At position 715 to 867, the domain is characterized as MyTH4.
+At position 914 to 1102, the domain is characterized as Rho-GAP.
+At position 35 to 319, the domain is characterized as Protein kinase.
+At position 515 to 629, the domain is characterized as SMC hinge.
+At position 61 to 186, the domain is characterized as EXPERA 1.
+At position 217 to 351, the domain is characterized as EXPERA 2.
+At position 326 to 389, the domain is characterized as SAM.
+At position 193 to 336, the domain is characterized as FCP1 homology.
+At position 38 to 257, the domain is characterized as Cupin type-1 1.
+At position 331 to 480, the domain is characterized as Cupin type-1 2.
+At position 114 to 301, the domain is characterized as FAD-binding PCMH-type.
+At position 12 to 78, the domain is characterized as SAM.
+At position 422 to 530, the domain is characterized as SH2.
+At position 292 to 426, the domain is characterized as DAGKc.
+At position 32 to 206, the domain is characterized as Exonuclease.
+At position 87 to 182, the domain is characterized as Toprim.
+At position 56 to 154, the domain is characterized as Rieske.
+At position 129 to 185, the domain is characterized as CBS 1.
+At position 189 to 246, the domain is characterized as CBS 2.
+At position 549 to 616, the domain is characterized as GRAM.
+At position 758 to 930, the domain is characterized as VASt 1.
+At position 967 to 1139, the domain is characterized as VASt 2.
+At position 14 to 104, the domain is characterized as CS.
+At position 763 to 914, the domain is characterized as CBM3.
+At position 120 to 250, the domain is characterized as GST C-terminal.
+At position 15 to 291, the domain is characterized as tr-type G.
+At position 353 to 420, the domain is characterized as S4 RNA-binding.
+At position 20 to 120, the domain is characterized as SRCR 1.
+At position 198 to 298, the domain is characterized as SRCR 2.
+At position 304 to 404, the domain is characterized as SRCR 3.
+At position 467 to 568, the domain is characterized as SRCR 4.
+At position 772 to 872, the domain is characterized as SRCR 5.
+At position 289 to 436, the domain is characterized as VPS9.
+At position 26 to 72, the domain is characterized as F-box.
+At position 81 to 135, the domain is characterized as bHLH.
+At position 254 to 451, the domain is characterized as Laminin G-like 2.
+At position 458 to 650, the domain is characterized as Laminin G-like 3.
+At position 654 to 691, the domain is characterized as EGF-like 2.
+At position 696 to 859, the domain is characterized as Laminin G-like 4.
+At position 876 to 1048, the domain is characterized as Laminin G-like 5.
+At position 1051 to 1088, the domain is characterized as EGF-like 3.
+At position 1092 to 1292, the domain is characterized as Laminin G-like 6.
+At position 43 to 153, the domain is characterized as TBDR plug.
+At position 158 to 733, the domain is characterized as TBDR beta-barrel.
+At position 61 to 105, the domain is characterized as CHCH.
+At position 341 to 390, the domain is characterized as FBD.
+At position 2 to 60, the domain is characterized as TRAM.
+At position 54 to 166, the domain is characterized as OmpA-like.
+At position 83 to 220, the domain is characterized as Thioredoxin.
+At position 112 to 162, the domain is characterized as DHHC.
+At position 239 to 414, the domain is characterized as TR mART core.
+At position 59 to 276, the domain is characterized as Radical SAM core.
+At position 5 to 118, the domain is characterized as Response regulatory.
+At position 6 to 94, the domain is characterized as ASCH.
+At position 75 to 155, the domain is characterized as GS beta-grasp.
+At position 159 to 428, the domain is characterized as GS catalytic.
+At position 7 to 86, the domain is characterized as GST N-terminal.
+At position 92 to 226, the domain is characterized as GST C-terminal.
+At position 93 to 198, the domain is characterized as DM10 1.
+At position 239 to 359, the domain is characterized as DM10 2.
+At position 416 to 520, the domain is characterized as DM10 3.
+At position 574 to 609, the domain is characterized as EF-hand.
+At position 139 to 245, the domain is characterized as C-type lectin.
+At position 143 to 388, the domain is characterized as Radical SAM core.
+At position 391 to 459, the domain is characterized as TRAM.
+At position 369 to 398, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 408 to 437, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 104, the domain is characterized as Ig-like V-type.
+At position 211 to 305, the domain is characterized as Fe2OG dioxygenase.
+At position 728 to 1163, the domain is characterized as ACD.
+At position 111 to 271, the domain is characterized as CP-type G.
+At position 22 to 133, the domain is characterized as MTTase N-terminal.
+At position 157 to 386, the domain is characterized as Radical SAM core.
+At position 389 to 460, the domain is characterized as TRAM.
+At position 40 to 250, the domain is characterized as GH11 1.
+At position 316 to 514, the domain is characterized as GH11 2.
+At position 21 to 104, the domain is characterized as GIY-YIG.
+At position 52 to 337, the domain is characterized as AB hydrolase-1.
+At position 6 to 81, the domain is characterized as H15.
+At position 4 to 275, the domain is characterized as CN hydrolase.
+At position 167 to 241, the domain is characterized as RRM.
+At position 169 to 232, the domain is characterized as MIT.
+At position 42 to 126, the domain is characterized as Doublecortin 1.
+At position 160 to 239, the domain is characterized as Doublecortin 2.
+At position 171 to 429, the domain is characterized as Protein kinase.
+At position 130 to 292, the domain is characterized as Integrase catalytic.
+At position 49 to 305, the domain is characterized as GB1/RHD3-type G.
+At position 61 to 169, the domain is characterized as Ig-like V-type.
+At position 51 to 98, the domain is characterized as F-box.
+At position 74 to 226, the domain is characterized as TIR.
+At position 1 to 146, the domain is characterized as SPX.
+At position 1 to 144, the domain is characterized as MGS-like.
+At position 273 to 344, the domain is characterized as PUA.
+At position 43 to 97, the domain is characterized as FHA.
+At position 14 to 126, the domain is characterized as VOC 1.
+At position 156 to 276, the domain is characterized as VOC 2.
+At position 62 to 91, the domain is characterized as EGF-like.
+At position 11 to 85, the domain is characterized as GIY-YIG.
+At position 194 to 229, the domain is characterized as UVR.
+At position 41 to 130, the domain is characterized as Ig-like C2-type.
+At position 46 to 260, the domain is characterized as Helicase ATP-binding.
+At position 295 to 460, the domain is characterized as Helicase C-terminal.
+At position 121 to 171, the domain is characterized as DHHC.
+At position 2 to 84, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 123 to 155, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 177 to 205, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 61 to 156, the domain is characterized as RAMA.
+At position 258 to 393, the domain is characterized as MPN.
+At position 43 to 231, the domain is characterized as GH11.
+At position 22 to 133, the domain is characterized as PH 1.
+At position 205 to 234, the domain is characterized as IQ.
+At position 243 to 429, the domain is characterized as DH.
+At position 470 to 588, the domain is characterized as PH 2.
+At position 635 to 756, the domain is characterized as N-terminal Ras-GEF.
+At position 1002 to 1234, the domain is characterized as Ras-GEF.
+At position 20 to 95, the domain is characterized as Ig-like C2-type 1.
+At position 111 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 207 to 293, the domain is characterized as Ig-like C2-type 3.
+At position 66 to 117, the domain is characterized as bHLH.
+At position 36 to 68, the domain is characterized as LRRNT.
+At position 198 to 252, the domain is characterized as LRRCT.
+At position 34 to 118, the domain is characterized as Ig-like 1.
+At position 124 to 207, the domain is characterized as Ig-like 2.
+At position 2 to 221, the domain is characterized as ABC transporter.
+At position 92 to 144, the domain is characterized as bHLH.
+At position 222 to 478, the domain is characterized as Fibrinogen C-terminal.
+At position 102 to 309, the domain is characterized as Alpha-type protein kinase.
+At position 231 to 352, the domain is characterized as C2 1.
+At position 363 to 496, the domain is characterized as C2 2.
+At position 204 to 391, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 404 to 598, the domain is characterized as Albumin 3.
+At position 1 to 153, the domain is characterized as RPW8.
+At position 53 to 344, the domain is characterized as YjeF C-terminal.
+At position 4 to 224, the domain is characterized as Radical SAM core.
+At position 125 to 301, the domain is characterized as Helicase ATP-binding.
+At position 329 to 483, the domain is characterized as Helicase C-terminal.
+At position 38 to 401, the domain is characterized as GH18.
+At position 87 to 122, the domain is characterized as Orange.
+At position 93 to 172, the domain is characterized as PUA.
+At position 1 to 269, the domain is characterized as SMP-LTD.
+At position 8 to 180, the domain is characterized as N-acetyltransferase.
+At position 253 to 429, the domain is characterized as GATase cobBQ-type.
+At position 38 to 225, the domain is characterized as Helicase ATP-binding.
+At position 251 to 409, the domain is characterized as Helicase C-terminal.
+At position 168 to 285, the domain is characterized as Rhodanese.
+At position 321 to 464, the domain is characterized as Tyrosine-protein phosphatase.
+At position 73 to 163, the domain is characterized as CTCK.
+At position 543 to 578, the domain is characterized as EF-hand.
+At position 332 to 538, the domain is characterized as MCM.
+At position 105 to 418, the domain is characterized as IF rod.
+At position 7 to 148, the domain is characterized as SprT-like.
+At position 314 to 442, the domain is characterized as C2 B9-type.
+At position 19 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 249 to 297, the domain is characterized as bHLH.
+At position 26 to 90, the domain is characterized as J.
+At position 1 to 70, the domain is characterized as KRAB.
+At position 254 to 326, the domain is characterized as PDZ.
+At position 428 to 502, the domain is characterized as DEP.
+At position 202 to 398, the domain is characterized as Peptidase M12B.
+At position 406 to 492, the domain is characterized as Disintegrin.
+At position 68 to 258, the domain is characterized as YrdC-like.
+At position 3 to 358, the domain is characterized as Kinesin motor.
+At position 480 to 544, the domain is characterized as FHA.
+At position 1177 to 1291, the domain is characterized as PX.
+At position 52 to 127, the domain is characterized as Rho RNA-BD.
+At position 114 to 670, the domain is characterized as PLA2c.
+At position 215 to 314, the domain is characterized as SH2.
+At position 580 to 848, the domain is characterized as Ras-GEF.
+At position 583 to 649, the domain is characterized as LIM zinc-binding.
+At position 52 to 202, the domain is characterized as Nudix hydrolase.
+At position 9 to 62, the domain is characterized as ClpX-type ZB.
+At position 164 to 486, the domain is characterized as Peptidase S8.
+At position 495 to 638, the domain is characterized as P/Homo B.
+At position 52 to 336, the domain is characterized as Protein kinase.
+At position 6 to 53, the domain is characterized as RPE1 insert.
+At position 115 to 134, the domain is characterized as SAP 1.
+At position 267 to 281, the domain is characterized as SAP 2.
+At position 1 to 53, the domain is characterized as Rubredoxin-like 1.
+At position 119 to 170, the domain is characterized as Rubredoxin-like 2.
+At position 53 to 116, the domain is characterized as S5 DRBM.
+At position 34 to 317, the domain is characterized as ABC transmembrane type-1.
+At position 352 to 592, the domain is characterized as ABC transporter.
+At position 162 to 247, the domain is characterized as PPIase FKBP-type.
+At position 42 to 299, the domain is characterized as Pterin-binding.
+At position 38 to 142, the domain is characterized as Cytochrome c 1.
+At position 186 to 294, the domain is characterized as Cytochrome c 2.
+At position 330 to 423, the domain is characterized as Cytochrome c 3.
+At position 577 to 637, the domain is characterized as KH.
+At position 654 to 721, the domain is characterized as S1 motif.
+At position 249 to 447, the domain is characterized as GATase cobBQ-type.
+At position 8 to 293, the domain is characterized as tr-type G.
+At position 217 to 373, the domain is characterized as TrmE-type G.
+At position 10 to 185, the domain is characterized as BPL/LPL catalytic.
+At position 58 to 153, the domain is characterized as Ricin B-type lectin.
+At position 681 to 710, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 735 to 766, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 26 to 129, the domain is characterized as NR LBD.
+At position 660 to 829, the domain is characterized as Integrase catalytic.
+At position 1338 to 1476, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1610 to 1752, the domain is characterized as RNase H Ty1/copia-type.
+At position 128 to 160, the domain is characterized as LisH.
+At position 166 to 224, the domain is characterized as CTLH.
+At position 8 to 127, the domain is characterized as Longin.
+At position 138 to 198, the domain is characterized as v-SNARE coiled-coil homology.
+At position 40 to 320, the domain is characterized as IF rod.
+At position 227 to 406, the domain is characterized as GAF.
+At position 621 to 692, the domain is characterized as PAS 1.
+At position 755 to 826, the domain is characterized as PAS 2.
+At position 903 to 1123, the domain is characterized as Histidine kinase.
+At position 29 to 145, the domain is characterized as Cadherin 1.
+At position 146 to 246, the domain is characterized as Cadherin 2.
+At position 2 to 145, the domain is characterized as SPX.
+At position 45 to 354, the domain is characterized as AB hydrolase-1.
+At position 5 to 79, the domain is characterized as PUA.
+At position 39 to 101, the domain is characterized as SH3.
+At position 111 to 294, the domain is characterized as Helicase ATP-binding.
+At position 328 to 479, the domain is characterized as Helicase C-terminal.
+At position 398 to 515, the domain is characterized as Thioredoxin.
+At position 381 to 451, the domain is characterized as J.
+At position 51 to 94, the domain is characterized as SMB 1.
+At position 95 to 139, the domain is characterized as SMB 2.
+At position 288 to 428, the domain is characterized as SIS 1.
+At position 460 to 599, the domain is characterized as SIS 2.
+At position 17 to 208, the domain is characterized as Albumin 1.
+At position 209 to 394, the domain is characterized as Albumin 2.
+At position 395 to 476, the domain is characterized as Albumin 3.
+At position 45 to 130, the domain is characterized as PB1.
+At position 5 to 190, the domain is characterized as UmuC.
+At position 15 to 240, the domain is characterized as ABC transporter.
+At position 5 to 185, the domain is characterized as YrdC-like.
+At position 501 to 755, the domain is characterized as Protein kinase.
+At position 129 to 161, the domain is characterized as EF-hand 4.
+At position 10 to 146, the domain is characterized as RNase III.
+At position 7 to 249, the domain is characterized as ABC transporter.
+At position 285 to 415, the domain is characterized as Nop.
+At position 152 to 228, the domain is characterized as Cache.
+At position 303 to 355, the domain is characterized as HAMP.
+At position 374 to 610, the domain is characterized as Methyl-accepting transducer.
+At position 221 to 457, the domain is characterized as Peptidase M12B.
+At position 458 to 552, the domain is characterized as Disintegrin.
+At position 1 to 122, the domain is characterized as MGS-like.
+At position 294 to 456, the domain is characterized as Helicase ATP-binding.
+At position 160 to 277, the domain is characterized as C-type lectin.
+At position 75 to 181, the domain is characterized as Ig-like C2-type 1.
+At position 192 to 268, the domain is characterized as Ig-like C2-type 2.
+At position 281 to 376, the domain is characterized as Fibronectin type-III 1.
+At position 381 to 478, the domain is characterized as Fibronectin type-III 2.
+At position 582 to 852, the domain is characterized as Protein kinase.
+At position 718 to 985, the domain is characterized as Protein kinase.
+At position 211 to 451, the domain is characterized as Asparagine synthetase.
+At position 1 to 25, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 3 to 82, the domain is characterized as GST N-terminal.
+At position 112 to 325, the domain is characterized as Lon N-terminal.
+At position 738 to 922, the domain is characterized as Lon proteolytic.
+At position 64 to 312, the domain is characterized as Radical SAM core.
+At position 209 to 306, the domain is characterized as HTH araC/xylS-type.
+At position 14 to 134, the domain is characterized as RWD.
+At position 1461 to 1685, the domain is characterized as Collagen IV NC1.
+At position 350 to 416, the domain is characterized as S4 RNA-binding.
+At position 397 to 426, the domain is characterized as IQ.
+At position 5 to 115, the domain is characterized as MTTase N-terminal.
+At position 134 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 440, the domain is characterized as TRAM.
+At position 593 to 668, the domain is characterized as RRM 1.
+At position 683 to 760, the domain is characterized as RRM 2.
+At position 2 to 256, the domain is characterized as ABC transporter.
+At position 27 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 13 to 126, the domain is characterized as Response regulatory.
+At position 39 to 232, the domain is characterized as Glutamine amidotransferase type-1.
+At position 233 to 425, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 83, the domain is characterized as Kringle 5.
+At position 104 to 331, the domain is characterized as Peptidase S1.
+At position 6 to 89, the domain is characterized as Core-binding (CB).
+At position 108 to 293, the domain is characterized as Tyr recombinase.
+At position 25 to 62, the domain is characterized as VM.
+At position 11 to 121, the domain is characterized as MTTase N-terminal.
+At position 80 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 458, the domain is characterized as ADPK.
+At position 39 to 152, the domain is characterized as tRNA-binding.
+At position 404 to 492, the domain is characterized as B5.
+At position 717 to 808, the domain is characterized as FDX-ACB.
+At position 14 to 239, the domain is characterized as ABC transporter.
+At position 136 to 572, the domain is characterized as Urease.
+At position 166 to 306, the domain is characterized as Guanylate cyclase.
+At position 122 to 195, the domain is characterized as PRC barrel.
+At position 3 to 412, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 9 to 435, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 930 to 1250, the domain is characterized as PKS/mFAS DH.
+At position 2267 to 2344, the domain is characterized as Carrier.
+At position 3 to 206, the domain is characterized as ABC transporter.
+At position 5 to 189, the domain is characterized as Glutamine amidotransferase type-1.
+At position 160 to 332, the domain is characterized as OBG-type G.
+At position 1 to 65, the domain is characterized as Disintegrin.
+At position 260 to 380, the domain is characterized as Sox C-terminal.
+At position 22 to 81, the domain is characterized as Sushi 1.
+At position 120 to 183, the domain is characterized as Sushi 2.
+At position 43 to 103, the domain is characterized as CBS 1.
+At position 125 to 187, the domain is characterized as CBS 2.
+At position 198 to 260, the domain is characterized as CBS 3.
+At position 272 to 329, the domain is characterized as CBS 4.
+At position 10 to 93, the domain is characterized as Toprim.
+At position 130 to 161, the domain is characterized as KOW.
+At position 22 to 274, the domain is characterized as Protein kinase.
+At position 106 to 135, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 136 to 165, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 132 to 350, the domain is characterized as ABC transporter.
+At position 13 to 204, the domain is characterized as ABC transmembrane type-1.
+At position 12 to 46, the domain is characterized as SAP.
+At position 112 to 272, the domain is characterized as PINIT.
+At position 194 to 546, the domain is characterized as Asparagine synthetase.
+At position 103 to 241, the domain is characterized as SET.
+At position 4 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 21 to 127, the domain is characterized as B30.2/SPRY.
+At position 420 to 499, the domain is characterized as Chromo 1.
+At position 533 to 597, the domain is characterized as Chromo 2.
+At position 637 to 809, the domain is characterized as Helicase ATP-binding.
+At position 943 to 1094, the domain is characterized as Helicase C-terminal.
+At position 46 to 168, the domain is characterized as Thioredoxin.
+At position 660 to 822, the domain is characterized as Helicase ATP-binding.
+At position 847 to 997, the domain is characterized as Helicase C-terminal.
+At position 10 to 46, the domain is characterized as LDL-receptor class A.
+At position 832 to 1236, the domain is characterized as GBD/FH3.
+At position 1595 to 1717, the domain is characterized as N-terminal Ras-GEF.
+At position 1747 to 1974, the domain is characterized as Ras-GEF.
+At position 124 to 488, the domain is characterized as TTL.
+At position 147 to 382, the domain is characterized as Radical SAM core.
+At position 385 to 446, the domain is characterized as TRAM.
+At position 189 to 394, the domain is characterized as GT92.
+At position 56 to 217, the domain is characterized as CP-type G.
+At position 46 to 150, the domain is characterized as Expansin-like EG45.
+At position 164 to 249, the domain is characterized as Expansin-like CBD.
+At position 25 to 96, the domain is characterized as BTB.
+At position 182 to 235, the domain is characterized as GPS.
+At position 5 to 83, the domain is characterized as RRM.
+At position 78 to 295, the domain is characterized as Radical SAM core.
+At position 17 to 104, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 288 to 474, the domain is characterized as FAD-binding PCMH-type.
+At position 26 to 260, the domain is characterized as ABC transporter.
+At position 127 to 225, the domain is characterized as Rhodanese.
+At position 29 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 138, the domain is characterized as Ig-like C2-type.
+At position 162 to 306, the domain is characterized as TIR.
+At position 7 to 283, the domain is characterized as Helicase ATP-binding.
+At position 47 to 129, the domain is characterized as Phosphagen kinase N-terminal.
+At position 159 to 396, the domain is characterized as Phosphagen kinase C-terminal.
+At position 8 to 94, the domain is characterized as RRM.
+At position 32 to 314, the domain is characterized as ABC transmembrane type-1.
+At position 346 to 582, the domain is characterized as ABC transporter.
+At position 2 to 214, the domain is characterized as Glutamine amidotransferase type-2.
+At position 231 to 578, the domain is characterized as GH16.
+At position 32 to 419, the domain is characterized as Helicase ATP-binding.
+At position 436 to 598, the domain is characterized as Helicase C-terminal.
+At position 147 to 284, the domain is characterized as OTU.
+At position 3 to 189, the domain is characterized as Prephenate dehydratase.
+At position 203 to 280, the domain is characterized as ACT.
+At position 440 to 573, the domain is characterized as Thioredoxin.
+At position 81 to 186, the domain is characterized as Ig-like C2-type 1.
+At position 197 to 273, the domain is characterized as Ig-like C2-type 2.
+At position 286 to 381, the domain is characterized as Fibronectin type-III 1.
+At position 386 to 484, the domain is characterized as Fibronectin type-III 2.
+At position 587 to 858, the domain is characterized as Protein kinase.
+At position 2 to 151, the domain is characterized as Jacalin-type lectin 1.
+At position 156 to 291, the domain is characterized as Jacalin-type lectin 2.
+At position 346 to 489, the domain is characterized as Jacalin-type lectin 3.
+At position 502 to 645, the domain is characterized as Jacalin-type lectin 4.
+At position 50 to 308, the domain is characterized as GB1/RHD3-type G.
+At position 188 to 528, the domain is characterized as PUM-HD.
+At position 31 to 170, the domain is characterized as MPN.
+At position 412 to 534, the domain is characterized as RCK N-terminal.
+At position 571 to 656, the domain is characterized as RCK C-terminal.
+At position 1 to 22, the domain is characterized as Peptidase S1.
+At position 28 to 722, the domain is characterized as GH81.
+At position 796 to 922, the domain is characterized as CBM6.
+At position 928 to 1020, the domain is characterized as CBM56.
+At position 1 to 85, the domain is characterized as Glutaredoxin.
+At position 5 to 268, the domain is characterized as Pyruvate carboxyltransferase.
+At position 37 to 292, the domain is characterized as ABC transporter.
+At position 369 to 575, the domain is characterized as ABC transmembrane type-2.
+At position 1 to 136, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 1 to 242, the domain is characterized as tr-type G.
+At position 385 to 427, the domain is characterized as CCT.
+At position 1305 to 1572, the domain is characterized as ASD2.
+At position 255 to 336, the domain is characterized as Toprim.
+At position 99 to 333, the domain is characterized as Radical SAM core.
+At position 34 to 85, the domain is characterized as FHA.
+At position 48 to 170, the domain is characterized as C2 1.
+At position 217 to 341, the domain is characterized as C2 2.
+At position 385 to 522, the domain is characterized as C2 3.
+At position 39 to 401, the domain is characterized as GH18.
+At position 71 to 275, the domain is characterized as ABC transmembrane type-1.
+At position 84 to 237, the domain is characterized as Ferritin-like diiron.
+At position 346 to 547, the domain is characterized as Protein kinase.
+At position 12 to 48, the domain is characterized as UBA.
+At position 357 to 439, the domain is characterized as UBX.
+At position 5 to 189, the domain is characterized as VWFA.
+At position 221 to 240, the domain is characterized as UIM 1.
+At position 291 to 310, the domain is characterized as UIM 2.
+At position 323 to 342, the domain is characterized as UIM 3.
+At position 34 to 97, the domain is characterized as PUB.
+At position 441 to 631, the domain is characterized as PAW.
+At position 115 to 165, the domain is characterized as DHHC.
+At position 41 to 384, the domain is characterized as TTL.
+At position 171 to 294, the domain is characterized as OTU.
+At position 41 to 194, the domain is characterized as DAGKc.
+At position 2 to 189, the domain is characterized as B30.2/SPRY.
+At position 217 to 249, the domain is characterized as LisH.
+At position 255 to 312, the domain is characterized as CTLH.
+At position 161 to 266, the domain is characterized as THUMP.
+At position 17 to 174, the domain is characterized as NHR.
+At position 251 to 367, the domain is characterized as C-type lectin.
+At position 27 to 152, the domain is characterized as Cyclin N-terminal.
+At position 28 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 28 to 193, the domain is characterized as NAC.
+At position 731 to 774, the domain is characterized as F-box.
+At position 504 to 665, the domain is characterized as HNH Cas9-type.
+At position 133 to 303, the domain is characterized as JmjC.
+At position 203 to 504, the domain is characterized as CP-type G.
+At position 108 to 172, the domain is characterized as S4 RNA-binding.
+At position 14 to 90, the domain is characterized as HTH rpiR-type.
+At position 134 to 274, the domain is characterized as SIS.
+At position 7 to 199, the domain is characterized as PfpI endopeptidase 1.
+At position 211 to 394, the domain is characterized as PfpI endopeptidase 2.
+At position 94 to 207, the domain is characterized as Ferric oxidoreductase.
+At position 238 to 363, the domain is characterized as FAD-binding FR-type.
+At position 8 to 287, the domain is characterized as Protein kinase.
+At position 329 to 750, the domain is characterized as PIPK.
+At position 270 to 385, the domain is characterized as NlpC/P60.
+At position 29 to 95, the domain is characterized as Chitin-binding type R&R.
+At position 362 to 733, the domain is characterized as USP.
+At position 23 to 303, the domain is characterized as Protein kinase.
+At position 323 to 405, the domain is characterized as RRM.
+At position 120 to 309, the domain is characterized as ATP-grasp.
+At position 602 to 678, the domain is characterized as BRCT.
+At position 75 to 145, the domain is characterized as BON.
+At position 28 to 57, the domain is characterized as LRRNT.
+At position 355 to 409, the domain is characterized as LRRCT.
+At position 78 to 349, the domain is characterized as PPM-type phosphatase.
+At position 569 to 632, the domain is characterized as SAM.
+At position 384 to 635, the domain is characterized as SF4 helicase.
+At position 101 to 345, the domain is characterized as Radical SAM core.
+At position 35 to 238, the domain is characterized as Lon N-terminal.
+At position 627 to 808, the domain is characterized as Lon proteolytic.
+At position 67 to 207, the domain is characterized as SCP.
+At position 47 to 101, the domain is characterized as bHLH.
+At position 4 to 224, the domain is characterized as ABC transporter.
+At position 14 to 67, the domain is characterized as ClpX-type ZB.
+At position 383 to 556, the domain is characterized as tr-type G.
+At position 24 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 185 to 438, the domain is characterized as SF4 helicase.
+At position 82 to 372, the domain is characterized as Radical SAM core.
+At position 396 to 547, the domain is characterized as N-acetyltransferase.
+At position 53 to 284, the domain is characterized as ABC transporter.
+At position 99 to 255, the domain is characterized as Nudix hydrolase.
+At position 1 to 126, the domain is characterized as PX.
+At position 157 to 216, the domain is characterized as SH3 1.
+At position 227 to 286, the domain is characterized as SH3 2.
+At position 4 to 64, the domain is characterized as HTH tetR-type.
+At position 185 to 225, the domain is characterized as GIY-YIG.
+At position 221 to 614, the domain is characterized as GRAS.
+At position 35 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 349 to 624, the domain is characterized as Protein kinase.
+At position 30 to 146, the domain is characterized as Plastocyanin-like 1.
+At position 156 to 309, the domain is characterized as Plastocyanin-like 2.
+At position 427 to 561, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 110, the domain is characterized as PA14.
+At position 1 to 232, the domain is characterized as ABC transporter 1.
+At position 315 to 593, the domain is characterized as ABC transporter 2.
+At position 604 to 935, the domain is characterized as ABC transporter 3.
+At position 15 to 134, the domain is characterized as MTTase N-terminal.
+At position 161 to 393, the domain is characterized as Radical SAM core.
+At position 396 to 457, the domain is characterized as TRAM.
+At position 41 to 110, the domain is characterized as KH type-2.
+At position 744 to 773, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 63 to 354, the domain is characterized as YjeF C-terminal.
+At position 40 to 128, the domain is characterized as BRCT 1.
+At position 154 to 179, the domain is characterized as BRCT 2.
+At position 5 to 108, the domain is characterized as SSB 1.
+At position 128 to 228, the domain is characterized as SSB 2.
+At position 524 to 730, the domain is characterized as MCM.
+At position 29 to 144, the domain is characterized as Response regulatory.
+At position 7 to 256, the domain is characterized as ABC transporter.
+At position 501 to 658, the domain is characterized as CBM3.
+At position 186 to 256, the domain is characterized as EB1 C-terminal.
+At position 54 to 162, the domain is characterized as sHSP.
+At position 108 to 288, the domain is characterized as NodB homology.
+At position 187 to 915, the domain is characterized as TBDR beta-barrel.
+At position 64 to 136, the domain is characterized as HTH merR-type.
+At position 100 to 297, the domain is characterized as ABC transmembrane type-1.
+At position 141 to 251, the domain is characterized as PH.
+At position 426 to 570, the domain is characterized as PI-PLC X-box.
+At position 618 to 734, the domain is characterized as PI-PLC Y-box.
+At position 734 to 863, the domain is characterized as C2.
+At position 150 to 205, the domain is characterized as BRX 1.
+At position 329 to 384, the domain is characterized as BRX 2.
+At position 7 to 121, the domain is characterized as VOC 1.
+At position 150 to 273, the domain is characterized as VOC 2.
+At position 62 to 322, the domain is characterized as Protein kinase.
+At position 365 to 400, the domain is characterized as EF-hand 1.
+At position 402 to 437, the domain is characterized as EF-hand 2.
+At position 444 to 479, the domain is characterized as EF-hand 3.
+At position 482 to 509, the domain is characterized as EF-hand 4.
+At position 502 to 577, the domain is characterized as PUA.
+At position 49 to 435, the domain is characterized as Helicase ATP-binding.
+At position 453 to 606, the domain is characterized as Helicase C-terminal.
+At position 674 to 709, the domain is characterized as UVR.
+At position 9 to 243, the domain is characterized as ABC transporter.
+At position 34 to 173, the domain is characterized as NEAT 1.
+At position 184 to 307, the domain is characterized as NEAT 2.
+At position 360 to 484, the domain is characterized as NEAT 3.
+At position 27 to 124, the domain is characterized as BRCT.
+At position 424 to 538, the domain is characterized as Toprim.
+At position 11 to 126, the domain is characterized as Response regulatory.
+At position 150 to 347, the domain is characterized as CheB-type methylesterase.
+At position 17 to 232, the domain is characterized as SET.
+At position 68 to 324, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 333 to 579, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 189 to 376, the domain is characterized as Glutamine amidotransferase type-1.
+At position 25 to 111, the domain is characterized as Core-binding (CB).
+At position 132 to 309, the domain is characterized as Tyr recombinase.
+At position 289 to 476, the domain is characterized as Helicase ATP-binding.
+At position 514 to 718, the domain is characterized as Helicase C-terminal.
+At position 775 to 1089, the domain is characterized as SEC63.
+At position 29 to 78, the domain is characterized as KH.
+At position 1 to 58, the domain is characterized as TGS.
+At position 561 to 620, the domain is characterized as KH.
+At position 630 to 697, the domain is characterized as S1 motif.
+At position 11 to 78, the domain is characterized as SAM.
+At position 641 to 847, the domain is characterized as Rho-GAP.
+At position 877 to 1084, the domain is characterized as START.
+At position 131 to 388, the domain is characterized as SMP-LTD.
+At position 1 to 129, the domain is characterized as CMP/dCMP-type deaminase.
+At position 1 to 85, the domain is characterized as HPr.
+At position 49 to 294, the domain is characterized as GB1/RHD3-type G.
+At position 5 to 61, the domain is characterized as HTH myb-type 1.
+At position 62 to 112, the domain is characterized as HTH myb-type 2.
+At position 26 to 205, the domain is characterized as VWFA 1.
+At position 228 to 406, the domain is characterized as VWFA 2.
+At position 435 to 605, the domain is characterized as VWFA 3.
+At position 621 to 790, the domain is characterized as VWFA 4.
+At position 808 to 981, the domain is characterized as VWFA 5.
+At position 999 to 1170, the domain is characterized as VWFA 6.
+At position 1186 to 1378, the domain is characterized as VWFA 7.
+At position 1756 to 1936, the domain is characterized as VWFA 8.
+At position 1964 to 2165, the domain is characterized as VWFA 9.
+At position 573 to 648, the domain is characterized as BRCT.
+At position 1 to 370, the domain is characterized as Trm1 methyltransferase.
+At position 13 to 136, the domain is characterized as RNase III.
+At position 151 to 358, the domain is characterized as ATP-grasp.
+At position 616 to 864, the domain is characterized as Protein kinase.
+At position 11 to 189, the domain is characterized as PBS-linker.
+At position 19 to 277, the domain is characterized as Alpha-carbonic anhydrase.
+At position 8 to 273, the domain is characterized as Pyruvate carboxyltransferase.
+At position 628 to 696, the domain is characterized as S1 motif.
+At position 24 to 161, the domain is characterized as ENTH.
+At position 39 to 167, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 254 to 317, the domain is characterized as bZIP.
+At position 98 to 170, the domain is characterized as PRC barrel.
+At position 358 to 439, the domain is characterized as OCT.
+At position 6 to 214, the domain is characterized as ABC transmembrane type-1.
+At position 6 to 52, the domain is characterized as SpoVT-AbrB 1.
+At position 56 to 89, the domain is characterized as WW.
+At position 126 to 500, the domain is characterized as Myotubularin phosphatase.
+At position 442 to 515, the domain is characterized as PAS.
+At position 45 to 390, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 3 to 60, the domain is characterized as DEK-C.
+At position 42 to 82, the domain is characterized as EGF-like 1; calcium-binding.
+At position 127 to 167, the domain is characterized as EGF-like 2; calcium-binding.
+At position 168 to 206, the domain is characterized as EGF-like 3; calcium-binding.
+At position 207 to 246, the domain is characterized as EGF-like 4; calcium-binding.
+At position 247 to 287, the domain is characterized as EGF-like 5; calcium-binding.
+At position 288 to 333, the domain is characterized as EGF-like 6; calcium-binding.
+At position 5 to 201, the domain is characterized as Ferric oxidoreductase.
+At position 201 to 311, the domain is characterized as FAD-binding FR-type.
+At position 1123 to 1657, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 29 to 76, the domain is characterized as F-box.
+At position 3 to 95, the domain is characterized as FAD-binding FR-type.
+At position 17 to 186, the domain is characterized as Era-type G.
+At position 217 to 293, the domain is characterized as KH type-2.
+At position 8 to 355, the domain is characterized as DhaK.
+At position 392 to 600, the domain is characterized as DhaL.
+At position 159 to 267, the domain is characterized as Ig-like C2-type.
+At position 276 to 366, the domain is characterized as Fibronectin type-III 1.
+At position 372 to 502, the domain is characterized as Fibronectin type-III 2.
+At position 793 to 1072, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1135 to 1403, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 29 to 254, the domain is characterized as Radical SAM core.
+At position 11 to 103, the domain is characterized as HTH arsR-type.
+At position 28 to 212, the domain is characterized as Radical SAM core.
+At position 173 to 311, the domain is characterized as CMP/dCMP-type deaminase.
+At position 30 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 29 to 190, the domain is characterized as E1.
+At position 286 to 344, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 354 to 545, the domain is characterized as E2.
+At position 277 to 346, the domain is characterized as BIG2.
+At position 194 to 307, the domain is characterized as PH.
+At position 364 to 462, the domain is characterized as SH2.
+At position 137 to 317, the domain is characterized as FAD-binding PCMH-type.
+At position 14 to 143, the domain is characterized as uDENN.
+At position 180 to 316, the domain is characterized as cDENN.
+At position 318 to 395, the domain is characterized as dDENN.
+At position 26 to 488, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 514 to 801, the domain is characterized as UvrD-like helicase C-terminal.
+At position 122 to 217, the domain is characterized as LRAT.
+At position 8 to 71, the domain is characterized as PQ-loop 1.
+At position 185 to 247, the domain is characterized as PQ-loop 2.
+At position 19 to 210, the domain is characterized as GH11.
+At position 306 to 500, the domain is characterized as B30.2/SPRY.
+At position 1 to 179, the domain is characterized as FAD-binding PCMH-type.
+At position 173 to 273, the domain is characterized as PH.
+At position 2 to 46, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 48 to 86, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 91 to 135, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 136 to 173, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 1 to 106, the domain is characterized as C2.
+At position 347 to 601, the domain is characterized as Protein kinase.
+At position 602 to 673, the domain is characterized as AGC-kinase C-terminal.
+At position 122 to 311, the domain is characterized as ATP-grasp.
+At position 98 to 171, the domain is characterized as PRC barrel.
+At position 33 to 97, the domain is characterized as BTB.
+At position 2 to 119, the domain is characterized as PLAT.
+At position 120 to 701, the domain is characterized as Lipoxygenase.
+At position 341 to 613, the domain is characterized as Protein kinase.
+At position 9 to 250, the domain is characterized as ABC transporter.
+At position 116 to 214, the domain is characterized as Fe2OG dioxygenase.
+At position 73 to 129, the domain is characterized as WHEP-TRS.
+At position 85 to 359, the domain is characterized as Pyruvate carboxyltransferase.
+At position 269 to 357, the domain is characterized as PPIase FKBP-type.
+At position 48 to 123, the domain is characterized as Rho RNA-BD.
+At position 151 to 254, the domain is characterized as Fibronectin type-III.
+At position 804 to 935, the domain is characterized as Ricin B-type lectin.
+At position 59 to 243, the domain is characterized as FAD-binding PCMH-type.
+At position 95 to 292, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 259, the domain is characterized as Pyruvate carboxyltransferase.
+At position 135 to 210, the domain is characterized as PRC barrel.
+At position 8 to 105, the domain is characterized as Yippee.
+At position 12 to 206, the domain is characterized as RNase H type-2.
+At position 243 to 351, the domain is characterized as Zinc-hook.
+At position 10 to 84, the domain is characterized as S1-like.
+At position 117 to 356, the domain is characterized as Radical SAM core.
+At position 24 to 65, the domain is characterized as Chitin-binding type-1.
+At position 308 to 403, the domain is characterized as PDZ.
+At position 59 to 239, the domain is characterized as hSac2.
+At position 67 to 280, the domain is characterized as START.
+At position 26 to 88, the domain is characterized as LCN-type CS-alpha/beta.
+At position 28 to 99, the domain is characterized as KRAB.
+At position 127 to 326, the domain is characterized as FtsK.
+At position 2 to 92, the domain is characterized as ATP-cone.
+At position 5 to 116, the domain is characterized as PH.
+At position 402 to 484, the domain is characterized as RCK C-terminal.
+At position 413 to 537, the domain is characterized as Ricin B-type lectin.
+At position 176 to 436, the domain is characterized as Asparagine synthetase.
+At position 37 to 110, the domain is characterized as H15.
+At position 80 to 180, the domain is characterized as Fe2OG dioxygenase.
+At position 20 to 77, the domain is characterized as CBS 1.
+At position 117 to 168, the domain is characterized as CBS 2.
+At position 26 to 196, the domain is characterized as PID.
+At position 56 to 88, the domain is characterized as LisH.
+At position 50 to 290, the domain is characterized as Cache.
+At position 383 to 437, the domain is characterized as HAMP.
+At position 442 to 678, the domain is characterized as Methyl-accepting transducer.
+At position 6 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 199 to 391, the domain is characterized as GMPS ATP-PPase.
+At position 139 to 216, the domain is characterized as RRM.
+At position 204 to 435, the domain is characterized as NR LBD.
+At position 3 to 61, the domain is characterized as TRAM.
+At position 20 to 85, the domain is characterized as LCN-type CS-alpha/beta.
+At position 69 to 257, the domain is characterized as RNase H type-2.
+At position 334 to 394, the domain is characterized as S4 RNA-binding.
+At position 12 to 250, the domain is characterized as ABC transporter.
+At position 159 to 339, the domain is characterized as OBG-type G.
+At position 23 to 107, the domain is characterized as UPAR/Ly6.
+At position 83 to 143, the domain is characterized as Sushi 1.
+At position 144 to 205, the domain is characterized as Sushi 2.
+At position 206 to 276, the domain is characterized as Sushi 3.
+At position 278 to 338, the domain is characterized as Sushi 4.
+At position 340 to 400, the domain is characterized as Sushi 5.
+At position 2 to 105, the domain is characterized as Thioredoxin.
+At position 127 to 305, the domain is characterized as SMP-LTD.
+At position 304 to 425, the domain is characterized as C2 1.
+At position 446 to 572, the domain is characterized as C2 2.
+At position 618 to 740, the domain is characterized as C2 3.
+At position 771 to 888, the domain is characterized as C2 4.
+At position 955 to 1077, the domain is characterized as C2 5.
+At position 73 to 102, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 296 to 381, the domain is characterized as SCD.
+At position 87 to 244, the domain is characterized as Upf1 CH-rich.
+At position 37 to 172, the domain is characterized as Thioredoxin.
+At position 17 to 249, the domain is characterized as VWFA.
+At position 162 to 246, the domain is characterized as CTCK.
+At position 152 to 373, the domain is characterized as TRUD.
+At position 10 to 45, the domain is characterized as EF-hand 1.
+At position 46 to 78, the domain is characterized as EF-hand 2.
+At position 118 to 151, the domain is characterized as EF-hand 4.
+At position 144 to 310, the domain is characterized as Helicase ATP-binding.
+At position 378 to 545, the domain is characterized as Helicase C-terminal.
+At position 945 to 1005, the domain is characterized as Tudor.
+At position 29 to 99, the domain is characterized as PAS.
+At position 163 to 381, the domain is characterized as Histidine kinase.
+At position 17 to 349, the domain is characterized as PTS EIIC type-2.
+At position 419 to 512, the domain is characterized as PTS EIIB type-2.
+At position 1 to 352, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 109 to 231, the domain is characterized as MPN.
+At position 16 to 85, the domain is characterized as KH type-2.
+At position 12 to 264, the domain is characterized as GP-PDE.
+At position 293 to 371, the domain is characterized as RRM.
+At position 27 to 218, the domain is characterized as GH16.
+At position 221 to 366, the domain is characterized as TrmE-type G.
+At position 4 to 172, the domain is characterized as Era-type G.
+At position 195 to 281, the domain is characterized as KH type-2.
+At position 1187 to 1262, the domain is characterized as DEP.
+At position 88 to 167, the domain is characterized as C-type lysozyme.
+At position 117 to 188, the domain is characterized as PAS 1.
+At position 333 to 400, the domain is characterized as PAS 2.
+At position 1059 to 1311, the domain is characterized as Protein kinase.
+At position 28 to 662, the domain is characterized as Vitellogenin.
+At position 43 to 117, the domain is characterized as KH type-2.
+At position 78 to 292, the domain is characterized as Radical SAM core.
+At position 651 to 718, the domain is characterized as SH3 1.
+At position 789 to 880, the domain is characterized as Fibronectin type-III 1.
+At position 882 to 974, the domain is characterized as Fibronectin type-III 2.
+At position 979 to 1077, the domain is characterized as Fibronectin type-III 3.
+At position 1617 to 1685, the domain is characterized as SH3 2.
+At position 1756 to 1823, the domain is characterized as SH3 3.
+At position 12 to 159, the domain is characterized as DAGKc.
+At position 220 to 456, the domain is characterized as Peptidase M12B.
+At position 457 to 551, the domain is characterized as Disintegrin.
+At position 87 to 174, the domain is characterized as Rieske.
+At position 309 to 667, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 16 to 246, the domain is characterized as ABC transporter.
+At position 453 to 567, the domain is characterized as Cadherin 5.
+At position 640 to 783, the domain is characterized as TIR.
+At position 19 to 88, the domain is characterized as BTB.
+At position 514 to 576, the domain is characterized as R3H.
+At position 633 to 679, the domain is characterized as G-patch.
+At position 882 to 933, the domain is characterized as GPS.
+At position 158 to 230, the domain is characterized as HTH crp-type.
+At position 110 to 321, the domain is characterized as CHASE.
+At position 389 to 675, the domain is characterized as Histidine kinase.
+At position 700 to 829, the domain is characterized as Response regulatory 1.
+At position 862 to 999, the domain is characterized as Response regulatory 2.
+At position 1 to 198, the domain is characterized as G-alpha.
+At position 20 to 44, the domain is characterized as LRRNT.
+At position 216 to 389, the domain is characterized as EngA-type G 2.
+At position 390 to 474, the domain is characterized as KH-like.
+At position 57 to 100, the domain is characterized as CWF21.
+At position 1 to 19, the domain is characterized as Peptidase S1.
+At position 86 to 781, the domain is characterized as Myosin motor.
+At position 784 to 813, the domain is characterized as IQ.
+At position 61 to 204, the domain is characterized as Flavodoxin-like.
+At position 266 to 529, the domain is characterized as FAD-binding FR-type.
+At position 212 to 405, the domain is characterized as Helicase ATP-binding.
+At position 416 to 576, the domain is characterized as Helicase C-terminal.
+At position 33 to 168, the domain is characterized as Ig-like V-type.
+At position 7 to 94, the domain is characterized as MtN3/slv 1.
+At position 130 to 213, the domain is characterized as MtN3/slv 2.
+At position 78 to 290, the domain is characterized as RNase H type-2.
+At position 289 to 366, the domain is characterized as RRM 3.
+At position 11 to 252, the domain is characterized as ABC transporter.
+At position 3 to 20, the domain is characterized as WH2 1.
+At position 40 to 57, the domain is characterized as WH2 2.
+At position 1 to 67, the domain is characterized as HMA.
+At position 2 to 89, the domain is characterized as Acylphosphatase-like.
+At position 301 to 334, the domain is characterized as WW.
+At position 498 to 565, the domain is characterized as DRBM 1.
+At position 606 to 673, the domain is characterized as DRBM 2.
+At position 7 to 192, the domain is characterized as Flavodoxin-like.
+At position 166 to 385, the domain is characterized as SMP-LTD.
+At position 23 to 120, the domain is characterized as Core-binding (CB).
+At position 163 to 351, the domain is characterized as Tyr recombinase.
+At position 1 to 64, the domain is characterized as Disintegrin.
+At position 45 to 272, the domain is characterized as Radical SAM core.
+At position 164 to 345, the domain is characterized as VWFA.
+At position 9 to 66, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 17 to 238, the domain is characterized as ABC transporter.
+At position 24 to 55, the domain is characterized as EGF-like 1.
+At position 59 to 86, the domain is characterized as EGF-like 2.
+At position 88 to 125, the domain is characterized as EGF-like 3.
+At position 127 to 168, the domain is characterized as EGF-like 4.
+At position 170 to 206, the domain is characterized as EGF-like 5.
+At position 208 to 245, the domain is characterized as EGF-like 6.
+At position 208 to 375, the domain is characterized as tr-type G.
+At position 576 to 677, the domain is characterized as tRNA-binding.
+At position 482 to 879, the domain is characterized as G-alpha.
+At position 390 to 528, the domain is characterized as N-terminal Ras-GEF.
+At position 676 to 911, the domain is characterized as Ras-GEF.
+At position 214 to 382, the domain is characterized as Helicase ATP-binding.
+At position 528 to 695, the domain is characterized as Helicase C-terminal.
+At position 77 to 109, the domain is characterized as EF-hand 2.
+At position 555 to 584, the domain is characterized as IQ 1.
+At position 917 to 946, the domain is characterized as IQ 2.
+At position 67 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 14 to 121, the domain is characterized as sHSP.
+At position 89 to 340, the domain is characterized as Protein kinase.
+At position 32 to 254, the domain is characterized as L-type lectin-like.
+At position 16 to 86, the domain is characterized as HTH gntR-type.
+At position 29 to 236, the domain is characterized as GH11.
+At position 624 to 952, the domain is characterized as GH10.
+At position 14 to 145, the domain is characterized as ENTH.
+At position 39 to 100, the domain is characterized as S1 motif 1.
+At position 118 to 184, the domain is characterized as S1 motif 2.
+At position 205 to 273, the domain is characterized as S1 motif 3.
+At position 290 to 360, the domain is characterized as S1 motif 4.
+At position 377 to 447, the domain is characterized as S1 motif 5.
+At position 464 to 533, the domain is characterized as S1 motif 6.
+At position 35 to 133, the domain is characterized as Cadherin 1.
+At position 138 to 242, the domain is characterized as Cadherin 2.
+At position 247 to 347, the domain is characterized as Cadherin 3.
+At position 352 to 451, the domain is characterized as Cadherin 4.
+At position 456 to 561, the domain is characterized as Cadherin 5.
+At position 568 to 671, the domain is characterized as Cadherin 6.
+At position 364 to 718, the domain is characterized as Kinesin motor.
+At position 111 to 304, the domain is characterized as Pentraxin (PTX).
+At position 535 to 584, the domain is characterized as GPS.
+At position 2 to 115, the domain is characterized as Response regulatory.
+At position 26 to 83, the domain is characterized as bHLH.
+At position 119 to 183, the domain is characterized as PAS.
+At position 25 to 71, the domain is characterized as F-box.
+At position 20 to 151, the domain is characterized as Cyclin N-terminal.
+At position 65 to 279, the domain is characterized as Radical SAM core.
+At position 2 to 137, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 1 to 105, the domain is characterized as C2 1.
+At position 116 to 232, the domain is characterized as C2 2.
+At position 302 to 512, the domain is characterized as Ras-GAP.
+At position 566 to 673, the domain is characterized as PH.
+At position 162 to 279, the domain is characterized as Thioredoxin.
+At position 300 to 333, the domain is characterized as WW 1.
+At position 330 to 363, the domain is characterized as WW 2.
+At position 405 to 437, the domain is characterized as WW 3.
+At position 444 to 477, the domain is characterized as WW 4.
+At position 536 to 870, the domain is characterized as HECT.
+At position 113 to 229, the domain is characterized as C2 1.
+At position 241 to 370, the domain is characterized as C2 2.
+At position 164 to 477, the domain is characterized as IF rod.
+At position 111 to 148, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 114 to 269, the domain is characterized as Thioredoxin.
+At position 13 to 156, the domain is characterized as SprT-like.
+At position 870 to 970, the domain is characterized as FH1.
+At position 983 to 1435, the domain is characterized as FH2.
+At position 39 to 151, the domain is characterized as tRNA-binding.
+At position 409 to 495, the domain is characterized as B5.
+At position 717 to 810, the domain is characterized as FDX-ACB.
+At position 639 to 857, the domain is characterized as Histidine kinase.
+At position 60 to 152, the domain is characterized as SH2.
+At position 154 to 213, the domain is characterized as SH3 2.
+At position 118 to 196, the domain is characterized as RRM.
+At position 348 to 622, the domain is characterized as Protein kinase.
+At position 84 to 449, the domain is characterized as GBD/FH3.
+At position 583 to 764, the domain is characterized as FH1.
+At position 769 to 1171, the domain is characterized as FH2.
+At position 1194 to 1222, the domain is characterized as DAD.
+At position 439 to 690, the domain is characterized as Clu.
+At position 137 to 331, the domain is characterized as SEC7.
+At position 381 to 494, the domain is characterized as PH.
+At position 35 to 84, the domain is characterized as F-box.
+At position 1089 to 1294, the domain is characterized as JmjC.
+At position 83 to 260, the domain is characterized as Helicase ATP-binding.
+At position 288 to 433, the domain is characterized as Helicase C-terminal.
+At position 86 to 779, the domain is characterized as Myosin motor.
+At position 782 to 811, the domain is characterized as IQ.
+At position 27 to 146, the domain is characterized as NTR.
+At position 2 to 228, the domain is characterized as Radical SAM core.
+At position 20 to 138, the domain is characterized as Response regulatory.
+At position 193 to 386, the domain is characterized as CheB-type methylesterase.
+At position 41 to 216, the domain is characterized as EngB-type G.
+At position 19 to 208, the domain is characterized as ABC transmembrane type-1.
+At position 625 to 801, the domain is characterized as PCI.
+At position 9 to 158, the domain is characterized as NAC.
+At position 33 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 142 to 253, the domain is characterized as Gnk2-homologous 2.
+At position 124 to 164, the domain is characterized as LRRCT.
+At position 17 to 108, the domain is characterized as Core-binding (CB).
+At position 129 to 312, the domain is characterized as Tyr recombinase.
+At position 6 to 296, the domain is characterized as Protein kinase.
+At position 48 to 150, the domain is characterized as AB hydrolase-1.
+At position 103 to 177, the domain is characterized as PRC barrel.
+At position 41 to 232, the domain is characterized as BPL/LPL catalytic.
+At position 126 to 282, the domain is characterized as PID.
+At position 538 to 724, the domain is characterized as Rab-GAP TBC.
+At position 18 to 93, the domain is characterized as Ubiquitin-like.
+At position 143 to 184, the domain is characterized as STI1 1.
+At position 197 to 236, the domain is characterized as STI1 2.
+At position 373 to 410, the domain is characterized as STI1 3.
+At position 414 to 449, the domain is characterized as STI1 4.
+At position 504 to 548, the domain is characterized as UBA.
+At position 31 to 284, the domain is characterized as Protein kinase.
+At position 679 to 727, the domain is characterized as KA1.
+At position 295 to 547, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 49, the domain is characterized as bHLH.
+At position 611 to 689, the domain is characterized as S1 motif.
+At position 317 to 485, the domain is characterized as Helicase ATP-binding.
+At position 655 to 829, the domain is characterized as Helicase C-terminal.
+At position 41 to 237, the domain is characterized as Peptidase M12A.
+At position 232 to 275, the domain is characterized as EGF-like.
+At position 7 to 238, the domain is characterized as Glutamine amidotransferase type-1.
+At position 64 to 185, the domain is characterized as NlpC/P60.
+At position 37 to 233, the domain is characterized as VWFA 1.
+At position 613 to 800, the domain is characterized as VWFA 2.
+At position 824 to 1012, the domain is characterized as VWFA 3.
+At position 15 to 114, the domain is characterized as Ras-associating.
+At position 146 to 954, the domain is characterized as Myosin motor.
+At position 958 to 978, the domain is characterized as IQ 1.
+At position 981 to 1001, the domain is characterized as IQ 2.
+At position 1002 to 1024, the domain is characterized as IQ 3.
+At position 1025 to 1054, the domain is characterized as IQ 4.
+At position 1663 to 1848, the domain is characterized as Rho-GAP.
+At position 635 to 734, the domain is characterized as Zinc-hook.
+At position 256 to 373, the domain is characterized as Sox C-terminal.
+At position 62 to 321, the domain is characterized as Protein kinase 1.
+At position 322 to 391, the domain is characterized as AGC-kinase C-terminal.
+At position 418 to 675, the domain is characterized as Protein kinase 2.
+At position 2 to 164, the domain is characterized as EngA-type G 1.
+At position 199 to 370, the domain is characterized as EngA-type G 2.
+At position 371 to 454, the domain is characterized as KH-like.
+At position 215 to 356, the domain is characterized as DAGKc.
+At position 142 to 306, the domain is characterized as N-acetyltransferase.
+At position 111 to 293, the domain is characterized as ATP-grasp.
+At position 11 to 222, the domain is characterized as ThyX.
+At position 158 to 412, the domain is characterized as ABC transporter 1.
+At position 853 to 1096, the domain is characterized as ABC transporter 2.
+At position 33 to 135, the domain is characterized as Gnk2-homologous 1.
+At position 141 to 252, the domain is characterized as Gnk2-homologous 2.
+At position 30 to 211, the domain is characterized as tr-type G.
+At position 51 to 114, the domain is characterized as S5 DRBM.
+At position 46 to 111, the domain is characterized as NAC-A/B.
+At position 165 to 204, the domain is characterized as UBA.
+At position 348 to 468, the domain is characterized as Fe2OG dioxygenase.
+At position 33 to 118, the domain is characterized as PPIase FKBP-type.
+At position 62 to 330, the domain is characterized as Protein kinase.
+At position 74 to 137, the domain is characterized as Pre-SET.
+At position 140 to 264, the domain is characterized as SET.
+At position 284 to 300, the domain is characterized as Post-SET.
+At position 51 to 155, the domain is characterized as Rieske.
+At position 1 to 180, the domain is characterized as AMMECR1.
+At position 6 to 241, the domain is characterized as tr-type G.
+At position 116 to 297, the domain is characterized as Helicase ATP-binding.
+At position 431 to 601, the domain is characterized as Helicase C-terminal.
+At position 634 to 724, the domain is characterized as Dicer dsRNA-binding fold.
+At position 882 to 1001, the domain is characterized as PAZ.
+At position 1026 to 1184, the domain is characterized as RNase III 1.
+At position 1235 to 1387, the domain is characterized as RNase III 2.
+At position 1421 to 1489, the domain is characterized as DRBM.
+At position 49 to 395, the domain is characterized as Kinesin motor.
+At position 326 to 515, the domain is characterized as Helicase ATP-binding.
+At position 542 to 693, the domain is characterized as Helicase C-terminal.
+At position 52 to 127, the domain is characterized as Carrier.
+At position 346 to 475, the domain is characterized as SET.
+At position 5 to 94, the domain is characterized as Acylphosphatase-like.
+At position 283 to 497, the domain is characterized as B30.2/SPRY.
+At position 27 to 516, the domain is characterized as Sema.
+At position 564 to 656, the domain is characterized as IPT/TIG 1.
+At position 658 to 740, the domain is characterized as IPT/TIG 2.
+At position 743 to 837, the domain is characterized as IPT/TIG 3.
+At position 1079 to 1346, the domain is characterized as Protein kinase.
+At position 6 to 257, the domain is characterized as ABC transporter.
+At position 76 to 148, the domain is characterized as RRM 1.
+At position 39 to 308, the domain is characterized as GP-PDE.
+At position 40 to 137, the domain is characterized as Radical SAM core.
+At position 37 to 136, the domain is characterized as Fibronectin type-III 1.
+At position 144 to 228, the domain is characterized as Fibronectin type-III 2.
+At position 560 to 694, the domain is characterized as N-acetyltransferase.
+At position 2 to 73, the domain is characterized as HTH merR-type.
+At position 162 to 288, the domain is characterized as B12-binding.
+At position 151 to 252, the domain is characterized as tRNA-binding.
+At position 30 to 83, the domain is characterized as Clip.
+At position 108 to 360, the domain is characterized as Peptidase S1.
+At position 37 to 173, the domain is characterized as PID.
+At position 186 to 266, the domain is characterized as KH.
+At position 18 to 107, the domain is characterized as Cystatin.
+At position 24 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 11 to 60, the domain is characterized as F-box.
+At position 23 to 117, the domain is characterized as Ig-like.
+At position 478 to 541, the domain is characterized as bZIP.
+At position 335 to 570, the domain is characterized as PRORP.
+At position 146 to 459, the domain is characterized as IF rod.
+At position 389 to 456, the domain is characterized as TRAM.
+At position 94 to 411, the domain is characterized as Lon N-terminal.
+At position 800 to 992, the domain is characterized as Lon proteolytic.
+At position 48 to 166, the domain is characterized as SEA.
+At position 192 to 422, the domain is characterized as Peptidase S1.
+At position 347 to 554, the domain is characterized as MCM.
+At position 82 to 184, the domain is characterized as C-type lectin.
+At position 265 to 465, the domain is characterized as Helicase ATP-binding.
+At position 511 to 679, the domain is characterized as Helicase C-terminal.
+At position 55 to 286, the domain is characterized as Dynamin-type G.
+At position 444 to 532, the domain is characterized as EH.
+At position 476 to 511, the domain is characterized as EF-hand.
+At position 33 to 188, the domain is characterized as SIS.
+At position 386 to 460, the domain is characterized as B5.
+At position 35 to 284, the domain is characterized as GB1/RHD3-type G.
+At position 70 to 168, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 317 to 482, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 31 to 76, the domain is characterized as WAP.
+At position 454 to 582, the domain is characterized as Guanylate cyclase.
+At position 104 to 201, the domain is characterized as WGR.
+At position 231 to 348, the domain is characterized as PARP alpha-helical.
+At position 356 to 583, the domain is characterized as PARP catalytic.
+At position 11 to 75, the domain is characterized as S5 DRBM.
+At position 8 to 126, the domain is characterized as Response regulatory.
+At position 152 to 337, the domain is characterized as CheB-type methylesterase.
+At position 25 to 86, the domain is characterized as LIM zinc-binding 1.
+At position 87 to 149, the domain is characterized as LIM zinc-binding 2.
+At position 128 to 567, the domain is characterized as Urease.
+At position 269 to 489, the domain is characterized as Fibrinogen C-terminal.
+At position 1 to 107, the domain is characterized as LOB.
+At position 2 to 475, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 507 to 806, the domain is characterized as UvrD-like helicase C-terminal.
+At position 470 to 531, the domain is characterized as LIM zinc-binding 1.
+At position 535 to 595, the domain is characterized as LIM zinc-binding 2.
+At position 595 to 664, the domain is characterized as LIM zinc-binding 3.
+At position 100 to 169, the domain is characterized as SH3.
+At position 585 to 663, the domain is characterized as BRCT.
+At position 24 to 240, the domain is characterized as tr-type G.
+At position 334 to 347, the domain is characterized as CRIB.
+At position 674 to 925, the domain is characterized as Protein kinase.
+At position 1 to 135, the domain is characterized as PTS EIIA type-4.
+At position 155 to 242, the domain is characterized as HPr.
+At position 452 to 821, the domain is characterized as USP.
+At position 871 to 1027, the domain is characterized as Exonuclease.
+At position 80 to 170, the domain is characterized as CTCK.
+At position 60 to 185, the domain is characterized as EXPERA 1.
+At position 216 to 350, the domain is characterized as EXPERA 2.
+At position 1328 to 1609, the domain is characterized as Autotransporter.
+At position 1 to 76, the domain is characterized as Sm.
+At position 97 to 291, the domain is characterized as AMMECR1.
+At position 212 to 275, the domain is characterized as bZIP.
+At position 100 to 186, the domain is characterized as PDZ.
+At position 187 to 336, the domain is characterized as Lon proteolytic.
+At position 38 to 85, the domain is characterized as SERTA.
+At position 33 to 94, the domain is characterized as Kazal-like.
+At position 3 to 118, the domain is characterized as MTTase N-terminal.
+At position 141 to 371, the domain is characterized as Radical SAM core.
+At position 374 to 442, the domain is characterized as TRAM.
+At position 10 to 277, the domain is characterized as tr-type G.
+At position 83 to 111, the domain is characterized as IQ 1.
+At position 112 to 134, the domain is characterized as IQ 2.
+At position 135 to 158, the domain is characterized as IQ 3.
+At position 99 to 160, the domain is characterized as S4 RNA-binding.
+At position 582 to 684, the domain is characterized as tRNA-binding.
+At position 112 to 184, the domain is characterized as S1 motif.
+At position 220 to 286, the domain is characterized as KH 1.
+At position 287 to 347, the domain is characterized as KH 2.
+At position 516 to 750, the domain is characterized as ABC transporter.
+At position 9 to 75, the domain is characterized as J.
+At position 160 to 330, the domain is characterized as TRUD.
+At position 310 to 587, the domain is characterized as ABC transporter 1.
+At position 607 to 937, the domain is characterized as ABC transporter 2.
+At position 81 to 298, the domain is characterized as Radical SAM core.
+At position 589 to 1075, the domain is characterized as Protein kinase.
+At position 21 to 101, the domain is characterized as NAB.
+At position 39 to 149, the domain is characterized as tRNA-binding.
+At position 403 to 478, the domain is characterized as B5.
+At position 12 to 68, the domain is characterized as S4 RNA-binding.
+At position 105 to 232, the domain is characterized as NEAT 1.
+At position 345 to 471, the domain is characterized as NEAT 2.
+At position 543 to 660, the domain is characterized as NEAT 3.
+At position 114 to 307, the domain is characterized as Peptidase M12A.
+At position 354 to 388, the domain is characterized as ShKT 1.
+At position 437 to 471, the domain is characterized as ShKT 2.
+At position 536 to 571, the domain is characterized as ShKT 3.
+At position 18 to 141, the domain is characterized as EamA.
+At position 207 to 360, the domain is characterized as OTU.
+At position 10 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 209 to 401, the domain is characterized as GMPS ATP-PPase.
+At position 2 to 57, the domain is characterized as IBB.
+At position 399 to 474, the domain is characterized as B5.
+At position 703 to 804, the domain is characterized as FDX-ACB.
+At position 19 to 319, the domain is characterized as GH16.
+At position 284 to 458, the domain is characterized as AMMECR1.
+At position 703 to 848, the domain is characterized as Tyrosine-protein phosphatase.
+At position 134 to 571, the domain is characterized as Urease.
+At position 23 to 81, the domain is characterized as Kazal-like 1.
+At position 96 to 156, the domain is characterized as Kazal-like 2.
+At position 230 to 363, the domain is characterized as Guanylate cyclase.
+At position 1 to 359, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 16 to 160, the domain is characterized as Flavodoxin-like.
+At position 215 to 502, the domain is characterized as FAD-binding FR-type.
+At position 419 to 597, the domain is characterized as Helicase ATP-binding.
+At position 629 to 780, the domain is characterized as Helicase C-terminal.
+At position 1 to 45, the domain is characterized as LEM.
+At position 603 to 682, the domain is characterized as BRCT.
+At position 6 to 161, the domain is characterized as Thioredoxin.
+At position 1 to 646, the domain is characterized as Myosin motor.
+At position 649 to 678, the domain is characterized as IQ.
+At position 391 to 463, the domain is characterized as PAS.
+At position 103 to 341, the domain is characterized as Radical SAM core.
+At position 258 to 445, the domain is characterized as GATase cobBQ-type.
+At position 124 to 206, the domain is characterized as PDZ.
+At position 191 to 452, the domain is characterized as NB-ARC.
+At position 37 to 162, the domain is characterized as Fido.
+At position 48 to 321, the domain is characterized as Pyruvate carboxyltransferase.
+At position 2 to 236, the domain is characterized as ABC transporter.
+At position 102 to 268, the domain is characterized as Helicase ATP-binding.
+At position 297 to 449, the domain is characterized as Helicase C-terminal.
+At position 148 to 194, the domain is characterized as G-patch.
+At position 590 to 768, the domain is characterized as Helicase ATP-binding.
+At position 795 to 945, the domain is characterized as Helicase C-terminal.
+At position 27 to 188, the domain is characterized as PPIase cyclophilin-type.
+At position 50 to 353, the domain is characterized as ABC transmembrane type-1 1.
+At position 388 to 624, the domain is characterized as ABC transporter 1.
+At position 707 to 996, the domain is characterized as ABC transmembrane type-1 2.
+At position 1031 to 1269, the domain is characterized as ABC transporter 2.
+At position 1 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 244 to 437, the domain is characterized as GATase cobBQ-type.
+At position 28 to 73, the domain is characterized as WAP.
+At position 77 to 127, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 19 to 198, the domain is characterized as Guanylate kinase-like.
+At position 6 to 228, the domain is characterized as ABC transporter.
+At position 446 to 562, the domain is characterized as HD.
+At position 687 to 766, the domain is characterized as ACT 1.
+At position 793 to 864, the domain is characterized as ACT 2.
+At position 1128 to 1502, the domain is characterized as HECT.
+At position 24 to 146, the domain is characterized as RNase III.
+At position 173 to 243, the domain is characterized as DRBM.
+At position 35 to 70, the domain is characterized as EF-hand.
+At position 155 to 299, the domain is characterized as PI-PLC X-box.
+At position 375 to 491, the domain is characterized as PI-PLC Y-box.
+At position 491 to 617, the domain is characterized as C2.
+At position 31 to 305, the domain is characterized as Pyruvate carboxyltransferase.
+At position 411 to 545, the domain is characterized as YTH.
+At position 293 to 582, the domain is characterized as ABC transmembrane type-1 1.
+At position 635 to 874, the domain is characterized as ABC transporter 1.
+At position 951 to 1255, the domain is characterized as ABC transmembrane type-1 2.
+At position 1294 to 1533, the domain is characterized as ABC transporter 2.
+At position 344 to 765, the domain is characterized as PIPK.
+At position 207 to 256, the domain is characterized as F-box.
+At position 441 to 704, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 25 to 113, the domain is characterized as Ig-like C1-type.
+At position 987 to 1153, the domain is characterized as PNPLA.
+At position 4 to 131, the domain is characterized as FAD-binding FR-type.
+At position 157 to 360, the domain is characterized as OBG-type G.
+At position 31 to 176, the domain is characterized as UBC core.
+At position 19 to 140, the domain is characterized as MsrB.
+At position 550 to 609, the domain is characterized as KH.
+At position 619 to 687, the domain is characterized as S1 motif.
+At position 306 to 415, the domain is characterized as SCP2.
+At position 62 to 558, the domain is characterized as Peptidase S8.
+At position 225 to 326, the domain is characterized as HD.
+At position 142 to 234, the domain is characterized as WSC 1.
+At position 245 to 340, the domain is characterized as WSC 2.
+At position 83 to 243, the domain is characterized as Bms1-type G.
+At position 121 to 273, the domain is characterized as Exonuclease.
+At position 99 to 178, the domain is characterized as RRM.
+At position 22 to 129, the domain is characterized as PH 1.
+At position 204 to 229, the domain is characterized as IQ.
+At position 240 to 426, the domain is characterized as DH.
+At position 467 to 584, the domain is characterized as PH 2.
+At position 644 to 761, the domain is characterized as N-terminal Ras-GEF.
+At position 1038 to 1270, the domain is characterized as Ras-GEF.
+At position 5 to 387, the domain is characterized as BRO1.
+At position 3 to 75, the domain is characterized as S4 RNA-binding.
+At position 621 to 656, the domain is characterized as UVR.
+At position 19 to 197, the domain is characterized as Guanylate kinase-like.
+At position 1073 to 1322, the domain is characterized as Glutamine amidotransferase type-1.
+At position 24 to 61, the domain is characterized as EGF-like 1.
+At position 64 to 108, the domain is characterized as EGF-like 2.
+At position 111 to 267, the domain is characterized as F5/8 type C 1.
+At position 272 to 427, the domain is characterized as F5/8 type C 2.
+At position 101 to 309, the domain is characterized as B30.2/SPRY.
+At position 110 to 259, the domain is characterized as N-acetyltransferase.
+At position 83 to 118, the domain is characterized as EF-hand 3.
+At position 119 to 154, the domain is characterized as EF-hand 4.
+At position 136 to 229, the domain is characterized as RRM.
+At position 132 to 456, the domain is characterized as Kinesin motor.
+At position 6 to 122, the domain is characterized as MTTase N-terminal.
+At position 132 to 361, the domain is characterized as Radical SAM core.
+At position 364 to 434, the domain is characterized as TRAM.
+At position 4 to 141, the domain is characterized as N-acetyltransferase 1.
+At position 152 to 315, the domain is characterized as N-acetyltransferase 2.
+At position 265 to 550, the domain is characterized as ABC transmembrane type-1.
+At position 584 to 818, the domain is characterized as ABC transporter.
+At position 208 to 260, the domain is characterized as KH.
+At position 1 to 170, the domain is characterized as TCTP.
+At position 29 to 180, the domain is characterized as Cyclin N-terminal.
+At position 31 to 135, the domain is characterized as Calponin-homology (CH) 1.
+At position 144 to 250, the domain is characterized as Calponin-homology (CH) 2.
+At position 746 to 781, the domain is characterized as EF-hand 1.
+At position 787 to 822, the domain is characterized as EF-hand 2.
+At position 46 to 109, the domain is characterized as S5 DRBM.
+At position 3 to 177, the domain is characterized as Miro 1.
+At position 193 to 228, the domain is characterized as EF-hand 1.
+At position 313 to 348, the domain is characterized as EF-hand 2.
+At position 452 to 618, the domain is characterized as Miro 2.
+At position 92 to 403, the domain is characterized as IF rod.
+At position 98 to 328, the domain is characterized as Radical SAM core.
+At position 452 to 590, the domain is characterized as SIS 2.
+At position 34 to 195, the domain is characterized as MAM.
+At position 197 to 288, the domain is characterized as Ig-like C2-type.
+At position 295 to 388, the domain is characterized as Fibronectin type-III 1.
+At position 393 to 487, the domain is characterized as Fibronectin type-III 2.
+At position 488 to 594, the domain is characterized as Fibronectin type-III 3.
+At position 670 to 767, the domain is characterized as Fibronectin type-III 4.
+At position 902 to 1156, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1188 to 1450, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 22 to 147, the domain is characterized as C2.
+At position 180 to 210, the domain is characterized as EF-hand 1.
+At position 76 to 246, the domain is characterized as VWFA.
+At position 216 to 291, the domain is characterized as Cytochrome b5 heme-binding.
+At position 389 to 423, the domain is characterized as SAP.
+At position 1 to 111, the domain is characterized as WH1.
+At position 7 to 209, the domain is characterized as ABC transporter.
+At position 129 to 219, the domain is characterized as Rhodanese.
+At position 45 to 341, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 77 to 248, the domain is characterized as Helicase ATP-binding.
+At position 275 to 419, the domain is characterized as Helicase C-terminal.
+At position 50 to 119, the domain is characterized as H15.
+At position 30 to 223, the domain is characterized as GH16.
+At position 533 to 608, the domain is characterized as Ubiquitin-like 8.
+At position 609 to 684, the domain is characterized as Ubiquitin-like 9.
+At position 685 to 760, the domain is characterized as Ubiquitin-like 10.
+At position 761 to 836, the domain is characterized as Ubiquitin-like 11.
+At position 108 to 199, the domain is characterized as Cytochrome c 1.
+At position 206 to 294, the domain is characterized as Cytochrome c 2.
+At position 476 to 607, the domain is characterized as Ricin B-type lectin.
+At position 63 to 506, the domain is characterized as Kinesin motor.
+At position 4 to 92, the domain is characterized as Ig-like C1-type.
+At position 1 to 143, the domain is characterized as MGS-like.
+At position 131 to 568, the domain is characterized as Urease.
+At position 55 to 284, the domain is characterized as Radical SAM core.
+At position 42 to 174, the domain is characterized as N-acetyltransferase.
+At position 158 to 447, the domain is characterized as ABC transmembrane type-1.
+At position 482 to 719, the domain is characterized as ABC transporter.
+At position 83 to 163, the domain is characterized as PA.
+At position 28 to 131, the domain is characterized as Calponin-homology (CH).
+At position 39 to 71, the domain is characterized as EF-hand 2.
+At position 80 to 653, the domain is characterized as Protein kinase.
+At position 288 to 370, the domain is characterized as PUA.
+At position 449 to 556, the domain is characterized as SH2.
+At position 582 to 705, the domain is characterized as PTB.
+At position 11 to 58, the domain is characterized as F-box.
+At position 191 to 209, the domain is characterized as TRAM.
+At position 46 to 225, the domain is characterized as PCI.
+At position 76 to 732, the domain is characterized as Peptidase M13.
+At position 21 to 141, the domain is characterized as EamA 1.
+At position 15 to 135, the domain is characterized as HEPN.
+At position 1 to 20, the domain is characterized as Vitellogenin.
+At position 3 to 63, the domain is characterized as L27.
+At position 138 to 225, the domain is characterized as PDZ 1.
+At position 258 to 338, the domain is characterized as PDZ 2.
+At position 545 to 626, the domain is characterized as PDZ 4.
+At position 692 to 778, the domain is characterized as PDZ 5.
+At position 995 to 1076, the domain is characterized as PDZ 6.
+At position 1138 to 1230, the domain is characterized as PDZ 7.
+At position 1337 to 1420, the domain is characterized as PDZ 8.
+At position 1470 to 1551, the domain is characterized as PDZ 9.
+At position 1613 to 1696, the domain is characterized as PDZ 10.
+At position 1709 to 1791, the domain is characterized as PDZ 11.
+At position 1846 to 1932, the domain is characterized as PDZ 12.
+At position 1971 to 2054, the domain is characterized as PDZ 13.
+At position 204 to 365, the domain is characterized as SSD.
+At position 27 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 285 to 509, the domain is characterized as ABC transmembrane type-1.
+At position 55 to 192, the domain is characterized as MPN.
+At position 220 to 255, the domain is characterized as EF-hand 1.
+At position 356 to 376, the domain is characterized as EF-hand 2.
+At position 410 to 445, the domain is characterized as EF-hand 3.
+At position 1 to 142, the domain is characterized as MGS-like.
+At position 4 to 47, the domain is characterized as SpoVT-AbrB 1.
+At position 31 to 212, the domain is characterized as SIS.
+At position 235 to 447, the domain is characterized as Histidine kinase.
+At position 16 to 45, the domain is characterized as IQ.
+At position 483 to 518, the domain is characterized as EF-hand 1.
+At position 566 to 601, the domain is characterized as EF-hand 2.
+At position 606 to 641, the domain is characterized as EF-hand 3.
+At position 1 to 63, the domain is characterized as Disintegrin.
+At position 250 to 406, the domain is characterized as TrmE-type G.
+At position 38 to 304, the domain is characterized as Septin-type G.
+At position 2 to 71, the domain is characterized as Glutamine amidotransferase type-2; first part.
+At position 198 to 253, the domain is characterized as HTH cro/C1-type.
+At position 278 to 413, the domain is characterized as DOD-type homing endonuclease.
+At position 571 to 723, the domain is characterized as Glutamine amidotransferase type-2; second part.
+At position 786 to 923, the domain is characterized as SIS 1.
+At position 948 to 1089, the domain is characterized as SIS 2.
+At position 308 to 566, the domain is characterized as ABC transporter 1.
+At position 586 to 913, the domain is characterized as ABC transporter 2.
+At position 15 to 98, the domain is characterized as GIY-YIG.
+At position 45 to 248, the domain is characterized as MARVEL.
+At position 381 to 489, the domain is characterized as OCEL.
+At position 15 to 238, the domain is characterized as Radical SAM core.
+At position 4 to 264, the domain is characterized as Pyruvate carboxyltransferase.
+At position 158 to 229, the domain is characterized as KRAB.
+At position 3 to 66, the domain is characterized as SAM.
+At position 453 to 775, the domain is characterized as Kinesin motor.
+At position 18 to 118, the domain is characterized as Ig-like.
+At position 3 to 59, the domain is characterized as WHEP-TRS.
+At position 95 to 290, the domain is characterized as Peptidase M12A.
+At position 353 to 427, the domain is characterized as ACT-like.
+At position 349 to 539, the domain is characterized as Rho-GAP.
+At position 5 to 236, the domain is characterized as ABC transporter.
+At position 178 to 240, the domain is characterized as t-SNARE coiled-coil homology.
+At position 18 to 231, the domain is characterized as RNase H type-2.
+At position 59 to 317, the domain is characterized as Protein kinase.
+At position 360 to 395, the domain is characterized as EF-hand 1.
+At position 396 to 431, the domain is characterized as EF-hand 2.
+At position 432 to 467, the domain is characterized as EF-hand 3.
+At position 468 to 504, the domain is characterized as EF-hand 4.
+At position 281 to 801, the domain is characterized as Protein kinase.
+At position 71 to 241, the domain is characterized as Helicase ATP-binding.
+At position 252 to 413, the domain is characterized as Helicase C-terminal.
+At position 37 to 113, the domain is characterized as Ubiquitin-like.
+At position 132 to 210, the domain is characterized as BAG.
+At position 25 to 59, the domain is characterized as SAP.
+At position 451 to 529, the domain is characterized as RRM.
+At position 79 to 291, the domain is characterized as ABC transmembrane type-1.
+At position 184 to 310, the domain is characterized as C2 1.
+At position 321 to 455, the domain is characterized as C2 2.
+At position 350 to 415, the domain is characterized as S4 RNA-binding.
+At position 15 to 62, the domain is characterized as F-box.
+At position 193 to 385, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 16 to 205, the domain is characterized as AMMECR1.
+At position 411 to 581, the domain is characterized as tr-type G.
+At position 17 to 197, the domain is characterized as Guanylate kinase-like.
+At position 46 to 300, the domain is characterized as Protein kinase.
+At position 724 to 773, the domain is characterized as KA1.
+At position 173 to 259, the domain is characterized as Toprim.
+At position 196 to 381, the domain is characterized as Glutamine amidotransferase type-1.
+At position 30 to 290, the domain is characterized as Alpha-carbonic anhydrase.
+At position 228 to 334, the domain is characterized as HD.
+At position 257 to 394, the domain is characterized as MPN.
+At position 510 to 571, the domain is characterized as SH3 1.
+At position 747 to 815, the domain is characterized as SH3 2.
+At position 140 to 250, the domain is characterized as C-type lectin.
+At position 46 to 162, the domain is characterized as RGS.
+At position 11 to 139, the domain is characterized as HTH marR-type.
+At position 63 to 223, the domain is characterized as CP-type G.
+At position 28 to 75, the domain is characterized as F-box.
+At position 307 to 404, the domain is characterized as Cyclin N-terminal.
+At position 144 to 352, the domain is characterized as ATP-grasp.
+At position 35 to 277, the domain is characterized as Peptidase S1.
+At position 1 to 126, the domain is characterized as C2.
+At position 327 to 366, the domain is characterized as PLD phosphodiesterase 1.
+At position 656 to 683, the domain is characterized as PLD phosphodiesterase 2.
+At position 79 to 565, the domain is characterized as Protein kinase.
+At position 214 to 359, the domain is characterized as TrmE-type G.
+At position 1018 to 1291, the domain is characterized as Autotransporter.
+At position 314 to 396, the domain is characterized as POTRA.
+At position 58 to 122, the domain is characterized as KH 1.
+At position 161 to 226, the domain is characterized as KH 2.
+At position 256 to 321, the domain is characterized as KH 3.
+At position 8 to 83, the domain is characterized as KRAB.
+At position 3 to 171, the domain is characterized as PfpI endopeptidase.
+At position 51 to 359, the domain is characterized as AB hydrolase-1.
+At position 58 to 176, the domain is characterized as sHSP.
+At position 284 to 614, the domain is characterized as NR LBD.
+At position 407 to 520, the domain is characterized as PAZ.
+At position 696 to 1016, the domain is characterized as Piwi.
+At position 658 to 814, the domain is characterized as MOSC.
+At position 316 to 408, the domain is characterized as SH2.
+At position 1 to 248, the domain is characterized as Deacetylase sirtuin-type.
+At position 43 to 194, the domain is characterized as DAGKc.
+At position 5 to 202, the domain is characterized as RNase H type-2.
+At position 61 to 378, the domain is characterized as Peptidase A1.
+At position 227 to 346, the domain is characterized as PAZ.
+At position 515 to 816, the domain is characterized as Piwi.
+At position 368 to 418, the domain is characterized as FBD.
+At position 224 to 494, the domain is characterized as Protein kinase.
+At position 32 to 201, the domain is characterized as Tyrosine-protein phosphatase.
+At position 564 to 827, the domain is characterized as DDHD.
+At position 26 to 173, the domain is characterized as PX.
+At position 203 to 406, the domain is characterized as BAR.
+At position 12 to 276, the domain is characterized as CN hydrolase.
+At position 78 to 182, the domain is characterized as Fe2OG dioxygenase.
+At position 7 to 88, the domain is characterized as Cytochrome b5 heme-binding.
+At position 29 to 70, the domain is characterized as Chitin-binding type-1 1.
+At position 71 to 113, the domain is characterized as Chitin-binding type-1 2.
+At position 114 to 156, the domain is characterized as Chitin-binding type-1 3.
+At position 157 to 199, the domain is characterized as Chitin-binding type-1 4.
+At position 189 to 374, the domain is characterized as Glutamine amidotransferase type-1.
+At position 14 to 255, the domain is characterized as ABC transporter.
+At position 6 to 135, the domain is characterized as RNase III.
+At position 161 to 230, the domain is characterized as DRBM.
+At position 223 to 377, the domain is characterized as TrmE-type G.
+At position 11 to 271, the domain is characterized as Protein kinase.
+At position 356 to 424, the domain is characterized as PASTA 1.
+At position 425 to 492, the domain is characterized as PASTA 2.
+At position 493 to 559, the domain is characterized as PASTA 3.
+At position 117 to 192, the domain is characterized as MIT.
+At position 538 to 601, the domain is characterized as SAM.
+At position 231 to 390, the domain is characterized as W2.
+At position 29 to 270, the domain is characterized as ABC transporter.
+At position 57 to 231, the domain is characterized as Helicase ATP-binding.
+At position 91 to 402, the domain is characterized as IF rod.
+At position 14 to 96, the domain is characterized as GIY-YIG.
+At position 470 to 592, the domain is characterized as HD.
+At position 711 to 790, the domain is characterized as ACT 1.
+At position 818 to 892, the domain is characterized as ACT 2.
+At position 255 to 366, the domain is characterized as SET.
+At position 10 to 69, the domain is characterized as TRAM.
+At position 70 to 144, the domain is characterized as HTH CENPB-type.
+At position 60 to 207, the domain is characterized as Tyrosine-protein phosphatase.
+At position 5 to 203, the domain is characterized as DPCK.
+At position 33 to 308, the domain is characterized as Pyruvate carboxyltransferase.
+At position 262 to 379, the domain is characterized as CobW C-terminal.
+At position 506 to 568, the domain is characterized as MucBP 1.
+At position 576 to 638, the domain is characterized as MucBP 2.
+At position 646 to 708, the domain is characterized as MucBP 3.
+At position 717 to 779, the domain is characterized as MucBP 4.
+At position 787 to 849, the domain is characterized as MucBP 5.
+At position 257 to 471, the domain is characterized as GT92.
+At position 44 to 350, the domain is characterized as AB hydrolase-1.
+At position 49 to 129, the domain is characterized as IGFBP N-terminal.
+At position 120 to 170, the domain is characterized as Kazal-like.
+At position 172 to 269, the domain is characterized as Ig-like C2-type.
+At position 277 to 391, the domain is characterized as DEUBAD.
+At position 49 to 95, the domain is characterized as F-box.
+At position 272 to 322, the domain is characterized as DHHC.
+At position 188 to 465, the domain is characterized as Protein kinase.
+At position 538 to 668, the domain is characterized as Guanylate cyclase.
+At position 146 to 459, the domain is characterized as NB-ARC.
+At position 7 to 188, the domain is characterized as tr-type G.
+At position 1 to 226, the domain is characterized as BAR.
+At position 266 to 361, the domain is characterized as PH.
+At position 399 to 520, the domain is characterized as Arf-GAP.
+At position 430 to 582, the domain is characterized as RNase NYN.
+At position 2 to 80, the domain is characterized as MIT.
+At position 235 to 337, the domain is characterized as PpiC 1.
+At position 349 to 447, the domain is characterized as PpiC 2.
+At position 9 to 175, the domain is characterized as PPIase cyclophilin-type.
+At position 336 to 398, the domain is characterized as S4 RNA-binding.
+At position 27 to 65, the domain is characterized as CHCH.
+At position 291 to 388, the domain is characterized as Rieske.
+At position 22 to 379, the domain is characterized as DZF.
+At position 332 to 396, the domain is characterized as SAM.
+At position 19 to 136, the domain is characterized as Ig-like V-type.
+At position 236 to 330, the domain is characterized as Ig-like C2-type 2.
+At position 30 to 303, the domain is characterized as Dynamin-type G.
+At position 540 to 626, the domain is characterized as GED.
+At position 233 to 416, the domain is characterized as Helicase ATP-binding.
+At position 459 to 608, the domain is characterized as Helicase C-terminal.
+At position 218 to 245, the domain is characterized as PLD phosphodiesterase 1.
+At position 392 to 419, the domain is characterized as PLD phosphodiesterase 2.
+At position 323 to 395, the domain is characterized as MBD.
+At position 524 to 588, the domain is characterized as DDT.
+At position 1290 to 1360, the domain is characterized as Bromo.
+At position 2 to 32, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 48 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 80 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 112 to 144, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 177 to 403, the domain is characterized as NR LBD.
+At position 221 to 281, the domain is characterized as SH3.
+At position 577 to 656, the domain is characterized as BRCT.
+At position 81 to 217, the domain is characterized as Clp R.
+At position 130 to 373, the domain is characterized as Radical SAM core.
+At position 219 to 254, the domain is characterized as UVR.
+At position 52 to 182, the domain is characterized as RUN.
+At position 99 to 294, the domain is characterized as ATP-grasp.
+At position 29 to 358, the domain is characterized as SET.
+At position 1 to 169, the domain is characterized as KaiA N-terminal.
+At position 179 to 287, the domain is characterized as KaiA C-terminal.
+At position 38 to 210, the domain is characterized as EngB-type G.
+At position 146 to 196, the domain is characterized as DHHC.
+At position 1 to 45, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 58 to 196, the domain is characterized as FAD-binding FR-type.
+At position 41 to 145, the domain is characterized as Expansin-like EG45.
+At position 155 to 234, the domain is characterized as Expansin-like CBD.
+At position 500 to 622, the domain is characterized as Ricin B-type lectin.
+At position 48 to 275, the domain is characterized as Radical SAM core.
+At position 1 to 264, the domain is characterized as F-BAR.
+At position 393 to 470, the domain is characterized as REM-1.
+At position 540 to 601, the domain is characterized as SH3.
+At position 480 to 659, the domain is characterized as DOC.
+At position 111 to 366, the domain is characterized as KIND.
+At position 436 to 454, the domain is characterized as WH2 1.
+At position 500 to 517, the domain is characterized as WH2 2.
+At position 9 to 198, the domain is characterized as Lon N-terminal.
+At position 587 to 766, the domain is characterized as Lon proteolytic.
+At position 178 to 418, the domain is characterized as CP-type G.
+At position 69 to 98, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 115 to 144, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 29 to 112, the domain is characterized as Collagen-like.
+At position 115 to 253, the domain is characterized as C1q.
+At position 12 to 72, the domain is characterized as v-SNARE coiled-coil homology.
+At position 39 to 198, the domain is characterized as SIS.
+At position 1 to 70, the domain is characterized as S1-like.
+At position 54 to 341, the domain is characterized as tr-type G.
+At position 530 to 642, the domain is characterized as SMC hinge.
+At position 8 to 85, the domain is characterized as ACT.
+At position 6 to 145, the domain is characterized as Nudix hydrolase.
+At position 17 to 67, the domain is characterized as KH 1.
+At position 101 to 154, the domain is characterized as KH 2.
+At position 241 to 293, the domain is characterized as KH 3.
+At position 355 to 453, the domain is characterized as Rhodanese.
+At position 4 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 810 to 876, the domain is characterized as SAM 1.
+At position 884 to 949, the domain is characterized as SAM 2.
+At position 1056 to 1213, the domain is characterized as PID.
+At position 183 to 331, the domain is characterized as KARI C-terminal knotted.
+At position 32 to 105, the domain is characterized as H15.
+At position 1 to 67, the domain is characterized as S4 RNA-binding.
+At position 396 to 529, the domain is characterized as DOD-type homing endonuclease.
+At position 116 to 348, the domain is characterized as ATP-grasp.
+At position 6 to 70, the domain is characterized as HMA.
+At position 35 to 188, the domain is characterized as Helicase ATP-binding.
+At position 438 to 604, the domain is characterized as Helicase C-terminal.
+At position 659 to 694, the domain is characterized as UVR.
+At position 88 to 270, the domain is characterized as tr-type G.
+At position 1 to 189, the domain is characterized as Peptidase S8.
+At position 140 to 262, the domain is characterized as MPN.
+At position 213 to 396, the domain is characterized as Velvet.
+At position 663 to 804, the domain is characterized as MHD1.
+At position 941 to 1051, the domain is characterized as MHD2.
+At position 38 to 218, the domain is characterized as Helicase ATP-binding.
+At position 230 to 424, the domain is characterized as Helicase C-terminal.
+At position 80 to 375, the domain is characterized as USP.
+At position 29 to 220, the domain is characterized as RNase H type-2.
+At position 26 to 130, the domain is characterized as Ig-like.
+At position 266 to 329, the domain is characterized as Tudor 1.
+At position 356 to 412, the domain is characterized as Tudor 2.
+At position 595 to 666, the domain is characterized as MBD.
+At position 728 to 801, the domain is characterized as Pre-SET.
+At position 804 to 1179, the domain is characterized as SET.
+At position 1188 to 1204, the domain is characterized as Post-SET.
+At position 654 to 908, the domain is characterized as Protein kinase.
+At position 7 to 252, the domain is characterized as ABC transporter.
+At position 13 to 81, the domain is characterized as HTH merR-type.
+At position 26 to 89, the domain is characterized as bZIP.
+At position 255 to 442, the domain is characterized as GATase cobBQ-type.
+At position 44 to 84, the domain is characterized as ShKT.
+At position 154 to 302, the domain is characterized as TRUD.
+At position 40 to 157, the domain is characterized as RabBD.
+At position 382 to 504, the domain is characterized as C2 1.
+At position 540 to 673, the domain is characterized as C2 2.
+At position 20 to 135, the domain is characterized as LRAT.
+At position 38 to 103, the domain is characterized as BTB.
+At position 205 to 503, the domain is characterized as NPH3.
+At position 387 to 454, the domain is characterized as TRAM.
+At position 222 to 430, the domain is characterized as Ku.
+At position 7 to 232, the domain is characterized as Radical SAM core.
+At position 490 to 644, the domain is characterized as Helicase C-terminal.
+At position 46 to 402, the domain is characterized as IF rod.
+At position 462 to 579, the domain is characterized as LTD.
+At position 74 to 87, the domain is characterized as CRIB.
+At position 249 to 499, the domain is characterized as Protein kinase.
+At position 88 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 4 to 114, the domain is characterized as PH.
+At position 147 to 252, the domain is characterized as IRS-type PTB.
+At position 97 to 173, the domain is characterized as WWE.
+At position 160 to 250, the domain is characterized as 5'-3' exonuclease.
+At position 129 to 187, the domain is characterized as bHLH.
+At position 68 to 184, the domain is characterized as sHSP.
+At position 176 to 264, the domain is characterized as Ras-associating.
+At position 272 to 319, the domain is characterized as SARAH.
+At position 109 to 265, the domain is characterized as Exonuclease.
+At position 77 to 143, the domain is characterized as SAM.
+At position 7 to 269, the domain is characterized as CN hydrolase.
+At position 456 to 730, the domain is characterized as ZP.
+At position 6 to 66, the domain is characterized as HTH tetR-type.
+At position 257 to 364, the domain is characterized as RRM 1.
+At position 381 to 452, the domain is characterized as RRM 2.
+At position 10 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 299 to 338, the domain is characterized as LIM interaction domain (LID).
+At position 162 to 419, the domain is characterized as Protein kinase.
+At position 132 to 185, the domain is characterized as HTH cro/C1-type.
+At position 245 to 320, the domain is characterized as PUA.
+At position 24 to 143, the domain is characterized as NTR.
+At position 5 to 618, the domain is characterized as PFL.
+At position 625 to 748, the domain is characterized as Glycine radical.
+At position 64 to 235, the domain is characterized as Helicase ATP-binding.
+At position 246 to 407, the domain is characterized as Helicase C-terminal.
+At position 53 to 223, the domain is characterized as Helicase ATP-binding.
+At position 234 to 395, the domain is characterized as Helicase C-terminal.
+At position 743 to 818, the domain is characterized as Smr.
+At position 81 to 321, the domain is characterized as uDENN.
+At position 361 to 506, the domain is characterized as cDENN.
+At position 508 to 613, the domain is characterized as dDENN.
+At position 118 to 357, the domain is characterized as Radical SAM core.
+At position 198 to 354, the domain is characterized as JmjC.
+At position 660 to 835, the domain is characterized as Integrase catalytic.
+At position 117 to 154, the domain is characterized as VM.
+At position 12 to 93, the domain is characterized as PDZ 1.
+At position 121 to 206, the domain is characterized as PDZ 2.
+At position 261 to 341, the domain is characterized as PDZ 3.
+At position 49 to 233, the domain is characterized as Helicase ATP-binding.
+At position 246 to 476, the domain is characterized as Helicase C-terminal.
+At position 1 to 146, the domain is characterized as C2.
+At position 578 to 640, the domain is characterized as FIP-RBD.
+At position 33 to 138, the domain is characterized as Glutaredoxin.
+At position 96 to 186, the domain is characterized as RRM.
+At position 86 to 121, the domain is characterized as EGF-like 1; calcium-binding.
+At position 129 to 164, the domain is characterized as EGF-like 2.
+At position 210 to 453, the domain is characterized as Peptidase S1.
+At position 113 to 470, the domain is characterized as PPM-type phosphatase.
+At position 135 to 197, the domain is characterized as CBS 1.
+At position 198 to 254, the domain is characterized as CBS 2.
+At position 1467 to 1691, the domain is characterized as Collagen IV NC1.
+At position 1 to 170, the domain is characterized as SPX.
+At position 228 to 443, the domain is characterized as VWFA.
+At position 453 to 532, the domain is characterized as Cache 1.
+At position 772 to 853, the domain is characterized as Cache 2.
+At position 38 to 98, the domain is characterized as HTH myb-type.
+At position 95 to 174, the domain is characterized as PRC barrel.
+At position 100 to 274, the domain is characterized as Helicase ATP-binding.
+At position 300 to 449, the domain is characterized as Helicase C-terminal.
+At position 232 to 470, the domain is characterized as NR LBD.
+At position 6 to 142, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 36 to 221, the domain is characterized as RNase H type-2.
+At position 79 to 301, the domain is characterized as Lon N-terminal.
+At position 756 to 940, the domain is characterized as Lon proteolytic.
+At position 272 to 486, the domain is characterized as Helicase ATP-binding.
+At position 711 to 876, the domain is characterized as Helicase C-terminal.
+At position 5 to 158, the domain is characterized as Tyrosine-protein phosphatase.
+At position 8 to 80, the domain is characterized as KRAB.
+At position 355 to 533, the domain is characterized as PCI.
+At position 48 to 151, the domain is characterized as Cyclin N-terminal.
+At position 153 to 369, the domain is characterized as Histidine kinase.
+At position 1 to 582, the domain is characterized as Protein kinase.
+At position 38 to 115, the domain is characterized as Ricin B-type lectin.
+At position 173 to 221, the domain is characterized as Fibronectin type-II.
+At position 229 to 353, the domain is characterized as C-type lectin 1.
+At position 357 to 500, the domain is characterized as C-type lectin 2.
+At position 504 to 641, the domain is characterized as C-type lectin 3.
+At position 646 to 795, the domain is characterized as C-type lectin 4.
+At position 799 to 937, the domain is characterized as C-type lectin 5.
+At position 941 to 1095, the domain is characterized as C-type lectin 6.
+At position 1099 to 1230, the domain is characterized as C-type lectin 7.
+At position 1235 to 1376, the domain is characterized as C-type lectin 8.
+At position 30 to 193, the domain is characterized as EngA-type G 1.
+At position 377 to 459, the domain is characterized as KH-like.
+At position 1 to 189, the domain is characterized as RNase H type-2.
+At position 25 to 293, the domain is characterized as Protein kinase.
+At position 46 to 285, the domain is characterized as Laminin N-terminal.
+At position 286 to 349, the domain is characterized as Laminin EGF-like 1.
+At position 350 to 412, the domain is characterized as Laminin EGF-like 2.
+At position 413 to 472, the domain is characterized as Laminin EGF-like 3.
+At position 473 to 524, the domain is characterized as Laminin EGF-like 4.
+At position 525 to 555, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 564 to 778, the domain is characterized as Laminin IV type B.
+At position 784 to 831, the domain is characterized as Laminin EGF-like 6.
+At position 832 to 877, the domain is characterized as Laminin EGF-like 7.
+At position 878 to 927, the domain is characterized as Laminin EGF-like 8.
+At position 928 to 986, the domain is characterized as Laminin EGF-like 9.
+At position 987 to 1038, the domain is characterized as Laminin EGF-like 10.
+At position 1039 to 1095, the domain is characterized as Laminin EGF-like 11.
+At position 1096 to 1143, the domain is characterized as Laminin EGF-like 12.
+At position 1144 to 1190, the domain is characterized as Laminin EGF-like 13.
+At position 138 to 493, the domain is characterized as Protein kinase.
+At position 1044 to 1297, the domain is characterized as Glutamine amidotransferase type-1.
+At position 31 to 414, the domain is characterized as Helicase ATP-binding.
+At position 436 to 589, the domain is characterized as Helicase C-terminal.
+At position 639 to 674, the domain is characterized as UVR.
+At position 30 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 23 to 86, the domain is characterized as bZIP.
+At position 165 to 255, the domain is characterized as PpiC.
+At position 456 to 594, the domain is characterized as SIS 2.
+At position 5 to 156, the domain is characterized as Thioredoxin.
+At position 4 to 58, the domain is characterized as bHLH.
+At position 226 to 298, the domain is characterized as Bromo 1.
+At position 403 to 475, the domain is characterized as Bromo 2.
+At position 593 to 672, the domain is characterized as NET.
+At position 54 to 97, the domain is characterized as SMB 1.
+At position 98 to 142, the domain is characterized as SMB 2.
+At position 20 to 80, the domain is characterized as HTH myb-type.
+At position 85 to 243, the domain is characterized as TNase-like.
+At position 260 to 295, the domain is characterized as CBM1.
+At position 36 to 81, the domain is characterized as EF-hand 1.
+At position 82 to 117, the domain is characterized as EF-hand 2.
+At position 119 to 154, the domain is characterized as EF-hand 3.
+At position 163 to 198, the domain is characterized as EF-hand 4.
+At position 23 to 370, the domain is characterized as DZF.
+At position 1 to 43, the domain is characterized as F-box.
+At position 322 to 504, the domain is characterized as Helicase ATP-binding.
+At position 659 to 812, the domain is characterized as Helicase C-terminal.
+At position 232 to 464, the domain is characterized as GT92.
+At position 18 to 115, the domain is characterized as Fibronectin type-III 1.
+At position 141 to 221, the domain is characterized as Fibronectin type-III 2.
+At position 574 to 674, the domain is characterized as tRNA-binding.
+At position 377 to 533, the domain is characterized as Fido.
+At position 3 to 131, the domain is characterized as C2 1.
+At position 137 to 264, the domain is characterized as C2 2.
+At position 305 to 507, the domain is characterized as VWFA.
+At position 1 to 84, the domain is characterized as Rieske.
+At position 146 to 315, the domain is characterized as tr-type G.
+At position 66 to 282, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 56, the domain is characterized as HTH gntR-type.
+At position 7 to 228, the domain is characterized as BAR.
+At position 231 to 340, the domain is characterized as PH.
+At position 342 to 538, the domain is characterized as Rho-GAP.
+At position 783 to 841, the domain is characterized as SH3.
+At position 321 to 587, the domain is characterized as Ku.
+At position 697 to 733, the domain is characterized as SAP.
+At position 175 to 245, the domain is characterized as PQ-loop.
+At position 128 to 183, the domain is characterized as HTH cro/C1-type.
+At position 255 to 407, the domain is characterized as GAF 1.
+At position 439 to 624, the domain is characterized as GAF 2.
+At position 654 to 977, the domain is characterized as PDEase.
+At position 431 to 538, the domain is characterized as Rhodanese.
+At position 18 to 183, the domain is characterized as EngB-type G.
+At position 38 to 274, the domain is characterized as ThyX 1.
+At position 309 to 511, the domain is characterized as ThyX 2.
+At position 323 to 510, the domain is characterized as B30.2/SPRY.
+At position 606 to 695, the domain is characterized as BRCT.
+At position 138 to 272, the domain is characterized as Fatty acid hydroxylase.
+At position 506 to 622, the domain is characterized as Ricin B-type lectin.
+At position 201 to 261, the domain is characterized as KH.
+At position 72 to 122, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 73 to 229, the domain is characterized as Nudix hydrolase.
+At position 127 to 219, the domain is characterized as PpiC.
+At position 20 to 436, the domain is characterized as Sema.
+At position 438 to 480, the domain is characterized as PSI 1.
+At position 571 to 608, the domain is characterized as PSI 2.
+At position 698 to 739, the domain is characterized as PSI 3.
+At position 741 to 829, the domain is characterized as IPT/TIG 1.
+At position 831 to 916, the domain is characterized as IPT/TIG 2.
+At position 919 to 1006, the domain is characterized as IPT/TIG 3.
+At position 20 to 137, the domain is characterized as Rhodanese.
+At position 173 to 314, the domain is characterized as Tyrosine-protein phosphatase.
+At position 103 to 180, the domain is characterized as RRM.
+At position 5 to 145, the domain is characterized as VOC 1.
+At position 152 to 273, the domain is characterized as VOC 2.
+At position 442 to 524, the domain is characterized as RRM.
+At position 297 to 549, the domain is characterized as Glutamine amidotransferase type-1.
+At position 84 to 250, the domain is characterized as PfpI endopeptidase 1.
+At position 287 to 453, the domain is characterized as PfpI endopeptidase 2.
+At position 4 to 68, the domain is characterized as SAM.
+At position 287 to 379, the domain is characterized as PH 1.
+At position 394 to 483, the domain is characterized as PH 2.
+At position 480 to 611, the domain is characterized as Arf-GAP.
+At position 907 to 1088, the domain is characterized as Rho-GAP.
+At position 1117 to 1210, the domain is characterized as Ras-associating.
+At position 1223 to 1325, the domain is characterized as PH 3.
+At position 402 to 488, the domain is characterized as Disintegrin.
+At position 171 to 328, the domain is characterized as CRAL-TRIO.
+At position 475 to 761, the domain is characterized as NB-ARC.
+At position 1181 to 1248, the domain is characterized as HMA.
+At position 228 to 272, the domain is characterized as PCI.
+At position 1324 to 1399, the domain is characterized as DEP.
+At position 222 to 344, the domain is characterized as SET.
+At position 295 to 468, the domain is characterized as CRAL-TRIO.
+At position 471 to 572, the domain is characterized as GOLD.
+At position 239 to 422, the domain is characterized as GATase cobBQ-type.
+At position 209 to 309, the domain is characterized as Fe2OG dioxygenase.
+At position 257 to 447, the domain is characterized as GATase cobBQ-type.
+At position 119 to 398, the domain is characterized as Protein kinase.
+At position 115 to 152, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 10 to 63, the domain is characterized as L27 1.
+At position 65 to 122, the domain is characterized as L27 2.
+At position 139 to 220, the domain is characterized as PDZ.
+At position 228 to 298, the domain is characterized as SH3.
+At position 368 to 560, the domain is characterized as Guanylate kinase-like.
+At position 107 to 129, the domain is characterized as OCA.
+At position 135 to 198, the domain is characterized as Chitin-binding type R&R.
+At position 20 to 198, the domain is characterized as Guanylate kinase-like.
+At position 285 to 563, the domain is characterized as ABC transmembrane type-1 1.
+At position 598 to 824, the domain is characterized as ABC transporter 1.
+At position 885 to 1210, the domain is characterized as ABC transmembrane type-1 2.
+At position 1246 to 1479, the domain is characterized as ABC transporter 2.
+At position 91 to 155, the domain is characterized as S4 RNA-binding.
+At position 24 to 126, the domain is characterized as CFEM.
+At position 6 to 39, the domain is characterized as WW 1.
+At position 653 to 776, the domain is characterized as C2.
+At position 64 to 282, the domain is characterized as Ch-type lysozyme.
+At position 180 to 281, the domain is characterized as Fe2OG dioxygenase.
+At position 803 to 894, the domain is characterized as PKD.
+At position 17 to 211, the domain is characterized as Lon N-terminal.
+At position 600 to 780, the domain is characterized as Lon proteolytic.
+At position 140 to 229, the domain is characterized as CS.
+At position 247 to 336, the domain is characterized as SGS.
+At position 580 to 662, the domain is characterized as BRCT.
+At position 415 to 498, the domain is characterized as Death.
+At position 21 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 105 to 195, the domain is characterized as Ig-like C2-type 2.
+At position 247 to 361, the domain is characterized as Ig-like C2-type 3.
+At position 364 to 459, the domain is characterized as Ig-like C2-type 4.
+At position 464 to 554, the domain is characterized as Ig-like C2-type 5.
+At position 688 to 1024, the domain is characterized as Protein kinase; inactive.
+At position 1 to 130, the domain is characterized as Protein kinase.
+At position 1 to 49, the domain is characterized as ClpX-type ZB.
+At position 2 to 227, the domain is characterized as Glutamine amidotransferase type-2.
+At position 56 to 95, the domain is characterized as Agouti.
+At position 217 to 455, the domain is characterized as NR LBD.
+At position 157 to 340, the domain is characterized as Integrase catalytic.
+At position 34 to 150, the domain is characterized as Plastocyanin-like 1.
+At position 160 to 312, the domain is characterized as Plastocyanin-like 2.
+At position 428 to 564, the domain is characterized as Plastocyanin-like 3.
+At position 304 to 379, the domain is characterized as RRM 1.
+At position 430 to 507, the domain is characterized as RRM 2.
+At position 856 to 932, the domain is characterized as RRM 3.
+At position 91 to 208, the domain is characterized as C-type lectin.
+At position 1 to 202, the domain is characterized as ThyX.
+At position 574 to 676, the domain is characterized as tRNA-binding.
+At position 519 to 682, the domain is characterized as Integrase catalytic.
+At position 982 to 1225, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 262 to 504, the domain is characterized as ABC transporter 2.
+At position 101 to 274, the domain is characterized as CRAL-TRIO.
+At position 60 to 171, the domain is characterized as SH2.
+At position 168 to 227, the domain is characterized as SH3 2.
+At position 79 to 393, the domain is characterized as GH18.
+At position 103 to 299, the domain is characterized as ATP-grasp.
+At position 9 to 265, the domain is characterized as DOG1.
+At position 16 to 143, the domain is characterized as C-type lysozyme.
+At position 159 to 404, the domain is characterized as Histidine kinase.
+At position 44 to 181, the domain is characterized as MPN.
+At position 11 to 213, the domain is characterized as YjeF N-terminal.
+At position 223 to 506, the domain is characterized as YjeF C-terminal.
+At position 24 to 95, the domain is characterized as KRAB.
+At position 131 to 170, the domain is characterized as STI1 1.
+At position 507 to 546, the domain is characterized as STI1 2.
+At position 236 to 283, the domain is characterized as F-box.
+At position 2 to 157, the domain is characterized as N-acetyltransferase.
+At position 86 to 363, the domain is characterized as Protein kinase.
+At position 1533 to 1760, the domain is characterized as Rap-GAP.
+At position 507 to 623, the domain is characterized as Fibronectin type-III 1.
+At position 624 to 729, the domain is characterized as Fibronectin type-III 2.
+At position 860 to 961, the domain is characterized as Fibronectin type-III 3.
+At position 1025 to 1302, the domain is characterized as Protein kinase.
+At position 54 to 410, the domain is characterized as IF rod.
+At position 461 to 588, the domain is characterized as LTD.
+At position 193 to 255, the domain is characterized as t-SNARE coiled-coil homology.
+At position 26 to 236, the domain is characterized as FAD-binding PCMH-type.
+At position 132 to 576, the domain is characterized as Urease.
+At position 666 to 857, the domain is characterized as ATP-grasp 2.
+At position 945 to 1099, the domain is characterized as MGS-like.
+At position 1 to 236, the domain is characterized as ABC transporter.
+At position 152 to 382, the domain is characterized as Radical SAM core.
+At position 12 to 114, the domain is characterized as Longin.
+At position 134 to 293, the domain is characterized as F5/8 type C.
+At position 155 to 240, the domain is characterized as APO 1.
+At position 329 to 414, the domain is characterized as APO 2.
+At position 11 to 160, the domain is characterized as MPN.
+At position 169 to 261, the domain is characterized as PPIase FKBP-type.
+At position 136 to 171, the domain is characterized as EF-hand 3.
+At position 171 to 206, the domain is characterized as QLQ.
+At position 460 to 532, the domain is characterized as HSA.
+At position 766 to 931, the domain is characterized as Helicase ATP-binding.
+At position 1084 to 1246, the domain is characterized as Helicase C-terminal.
+At position 1443 to 1513, the domain is characterized as Bromo.
+At position 58 to 169, the domain is characterized as Expansin-like EG45.
+At position 182 to 263, the domain is characterized as Expansin-like CBD.
+At position 408 to 788, the domain is characterized as USP.
+At position 147 to 302, the domain is characterized as C1q.
+At position 155 to 206, the domain is characterized as HTH bat-type.
+At position 7 to 191, the domain is characterized as tr-type G.
+At position 33 to 115, the domain is characterized as Lipoyl-binding.
+At position 418 to 585, the domain is characterized as tr-type G.
+At position 58 to 118, the domain is characterized as SH3.
+At position 124 to 220, the domain is characterized as SH2.
+At position 241 to 494, the domain is characterized as Protein kinase.
+At position 144 to 378, the domain is characterized as Radical SAM core.
+At position 2 to 86, the domain is characterized as Core-binding (CB).
+At position 107 to 291, the domain is characterized as Tyr recombinase.
+At position 1005 to 1192, the domain is characterized as Reticulon.
+At position 93 to 323, the domain is characterized as ATP-grasp.
+At position 1 to 124, the domain is characterized as Arf-GAP.
+At position 4 to 49, the domain is characterized as F-box.
+At position 257 to 316, the domain is characterized as LIM zinc-binding.
+At position 26 to 134, the domain is characterized as Ig-like V-type.
+At position 97 to 160, the domain is characterized as Sushi 2.
+At position 161 to 222, the domain is characterized as Sushi 3.
+At position 223 to 286, the domain is characterized as Sushi 4.
+At position 4 to 127, the domain is characterized as RNase III.
+At position 297 to 528, the domain is characterized as ABC transporter 2.
+At position 10 to 106, the domain is characterized as SH2 1.
+At position 288 to 403, the domain is characterized as SH2 2.
+At position 662 to 921, the domain is characterized as Protein kinase.
+At position 134 to 163, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 9 to 70, the domain is characterized as SH3.
+At position 82 to 171, the domain is characterized as SH2.
+At position 195 to 445, the domain is characterized as Protein kinase.
+At position 8 to 145, the domain is characterized as TIR.
+At position 181 to 317, the domain is characterized as DBB.
+At position 295 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 135, the domain is characterized as Galectin.
+At position 1 to 108, the domain is characterized as PX.
+At position 114 to 205, the domain is characterized as Ras-associating.
+At position 32 to 183, the domain is characterized as N-acetyltransferase.
+At position 36 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 79 to 251, the domain is characterized as FAD-binding PCMH-type.
+At position 465 to 634, the domain is characterized as tr-type G.
+At position 99 to 379, the domain is characterized as Radical SAM core.
+At position 6 to 331, the domain is characterized as Kinesin motor.
+At position 152 to 257, the domain is characterized as Fe2OG dioxygenase.
+At position 287 to 345, the domain is characterized as KARI C-terminal knotted 2.
+At position 52 to 162, the domain is characterized as sHSP.
+At position 2 to 135, the domain is characterized as RNase III.
+At position 216 to 316, the domain is characterized as HTH araC/xylS-type.
+At position 90 to 222, the domain is characterized as GST C-terminal.
+At position 521 to 808, the domain is characterized as NB-ARC.
+At position 1240 to 1306, the domain is characterized as HMA.
+At position 58 to 196, the domain is characterized as PI-PLC X-box.
+At position 6 to 100, the domain is characterized as Ig-like.
+At position 136 to 419, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 406 to 423, the domain is characterized as WH2.
+At position 191 to 380, the domain is characterized as GMPS ATP-PPase.
+At position 410 to 471, the domain is characterized as J.
+At position 31 to 143, the domain is characterized as EamA 1.
+At position 225 to 345, the domain is characterized as EamA 2.
+At position 32 to 515, the domain is characterized as Sema.
+At position 579 to 668, the domain is characterized as Ig-like C2-type.
+At position 2 to 235, the domain is characterized as ABC transporter.
+At position 121 to 319, the domain is characterized as Peptidase M12A.
+At position 324 to 354, the domain is characterized as EGF-like.
+At position 364 to 483, the domain is characterized as CUB.
+At position 941 to 1019, the domain is characterized as Carrier.
+At position 150 to 255, the domain is characterized as FAD-binding FR-type.
+At position 47 to 266, the domain is characterized as YjeF N-terminal.
+At position 400 to 475, the domain is characterized as B5.
+At position 401 to 477, the domain is characterized as B5.
+At position 9 to 151, the domain is characterized as Toprim.
+At position 23 to 279, the domain is characterized as Protein kinase.
+At position 929 to 1160, the domain is characterized as ABC transporter 1.
+At position 1937 to 2169, the domain is characterized as ABC transporter 2.
+At position 1 to 59, the domain is characterized as Response regulatory.
+At position 46 to 95, the domain is characterized as P-type 1.
+At position 917 to 962, the domain is characterized as P-type 2.
+At position 48 to 113, the domain is characterized as NAC-A/B.
+At position 166 to 205, the domain is characterized as UBA.
+At position 29 to 303, the domain is characterized as Helicase ATP-binding.
+At position 28 to 109, the domain is characterized as Toprim.
+At position 72 to 217, the domain is characterized as HD.
+At position 5 to 228, the domain is characterized as ABC transporter.
+At position 297 to 413, the domain is characterized as C-type lectin.
+At position 1 to 122, the domain is characterized as CMP/dCMP-type deaminase.
+At position 381 to 476, the domain is characterized as SH2.
+At position 471 to 520, the domain is characterized as SOCS box.
+At position 24 to 171, the domain is characterized as CENP-V/GFA.
+At position 1141 to 1219, the domain is characterized as Carrier.
+At position 1262 to 1714, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 146 to 330, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 143, the domain is characterized as Flavodoxin-like.
+At position 124 to 193, the domain is characterized as COMM.
+At position 25 to 101, the domain is characterized as MBD.
+At position 203 to 345, the domain is characterized as AXH.
+At position 214 to 342, the domain is characterized as GGDEF.
+At position 11 to 195, the domain is characterized as Ku.
+At position 20 to 276, the domain is characterized as Protein kinase.
+At position 3 to 102, the domain is characterized as SSB.
+At position 579 to 629, the domain is characterized as LRRCT.
+At position 672 to 815, the domain is characterized as TIR.
+At position 199 to 262, the domain is characterized as KH.
+At position 258 to 455, the domain is characterized as GATase cobBQ-type.
+At position 17 to 320, the domain is characterized as Peptidase A1.
+At position 241 to 284, the domain is characterized as LysM 1.
+At position 321 to 364, the domain is characterized as LysM 2.
+At position 395 to 438, the domain is characterized as LysM 3.
+At position 198 to 310, the domain is characterized as HD.
+At position 30 to 108, the domain is characterized as RRM.
+At position 83 to 300, the domain is characterized as RNase H type-2.
+At position 490 to 645, the domain is characterized as PPIase cyclophilin-type.
+At position 31 to 98, the domain is characterized as BTB.
+At position 76 to 203, the domain is characterized as HD.
+At position 127 to 234, the domain is characterized as Rieske.
+At position 107 to 349, the domain is characterized as NodB homology.
+At position 442 to 609, the domain is characterized as tr-type G.
+At position 82 to 162, the domain is characterized as RRM.
+At position 89 to 151, the domain is characterized as S4 RNA-binding.
+At position 153 to 241, the domain is characterized as PPIase FKBP-type.
+At position 43 to 139, the domain is characterized as KH type-2.
+At position 114 to 418, the domain is characterized as NB-ARC.
+At position 111 to 318, the domain is characterized as ATP-grasp.
+At position 4 to 259, the domain is characterized as Protein kinase.
+At position 4 to 88, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 402 to 609, the domain is characterized as MCM.
+At position 193 to 446, the domain is characterized as Protein kinase.
+At position 54 to 224, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 98, the domain is characterized as Phosphagen kinase N-terminal.
+At position 125 to 367, the domain is characterized as Phosphagen kinase C-terminal.
+At position 207 to 317, the domain is characterized as Fe2OG dioxygenase.
+At position 278 to 359, the domain is characterized as KH.
+At position 404 to 497, the domain is characterized as HD.
+At position 420 to 603, the domain is characterized as MIF4G.
+At position 710 to 826, the domain is characterized as MI.
+At position 384 to 416, the domain is characterized as EGF-like 2.
+At position 540 to 592, the domain is characterized as TB 1.
+At position 610 to 650, the domain is characterized as EGF-like 3; calcium-binding.
+At position 660 to 712, the domain is characterized as TB 2.
+At position 836 to 878, the domain is characterized as EGF-like 4.
+At position 879 to 921, the domain is characterized as EGF-like 5; calcium-binding.
+At position 922 to 961, the domain is characterized as EGF-like 6; calcium-binding.
+At position 962 to 1001, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1002 to 1042, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1043 to 1084, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1085 to 1126, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1127 to 1167, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1168 to 1209, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1210 to 1250, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1251 to 1294, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1295 to 1336, the domain is characterized as EGF-like 15; calcium-binding.
+At position 1337 to 1379, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1403 to 1455, the domain is characterized as TB 3.
+At position 1477 to 1519, the domain is characterized as EGF-like 17; calcium-binding.
+At position 1520 to 1559, the domain is characterized as EGF-like 18; calcium-binding.
+At position 1576 to 1628, the domain is characterized as TB 4.
+At position 1754 to 1794, the domain is characterized as EGF-like 19; calcium-binding.
+At position 1795 to 1839, the domain is characterized as EGF-like 20; calcium-binding.
+At position 109 to 292, the domain is characterized as Tyr recombinase.
+At position 84 to 259, the domain is characterized as FCP1 homology 1.
+At position 381 to 553, the domain is characterized as FCP1 homology 2.
+At position 76 to 185, the domain is characterized as sHSP.
+At position 25 to 127, the domain is characterized as Ig-like V-type 1.
+At position 131 to 229, the domain is characterized as Ig-like V-type 2.
+At position 239 to 323, the domain is characterized as Ig-like C2-type 1.
+At position 340 to 399, the domain is characterized as Ig-like C2-type 2.
+At position 406 to 484, the domain is characterized as Ig-like C2-type 3.
+At position 224 to 378, the domain is characterized as TrmE-type G.
+At position 167 to 322, the domain is characterized as CMP/dCMP-type deaminase.
+At position 47 to 313, the domain is characterized as ABC transporter.
+At position 411 to 665, the domain is characterized as ABC transmembrane type-2.
+At position 95 to 145, the domain is characterized as DHHC.
+At position 196 to 235, the domain is characterized as GRAM 1.
+At position 248 to 347, the domain is characterized as PH.
+At position 586 to 652, the domain is characterized as GRAM 2.
+At position 131 to 167, the domain is characterized as GIY-YIG.
+At position 28 to 659, the domain is characterized as Vitellogenin.
+At position 28 to 91, the domain is characterized as S5 DRBM.
+At position 169 to 271, the domain is characterized as AB hydrolase-1.
+At position 490 to 610, the domain is characterized as Fibronectin type-III 1.
+At position 611 to 709, the domain is characterized as Fibronectin type-III 2.
+At position 735 to 829, the domain is characterized as Fibronectin type-III 3.
+At position 835 to 928, the domain is characterized as Fibronectin type-III 4.
+At position 1000 to 1276, the domain is characterized as Protein kinase.
+At position 1 to 43, the domain is characterized as Fibronectin type-III 1.
+At position 49 to 142, the domain is characterized as Fibronectin type-III 2.
+At position 643 to 814, the domain is characterized as PCI.
+At position 22 to 99, the domain is characterized as UPAR/Ly6.
+At position 793 to 861, the domain is characterized as SAM.
+At position 46 to 295, the domain is characterized as Peptidase S1 1.
+At position 309 to 419, the domain is characterized as CUB 1.
+At position 429 to 541, the domain is characterized as CUB 2.
+At position 580 to 820, the domain is characterized as Peptidase S1 2.
+At position 27 to 109, the domain is characterized as PDZ.
+At position 185 to 229, the domain is characterized as DSL.
+At position 230 to 263, the domain is characterized as EGF-like 1.
+At position 264 to 294, the domain is characterized as EGF-like 2; atypical.
+At position 296 to 334, the domain is characterized as EGF-like 3.
+At position 336 to 372, the domain is characterized as EGF-like 4.
+At position 374 to 410, the domain is characterized as EGF-like 5; calcium-binding.
+At position 412 to 448, the domain is characterized as EGF-like 6; calcium-binding.
+At position 450 to 485, the domain is characterized as EGF-like 7; calcium-binding.
+At position 487 to 523, the domain is characterized as EGF-like 8; calcium-binding.
+At position 525 to 561, the domain is characterized as EGF-like 9.
+At position 586 to 627, the domain is characterized as EGF-like 10.
+At position 629 to 665, the domain is characterized as EGF-like 11; calcium-binding.
+At position 667 to 703, the domain is characterized as EGF-like 12; calcium-binding.
+At position 705 to 741, the domain is characterized as EGF-like 13.
+At position 744 to 780, the domain is characterized as EGF-like 14.
+At position 782 to 818, the domain is characterized as EGF-like 15; calcium-binding.
+At position 820 to 856, the domain is characterized as EGF-like 16; calcium-binding.
+At position 36 to 232, the domain is characterized as Cupin type-1 1.
+At position 345 to 494, the domain is characterized as Cupin type-1 2.
+At position 119 to 403, the domain is characterized as Protein kinase.
+At position 19 to 142, the domain is characterized as Ig-like V-type 1.
+At position 143 to 269, the domain is characterized as Ig-like V-type 2.
+At position 275 to 358, the domain is characterized as Ig-like C2-type 1.
+At position 365 to 462, the domain is characterized as Ig-like C2-type 2.
+At position 84 to 120, the domain is characterized as LDL-receptor class A.
+At position 5 to 274, the domain is characterized as Peptidase S8.
+At position 10 to 75, the domain is characterized as J.
+At position 289 to 341, the domain is characterized as TSP type-1.
+At position 12 to 70, the domain is characterized as Chromo.
+At position 8 to 270, the domain is characterized as Pyruvate carboxyltransferase.
+At position 73 to 290, the domain is characterized as ABC transmembrane type-1.
+At position 8 to 288, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 289 to 559, the domain is characterized as UvrD-like helicase C-terminal.
+At position 46 to 315, the domain is characterized as Protein kinase.
+At position 52 to 192, the domain is characterized as FAS1 1.
+At position 195 to 365, the domain is characterized as FAS1 2.
+At position 142 to 161, the domain is characterized as UIM.
+At position 42 to 246, the domain is characterized as BPL/LPL catalytic.
+At position 483 to 603, the domain is characterized as Fibronectin type-III 1.
+At position 607 to 707, the domain is characterized as Fibronectin type-III 2.
+At position 818 to 913, the domain is characterized as Fibronectin type-III 3.
+At position 979 to 1254, the domain is characterized as Protein kinase.
+At position 188 to 564, the domain is characterized as USP.
+At position 3 to 417, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 2 to 245, the domain is characterized as ABC transporter.
+At position 1 to 401, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 279 to 582, the domain is characterized as UvrD-like helicase C-terminal.
+At position 570 to 935, the domain is characterized as DZF.
+At position 121 to 321, the domain is characterized as AH.
+At position 116 to 196, the domain is characterized as CTCK.
+At position 210 to 454, the domain is characterized as Peptidase S1.
+At position 163 to 281, the domain is characterized as Response regulatory.
+At position 215 to 441, the domain is characterized as CN hydrolase.
+At position 622 to 692, the domain is characterized as S1 motif.
+At position 11 to 299, the domain is characterized as FERM.
+At position 1 to 72, the domain is characterized as Glutaredoxin.
+At position 337 to 401, the domain is characterized as S4 RNA-binding.
+At position 176 to 228, the domain is characterized as HAMP.
+At position 393 to 587, the domain is characterized as Histidine kinase.
+At position 42 to 204, the domain is characterized as PCI.
+At position 10 to 98, the domain is characterized as MtN3/slv 1.
+At position 133 to 216, the domain is characterized as MtN3/slv 2.
+At position 43 to 336, the domain is characterized as Calpain catalytic.
+At position 557 to 592, the domain is characterized as EF-hand 1.
+At position 586 to 621, the domain is characterized as EF-hand 2.
+At position 651 to 684, the domain is characterized as EF-hand 3.
+At position 387 to 448, the domain is characterized as SAM.
+At position 319 to 501, the domain is characterized as PCI.
+At position 2 to 318, the domain is characterized as Glutamine amidotransferase type-2.
+At position 390 to 529, the domain is characterized as SIS 1.
+At position 562 to 707, the domain is characterized as SIS 2.
+At position 81 to 271, the domain is characterized as RNase H type-2.
+At position 31 to 188, the domain is characterized as Helicase ATP-binding.
+At position 114 to 174, the domain is characterized as CBS 1.
+At position 20 to 121, the domain is characterized as Ig-like.
+At position 181 to 463, the domain is characterized as GT92.
+At position 125 to 508, the domain is characterized as GRAS.
+At position 24 to 238, the domain is characterized as tr-type G.
+At position 2 to 189, the domain is characterized as N-acetyltransferase.
+At position 4 to 76, the domain is characterized as KRAB.
+At position 788 to 864, the domain is characterized as Carrier.
+At position 164 to 227, the domain is characterized as bZIP.
+At position 233 to 449, the domain is characterized as DOG1.
+At position 581 to 663, the domain is characterized as BRCT.
+At position 3 to 414, the domain is characterized as PTS EIIC type-1.
+At position 425 to 506, the domain is characterized as PTS EIIB type-1.
+At position 551 to 655, the domain is characterized as PTS EIIA type-1.
+At position 66 to 280, the domain is characterized as Radical SAM core.
+At position 33 to 169, the domain is characterized as VHS.
+At position 196 to 321, the domain is characterized as GAT.
+At position 466 to 581, the domain is characterized as GAE.
+At position 2 to 70, the domain is characterized as DRBM 1.
+At position 169 to 241, the domain is characterized as DRBM 2.
+At position 394 to 560, the domain is characterized as Helicase ATP-binding.
+At position 639 to 813, the domain is characterized as Helicase C-terminal.
+At position 147 to 250, the domain is characterized as Fibronectin type-III.
+At position 772 to 858, the domain is characterized as KHA.
+At position 44 to 93, the domain is characterized as F-box.
+At position 56 to 129, the domain is characterized as RRM 1.
+At position 135 to 220, the domain is characterized as RRM 2.
+At position 25 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 158 to 246, the domain is characterized as Ig-like C2-type 2.
+At position 255 to 357, the domain is characterized as Ig-like C2-type 3.
+At position 478 to 767, the domain is characterized as Protein kinase.
+At position 6 to 237, the domain is characterized as ABC transporter.
+At position 21 to 106, the domain is characterized as Core-binding (CB).
+At position 127 to 318, the domain is characterized as Tyr recombinase.
+At position 3 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 479 to 864, the domain is characterized as USP.
+At position 916 to 1085, the domain is characterized as Exonuclease.
+At position 13 to 218, the domain is characterized as ThyX.
+At position 154 to 232, the domain is characterized as HTH crp-type.
+At position 25 to 256, the domain is characterized as Peptidase S1.
+At position 103 to 340, the domain is characterized as Radical SAM core.
+At position 8 to 160, the domain is characterized as Nudix hydrolase.
+At position 23 to 79, the domain is characterized as HTH myb-type 1.
+At position 80 to 130, the domain is characterized as HTH myb-type 2.
+At position 423 to 460, the domain is characterized as EGF-like.
+At position 514 to 699, the domain is characterized as VWFA.
+At position 10 to 233, the domain is characterized as ABC transporter.
+At position 26 to 128, the domain is characterized as Rieske.
+At position 79 to 296, the domain is characterized as Radical SAM core.
+At position 601 to 870, the domain is characterized as Protein kinase.
+At position 123 to 161, the domain is characterized as LRRCT.
+At position 87 to 187, the domain is characterized as HD.
+At position 449 to 484, the domain is characterized as EF-hand 1.
+At position 486 to 518, the domain is characterized as EF-hand 2.
+At position 15 to 298, the domain is characterized as ABC transmembrane type-1.
+At position 330 to 563, the domain is characterized as ABC transporter.
+At position 684 to 744, the domain is characterized as PWWP.
+At position 5 to 279, the domain is characterized as tr-type G.
+At position 21 to 173, the domain is characterized as GAF 1.
+At position 205 to 390, the domain is characterized as GAF 2.
+At position 420 to 743, the domain is characterized as PDEase.
+At position 17 to 207, the domain is characterized as GH11.
+At position 664 to 717, the domain is characterized as HTH myb-type.
+At position 6 to 111, the domain is characterized as SSB.
+At position 195 to 238, the domain is characterized as LysM.
+At position 351 to 643, the domain is characterized as Protein kinase.
+At position 1 to 113, the domain is characterized as Ig-like.
+At position 108 to 311, the domain is characterized as ATP-grasp.
+At position 221 to 413, the domain is characterized as Peptidase M12B.
+At position 419 to 505, the domain is characterized as Disintegrin.
+At position 660 to 676, the domain is characterized as EGF-like.
+At position 87 to 139, the domain is characterized as bHLH.
+At position 269 to 413, the domain is characterized as GAF.
+At position 457 to 691, the domain is characterized as Histidine kinase.
+At position 718 to 834, the domain is characterized as Response regulatory.
+At position 181 to 374, the domain is characterized as CheB-type methylesterase.
+At position 741 to 821, the domain is characterized as BRCT.
+At position 414 to 507, the domain is characterized as B5.
+At position 730 to 823, the domain is characterized as FDX-ACB.
+At position 145 to 180, the domain is characterized as UVR.
+At position 44 to 225, the domain is characterized as Rab-GAP TBC.
+At position 334 to 446, the domain is characterized as Rhodanese.
+At position 162 to 309, the domain is characterized as TRUD.
+At position 133 to 370, the domain is characterized as Radical SAM core.
+At position 373 to 439, the domain is characterized as TRAM.
+At position 208 to 521, the domain is characterized as Protein kinase.
+At position 1 to 126, the domain is characterized as Jacalin-type lectin 1.
+At position 430 to 572, the domain is characterized as Jacalin-type lectin 2.
+At position 584 to 727, the domain is characterized as Jacalin-type lectin 3.
+At position 119 to 351, the domain is characterized as NR LBD.
+At position 36 to 82, the domain is characterized as F-box.
+At position 120 to 296, the domain is characterized as Helicase ATP-binding.
+At position 310 to 480, the domain is characterized as Helicase C-terminal.
+At position 38 to 86, the domain is characterized as SANT.
+At position 20 to 62, the domain is characterized as F-box.
+At position 278 to 365, the domain is characterized as SCD.
+At position 4 to 111, the domain is characterized as PH.
+At position 417 to 675, the domain is characterized as Protein kinase.
+At position 252 to 383, the domain is characterized as GOLD.
+At position 846 to 865, the domain is characterized as UIM.
+At position 75 to 317, the domain is characterized as ABC transporter.
+At position 402 to 612, the domain is characterized as ABC transmembrane type-2.
+At position 118 to 369, the domain is characterized as Alpha-carbonic anhydrase.
+At position 9 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 212 to 404, the domain is characterized as GMPS ATP-PPase.
+At position 36 to 124, the domain is characterized as Cystatin.
+At position 409 to 578, the domain is characterized as tr-type G.
+At position 193 to 222, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 29 to 160, the domain is characterized as PLAT.
+At position 163 to 861, the domain is characterized as Lipoxygenase.
+At position 67 to 291, the domain is characterized as SET.
+At position 76 to 176, the domain is characterized as GS beta-grasp.
+At position 183 to 521, the domain is characterized as GS catalytic.
+At position 80 to 170, the domain is characterized as K-box.
+At position 165 to 231, the domain is characterized as DRBM.
+At position 99 to 165, the domain is characterized as S4 RNA-binding.
+At position 47 to 284, the domain is characterized as Laminin N-terminal.
+At position 285 to 340, the domain is characterized as Laminin EGF-like 1.
+At position 341 to 403, the domain is characterized as Laminin EGF-like 2.
+At position 404 to 453, the domain is characterized as Laminin EGF-like 3.
+At position 472 to 601, the domain is characterized as NTR.
+At position 24 to 150, the domain is characterized as Bulb-type lectin.
+At position 290 to 341, the domain is characterized as EGF-like; atypical.
+At position 349 to 426, the domain is characterized as PAN.
+At position 514 to 790, the domain is characterized as Protein kinase.
+At position 410 to 592, the domain is characterized as RHD.
+At position 502 to 675, the domain is characterized as tr-type G.
+At position 69 to 239, the domain is characterized as Helicase ATP-binding.
+At position 250 to 411, the domain is characterized as Helicase C-terminal.
+At position 88 to 140, the domain is characterized as bHLH.
+At position 7 to 81, the domain is characterized as ACT.
+At position 633 to 894, the domain is characterized as Protein kinase.
+At position 923 to 987, the domain is characterized as SAM.
+At position 217 to 382, the domain is characterized as Helicase ATP-binding.
+At position 413 to 562, the domain is characterized as Helicase C-terminal.
+At position 55 to 326, the domain is characterized as GH10.
+At position 233 to 449, the domain is characterized as Helicase ATP-binding.
+At position 490 to 658, the domain is characterized as Helicase C-terminal.
+At position 428 to 550, the domain is characterized as Ricin B-type lectin.
+At position 144 to 225, the domain is characterized as PRC barrel.
+At position 172 to 211, the domain is characterized as UBA.
+At position 6 to 156, the domain is characterized as YEATS.
+At position 1 to 137, the domain is characterized as YEATS.
+At position 5 to 360, the domain is characterized as DZF.
+At position 387 to 453, the domain is characterized as DRBM 1.
+At position 123 to 302, the domain is characterized as Helicase ATP-binding.
+At position 319 to 481, the domain is characterized as Helicase C-terminal.
+At position 18 to 451, the domain is characterized as Trm1 methyltransferase.
+At position 20 to 103, the domain is characterized as RRM 1.
+At position 419 to 499, the domain is characterized as RRM 2.
+At position 82 to 152, the domain is characterized as CSD.
+At position 380 to 549, the domain is characterized as tr-type G.
+At position 54 to 118, the domain is characterized as Sushi 1.
+At position 119 to 178, the domain is characterized as Sushi 2.
+At position 177 to 238, the domain is characterized as Sushi 3.
+At position 240 to 303, the domain is characterized as Sushi 4.
+At position 55 to 204, the domain is characterized as uDENN.
+At position 226 to 359, the domain is characterized as cDENN.
+At position 361 to 445, the domain is characterized as dDENN.
+At position 461 to 583, the domain is characterized as HD.
+At position 706 to 784, the domain is characterized as ACT 1.
+At position 816 to 900, the domain is characterized as ACT 2.
+At position 88 to 189, the domain is characterized as SWIRM.
+At position 207 to 587, the domain is characterized as GRAS.
+At position 122 to 519, the domain is characterized as Protein kinase.
+At position 58 to 369, the domain is characterized as Protein kinase.
+At position 836 to 968, the domain is characterized as Calponin-homology (CH).
+At position 1004 to 1033, the domain is characterized as IQ 1.
+At position 1386 to 1415, the domain is characterized as IQ 2.
+At position 1467 to 1496, the domain is characterized as IQ 3.
+At position 1656 to 1687, the domain is characterized as IQ 4.
+At position 1690 to 1721, the domain is characterized as IQ 5.
+At position 32 to 208, the domain is characterized as Helicase ATP-binding.
+At position 219 to 381, the domain is characterized as Helicase C-terminal.
+At position 428 to 542, the domain is characterized as Toprim.
+At position 93 to 276, the domain is characterized as Brix.
+At position 6 to 169, the domain is characterized as PPIase cyclophilin-type.
+At position 37 to 154, the domain is characterized as MTTase N-terminal.
+At position 177 to 416, the domain is characterized as Radical SAM core.
+At position 417 to 480, the domain is characterized as TRAM.
+At position 706 to 800, the domain is characterized as FDX-ACB.
+At position 28 to 232, the domain is characterized as Brix.
+At position 145 to 180, the domain is characterized as EF-hand 1.
+At position 189 to 222, the domain is characterized as EF-hand 2.
+At position 17 to 83, the domain is characterized as Cytochrome b5 heme-binding.
+At position 1 to 90, the domain is characterized as CS.
+At position 2 to 77, the domain is characterized as Ubiquitin-like.
+At position 411 to 450, the domain is characterized as UBA.
+At position 18 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 337 to 571, the domain is characterized as ABC transporter.
+At position 5 to 134, the domain is characterized as RNase III.
+At position 4 to 50, the domain is characterized as F-box.
+At position 355 to 407, the domain is characterized as FBD.
+At position 119 to 301, the domain is characterized as FAD-binding PCMH-type.
+At position 142 to 428, the domain is characterized as Protein kinase.
+At position 14 to 99, the domain is characterized as GIY-YIG.
+At position 53 to 89, the domain is characterized as EF-hand 2.
+At position 145 to 180, the domain is characterized as EF-hand 4.
+At position 193 to 228, the domain is characterized as EF-hand 5.
+At position 237 to 272, the domain is characterized as EF-hand 6.
+At position 384 to 441, the domain is characterized as CBS 1.
+At position 446 to 500, the domain is characterized as CBS 2.
+At position 4 to 121, the domain is characterized as RNase III.
+At position 151 to 219, the domain is characterized as DRBM.
+At position 18 to 53, the domain is characterized as CBM1.
+At position 23 to 130, the domain is characterized as CMP/dCMP-type deaminase.
+At position 559 to 762, the domain is characterized as Helicase ATP-binding.
+At position 971 to 1133, the domain is characterized as Helicase C-terminal.
+At position 125 to 219, the domain is characterized as Rhodanese.
+At position 326 to 531, the domain is characterized as MCM.
+At position 3 to 232, the domain is characterized as ABC transporter.
+At position 45 to 149, the domain is characterized as Calponin-homology (CH) 1.
+At position 158 to 264, the domain is characterized as Calponin-homology (CH) 2.
+At position 760 to 795, the domain is characterized as EF-hand 1.
+At position 796 to 831, the domain is characterized as EF-hand 2.
+At position 521 to 742, the domain is characterized as tr-type G.
+At position 108 to 196, the domain is characterized as Cytochrome c 1.
+At position 203 to 284, the domain is characterized as Cytochrome c 2.
+At position 304 to 369, the domain is characterized as Mop.
+At position 15 to 131, the domain is characterized as NTF2.
+At position 293 to 370, the domain is characterized as RRM.
+At position 303 to 596, the domain is characterized as Protein kinase.
+At position 292 to 543, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 288, the domain is characterized as tr-type G.
+At position 62 to 142, the domain is characterized as Saposin B-type.
+At position 4 to 162, the domain is characterized as Thioredoxin.
+At position 876 to 1056, the domain is characterized as RNase III 1.
+At position 1107 to 1233, the domain is characterized as RNase III 2.
+At position 1260 to 1334, the domain is characterized as DRBM.
+At position 3 to 92, the domain is characterized as ATP-cone.
+At position 583 to 708, the domain is characterized as Glycine radical.
+At position 192 to 227, the domain is characterized as UVR.
+At position 51 to 333, the domain is characterized as Protein kinase.
+At position 263 to 503, the domain is characterized as ABC transporter 2.
+At position 47 to 151, the domain is characterized as FAD-binding FR-type.
+At position 79 to 199, the domain is characterized as BAH.
+At position 225 to 768, the domain is characterized as SAM-dependent MTase C5-type.
+At position 339 to 404, the domain is characterized as Chromo.
+At position 20 to 209, the domain is characterized as RNase H type-2.
+At position 449 to 912, the domain is characterized as Protein kinase.
+At position 20 to 148, the domain is characterized as C-type lysozyme.
+At position 288 to 405, the domain is characterized as Cyclin N-terminal.
+At position 680 to 757, the domain is characterized as Ubiquitin-like.
+At position 24 to 146, the domain is characterized as C-type lectin.
+At position 16 to 75, the domain is characterized as F-box.
+At position 296 to 348, the domain is characterized as FBD.
+At position 229 to 288, the domain is characterized as SH3.
+At position 1 to 310, the domain is characterized as 5'-3' exonuclease.
+At position 48 to 90, the domain is characterized as CAP-Gly.
+At position 19 to 298, the domain is characterized as Protein kinase.
+At position 78 to 167, the domain is characterized as VPS37 C-terminal.
+At position 785 to 1066, the domain is characterized as Protein kinase.
+At position 336 to 493, the domain is characterized as VPS9.
+At position 26 to 89, the domain is characterized as LCN-type CS-alpha/beta.
+At position 975 to 1045, the domain is characterized as Bromo.
+At position 161 to 338, the domain is characterized as OBG-type G.
+At position 358 to 436, the domain is characterized as OCT.
+At position 52 to 355, the domain is characterized as Helicase ATP-binding.
+At position 36 to 78, the domain is characterized as Fibronectin type-I.
+At position 79 to 117, the domain is characterized as EGF-like.
+At position 124 to 205, the domain is characterized as Kringle 1.
+At position 213 to 294, the domain is characterized as Kringle 2.
+At position 309 to 558, the domain is characterized as Peptidase S1.
+At position 283 to 374, the domain is characterized as CobW C-terminal.
+At position 157 to 347, the domain is characterized as NodB homology.
+At position 470 to 584, the domain is characterized as STAS.
+At position 330 to 407, the domain is characterized as ACT.
+At position 223 to 288, the domain is characterized as FF.
+At position 44 to 217, the domain is characterized as EngB-type G.
+At position 866 to 978, the domain is characterized as VRR-NUC.
+At position 23 to 197, the domain is characterized as EngB-type G.
+At position 3 to 268, the domain is characterized as Protein kinase.
+At position 25 to 148, the domain is characterized as Rhodanese.
+At position 179 to 283, the domain is characterized as Fe2OG dioxygenase.
+At position 25 to 347, the domain is characterized as Transferrin-like 1.
+At position 361 to 683, the domain is characterized as Transferrin-like 2.
+At position 11 to 261, the domain is characterized as ABC transporter.
+At position 353 to 422, the domain is characterized as S4 RNA-binding.
+At position 57 to 479, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 994 to 1307, the domain is characterized as PKS/mFAS DH.
+At position 2328 to 2405, the domain is characterized as Carrier.
+At position 11 to 147, the domain is characterized as Response regulatory.
+At position 1 to 70, the domain is characterized as DRBM 1.
+At position 87 to 155, the domain is characterized as DRBM 2.
+At position 3 to 102, the domain is characterized as PB1.
+At position 391 to 436, the domain is characterized as UBA.
+At position 134 to 376, the domain is characterized as MHD.
+At position 12 to 265, the domain is characterized as Protein kinase.
+At position 376 to 493, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 494 to 598, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 643 to 734, the domain is characterized as POLO box.
+At position 26 to 139, the domain is characterized as Cadherin 1.
+At position 16 to 147, the domain is characterized as VHS.
+At position 261 to 280, the domain is characterized as UIM 1.
+At position 307 to 326, the domain is characterized as UIM 2.
+At position 7 to 123, the domain is characterized as PH.
+At position 157 to 261, the domain is characterized as IRS-type PTB.
+At position 30 to 141, the domain is characterized as SSB.
+At position 230 to 447, the domain is characterized as Helicase ATP-binding.
+At position 484 to 645, the domain is characterized as Helicase C-terminal.
+At position 191 to 254, the domain is characterized as bZIP.
+At position 641 to 731, the domain is characterized as BRCT.
+At position 417 to 740, the domain is characterized as FERM.
+At position 3 to 158, the domain is characterized as Thioredoxin.
+At position 104 to 357, the domain is characterized as ABC transporter 1.
+At position 796 to 1038, the domain is characterized as ABC transporter 2.
+At position 289 to 360, the domain is characterized as S1 motif.
+At position 599 to 762, the domain is characterized as Helicase ATP-binding.
+At position 780 to 960, the domain is characterized as Helicase C-terminal.
+At position 191 to 289, the domain is characterized as HTH araC/xylS-type.
+At position 34 to 173, the domain is characterized as CheW-like.
+At position 34 to 147, the domain is characterized as C-type lectin.
+At position 309 to 336, the domain is characterized as KOW 1.
+At position 460 to 487, the domain is characterized as KOW 2.
+At position 513 to 545, the domain is characterized as KOW 3.
+At position 635 to 668, the domain is characterized as KOW 4.
+At position 740 to 773, the domain is characterized as KOW 5.
+At position 16 to 241, the domain is characterized as AB hydrolase-1.
+At position 35 to 208, the domain is characterized as CP-type G.
+At position 38 to 262, the domain is characterized as Radical SAM core.
+At position 1 to 446, the domain is characterized as SMP-LTD.
+At position 148 to 198, the domain is characterized as DHHC.
+At position 51 to 140, the domain is characterized as CS 1.
+At position 322 to 424, the domain is characterized as CS 2.
+At position 539 to 1256, the domain is characterized as USP.
+At position 130 to 379, the domain is characterized as Radical SAM core.
+At position 557 to 589, the domain is characterized as LisH.
+At position 673 to 804, the domain is characterized as N-terminal Ras-GEF.
+At position 835 to 1062, the domain is characterized as Ras-GEF.
+At position 1 to 158, the domain is characterized as DHFR.
+At position 1 to 124, the domain is characterized as CBM20.
+At position 156 to 323, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 16, the domain is characterized as C-type lectin.
+At position 162 to 283, the domain is characterized as GGDEF.
+At position 28 to 84, the domain is characterized as F-box.
+At position 35 to 276, the domain is characterized as GB1/RHD3-type G.
+At position 7 to 170, the domain is characterized as Exonuclease.
+At position 139 to 192, the domain is characterized as bHLH.
+At position 58 to 161, the domain is characterized as HD.
+At position 404 to 465, the domain is characterized as TGS.
+At position 670 to 743, the domain is characterized as ACT.
+At position 7 to 262, the domain is characterized as BAR.
+At position 265 to 374, the domain is characterized as PH.
+At position 376 to 572, the domain is characterized as Rho-GAP.
+At position 816 to 874, the domain is characterized as SH3.
+At position 18 to 194, the domain is characterized as DHFR.
+At position 3 to 182, the domain is characterized as Miro 1.
+At position 198 to 233, the domain is characterized as EF-hand 1.
+At position 327 to 362, the domain is characterized as EF-hand 2.
+At position 443 to 608, the domain is characterized as Miro 2.
+At position 29 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 176 to 203, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 152, the domain is characterized as N-acetyltransferase.
+At position 355 to 578, the domain is characterized as B30.2/SPRY.
+At position 36 to 177, the domain is characterized as Ig-like V-type.
+At position 331 to 537, the domain is characterized as PCI.
+At position 138 to 427, the domain is characterized as Protein kinase.
+At position 135 to 229, the domain is characterized as GS beta-grasp.
+At position 236 to 561, the domain is characterized as GS catalytic.
+At position 170 to 474, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 36 to 79, the domain is characterized as LDL-receptor class A 1.
+At position 77 to 115, the domain is characterized as LDL-receptor class A 2.
+At position 116 to 155, the domain is characterized as LDL-receptor class A 3.
+At position 156 to 196, the domain is characterized as LDL-receptor class A 4.
+At position 195 to 232, the domain is characterized as LDL-receptor class A 5.
+At position 231 to 269, the domain is characterized as LDL-receptor class A 6.
+At position 272 to 318, the domain is characterized as LDL-receptor class A 7.
+At position 320 to 363, the domain is characterized as LDL-receptor class A 8.
+At position 365 to 403, the domain is characterized as LDL-receptor class A 9.
+At position 404 to 442, the domain is characterized as LDL-receptor class A 10.
+At position 444 to 485, the domain is characterized as LDL-receptor class A 11.
+At position 486 to 525, the domain is characterized as LDL-receptor class A 12.
+At position 518 to 562, the domain is characterized as LRRNT.
+At position 401 to 570, the domain is characterized as tr-type G.
+At position 29 to 243, the domain is characterized as Radical SAM core.
+At position 13 to 98, the domain is characterized as MtN3/slv 1.
+At position 133 to 217, the domain is characterized as MtN3/slv 2.
+At position 25 to 124, the domain is characterized as Ig-like V-type.
+At position 113 to 208, the domain is characterized as Ig-like C2-type.
+At position 98 to 175, the domain is characterized as PRC barrel.
+At position 54 to 137, the domain is characterized as Ig-like C2-type.
+At position 11 to 83, the domain is characterized as KRAB.
+At position 2 to 171, the domain is characterized as PRELI/MSF1.
+At position 228 to 324, the domain is characterized as Fibronectin type-III.
+At position 22 to 198, the domain is characterized as EngB-type G.
+At position 38 to 415, the domain is characterized as PIPK.
+At position 19 to 85, the domain is characterized as HMA.
+At position 177 to 269, the domain is characterized as Ig-like C2-type 1.
+At position 270 to 347, the domain is characterized as Ig-like C2-type 2.
+At position 378 to 438, the domain is characterized as Ig-like C2-type 3.
+At position 9 to 290, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 291 to 568, the domain is characterized as UvrD-like helicase C-terminal.
+At position 194 to 257, the domain is characterized as bZIP.
+At position 39 to 152, the domain is characterized as Thioredoxin.
+At position 166 to 353, the domain is characterized as TRUD.
+At position 261 to 494, the domain is characterized as NR LBD.
+At position 35 to 142, the domain is characterized as Ig-like V-type.
+At position 239 to 319, the domain is characterized as Ig-like C2-type 2.
+At position 323 to 411, the domain is characterized as Ig-like C2-type 3.
+At position 4 to 279, the domain is characterized as DegV.
+At position 272 to 510, the domain is characterized as NR LBD.
+At position 117 to 171, the domain is characterized as TCP.
+At position 553 to 582, the domain is characterized as IQ 1.
+At position 615 to 644, the domain is characterized as IQ 2.
+At position 193 to 299, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 234, the domain is characterized as CN hydrolase.
+At position 208 to 473, the domain is characterized as NR LBD.
+At position 4 to 407, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 4 to 274, the domain is characterized as CN hydrolase.
+At position 14 to 167, the domain is characterized as Nudix hydrolase.
+At position 32 to 61, the domain is characterized as IQ 1.
+At position 55 to 84, the domain is characterized as IQ 2.
+At position 91 to 120, the domain is characterized as IQ 3.
+At position 516 to 632, the domain is characterized as HD.
+At position 757 to 834, the domain is characterized as ACT 1.
+At position 870 to 949, the domain is characterized as ACT 2.
+At position 285 to 447, the domain is characterized as Helicase ATP-binding.
+At position 465 to 622, the domain is characterized as Helicase C-terminal.
+At position 161 to 353, the domain is characterized as CheB-type methylesterase.
+At position 222 to 552, the domain is characterized as Kinesin motor.
+At position 94 to 129, the domain is characterized as EF-hand 3.
+At position 130 to 163, the domain is characterized as EF-hand 4.
+At position 290 to 544, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 248, the domain is characterized as NodB homology.
+At position 1 to 40, the domain is characterized as Albumin.
+At position 398 to 510, the domain is characterized as PH.
+At position 552 to 808, the domain is characterized as Protein kinase.
+At position 295 to 358, the domain is characterized as FHA.
+At position 38 to 142, the domain is characterized as CBM2.
+At position 11 to 144, the domain is characterized as Nudix hydrolase.
+At position 17 to 80, the domain is characterized as bZIP.
+At position 113 to 402, the domain is characterized as FAE.
+At position 60 to 365, the domain is characterized as AB hydrolase-1.
+At position 147 to 261, the domain is characterized as C-type lectin.
+At position 18 to 116, the domain is characterized as HTH hxlR-type.
+At position 30 to 132, the domain is characterized as CUB.
+At position 64 to 100, the domain is characterized as LRRNT 1.
+At position 254 to 304, the domain is characterized as LRRCT 1.
+At position 310 to 346, the domain is characterized as LRRNT 2.
+At position 476 to 526, the domain is characterized as LRRCT 2.
+At position 534 to 570, the domain is characterized as LRRNT 3.
+At position 677 to 727, the domain is characterized as LRRCT 3.
+At position 730 to 766, the domain is characterized as LRRNT 4.
+At position 872 to 922, the domain is characterized as LRRCT 4.
+At position 931 to 968, the domain is characterized as EGF-like 1.
+At position 970 to 1007, the domain is characterized as EGF-like 2.
+At position 1009 to 1046, the domain is characterized as EGF-like 3; calcium-binding.
+At position 1048 to 1086, the domain is characterized as EGF-like 4.
+At position 1088 to 1124, the domain is characterized as EGF-like 5; calcium-binding.
+At position 1135 to 1173, the domain is characterized as EGF-like 6.
+At position 1176 to 1349, the domain is characterized as Laminin G-like.
+At position 1377 to 1416, the domain is characterized as EGF-like 7.
+At position 1433 to 1504, the domain is characterized as CTCK.
+At position 9 to 99, the domain is characterized as ABM.
+At position 11 to 193, the domain is characterized as PBS-linker.
+At position 68 to 112, the domain is characterized as LysM.
+At position 134 to 401, the domain is characterized as Olfactomedin-like.
+At position 442 to 677, the domain is characterized as NR LBD.
+At position 1 to 100, the domain is characterized as PTS EIIB type-2.
+At position 130 to 306, the domain is characterized as TNase-like.
+At position 191 to 225, the domain is characterized as KH.
+At position 232 to 292, the domain is characterized as HTH myb-type.
+At position 26 to 89, the domain is characterized as HMA.
+At position 1 to 191, the domain is characterized as AMMECR1.
+At position 5 to 126, the domain is characterized as MsrB.
+At position 428 to 490, the domain is characterized as HTH myb-type 1.
+At position 491 to 542, the domain is characterized as HTH myb-type 2.
+At position 540 to 598, the domain is characterized as Myb-like.
+At position 45 to 343, the domain is characterized as Dynamin-type G.
+At position 39 to 115, the domain is characterized as KH type-2.
+At position 51 to 270, the domain is characterized as Radical SAM core.
+At position 55 to 285, the domain is characterized as Radical SAM core.
+At position 45 to 110, the domain is characterized as NAC-A/B.
+At position 163 to 202, the domain is characterized as UBA.
+At position 87 to 360, the domain is characterized as Pyruvate carboxyltransferase.
+At position 43 to 160, the domain is characterized as SEA.
+At position 185 to 415, the domain is characterized as Peptidase S1.
+At position 121 to 451, the domain is characterized as SAC.
+At position 16 to 110, the domain is characterized as WSC 1.
+At position 127 to 222, the domain is characterized as WSC 2.
+At position 2 to 223, the domain is characterized as Glutamine amidotransferase type-2.
+At position 461 to 602, the domain is characterized as SIS 2.
+At position 229 to 300, the domain is characterized as KRAB.
+At position 5 to 126, the domain is characterized as Response regulatory.
+At position 140 to 392, the domain is characterized as EAL.
+At position 58 to 162, the domain is characterized as THUMP.
+At position 6 to 119, the domain is characterized as Longin.
+At position 134 to 194, the domain is characterized as v-SNARE coiled-coil homology.
+At position 180 to 260, the domain is characterized as ACT.
+At position 292 to 545, the domain is characterized as Protein kinase.
+At position 21 to 250, the domain is characterized as Sigma-54 factor interaction.
+At position 17 to 75, the domain is characterized as CpcD-like.
+At position 31 to 210, the domain is characterized as FAD-binding PCMH-type.
+At position 275 to 466, the domain is characterized as PNPLA.
+At position 164 to 430, the domain is characterized as CP-type G.
+At position 2 to 94, the domain is characterized as ABM.
+At position 146 to 310, the domain is characterized as JmjC.
+At position 29 to 204, the domain is characterized as BPL/LPL catalytic.
+At position 94 to 184, the domain is characterized as ACB.
+At position 13 to 95, the domain is characterized as KRAB.
+At position 145 to 348, the domain is characterized as ATP-grasp.
+At position 62 to 202, the domain is characterized as Thioredoxin.
+At position 95 to 477, the domain is characterized as GRAS.
+At position 39 to 198, the domain is characterized as PPIase cyclophilin-type.
+At position 134 to 183, the domain is characterized as bHLH.
+At position 191 to 295, the domain is characterized as Fe2OG dioxygenase.
+At position 386 to 536, the domain is characterized as NTF2.
+At position 565 to 619, the domain is characterized as TAP-C.
+At position 89 to 122, the domain is characterized as EF-hand 2.
+At position 155 to 180, the domain is characterized as EF-hand 4.
+At position 39 to 284, the domain is characterized as ATP-grasp.
+At position 25 to 318, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 86 to 403, the domain is characterized as Peptidase A1.
+At position 45 to 157, the domain is characterized as TBDR plug.
+At position 168 to 745, the domain is characterized as TBDR beta-barrel.
+At position 179 to 370, the domain is characterized as CheB-type methylesterase.
+At position 76 to 111, the domain is characterized as EF-hand 3.
+At position 112 to 137, the domain is characterized as EF-hand 4.
+At position 297 to 504, the domain is characterized as MCM.
+At position 95 to 311, the domain is characterized as RNase H type-2.
+At position 32 to 134, the domain is characterized as Gnk2-homologous 1.
+At position 140 to 250, the domain is characterized as Gnk2-homologous 2.
+At position 2 to 74, the domain is characterized as RRM.
+At position 136 to 422, the domain is characterized as Protein kinase.
+At position 169 to 232, the domain is characterized as R3H.
+At position 233 to 310, the domain is characterized as SUZ.
+At position 536 to 725, the domain is characterized as Helicase ATP-binding.
+At position 746 to 904, the domain is characterized as Helicase C-terminal.
+At position 11 to 56, the domain is characterized as F-box.
+At position 987 to 1200, the domain is characterized as FtsK.
+At position 29 to 138, the domain is characterized as Ig-like V-type.
+At position 144 to 223, the domain is characterized as Ig-like C2-type.
+At position 23 to 221, the domain is characterized as ABC transmembrane type-1.
+At position 386 to 440, the domain is characterized as PAP-associated.
+At position 450 to 572, the domain is characterized as HD.
+At position 692 to 771, the domain is characterized as ACT 1.
+At position 798 to 869, the domain is characterized as ACT 2.
+At position 503 to 656, the domain is characterized as N-acetyltransferase.
+At position 745 to 815, the domain is characterized as Bromo.
+At position 235 to 286, the domain is characterized as LRRCT 1.
+At position 365 to 407, the domain is characterized as LRRNT.
+At position 563 to 614, the domain is characterized as LRRCT 2.
+At position 32 to 319, the domain is characterized as Protein kinase.
+At position 109 to 279, the domain is characterized as PA14.
+At position 6 to 259, the domain is characterized as ABC transporter 1.
+At position 324 to 550, the domain is characterized as ABC transporter 2.
+At position 36 to 102, the domain is characterized as BTB.
+At position 4 to 85, the domain is characterized as GST N-terminal.
+At position 90 to 223, the domain is characterized as GST C-terminal.
+At position 1 to 185, the domain is characterized as YrdC-like.
+At position 31 to 135, the domain is characterized as PTS EIIA type-1.
+At position 321 to 428, the domain is characterized as Rhodanese.
+At position 227 to 396, the domain is characterized as tr-type G.
+At position 291 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 53 to 145, the domain is characterized as BRICHOS.
+At position 110 to 289, the domain is characterized as FAD-binding PCMH-type.
+At position 103 to 174, the domain is characterized as S4 RNA-binding.
+At position 98 to 198, the domain is characterized as BRCT.
+At position 112 to 281, the domain is characterized as tr-type G.
+At position 46 to 242, the domain is characterized as Peptidase M12B.
+At position 250 to 322, the domain is characterized as Disintegrin.
+At position 30 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 122 to 204, the domain is characterized as SCAN box.
+At position 9 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 180 to 306, the domain is characterized as C2 1.
+At position 317 to 451, the domain is characterized as C2 2.
+At position 197 to 392, the domain is characterized as Peptidase M12B.
+At position 572 to 626, the domain is characterized as F-box.
+At position 35 to 81, the domain is characterized as F-box.
+At position 361 to 411, the domain is characterized as FBD.
+At position 40 to 155, the domain is characterized as tRNA-binding.
+At position 409 to 484, the domain is characterized as B5.
+At position 710 to 803, the domain is characterized as FDX-ACB.
+At position 420 to 589, the domain is characterized as tr-type G.
+At position 30 to 134, the domain is characterized as Ig-like C2-type.
+At position 43 to 266, the domain is characterized as Radical SAM core.
+At position 130 to 349, the domain is characterized as Histidine kinase.
+At position 208 to 432, the domain is characterized as MIF4G.
+At position 612 to 734, the domain is characterized as MI.
+At position 12 to 264, the domain is characterized as Pyruvate carboxyltransferase.
+At position 75 to 88, the domain is characterized as CRIB.
+At position 269 to 520, the domain is characterized as Protein kinase.
+At position 46 to 81, the domain is characterized as EF-hand 2.
+At position 145 to 324, the domain is characterized as ABC transmembrane type-1.
+At position 72 to 271, the domain is characterized as Peptidase M12A.
+At position 67 to 349, the domain is characterized as ABC transmembrane type-1.
+At position 382 to 618, the domain is characterized as ABC transporter.
+At position 32 to 297, the domain is characterized as Protein kinase.
+At position 613 to 693, the domain is characterized as PB1.
+At position 490 to 607, the domain is characterized as Toprim.
+At position 239 to 457, the domain is characterized as Peptidase M12B.
+At position 460 to 546, the domain is characterized as Disintegrin.
+At position 547 to 602, the domain is characterized as TSP type-1 1.
+At position 825 to 885, the domain is characterized as TSP type-1 2.
+At position 888 to 943, the domain is characterized as TSP type-1 3.
+At position 944 to 1003, the domain is characterized as TSP type-1 4.
+At position 1004 to 1058, the domain is characterized as TSP type-1 5.
+At position 1066 to 1104, the domain is characterized as PLAC.
+At position 160 to 240, the domain is characterized as PPIase FKBP-type.
+At position 130 to 370, the domain is characterized as Radical SAM core.
+At position 24 to 124, the domain is characterized as SRCR.
+At position 153 to 221, the domain is characterized as BTB.
+At position 260 to 360, the domain is characterized as BACK.
+At position 133 to 371, the domain is characterized as Radical SAM core.
+At position 129 to 268, the domain is characterized as PPC.
+At position 12 to 308, the domain is characterized as Protein kinase.
+At position 10 to 126, the domain is characterized as MTTase N-terminal.
+At position 150 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 451, the domain is characterized as TRAM.
+At position 193 to 244, the domain is characterized as Collagen-like 1.
+At position 285 to 329, the domain is characterized as Collagen-like 2.
+At position 372 to 509, the domain is characterized as C1q.
+At position 464 to 600, the domain is characterized as Thioredoxin.
+At position 182 to 376, the domain is characterized as Helicase ATP-binding.
+At position 414 to 607, the domain is characterized as Helicase C-terminal.
+At position 37 to 197, the domain is characterized as SIS.
+At position 1 to 152, the domain is characterized as SPX.
+At position 62 to 265, the domain is characterized as FAD-binding PCMH-type.
+At position 794 to 1254, the domain is characterized as Protein kinase.
+At position 1255 to 1320, the domain is characterized as AGC-kinase C-terminal.
+At position 1636 to 1750, the domain is characterized as Response regulatory.
+At position 2 to 233, the domain is characterized as Glutamine amidotransferase type-2.
+At position 276 to 338, the domain is characterized as SAM.
+At position 18 to 175, the domain is characterized as MRH.
+At position 10 to 213, the domain is characterized as tr-type G.
+At position 7 to 90, the domain is characterized as ACT.
+At position 1 to 38, the domain is characterized as Plastocyanin-like.
+At position 197 to 384, the domain is characterized as Glutamine amidotransferase type-1.
+At position 44 to 102, the domain is characterized as Inhibitor I9.
+At position 110 to 378, the domain is characterized as Peptidase S8.
+At position 179 to 246, the domain is characterized as PAS 1.
+At position 319 to 385, the domain is characterized as PAS 2.
+At position 393 to 436, the domain is characterized as PAC.
+At position 6 to 326, the domain is characterized as Kinesin motor.
+At position 621 to 691, the domain is characterized as S1 motif.
+At position 31 to 87, the domain is characterized as RabBD.
+At position 266 to 385, the domain is characterized as C2 1.
+At position 398 to 527, the domain is characterized as C2 2.
+At position 3 to 67, the domain is characterized as J.
+At position 150 to 265, the domain is characterized as STAS.
+At position 4 to 138, the domain is characterized as SprT-like.
+At position 173 to 211, the domain is characterized as LRRCT.
+At position 53 to 216, the domain is characterized as SIS.
+At position 84 to 119, the domain is characterized as EF-hand 1.
+At position 154 to 189, the domain is characterized as EF-hand 2.
+At position 190 to 225, the domain is characterized as EF-hand 3.
+At position 125 to 319, the domain is characterized as ATP-grasp.
+At position 36 to 253, the domain is characterized as Radical SAM core.
+At position 370 to 649, the domain is characterized as Protein kinase.
+At position 105 to 164, the domain is characterized as bHLH.
+At position 120 to 195, the domain is characterized as MIT.
+At position 505 to 572, the domain is characterized as PAP-associated.
+At position 264 to 379, the domain is characterized as Sox C-terminal.
+At position 50 to 191, the domain is characterized as Tyrosine-protein phosphatase.
+At position 5 to 147, the domain is characterized as Flavodoxin-like.
+At position 271 to 533, the domain is characterized as FAD-binding FR-type.
+At position 3 to 194, the domain is characterized as Flavodoxin-like.
+At position 277 to 340, the domain is characterized as bZIP.
+At position 181 to 319, the domain is characterized as Helicase ATP-binding.
+At position 343 to 499, the domain is characterized as Helicase C-terminal.
+At position 161 to 460, the domain is characterized as Reverse transcriptase.
+At position 63 to 241, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 226, the domain is characterized as Radical SAM core.
+At position 150 to 255, the domain is characterized as HIT.
+At position 203 to 378, the domain is characterized as EngA-type G 2.
+At position 379 to 463, the domain is characterized as KH-like.
+At position 34 to 232, the domain is characterized as Eph LBD.
+At position 364 to 479, the domain is characterized as Fibronectin type-III 1.
+At position 480 to 575, the domain is characterized as Fibronectin type-III 2.
+At position 663 to 912, the domain is characterized as Protein kinase.
+At position 941 to 1005, the domain is characterized as SAM.
+At position 34 to 133, the domain is characterized as Cadherin 1.
+At position 11 to 137, the domain is characterized as RWD.
+At position 26 to 184, the domain is characterized as Helicase ATP-binding.
+At position 259 to 463, the domain is characterized as Helicase C-terminal.
+At position 113 to 176, the domain is characterized as bZIP.
+At position 1 to 18, the domain is characterized as Thioredoxin.
+At position 11 to 115, the domain is characterized as Thioredoxin.
+At position 2 to 220, the domain is characterized as Glutamine amidotransferase type-2.
+At position 460 to 605, the domain is characterized as SIS 2.
+At position 26 to 200, the domain is characterized as EngB-type G.
+At position 221 to 315, the domain is characterized as Ig-like V-type.
+At position 288 to 508, the domain is characterized as Fibrinogen C-terminal.
+At position 70 to 381, the domain is characterized as IF rod.
+At position 148 to 225, the domain is characterized as REM-1 2.
+At position 231 to 349, the domain is characterized as C2.
+At position 771 to 1030, the domain is characterized as Protein kinase.
+At position 1031 to 1096, the domain is characterized as AGC-kinase C-terminal.
+At position 22 to 142, the domain is characterized as FZ.
+At position 170 to 290, the domain is characterized as NTR.
+At position 403 to 489, the domain is characterized as Disintegrin.
+At position 110 to 240, the domain is characterized as Galectin.
+At position 705 to 783, the domain is characterized as BRCT.
+At position 102 to 287, the domain is characterized as DCUN1.
+At position 152 to 253, the domain is characterized as Fe2OG dioxygenase.
+At position 662 to 978, the domain is characterized as Autotransporter.
+At position 68 to 384, the domain is characterized as Peptidase A1.
+At position 617 to 844, the domain is characterized as PARP catalytic.
+At position 25 to 283, the domain is characterized as Protein kinase.
+At position 22 to 264, the domain is characterized as ABC transporter.
+At position 85 to 372, the domain is characterized as ABC transmembrane type-1.
+At position 440 to 659, the domain is characterized as ABC transporter.
+At position 68 to 117, the domain is characterized as FHA.
+At position 73 to 290, the domain is characterized as Radical SAM core.
+At position 975 to 1162, the domain is characterized as Reticulon.
+At position 349 to 619, the domain is characterized as Protein kinase.
+At position 39 to 70, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 71 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 101 to 130, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 172 to 201, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 195 to 224, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 220 to 249, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 257 to 286, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 286 to 315, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 341 to 372, the domain is characterized as 4Fe-4S ferredoxin-type 9.
+At position 373 to 402, the domain is characterized as 4Fe-4S ferredoxin-type 10.
+At position 403 to 432, the domain is characterized as 4Fe-4S ferredoxin-type 11.
+At position 442 to 471, the domain is characterized as 4Fe-4S ferredoxin-type 12.
+At position 467 to 496, the domain is characterized as 4Fe-4S ferredoxin-type 13.
+At position 56 to 121, the domain is characterized as SAM.
+At position 129 to 225, the domain is characterized as CRIC.
+At position 262 to 344, the domain is characterized as PDZ.
+At position 632 to 736, the domain is characterized as PH.
+At position 223 to 258, the domain is characterized as DMA.
+At position 2 to 109, the domain is characterized as Thioredoxin.
+At position 638 to 719, the domain is characterized as BRCT.
+At position 191 to 301, the domain is characterized as Ig-like.
+At position 44 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 230 to 326, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 415, the domain is characterized as Ig-like C2-type 4.
+At position 422 to 552, the domain is characterized as Ig-like C2-type 5.
+At position 555 to 671, the domain is characterized as Ig-like C2-type 6.
+At position 678 to 764, the domain is characterized as Ig-like C2-type 7.
+At position 845 to 1173, the domain is characterized as Protein kinase.
+At position 823 to 888, the domain is characterized as HP.
+At position 1 to 20, the domain is characterized as Barwin.
+At position 1 to 47, the domain is characterized as H15.
+At position 19 to 126, the domain is characterized as Rhodanese 1.
+At position 160 to 280, the domain is characterized as Rhodanese 2.
+At position 95 to 156, the domain is characterized as SH3.
+At position 162 to 259, the domain is characterized as SH2.
+At position 284 to 537, the domain is characterized as Protein kinase.
+At position 50 to 299, the domain is characterized as GB1/RHD3-type G.
+At position 251 to 442, the domain is characterized as PNPLA.
+At position 10 to 66, the domain is characterized as HTH myb-type 1.
+At position 67 to 117, the domain is characterized as HTH myb-type 2.
+At position 157 to 195, the domain is characterized as LRRCT.
+At position 236 to 496, the domain is characterized as Deacetylase sirtuin-type.
+At position 51 to 240, the domain is characterized as GH11.
+At position 36 to 197, the domain is characterized as SIS.
+At position 25 to 103, the domain is characterized as DED.
+At position 1 to 237, the domain is characterized as Deacetylase sirtuin-type.
+At position 116 to 267, the domain is characterized as Exonuclease.
+At position 5 to 54, the domain is characterized as F-box.
+At position 342 to 391, the domain is characterized as FBD.
+At position 272 to 336, the domain is characterized as SH3.
+At position 30 to 298, the domain is characterized as GH18.
+At position 168 to 384, the domain is characterized as TLC.
+At position 36 to 264, the domain is characterized as Radical SAM core.
+At position 36 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 119 to 201, the domain is characterized as Ig-like C2-type 2.
+At position 16 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 206 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 321 to 450, the domain is characterized as NlpC/P60.
+At position 220 to 499, the domain is characterized as CN hydrolase.
+At position 47 to 144, the domain is characterized as PH.
+At position 631 to 823, the domain is characterized as Rab-GAP TBC.
+At position 26 to 61, the domain is characterized as EF-hand 1.
+At position 132 to 167, the domain is characterized as EF-hand 3.
+At position 44 to 162, the domain is characterized as tRNA-binding.
+At position 430 to 513, the domain is characterized as B5.
+At position 730 to 822, the domain is characterized as FDX-ACB.
+At position 98 to 295, the domain is characterized as VWFA.
+At position 108 to 147, the domain is characterized as LRRCT.
+At position 1 to 427, the domain is characterized as BRO1.
+At position 246 to 432, the domain is characterized as GATase cobBQ-type.
+At position 26 to 45, the domain is characterized as UIM.
+At position 580 to 634, the domain is characterized as SOCS box.
+At position 399 to 502, the domain is characterized as B5.
+At position 728 to 821, the domain is characterized as FDX-ACB.
+At position 390 to 452, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 545 to 607, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 147 to 206, the domain is characterized as SH3.
+At position 240 to 424, the domain is characterized as DH.
+At position 455 to 561, the domain is characterized as PH.
+At position 35 to 452, the domain is characterized as Sema.
+At position 6 to 44, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 45 to 87, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 94 to 134, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 135 to 177, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 1 to 93, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 1 to 131, the domain is characterized as VIT.
+At position 281 to 469, the domain is characterized as VWFA.
+At position 442 to 516, the domain is characterized as GW 1.
+At position 518 to 592, the domain is characterized as GW 2.
+At position 611 to 685, the domain is characterized as GW 3.
+At position 687 to 761, the domain is characterized as GW 4.
+At position 783 to 858, the domain is characterized as GW 5.
+At position 860 to 935, the domain is characterized as GW 6.
+At position 942 to 1016, the domain is characterized as GW 7.
+At position 125 to 270, the domain is characterized as SGF29 C-terminal.
+At position 93 to 139, the domain is characterized as F-box.
+At position 26 to 145, the domain is characterized as Ig-like V-type.
+At position 134 to 229, the domain is characterized as Ig-like C2-type.
+At position 156 to 441, the domain is characterized as GT92.
+At position 48 to 138, the domain is characterized as ATP-cone.
+At position 30 to 331, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 33 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 44 to 151, the domain is characterized as Calponin-homology (CH) 1.
+At position 210 to 317, the domain is characterized as Calponin-homology (CH) 2.
+At position 47 to 191, the domain is characterized as N-acetyltransferase.
+At position 103 to 262, the domain is characterized as CP-type G.
+At position 83 to 120, the domain is characterized as UBA-like.
+At position 134 to 345, the domain is characterized as DCUN1.
+At position 92 to 153, the domain is characterized as S1 motif.
+At position 2 to 228, the domain is characterized as Glutamine amidotransferase type-2.
+At position 295 to 435, the domain is characterized as SIS 1.
+At position 468 to 613, the domain is characterized as SIS 2.
+At position 37 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 106 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 383 to 474, the domain is characterized as Ig-like C2-type 4.
+At position 487 to 567, the domain is characterized as Ig-like C2-type 5.
+At position 641 to 963, the domain is characterized as Protein kinase.
+At position 897 to 1031, the domain is characterized as C1q.
+At position 10 to 206, the domain is characterized as HORMA.
+At position 11 to 59, the domain is characterized as F-box.
+At position 364 to 412, the domain is characterized as FBD.
+At position 49 to 152, the domain is characterized as PA.
+At position 46 to 572, the domain is characterized as PLA2c.
+At position 28 to 175, the domain is characterized as UBC core.
+At position 62 to 218, the domain is characterized as CP-type G.
+At position 98 to 151, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 447 to 634, the domain is characterized as DH.
+At position 670 to 805, the domain is characterized as PH.
+At position 825 to 1120, the domain is characterized as CNH.
+At position 560 to 653, the domain is characterized as BRCT 1.
+At position 667 to 777, the domain is characterized as BRCT 2.
+At position 183 to 376, the domain is characterized as CheB-type methylesterase.
+At position 20 to 98, the domain is characterized as PAN.
+At position 103 to 181, the domain is characterized as Kringle 1.
+At position 184 to 262, the domain is characterized as Kringle 2.
+At position 275 to 352, the domain is characterized as Kringle 3.
+At position 377 to 454, the domain is characterized as Kringle 4.
+At position 481 to 560, the domain is characterized as Kringle 5.
+At position 581 to 808, the domain is characterized as Peptidase S1.
+At position 293 to 324, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 375 to 405, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 29 to 58, the domain is characterized as IQ.
+At position 706 to 1072, the domain is characterized as HECT.
+At position 208 to 296, the domain is characterized as Ig-like C1-type.
+At position 544 to 621, the domain is characterized as Carrier.
+At position 3 to 101, the domain is characterized as PTS EIIA type-3.
+At position 36 to 158, the domain is characterized as MPN.
+At position 19 to 171, the domain is characterized as FAS1 1.
+At position 173 to 302, the domain is characterized as FAS1 2.
+At position 1 to 173, the domain is characterized as TCTP.
+At position 267 to 510, the domain is characterized as Protein kinase.
+At position 1 to 125, the domain is characterized as Peptidase C39.
+At position 187 to 384, the domain is characterized as Peptidase M12B.
+At position 395 to 484, the domain is characterized as Disintegrin.
+At position 619 to 653, the domain is characterized as EGF-like.
+At position 598 to 774, the domain is characterized as PCI.
+At position 14 to 131, the domain is characterized as MSP.
+At position 35 to 332, the domain is characterized as Protein kinase.
+At position 197 to 525, the domain is characterized as Protein kinase.
+At position 112 to 279, the domain is characterized as tr-type G.
+At position 222 to 564, the domain is characterized as PUM-HD.
+At position 42 to 154, the domain is characterized as THUMP.
+At position 42 to 319, the domain is characterized as tr-type G.
+At position 951 to 1240, the domain is characterized as Protein kinase.
+At position 106 to 346, the domain is characterized as Radical SAM core.
+At position 89 to 242, the domain is characterized as Ferritin-like diiron.
+At position 47 to 354, the domain is characterized as AB hydrolase-1.
+At position 375 to 434, the domain is characterized as CBS 1.
+At position 436 to 489, the domain is characterized as CBS 2.
+At position 23 to 63, the domain is characterized as Chitin-binding type-1.
+At position 85 to 207, the domain is characterized as GST C-terminal.
+At position 24 to 73, the domain is characterized as WAP; atypical.
+At position 260 to 341, the domain is characterized as BCNT-C.
+At position 6 to 75, the domain is characterized as KRAB.
+At position 1 to 146, the domain is characterized as N-acetyltransferase.
+At position 60 to 188, the domain is characterized as VIT.
+At position 312 to 480, the domain is characterized as VWFA.
+At position 4 to 125, the domain is characterized as PINc.
+At position 186 to 298, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 2 to 130, the domain is characterized as RNase III.
+At position 17 to 63, the domain is characterized as UMA.
+At position 389 to 430, the domain is characterized as UBA 1.
+At position 451 to 498, the domain is characterized as UBA 2.
+At position 4 to 233, the domain is characterized as Radical SAM core.
+At position 53 to 122, the domain is characterized as BTB.
+At position 161 to 261, the domain is characterized as BACK.
+At position 1 to 178, the domain is characterized as Macro.
+At position 11 to 241, the domain is characterized as ABC transporter.
+At position 32 to 308, the domain is characterized as GH16.
+At position 135 to 343, the domain is characterized as ATP-grasp.
+At position 545 to 636, the domain is characterized as Fibronectin type-III 2.
+At position 641 to 735, the domain is characterized as Fibronectin type-III 3.
+At position 824 to 1096, the domain is characterized as Protein kinase.
+At position 428 to 584, the domain is characterized as Exonuclease.
+At position 108 to 182, the domain is characterized as S4 RNA-binding.
+At position 45 to 459, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 30 to 204, the domain is characterized as EngB-type G.
+At position 21 to 301, the domain is characterized as ABC transmembrane type-1.
+At position 335 to 569, the domain is characterized as ABC transporter.
+At position 35 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 340 to 404, the domain is characterized as S4 RNA-binding.
+At position 30 to 93, the domain is characterized as SLH 1.
+At position 94 to 150, the domain is characterized as SLH 2.
+At position 152 to 215, the domain is characterized as SLH 3.
+At position 403 to 480, the domain is characterized as BIG2.
+At position 51 to 136, the domain is characterized as Ig-like C2-type 1.
+At position 142 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 153 to 254, the domain is characterized as Fe2OG dioxygenase.
+At position 77 to 149, the domain is characterized as Inhibitor I9.
+At position 155 to 461, the domain is characterized as Peptidase S8.
+At position 1 to 61, the domain is characterized as S4 RNA-binding.
+At position 53 to 146, the domain is characterized as PH.
+At position 317 to 451, the domain is characterized as DAGKc.
+At position 1151 to 1214, the domain is characterized as SAM.
+At position 7 to 159, the domain is characterized as NAC.
+At position 100 to 113, the domain is characterized as CRIB.
+At position 361 to 612, the domain is characterized as Protein kinase.
+At position 25 to 260, the domain is characterized as Peptidase S1.
+At position 4 to 73, the domain is characterized as BON 1.
+At position 119 to 188, the domain is characterized as BON 2.
+At position 204 to 251, the domain is characterized as LysM.
+At position 6 to 89, the domain is characterized as Ras-associating.
+At position 127 to 188, the domain is characterized as S4 RNA-binding.
+At position 602 to 776, the domain is characterized as PCI.
+At position 145 to 367, the domain is characterized as NR LBD.
+At position 58 to 136, the domain is characterized as RRM 1.
+At position 545 to 626, the domain is characterized as PABC.
+At position 11 to 159, the domain is characterized as N-acetyltransferase 1.
+At position 162 to 327, the domain is characterized as N-acetyltransferase 2.
+At position 1347 to 1464, the domain is characterized as SET.
+At position 1470 to 1486, the domain is characterized as Post-SET.
+At position 254 to 447, the domain is characterized as HDOD.
+At position 1 to 59, the domain is characterized as LCN-type CS-alpha/beta.
+At position 3 to 99, the domain is characterized as Histone-fold.
+At position 275 to 474, the domain is characterized as B30.2/SPRY.
+At position 356 to 440, the domain is characterized as PDZ.
+At position 92 to 157, the domain is characterized as S4 RNA-binding.
+At position 7 to 83, the domain is characterized as CIDE-N.
+At position 23 to 264, the domain is characterized as ABC transporter.
+At position 37 to 211, the domain is characterized as VWFA.
+At position 230 to 412, the domain is characterized as Laminin G-like.
+At position 448 to 501, the domain is characterized as Collagen-like 1.
+At position 502 to 543, the domain is characterized as Collagen-like 2.
+At position 544 to 591, the domain is characterized as Collagen-like 3.
+At position 592 to 642, the domain is characterized as Collagen-like 4.
+At position 643 to 684, the domain is characterized as Collagen-like 5.
+At position 685 to 741, the domain is characterized as Collagen-like 6.
+At position 742 to 786, the domain is characterized as Collagen-like 7.
+At position 825 to 882, the domain is characterized as Collagen-like 8.
+At position 499 to 613, the domain is characterized as Toprim.
+At position 275 to 354, the domain is characterized as PUA.
+At position 3 to 145, the domain is characterized as RNase H type-1.
+At position 40 to 313, the domain is characterized as Protein kinase.
+At position 142 to 349, the domain is characterized as CP-type G.
+At position 206 to 377, the domain is characterized as PCI.
+At position 108 to 266, the domain is characterized as N-acetyltransferase.
+At position 417 to 540, the domain is characterized as CUB.
+At position 1611 to 1839, the domain is characterized as Fibrillar collagen NC1.
+At position 102 to 163, the domain is characterized as CBS 1.
+At position 165 to 221, the domain is characterized as CBS 2.
+At position 48 to 301, the domain is characterized as AB hydrolase-1.
+At position 44 to 131, the domain is characterized as GST N-terminal.
+At position 134 to 263, the domain is characterized as GST C-terminal.
+At position 721 to 784, the domain is characterized as R3H.
+At position 3 to 106, the domain is characterized as Thioredoxin.
+At position 56 to 260, the domain is characterized as TNase-like.
+At position 108 to 166, the domain is characterized as SCAN box.
+At position 237 to 314, the domain is characterized as PUA.
+At position 16 to 122, the domain is characterized as Calponin-homology (CH) 1.
+At position 139 to 242, the domain is characterized as Calponin-homology (CH) 2.
+At position 141 to 336, the domain is characterized as CheB-type methylesterase.
+At position 579 to 667, the domain is characterized as ABM.
+At position 33 to 122, the domain is characterized as Ig-like C2-type.
+At position 108 to 127, the domain is characterized as HhH.
+At position 1 to 194, the domain is characterized as Phosphatase tensin-type.
+At position 200 to 339, the domain is characterized as C2 tensin-type.
+At position 1237 to 1635, the domain is characterized as FH2.
+At position 6 to 131, the domain is characterized as MATH.
+At position 38 to 140, the domain is characterized as Gnk2-homologous 1.
+At position 146 to 253, the domain is characterized as Gnk2-homologous 2.
+At position 146 to 378, the domain is characterized as Radical SAM core.
+At position 24 to 147, the domain is characterized as NTR.
+At position 11 to 164, the domain is characterized as Nudix hydrolase.
+At position 142 to 352, the domain is characterized as B30.2/SPRY.
+At position 147 to 408, the domain is characterized as Peptidase M66.
+At position 192 to 276, the domain is characterized as PDZ.
+At position 19 to 133, the domain is characterized as Rhodanese.
+At position 40 to 290, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 4 to 125, the domain is characterized as PX.
+At position 156 to 215, the domain is characterized as SH3 1.
+At position 226 to 285, the domain is characterized as SH3 2.
+At position 78 to 429, the domain is characterized as Peptidase A1.
+At position 152 to 333, the domain is characterized as Era-type G.
+At position 361 to 437, the domain is characterized as KH type-2.
+At position 100 to 162, the domain is characterized as S4 RNA-binding.
+At position 108 to 294, the domain is characterized as Tyr recombinase.
+At position 215 to 241, the domain is characterized as PLD phosphodiesterase 1.
+At position 460 to 493, the domain is characterized as PLD phosphodiesterase 2.
+At position 221 to 374, the domain is characterized as TrmE-type G.
+At position 1 to 104, the domain is characterized as PLAT.
+At position 138 to 178, the domain is characterized as LRRCT.
+At position 93 to 187, the domain is characterized as PB1.
+At position 32 to 127, the domain is characterized as HD.
+At position 139 to 262, the domain is characterized as Nudix hydrolase.
+At position 281 to 347, the domain is characterized as SH3.
+At position 488 to 551, the domain is characterized as SAM 1.
+At position 557 to 621, the domain is characterized as SAM 2.
+At position 232 to 324, the domain is characterized as ARID.
+At position 429 to 523, the domain is characterized as REKLES.
+At position 11 to 145, the domain is characterized as MPN.
+At position 1 to 256, the domain is characterized as SPX.
+At position 44 to 298, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 32 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 122 to 208, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 308, the domain is characterized as Ig-like C2-type 3.
+At position 318 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 408 to 495, the domain is characterized as Ig-like C2-type 5.
+At position 499 to 587, the domain is characterized as Ig-like C2-type 6.
+At position 600 to 698, the domain is characterized as Fibronectin type-III 1.
+At position 703 to 800, the domain is characterized as Fibronectin type-III 2.
+At position 805 to 901, the domain is characterized as Fibronectin type-III 3.
+At position 902 to 996, the domain is characterized as Fibronectin type-III 4.
+At position 1 to 221, the domain is characterized as PABS.
+At position 6 to 165, the domain is characterized as Thioredoxin.
+At position 63 to 275, the domain is characterized as ABC transmembrane type-1.
+At position 100 to 321, the domain is characterized as Radical SAM core.
+At position 1 to 265, the domain is characterized as Pterin-binding.
+At position 84 to 249, the domain is characterized as TNase-like.
+At position 54 to 135, the domain is characterized as RRM 1.
+At position 152 to 232, the domain is characterized as RRM 2.
+At position 406 to 479, the domain is characterized as RRM 3.
+At position 1 to 81, the domain is characterized as GST N-terminal.
+At position 88 to 209, the domain is characterized as GST C-terminal.
+At position 64 to 99, the domain is characterized as QLQ.
+At position 125 to 169, the domain is characterized as WRC.
+At position 19 to 338, the domain is characterized as Hcy-binding.
+At position 371 to 632, the domain is characterized as Pterin-binding.
+At position 662 to 759, the domain is characterized as B12-binding N-terminal.
+At position 772 to 907, the domain is characterized as B12-binding.
+At position 923 to 1265, the domain is characterized as AdoMet activation.
+At position 342 to 418, the domain is characterized as HTH rpiR-type.
+At position 462 to 601, the domain is characterized as SIS.
+At position 38 to 124, the domain is characterized as PAN.
+At position 129 to 207, the domain is characterized as Kringle 1.
+At position 212 to 289, the domain is characterized as Kringle 2.
+At position 306 to 384, the domain is characterized as Kringle 3.
+At position 392 to 470, the domain is characterized as Kringle 4.
+At position 496 to 724, the domain is characterized as Peptidase S1.
+At position 26 to 193, the domain is characterized as PCI.
+At position 11 to 122, the domain is characterized as DUSP.
+At position 142 to 226, the domain is characterized as Ubiquitin-like 1.
+At position 302 to 923, the domain is characterized as USP.
+At position 483 to 571, the domain is characterized as Ubiquitin-like 2.
+At position 82 to 246, the domain is characterized as Helicase ATP-binding.
+At position 271 to 451, the domain is characterized as Helicase C-terminal.
+At position 127 to 202, the domain is characterized as HTH OST-type 2.
+At position 297 to 371, the domain is characterized as HTH OST-type 3.
+At position 527 to 586, the domain is characterized as Tudor.
+At position 2 to 97, the domain is characterized as Core-binding (CB).
+At position 118 to 300, the domain is characterized as Tyr recombinase.
+At position 6 to 54, the domain is characterized as F-box.
+At position 64 to 256, the domain is characterized as B30.2/SPRY.
+At position 170 to 255, the domain is characterized as PPIase FKBP-type.
+At position 18 to 73, the domain is characterized as Myb-like.
+At position 136 to 192, the domain is characterized as HTH myb-type.
+At position 40 to 193, the domain is characterized as Ferritin-like diiron.
+At position 209 to 295, the domain is characterized as Ig-like C1-type.
+At position 341 to 508, the domain is characterized as tr-type G.
+At position 170 to 406, the domain is characterized as NR LBD.
+At position 52 to 115, the domain is characterized as KH 1.
+At position 124 to 190, the domain is characterized as KH 2.
+At position 353 to 412, the domain is characterized as Tudor.
+At position 66 to 292, the domain is characterized as OBG-type G.
+At position 292 to 368, the domain is characterized as TGS.
+At position 11 to 92, the domain is characterized as Carrier.
+At position 84 to 143, the domain is characterized as S4 RNA-binding.
+At position 283 to 561, the domain is characterized as ABC transmembrane type-1 1.
+At position 626 to 853, the domain is characterized as ABC transporter 1.
+At position 933 to 1182, the domain is characterized as ABC transmembrane type-1 2.
+At position 1219 to 1449, the domain is characterized as ABC transporter 2.
+At position 73 to 217, the domain is characterized as HD.
+At position 7 to 129, the domain is characterized as CMP/dCMP-type deaminase.
+At position 583 to 689, the domain is characterized as tRNA-binding.
+At position 44 to 249, the domain is characterized as BPL/LPL catalytic.
+At position 172 to 204, the domain is characterized as LisH.
+At position 206 to 258, the domain is characterized as CTLH.
+At position 25 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 5 to 89, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 87 to 138, the domain is characterized as FHA.
+At position 40 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 599 to 679, the domain is characterized as BRCT.
+At position 10 to 173, the domain is characterized as uDENN.
+At position 195 to 360, the domain is characterized as cDENN.
+At position 362 to 464, the domain is characterized as dDENN.
+At position 14 to 70, the domain is characterized as CBS 1.
+At position 79 to 138, the domain is characterized as CBS 2.
+At position 31 to 172, the domain is characterized as MATH.
+At position 193 to 503, the domain is characterized as USP.
+At position 353 to 623, the domain is characterized as Protein kinase.
+At position 93 to 350, the domain is characterized as Protein kinase 1.
+At position 351 to 420, the domain is characterized as AGC-kinase C-terminal.
+At position 446 to 706, the domain is characterized as Protein kinase 2.
+At position 183 to 295, the domain is characterized as MaoC-like.
+At position 465 to 778, the domain is characterized as Deacetylase sirtuin-type.
+At position 2 to 113, the domain is characterized as WH1.
+At position 193 to 228, the domain is characterized as UVR.
+At position 16 to 105, the domain is characterized as PI3K-ABD.
+At position 187 to 289, the domain is characterized as PI3K-RBD.
+At position 330 to 487, the domain is characterized as C2 PI3K-type.
+At position 517 to 694, the domain is characterized as PIK helical.
+At position 765 to 1051, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 66, the domain is characterized as Ubiquitin-like.
+At position 1 to 153, the domain is characterized as CRAL-TRIO.
+At position 4 to 65, the domain is characterized as HTH asnC-type.
+At position 427 to 603, the domain is characterized as Helicase ATP-binding.
+At position 834 to 999, the domain is characterized as Helicase C-terminal.
+At position 9 to 181, the domain is characterized as Ku.
+At position 150 to 192, the domain is characterized as LRRCT.
+At position 115 to 237, the domain is characterized as MPN.
+At position 55 to 133, the domain is characterized as Lipoyl-binding.
+At position 187 to 224, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 50 to 231, the domain is characterized as Laminin G-like.
+At position 375 to 424, the domain is characterized as Collagen-like 1.
+At position 590 to 643, the domain is characterized as Collagen-like 2.
+At position 676 to 725, the domain is characterized as Collagen-like 3.
+At position 797 to 848, the domain is characterized as Collagen-like 4.
+At position 1006 to 1063, the domain is characterized as Collagen-like 5.
+At position 1210 to 1263, the domain is characterized as Collagen-like 6.
+At position 1350 to 1407, the domain is characterized as Collagen-like 7.
+At position 1448 to 1500, the domain is characterized as Collagen-like 8.
+At position 1504 to 1552, the domain is characterized as Collagen-like 9.
+At position 29 to 74, the domain is characterized as WAP 1.
+At position 125 to 173, the domain is characterized as WAP 2.
+At position 652 to 908, the domain is characterized as Protein kinase.
+At position 457 to 570, the domain is characterized as PAZ.
+At position 746 to 1067, the domain is characterized as Piwi.
+At position 55 to 98, the domain is characterized as CWF21.
+At position 29 to 207, the domain is characterized as Eph LBD.
+At position 325 to 435, the domain is characterized as Fibronectin type-III 1.
+At position 436 to 531, the domain is characterized as Fibronectin type-III 2.
+At position 33 to 169, the domain is characterized as MPN.
+At position 21 to 63, the domain is characterized as Chitin-binding type-1.
+At position 33 to 306, the domain is characterized as Dynamin-type G.
+At position 543 to 631, the domain is characterized as GED.
+At position 62 to 356, the domain is characterized as Protein kinase.
+At position 223 to 474, the domain is characterized as Peptidase M12B.
+At position 475 to 563, the domain is characterized as Disintegrin.
+At position 20 to 255, the domain is characterized as ABC transporter 1.
+At position 268 to 511, the domain is characterized as ABC transporter 2.
+At position 70 to 114, the domain is characterized as CWF21.
+At position 11 to 347, the domain is characterized as Protein kinase.
+At position 17 to 241, the domain is characterized as ThyX.
+At position 37 to 68, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 257 to 311, the domain is characterized as TSP type-1 1.
+At position 350 to 403, the domain is characterized as TSP type-1 2.
+At position 405 to 458, the domain is characterized as TSP type-1 3.
+At position 463 to 516, the domain is characterized as TSP type-1 4.
+At position 518 to 571, the domain is characterized as TSP type-1 5.
+At position 877 to 934, the domain is characterized as GPS.
+At position 230 to 397, the domain is characterized as Helicase ATP-binding.
+At position 484 to 658, the domain is characterized as Helicase C-terminal.
+At position 1 to 60, the domain is characterized as S4 RNA-binding.
+At position 91 to 183, the domain is characterized as Ig-like C1-type.
+At position 461 to 627, the domain is characterized as JmjC.
+At position 7 to 146, the domain is characterized as ENTH.
+At position 252 to 440, the domain is characterized as GATase cobBQ-type.
+At position 411 to 440, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 478 to 496, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 307 to 361, the domain is characterized as HAMP.
+At position 378 to 589, the domain is characterized as Histidine kinase.
+At position 41 to 217, the domain is characterized as Helicase ATP-binding.
+At position 424 to 593, the domain is characterized as Helicase C-terminal.
+At position 621 to 713, the domain is characterized as Dicer dsRNA-binding fold.
+At position 886 to 1036, the domain is characterized as PAZ.
+At position 1249 to 1380, the domain is characterized as RNase III 1.
+At position 1637 to 1795, the domain is characterized as RNase III 2.
+At position 1820 to 1885, the domain is characterized as DRBM.
+At position 425 to 581, the domain is characterized as Exonuclease.
+At position 2 to 104, the domain is characterized as PINc.
+At position 3 to 74, the domain is characterized as PINc.
+At position 157 to 390, the domain is characterized as Radical SAM core.
+At position 220 to 376, the domain is characterized as TrmE-type G.
+At position 1 to 218, the domain is characterized as SMP-LTD.
+At position 199 to 355, the domain is characterized as JmjC.
+At position 19 to 182, the domain is characterized as TIR.
+At position 28 to 251, the domain is characterized as RNase H type-2.
+At position 48 to 156, the domain is characterized as SH2.
+At position 151 to 197, the domain is characterized as SOCS box.
+At position 49 to 332, the domain is characterized as AB hydrolase-1.
+At position 9 to 144, the domain is characterized as UBC core.
+At position 51 to 86, the domain is characterized as EF-hand 2.
+At position 128 to 160, the domain is characterized as EF-hand 4.
+At position 749 to 831, the domain is characterized as BRCT.
+At position 101 to 347, the domain is characterized as Radical SAM core.
+At position 1 to 92, the domain is characterized as ATP-cone.
+At position 158 to 242, the domain is characterized as PPIase FKBP-type.
+At position 88 to 224, the domain is characterized as C1q.
+At position 6 to 68, the domain is characterized as HTH IS21-type.
+At position 122 to 302, the domain is characterized as Integrase catalytic.
+At position 566 to 726, the domain is characterized as PI-PLC X-box.
+At position 794 to 912, the domain is characterized as PI-PLC Y-box.
+At position 917 to 1071, the domain is characterized as C2.
+At position 24 to 145, the domain is characterized as MTTase N-terminal.
+At position 172 to 404, the domain is characterized as Radical SAM core.
+At position 407 to 469, the domain is characterized as TRAM.
+At position 118 to 286, the domain is characterized as Helicase ATP-binding.
+At position 450 to 619, the domain is characterized as Helicase C-terminal.
+At position 96 to 285, the domain is characterized as Helicase ATP-binding.
+At position 580 to 743, the domain is characterized as Toprim.
+At position 112 to 198, the domain is characterized as PNT.
+At position 90 to 140, the domain is characterized as DHHC.
+At position 1 to 164, the domain is characterized as BAH.
+At position 165 to 276, the domain is characterized as ELM2.
+At position 283 to 335, the domain is characterized as SANT.
+At position 87 to 145, the domain is characterized as TCP.
+At position 216 to 233, the domain is characterized as R.
+At position 103 to 418, the domain is characterized as RHD.
+At position 19 to 115, the domain is characterized as GS beta-grasp.
+At position 122 to 459, the domain is characterized as GS catalytic.
+At position 133 to 391, the domain is characterized as Protein kinase.
+At position 434 to 469, the domain is characterized as EF-hand 1.
+At position 470 to 505, the domain is characterized as EF-hand 2.
+At position 506 to 541, the domain is characterized as EF-hand 3.
+At position 544 to 575, the domain is characterized as EF-hand 4.
+At position 17 to 154, the domain is characterized as MARVEL 1.
+At position 159 to 303, the domain is characterized as MARVEL 2.
+At position 13 to 157, the domain is characterized as uDENN.
+At position 182 to 318, the domain is characterized as cDENN.
+At position 320 to 398, the domain is characterized as dDENN.
+At position 34 to 158, the domain is characterized as AB hydrolase-1.
+At position 57 to 183, the domain is characterized as Plastocyanin-like.
+At position 9 to 229, the domain is characterized as DHFR.
+At position 80 to 120, the domain is characterized as UBA.
+At position 42 to 96, the domain is characterized as HTH cro/C1-type.
+At position 238 to 466, the domain is characterized as NR LBD.
+At position 73 to 167, the domain is characterized as CS.
+At position 168 to 228, the domain is characterized as SGS.
+At position 1 to 85, the domain is characterized as PDZ.
+At position 280 to 338, the domain is characterized as LIM zinc-binding 1.
+At position 339 to 398, the domain is characterized as LIM zinc-binding 2.
+At position 399 to 457, the domain is characterized as LIM zinc-binding 3.
+At position 208 to 388, the domain is characterized as Helicase ATP-binding.
+At position 419 to 578, the domain is characterized as Helicase C-terminal.
+At position 57 to 120, the domain is characterized as S5 DRBM.
+At position 624 to 812, the domain is characterized as SEC7.
+At position 63 to 130, the domain is characterized as BTB.
+At position 165 to 267, the domain is characterized as BACK.
+At position 47 to 145, the domain is characterized as GOLD.
+At position 388 to 463, the domain is characterized as Rhodanese.
+At position 1 to 164, the domain is characterized as Protein kinase.
+At position 6 to 249, the domain is characterized as ABC transporter.
+At position 2 to 126, the domain is characterized as VOC.
+At position 6 to 169, the domain is characterized as Ku.
+At position 485 to 923, the domain is characterized as USP.
+At position 974 to 1146, the domain is characterized as Exonuclease.
+At position 456 to 656, the domain is characterized as FtsK 1.
+At position 813 to 1004, the domain is characterized as FtsK 2.
+At position 1099 to 1282, the domain is characterized as FtsK 3.
+At position 278 to 339, the domain is characterized as SH3.
+At position 1353 to 1388, the domain is characterized as EF-hand.
+At position 39 to 101, the domain is characterized as KH 1.
+At position 117 to 182, the domain is characterized as KH 2.
+At position 351 to 415, the domain is characterized as KH 3.
+At position 60 to 213, the domain is characterized as Cupin type-1.
+At position 34 to 101, the domain is characterized as DRBM 1.
+At position 126 to 194, the domain is characterized as DRBM 2.
+At position 240 to 308, the domain is characterized as DRBM 3.
+At position 178 to 225, the domain is characterized as F-box.
+At position 40 to 191, the domain is characterized as Cupin type-1.
+At position 457 to 590, the domain is characterized as Thioredoxin.
+At position 279 to 340, the domain is characterized as SH3.
+At position 451 to 510, the domain is characterized as SH3.
+At position 7 to 70, the domain is characterized as HMA.
+At position 30 to 190, the domain is characterized as PPIase cyclophilin-type.
+At position 4 to 78, the domain is characterized as Lipoyl-binding 1.
+At position 122 to 196, the domain is characterized as Lipoyl-binding 2.
+At position 250 to 287, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 284 to 513, the domain is characterized as AIG1-type G.
+At position 20 to 78, the domain is characterized as Chromo 1.
+At position 121 to 179, the domain is characterized as Chromo 2; shadow subtype.
+At position 35 to 109, the domain is characterized as Cystatin.
+At position 2 to 252, the domain is characterized as ABC transporter 1.
+At position 320 to 526, the domain is characterized as ABC transporter 2.
+At position 38 to 270, the domain is characterized as Peptidase S1.
+At position 5 to 84, the domain is characterized as GST N-terminal.
+At position 97 to 220, the domain is characterized as GST C-terminal.
+At position 9 to 257, the domain is characterized as Pyruvate carboxyltransferase.
+At position 337 to 424, the domain is characterized as PDZ.
+At position 305 to 513, the domain is characterized as PCI.
+At position 107 to 293, the domain is characterized as CNNM transmembrane.
+At position 317 to 381, the domain is characterized as CBS 1.
+At position 394 to 461, the domain is characterized as CBS 2.
+At position 23 to 357, the domain is characterized as Transferrin-like 1.
+At position 366 to 706, the domain is characterized as Transferrin-like 2.
+At position 97 to 327, the domain is characterized as Radical SAM core.
+At position 28 to 241, the domain is characterized as MIF4G.
+At position 230 to 489, the domain is characterized as Olfactomedin-like.
+At position 570 to 624, the domain is characterized as F-box.
+At position 469 to 505, the domain is characterized as CBM1.
+At position 14 to 85, the domain is characterized as KRAB 1.
+At position 161 to 243, the domain is characterized as SCAN box.
+At position 287 to 360, the domain is characterized as KRAB 2.
+At position 803 to 914, the domain is characterized as N-terminal Ras-GEF.
+At position 4 to 285, the domain is characterized as Protein kinase.
+At position 14 to 193, the domain is characterized as YrdC-like.
+At position 53 to 165, the domain is characterized as Plastocyanin-like 1.
+At position 229 to 295, the domain is characterized as Plastocyanin-like 2.
+At position 424 to 536, the domain is characterized as Plastocyanin-like 3.
+At position 28 to 91, the domain is characterized as Clip.
+At position 138 to 399, the domain is characterized as Peptidase S1.
+At position 615 to 842, the domain is characterized as PARP catalytic.
+At position 80 to 293, the domain is characterized as Peptidase S1.
+At position 371 to 400, the domain is characterized as IQ.
+At position 11 to 151, the domain is characterized as N-acetyltransferase 1.
+At position 154 to 337, the domain is characterized as N-acetyltransferase 2.
+At position 384 to 659, the domain is characterized as Protein kinase.
+At position 101 to 293, the domain is characterized as Rab-GAP TBC.
+At position 5 to 123, the domain is characterized as Response regulatory.
+At position 27 to 74, the domain is characterized as WAP.
+At position 134 to 397, the domain is characterized as Radical SAM core.
+At position 7 to 57, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 63 to 113, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 176 to 215, the domain is characterized as DSL.
+At position 216 to 249, the domain is characterized as EGF-like 1.
+At position 274 to 310, the domain is characterized as EGF-like 2.
+At position 312 to 351, the domain is characterized as EGF-like 3.
+At position 353 to 389, the domain is characterized as EGF-like 4.
+At position 391 to 427, the domain is characterized as EGF-like 5.
+At position 429 to 465, the domain is characterized as EGF-like 6.
+At position 12 to 94, the domain is characterized as PDZ 1.
+At position 143 to 225, the domain is characterized as PDZ 2.
+At position 458 to 624, the domain is characterized as JmjC.
+At position 69 to 163, the domain is characterized as SH2.
+At position 456 to 598, the domain is characterized as VPS9.
+At position 624 to 706, the domain is characterized as Ras-associating.
+At position 40 to 223, the domain is characterized as Helicase ATP-binding.
+At position 254 to 402, the domain is characterized as Helicase C-terminal.
+At position 61 to 166, the domain is characterized as FAD-binding FR-type.
+At position 2 to 28, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 56 to 161, the domain is characterized as Expansin-like EG45.
+At position 175 to 258, the domain is characterized as Expansin-like CBD.
+At position 948 to 1232, the domain is characterized as Protein kinase.
+At position 97 to 281, the domain is characterized as ABC transmembrane type-1.
+At position 188 to 208, the domain is characterized as ELK.
+At position 58 to 250, the domain is characterized as B30.2/SPRY.
+At position 26 to 267, the domain is characterized as Radical SAM core.
+At position 132 to 326, the domain is characterized as ATP-grasp.
+At position 34 to 94, the domain is characterized as Clip.
+At position 135 to 399, the domain is characterized as Peptidase S1.
+At position 9 to 254, the domain is characterized as ABC transporter.
+At position 13 to 90, the domain is characterized as GIY-YIG.
+At position 51 to 152, the domain is characterized as DUSP.
+At position 311 to 977, the domain is characterized as USP.
+At position 113 to 446, the domain is characterized as Kinesin motor.
+At position 6 to 206, the domain is characterized as tr-type G.
+At position 50 to 288, the domain is characterized as Ras-GEF.
+At position 458 to 570, the domain is characterized as PH.
+At position 128 to 177, the domain is characterized as bHLH.
+At position 18 to 117, the domain is characterized as HD.
+At position 360 to 421, the domain is characterized as TGS.
+At position 601 to 675, the domain is characterized as ACT.
+At position 1 to 115, the domain is characterized as MTTase N-terminal.
+At position 134 to 367, the domain is characterized as Radical SAM core.
+At position 370 to 436, the domain is characterized as TRAM.
+At position 21 to 130, the domain is characterized as Thioredoxin 1.
+At position 342 to 470, the domain is characterized as Thioredoxin 2.
+At position 233 to 501, the domain is characterized as Peptidase M66.
+At position 97 to 183, the domain is characterized as Doublecortin.
+At position 514 to 771, the domain is characterized as Protein kinase.
+At position 56 to 381, the domain is characterized as G-alpha.
+At position 1366 to 1491, the domain is characterized as BEACH-type PH.
+At position 1504 to 1795, the domain is characterized as BEACH.
+At position 60 to 166, the domain is characterized as THUMP.
+At position 103 to 380, the domain is characterized as Protein kinase.
+At position 133 to 374, the domain is characterized as Radical SAM core.
+At position 82 to 332, the domain is characterized as Protein kinase.
+At position 1 to 131, the domain is characterized as PTS EIIA type-4.
+At position 44 to 133, the domain is characterized as ACB.
+At position 2 to 145, the domain is characterized as C2 NT-type.
+At position 72 to 138, the domain is characterized as ACT 1.
+At position 260 to 321, the domain is characterized as ACT 2.
+At position 102 to 267, the domain is characterized as JmjC.
+At position 80 to 174, the domain is characterized as Fe2OG dioxygenase.
+At position 174 to 518, the domain is characterized as USP.
+At position 143 to 210, the domain is characterized as GRAM 1.
+At position 283 to 351, the domain is characterized as GRAM 2.
+At position 469 to 656, the domain is characterized as Rab-GAP TBC.
+At position 822 to 857, the domain is characterized as EF-hand.
+At position 41 to 374, the domain is characterized as G-alpha.
+At position 44 to 141, the domain is characterized as Ig-like.
+At position 155 to 238, the domain is characterized as Ig-like C2-type.
+At position 242 to 296, the domain is characterized as TSP type-1 1.
+At position 298 to 350, the domain is characterized as TSP type-1 2.
+At position 497 to 640, the domain is characterized as ZU5.
+At position 817 to 897, the domain is characterized as Death.
+At position 134 to 196, the domain is characterized as 4Fe-4S.
+At position 22 to 809, the domain is characterized as Vitellogenin.
+At position 1442 to 1635, the domain is characterized as VWFD.
+At position 17 to 127, the domain is characterized as MTTase N-terminal.
+At position 146 to 383, the domain is characterized as Radical SAM core.
+At position 386 to 451, the domain is characterized as TRAM.
+At position 7 to 134, the domain is characterized as RNase III.
+At position 485 to 521, the domain is characterized as CBM1.
+At position 569 to 588, the domain is characterized as WH2.
+At position 53 to 241, the domain is characterized as B30.2/SPRY.
+At position 272 to 304, the domain is characterized as LisH.
+At position 305 to 362, the domain is characterized as CTLH.
+At position 54 to 142, the domain is characterized as PPIase FKBP-type 1.
+At position 166 to 254, the domain is characterized as PPIase FKBP-type 2.
+At position 278 to 365, the domain is characterized as PPIase FKBP-type 3.
+At position 389 to 477, the domain is characterized as PPIase FKBP-type 4.
+At position 488 to 523, the domain is characterized as EF-hand 1.
+At position 533 to 568, the domain is characterized as EF-hand 2.
+At position 30 to 165, the domain is characterized as MPN.
+At position 162 to 415, the domain is characterized as NR LBD.
+At position 1 to 352, the domain is characterized as Helicase ATP-binding.
+At position 366 to 632, the domain is characterized as ZP.
+At position 4 to 250, the domain is characterized as ABC transporter.
+At position 27 to 77, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 4 to 431, the domain is characterized as Helicase ATP-binding.
+At position 1 to 60, the domain is characterized as 4Fe-4S.
+At position 174 to 276, the domain is characterized as PpiC 1.
+At position 289 to 388, the domain is characterized as PpiC 2.
+At position 27 to 96, the domain is characterized as S4 RNA-binding.
+At position 2 to 102, the domain is characterized as FAD-binding FR-type.
+At position 22 to 327, the domain is characterized as Protein kinase.
+At position 77 to 152, the domain is characterized as WWE.
+At position 245 to 463, the domain is characterized as PARP catalytic.
+At position 497 to 568, the domain is characterized as RST.
+At position 37 to 188, the domain is characterized as Tyrosine-protein phosphatase.
+At position 100 to 142, the domain is characterized as CAP-Gly 1.
+At position 240 to 282, the domain is characterized as CAP-Gly 2.
+At position 143 to 506, the domain is characterized as GRAS.
+At position 309 to 586, the domain is characterized as ABC transporter 1.
+At position 606 to 936, the domain is characterized as ABC transporter 2.
+At position 205 to 251, the domain is characterized as F-box.
+At position 12 to 53, the domain is characterized as UBA.
+At position 252 to 394, the domain is characterized as VPS9.
+At position 30 to 100, the domain is characterized as BTB.
+At position 217 to 257, the domain is characterized as P-type.
+At position 262 to 533, the domain is characterized as ZP.
+At position 8 to 166, the domain is characterized as N-acetyltransferase.
+At position 56 to 166, the domain is characterized as Expansin-like EG45.
+At position 179 to 265, the domain is characterized as Expansin-like CBD.
+At position 50 to 287, the domain is characterized as Laminin N-terminal.
+At position 288 to 354, the domain is characterized as Laminin EGF-like 1.
+At position 355 to 417, the domain is characterized as Laminin EGF-like 2.
+At position 418 to 477, the domain is characterized as Laminin EGF-like 3.
+At position 478 to 528, the domain is characterized as Laminin EGF-like 4.
+At position 529 to 559, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 567 to 783, the domain is characterized as Laminin IV type B.
+At position 789 to 836, the domain is characterized as Laminin EGF-like 6.
+At position 837 to 882, the domain is characterized as Laminin EGF-like 7.
+At position 883 to 932, the domain is characterized as Laminin EGF-like 8.
+At position 933 to 990, the domain is characterized as Laminin EGF-like 9.
+At position 991 to 1042, the domain is characterized as Laminin EGF-like 10.
+At position 1043 to 1093, the domain is characterized as Laminin EGF-like 11.
+At position 1094 to 1141, the domain is characterized as Laminin EGF-like 12.
+At position 1142 to 1188, the domain is characterized as Laminin EGF-like 13.
+At position 10 to 283, the domain is characterized as tr-type G.
+At position 311 to 387, the domain is characterized as RRM 1.
+At position 411 to 492, the domain is characterized as RRM 2.
+At position 9 to 141, the domain is characterized as RNase III.
+At position 168 to 237, the domain is characterized as DRBM.
+At position 6 to 166, the domain is characterized as UBC core.
+At position 89 to 179, the domain is characterized as K-box.
+At position 512 to 667, the domain is characterized as HNH Cas9-type.
+At position 11 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 203 to 392, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 235, the domain is characterized as Radical SAM core.
+At position 76 to 121, the domain is characterized as SpoVT-AbrB 2.
+At position 15 to 130, the domain is characterized as MTTase N-terminal.
+At position 147 to 392, the domain is characterized as Radical SAM core.
+At position 395 to 463, the domain is characterized as TRAM.
+At position 17 to 95, the domain is characterized as RRM 1.
+At position 109 to 196, the domain is characterized as RRM 2.
+At position 242 to 322, the domain is characterized as RRM 3.
+At position 20 to 95, the domain is characterized as Importin N-terminal.
+At position 61 to 281, the domain is characterized as Fibrinogen C-terminal.
+At position 1649 to 1952, the domain is characterized as Autotransporter.
+At position 1 to 212, the domain is characterized as START.
+At position 210 to 383, the domain is characterized as EngA-type G 2.
+At position 384 to 468, the domain is characterized as KH-like.
+At position 66 to 124, the domain is characterized as CBS 1.
+At position 132 to 187, the domain is characterized as CBS 2.
+At position 228 to 287, the domain is characterized as CBS 3.
+At position 295 to 354, the domain is characterized as CBS 4.
+At position 406 to 489, the domain is characterized as PB1.
+At position 473 to 685, the domain is characterized as FtsK.
+At position 35 to 349, the domain is characterized as G-alpha.
+At position 18 to 95, the domain is characterized as PDZ.
+At position 842 to 967, the domain is characterized as RGS.
+At position 267 to 538, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 222 to 391, the domain is characterized as Helicase ATP-binding.
+At position 540 to 693, the domain is characterized as Helicase C-terminal.
+At position 613 to 686, the domain is characterized as SH3.
+At position 284 to 551, the domain is characterized as ABC transmembrane type-1 1.
+At position 605 to 834, the domain is characterized as ABC transporter 1.
+At position 900 to 1139, the domain is characterized as ABC transmembrane type-1 2.
+At position 1218 to 1468, the domain is characterized as ABC transporter 2.
+At position 99 to 172, the domain is characterized as PRC barrel.
+At position 281 to 505, the domain is characterized as ABC transmembrane type-1.
+At position 30 to 348, the domain is characterized as Protein kinase.
+At position 350 to 592, the domain is characterized as NR LBD.
+At position 2 to 79, the domain is characterized as RRM.
+At position 15 to 139, the domain is characterized as EamA 1.
+At position 161 to 287, the domain is characterized as EamA 2.
+At position 122 to 199, the domain is characterized as FBD.
+At position 101 to 225, the domain is characterized as OTU.
+At position 281 to 493, the domain is characterized as B30.2/SPRY.
+At position 261 to 429, the domain is characterized as tr-type G.
+At position 95 to 385, the domain is characterized as ABC transmembrane type-1 1.
+At position 420 to 665, the domain is characterized as ABC transporter 1.
+At position 795 to 1083, the domain is characterized as ABC transmembrane type-1 2.
+At position 1119 to 1356, the domain is characterized as ABC transporter 2.
+At position 8 to 191, the domain is characterized as CNNM transmembrane.
+At position 210 to 271, the domain is characterized as CBS 1.
+At position 274 to 334, the domain is characterized as CBS 2.
+At position 366 to 435, the domain is characterized as CBS 3.
+At position 204 to 260, the domain is characterized as FHA.
+At position 1 to 62, the domain is characterized as TRAM.
+At position 178 to 360, the domain is characterized as Letm1 RBD.
+At position 5 to 70, the domain is characterized as HTH luxR-type.
+At position 19 to 103, the domain is characterized as RRM.
+At position 5 to 255, the domain is characterized as ABC transporter.
+At position 1 to 60, the domain is characterized as IBB.
+At position 122 to 183, the domain is characterized as CBS 1.
+At position 185 to 241, the domain is characterized as CBS 2.
+At position 34 to 157, the domain is characterized as EamA 1.
+At position 189 to 313, the domain is characterized as EamA 2.
+At position 49 to 175, the domain is characterized as N-terminal Ras-GEF.
+At position 201 to 432, the domain is characterized as Ras-GEF.
+At position 466 to 501, the domain is characterized as EF-hand.
+At position 8 to 79, the domain is characterized as KRAB.
+At position 62 to 280, the domain is characterized as ABC transmembrane type-1.
+At position 232 to 295, the domain is characterized as SOCS box.
+At position 20 to 162, the domain is characterized as SprT-like.
+At position 165 to 395, the domain is characterized as SMP-LTD.
+At position 55 to 619, the domain is characterized as Lipoxygenase.
+At position 1 to 20, the domain is characterized as Pentraxin (PTX).
+At position 543 to 657, the domain is characterized as Fe2OG dioxygenase.
+At position 57 to 284, the domain is characterized as Radical SAM core.
+At position 827 to 939, the domain is characterized as OCEL.
+At position 8 to 210, the domain is characterized as tr-type G.
+At position 46 to 208, the domain is characterized as PCI.
+At position 3 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 84 to 164, the domain is characterized as RRM 1.
+At position 177 to 256, the domain is characterized as RRM 2.
+At position 295 to 367, the domain is characterized as RRM 3.
+At position 297 to 367, the domain is characterized as Mop.
+At position 45 to 142, the domain is characterized as Ig-like C2-type 1.
+At position 155 to 232, the domain is characterized as Ig-like C2-type 2.
+At position 346 to 432, the domain is characterized as Ig-like C2-type 4.
+At position 461 to 567, the domain is characterized as Fibronectin type-III 1.
+At position 575 to 670, the domain is characterized as Fibronectin type-III 2.
+At position 30 to 837, the domain is characterized as Protein kinase.
+At position 838 to 881, the domain is characterized as AGC-kinase C-terminal.
+At position 21 to 92, the domain is characterized as KH type-2.
+At position 3 to 91, the domain is characterized as CS.
+At position 45 to 160, the domain is characterized as Ricin B-type lectin.
+At position 24 to 220, the domain is characterized as Velvet.
+At position 90 to 158, the domain is characterized as Myb-like.
+At position 4 to 296, the domain is characterized as Protein kinase.
+At position 5 to 192, the domain is characterized as Flavodoxin-like.
+At position 347 to 545, the domain is characterized as B30.2/SPRY.
+At position 41 to 258, the domain is characterized as ThyX.
+At position 25 to 139, the domain is characterized as Response regulatory.
+At position 40 to 218, the domain is characterized as Helicase ATP-binding.
+At position 231 to 393, the domain is characterized as Helicase C-terminal.
+At position 123 to 173, the domain is characterized as DHHC.
+At position 124 to 162, the domain is characterized as LDL-receptor class A 1.
+At position 163 to 215, the domain is characterized as LDL-receptor class A 2.
+At position 217 to 254, the domain is characterized as LDL-receptor class A 3.
+At position 255 to 290, the domain is characterized as LDL-receptor class A 4.
+At position 293 to 330, the domain is characterized as LDL-receptor class A 5.
+At position 372 to 414, the domain is characterized as LDL-receptor class A 6.
+At position 418 to 456, the domain is characterized as LDL-receptor class A 7.
+At position 457 to 494, the domain is characterized as LDL-receptor class A 8.
+At position 28 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 99 to 151, the domain is characterized as bHLH.
+At position 214 to 424, the domain is characterized as Peptidase M12B.
+At position 433 to 515, the domain is characterized as Disintegrin.
+At position 516 to 571, the domain is characterized as TSP type-1.
+At position 4 to 137, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 402 to 528, the domain is characterized as N-terminal Ras-GEF.
+At position 727 to 944, the domain is characterized as Ras-GEF.
+At position 239 to 444, the domain is characterized as Ku.
+At position 109 to 205, the domain is characterized as Rieske.
+At position 21 to 142, the domain is characterized as EamA 1.
+At position 194 to 317, the domain is characterized as EamA 2.
+At position 44 to 100, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 251 to 536, the domain is characterized as Letm1 RBD.
+At position 662 to 697, the domain is characterized as EF-hand.
+At position 250 to 440, the domain is characterized as GATase cobBQ-type.
+At position 348 to 411, the domain is characterized as S4 RNA-binding.
+At position 58 to 401, the domain is characterized as TTL.
+At position 160 to 424, the domain is characterized as PPM-type phosphatase.
+At position 3 to 80, the domain is characterized as TFIIS N-terminal.
+At position 140 to 256, the domain is characterized as TFIIS central.
+At position 50 to 157, the domain is characterized as ZP.
+At position 171 to 338, the domain is characterized as PCI.
+At position 35 to 140, the domain is characterized as sHSP.
+At position 90 to 161, the domain is characterized as PRC barrel.
+At position 933 to 979, the domain is characterized as EGF-like.
+At position 983 to 1021, the domain is characterized as LDL-receptor class A 1.
+At position 1022 to 1062, the domain is characterized as LDL-receptor class A 2.
+At position 1063 to 1100, the domain is characterized as LDL-receptor class A 3.
+At position 1103 to 1142, the domain is characterized as LDL-receptor class A 4.
+At position 1144 to 1179, the domain is characterized as LDL-receptor class A 5.
+At position 1180 to 1224, the domain is characterized as LDL-receptor class A 6.
+At position 1230 to 1268, the domain is characterized as LDL-receptor class A 7.
+At position 1273 to 1312, the domain is characterized as LDL-receptor class A 8.
+At position 1324 to 1362, the domain is characterized as LDL-receptor class A 9.
+At position 1376 to 1415, the domain is characterized as LDL-receptor class A 10.
+At position 1419 to 1457, the domain is characterized as LDL-receptor class A 11.
+At position 1463 to 1555, the domain is characterized as Fibronectin type-III 1.
+At position 1559 to 1592, the domain is characterized as Fibronectin type-III 2.
+At position 5 to 71, the domain is characterized as J.
+At position 39 to 327, the domain is characterized as tr-type G.
+At position 513 to 786, the domain is characterized as Protein kinase.
+At position 861 to 991, the domain is characterized as Guanylate cyclase.
+At position 483 to 546, the domain is characterized as bZIP.
+At position 12 to 110, the domain is characterized as HTH araC/xylS-type.
+At position 46 to 130, the domain is characterized as RRM.
+At position 39 to 218, the domain is characterized as uDENN.
+At position 244 to 369, the domain is characterized as cDENN.
+At position 371 to 504, the domain is characterized as dDENN.
+At position 4 to 171, the domain is characterized as N-acetyltransferase.
+At position 143 to 344, the domain is characterized as ATP-grasp.
+At position 251 to 451, the domain is characterized as GATase cobBQ-type.
+At position 143 to 318, the domain is characterized as CRAL-TRIO.
+At position 161 to 201, the domain is characterized as UBA 1.
+At position 297 to 338, the domain is characterized as UBA 2.
+At position 5 to 101, the domain is characterized as Fibronectin type-III 1.
+At position 107 to 200, the domain is characterized as Fibronectin type-III 2.
+At position 272 to 547, the domain is characterized as Protein kinase.
+At position 246 to 327, the domain is characterized as Toprim.
+At position 27 to 269, the domain is characterized as ABC transporter.
+At position 438 to 707, the domain is characterized as Radical SAM core.
+At position 128 to 194, the domain is characterized as Mop 1.
+At position 200 to 266, the domain is characterized as Mop 2.
+At position 1 to 92, the domain is characterized as B12-binding N-terminal.
+At position 94 to 216, the domain is characterized as B12-binding.
+At position 7 to 82, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 19 to 207, the domain is characterized as ABC transmembrane type-1.
+At position 30 to 73, the domain is characterized as P-type.
+At position 29 to 92, the domain is characterized as HMA.
+At position 27 to 112, the domain is characterized as MtN3/slv 1.
+At position 147 to 229, the domain is characterized as MtN3/slv 2.
+At position 11 to 279, the domain is characterized as tr-type G.
+At position 281 to 339, the domain is characterized as GYF.
+At position 105 to 176, the domain is characterized as PA.
+At position 11 to 90, the domain is characterized as GIY-YIG.
+At position 200 to 235, the domain is characterized as UVR.
+At position 55 to 213, the domain is characterized as Thioredoxin.
+At position 8 to 286, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 514 to 569, the domain is characterized as PSI.
+At position 116 to 294, the domain is characterized as CRAL-TRIO.
+At position 270 to 404, the domain is characterized as GOLD.
+At position 226 to 274, the domain is characterized as Fibronectin type-II 1.
+At position 284 to 332, the domain is characterized as Fibronectin type-II 2.
+At position 343 to 391, the domain is characterized as Fibronectin type-II 3.
+At position 303 to 388, the domain is characterized as SCD.
+At position 1 to 258, the domain is characterized as F-BAR.
+At position 458 to 547, the domain is characterized as SH2.
+At position 559 to 820, the domain is characterized as Protein kinase.
+At position 1 to 160, the domain is characterized as Obg.
+At position 161 to 328, the domain is characterized as OBG-type G.
+At position 349 to 424, the domain is characterized as OCT.
+At position 536 to 667, the domain is characterized as AXH.
+At position 341 to 405, the domain is characterized as S4 RNA-binding.
+At position 25 to 126, the domain is characterized as Ig-like V-type.
+At position 6 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 48 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 145 to 304, the domain is characterized as N-acetyltransferase.
+At position 24 to 819, the domain is characterized as Vitellogenin.
+At position 1448 to 1636, the domain is characterized as VWFD.
+At position 315 to 498, the domain is characterized as PCI.
+At position 51 to 265, the domain is characterized as Cupin type-1 1.
+At position 326 to 475, the domain is characterized as Cupin type-1 2.
+At position 20 to 125, the domain is characterized as Ig-like.
+At position 45 to 108, the domain is characterized as S5 DRBM.
+At position 502 to 803, the domain is characterized as UvrD-like helicase C-terminal.
+At position 15 to 130, the domain is characterized as NTF2.
+At position 6 to 94, the domain is characterized as Acylphosphatase-like.
+At position 239 to 317, the domain is characterized as RRM.
+At position 140 to 362, the domain is characterized as Radical SAM core.
+At position 17 to 54, the domain is characterized as RIIa.
+At position 6 to 164, the domain is characterized as Thioredoxin.
+At position 69 to 258, the domain is characterized as ABC transmembrane type-1.
+At position 3 to 64, the domain is characterized as TGS.
+At position 422 to 715, the domain is characterized as Tyrosine-protein phosphatase.
+At position 5 to 50, the domain is characterized as SpoVT-AbrB.
+At position 10 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 201 to 390, the domain is characterized as GMPS ATP-PPase.
+At position 5 to 151, the domain is characterized as N-acetyltransferase 1.
+At position 214 to 365, the domain is characterized as N-acetyltransferase 2.
+At position 1553 to 1891, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1895 to 2211, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 482 to 554, the domain is characterized as ACT.
+At position 1139 to 1242, the domain is characterized as PH.
+At position 15 to 74, the domain is characterized as SH3.
+At position 110 to 294, the domain is characterized as DH.
+At position 325 to 432, the domain is characterized as PH.
+At position 35 to 164, the domain is characterized as PTB.
+At position 477 to 536, the domain is characterized as SH3.
+At position 40 to 82, the domain is characterized as CHCH.
+At position 1 to 412, the domain is characterized as BRO1.
+At position 1 to 135, the domain is characterized as CID.
+At position 28 to 90, the domain is characterized as LIM zinc-binding 1.
+At position 101 to 333, the domain is characterized as ATP-grasp.
+At position 18 to 186, the domain is characterized as EngB-type G.
+At position 60 to 165, the domain is characterized as FAD-binding FR-type.
+At position 165 to 239, the domain is characterized as PPIase FKBP-type.
+At position 693 to 728, the domain is characterized as Anaphylatoxin-like.
+At position 1518 to 1661, the domain is characterized as NTR.
+At position 37 to 169, the domain is characterized as RUN.
+At position 22 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 113 to 436, the domain is characterized as AB hydrolase-1.
+At position 472 to 542, the domain is characterized as PAS.
+At position 598 to 928, the domain is characterized as Reverse transcriptase.
+At position 530 to 601, the domain is characterized as KHA.
+At position 33 to 114, the domain is characterized as GST N-terminal.
+At position 120 to 252, the domain is characterized as GST C-terminal.
+At position 99 to 170, the domain is characterized as S4 RNA-binding.
+At position 3 to 62, the domain is characterized as CSD.
+At position 26 to 112, the domain is characterized as Disintegrin.
+At position 224 to 478, the domain is characterized as ATP-grasp.
+At position 12 to 249, the domain is characterized as ABC transporter 1.
+At position 259 to 504, the domain is characterized as ABC transporter 2.
+At position 33 to 106, the domain is characterized as KRAB.
+At position 35 to 192, the domain is characterized as SIS.
+At position 338 to 664, the domain is characterized as ABC transmembrane type-1 1.
+At position 700 to 949, the domain is characterized as ABC transporter 1.
+At position 1028 to 1351, the domain is characterized as ABC transmembrane type-1 2.
+At position 1392 to 1649, the domain is characterized as ABC transporter 2.
+At position 50 to 143, the domain is characterized as Rhodanese.
+At position 30 to 277, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 18 to 100, the domain is characterized as SCAN box.
+At position 3 to 79, the domain is characterized as Cytochrome b5 heme-binding.
+At position 65 to 147, the domain is characterized as RRM.
+At position 1 to 449, the domain is characterized as ADPK.
+At position 159 to 259, the domain is characterized as Fe2OG dioxygenase.
+At position 26 to 335, the domain is characterized as SET.
+At position 12 to 48, the domain is characterized as UBA-like.
+At position 59 to 273, the domain is characterized as DCUN1.
+At position 458 to 599, the domain is characterized as SIS 2.
+At position 36 to 94, the domain is characterized as VWFC.
+At position 1252 to 1486, the domain is characterized as Fibrillar collagen NC1.
+At position 175 to 239, the domain is characterized as KH.
+At position 283 to 394, the domain is characterized as SCP.
+At position 57 to 353, the domain is characterized as tr-type G.
+At position 489 to 581, the domain is characterized as Carrier.
+At position 15 to 245, the domain is characterized as Phosphagen kinase C-terminal.
+At position 1 to 21, the domain is characterized as ELK.
+At position 307 to 383, the domain is characterized as RRM 1.
+At position 393 to 466, the domain is characterized as RRM 2.
+At position 486 to 560, the domain is characterized as RRM 3.
+At position 572 to 647, the domain is characterized as RRM 4.
+At position 24 to 223, the domain is characterized as Pentraxin (PTX).
+At position 183 to 236, the domain is characterized as HAMP.
+At position 279 to 415, the domain is characterized as GGDEF.
+At position 272 to 424, the domain is characterized as GAF 1.
+At position 456 to 637, the domain is characterized as GAF 2.
+At position 667 to 990, the domain is characterized as PDEase.
+At position 17 to 80, the domain is characterized as HMA.
+At position 5 to 196, the domain is characterized as AMMECR1.
+At position 14 to 135, the domain is characterized as MsrB.
+At position 194 to 413, the domain is characterized as MurNAc-LAA.
+At position 23 to 73, the domain is characterized as FHA.
+At position 17 to 128, the domain is characterized as RWD.
+At position 256 to 527, the domain is characterized as Protein kinase 1.
+At position 599 to 981, the domain is characterized as Protein kinase 2.
+At position 146 to 321, the domain is characterized as Helicase ATP-binding.
+At position 335 to 495, the domain is characterized as Helicase C-terminal.
+At position 45 to 355, the domain is characterized as AB hydrolase-1.
+At position 31 to 112, the domain is characterized as Collagen-like.
+At position 115 to 245, the domain is characterized as C1q.
+At position 352 to 413, the domain is characterized as S4 RNA-binding.
+At position 14 to 94, the domain is characterized as PAS.
+At position 12 to 485, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 505 to 805, the domain is characterized as UvrD-like helicase C-terminal.
+At position 7 to 149, the domain is characterized as PPPDE.
+At position 20 to 100, the domain is characterized as Toprim.
+At position 566 to 934, the domain is characterized as Protein kinase.
+At position 935 to 1044, the domain is characterized as AGC-kinase C-terminal.
+At position 1200 to 1316, the domain is characterized as Response regulatory.
+At position 63 to 298, the domain is characterized as Laminin N-terminal.
+At position 299 to 358, the domain is characterized as Laminin EGF-like 1.
+At position 359 to 413, the domain is characterized as Laminin EGF-like 2.
+At position 414 to 460, the domain is characterized as Laminin EGF-like 3.
+At position 461 to 513, the domain is characterized as Laminin EGF-like 4.
+At position 514 to 523, the domain is characterized as Laminin EGF-like 5; first part.
+At position 533 to 709, the domain is characterized as Laminin IV type A.
+At position 710 to 743, the domain is characterized as Laminin EGF-like 5; second part.
+At position 744 to 792, the domain is characterized as Laminin EGF-like 6.
+At position 793 to 846, the domain is characterized as Laminin EGF-like 7.
+At position 847 to 901, the domain is characterized as Laminin EGF-like 8.
+At position 902 to 955, the domain is characterized as Laminin EGF-like 9.
+At position 956 to 1003, the domain is characterized as Laminin EGF-like 10.
+At position 1004 to 1049, the domain is characterized as Laminin EGF-like 11.
+At position 1025 to 1071, the domain is characterized as EGF-like.
+At position 1075 to 1113, the domain is characterized as LDL-receptor class A 1.
+At position 1114 to 1154, the domain is characterized as LDL-receptor class A 2.
+At position 1155 to 1193, the domain is characterized as LDL-receptor class A 3.
+At position 1196 to 1235, the domain is characterized as LDL-receptor class A 4.
+At position 1237 to 1271, the domain is characterized as LDL-receptor class A 5.
+At position 1272 to 1316, the domain is characterized as LDL-receptor class A 6.
+At position 1322 to 1360, the domain is characterized as LDL-receptor class A 7.
+At position 1365 to 1404, the domain is characterized as LDL-receptor class A 8.
+At position 1416 to 1454, the domain is characterized as LDL-receptor class A 9.
+At position 1468 to 1507, the domain is characterized as LDL-receptor class A 10.
+At position 1511 to 1550, the domain is characterized as LDL-receptor class A 11.
+At position 1556 to 1648, the domain is characterized as Fibronectin type-III 1.
+At position 1652 to 1744, the domain is characterized as Fibronectin type-III 2.
+At position 1748 to 1843, the domain is characterized as Fibronectin type-III 3.
+At position 1842 to 1926, the domain is characterized as Fibronectin type-III 4.
+At position 1933 to 2028, the domain is characterized as Fibronectin type-III 5.
+At position 2029 to 2117, the domain is characterized as Fibronectin type-III 6.
+At position 13 to 88, the domain is characterized as GIY-YIG.
+At position 14 to 285, the domain is characterized as Protein kinase.
+At position 399 to 467, the domain is characterized as PASTA 1.
+At position 468 to 536, the domain is characterized as PASTA 2.
+At position 540 to 601, the domain is characterized as PASTA 3.
+At position 602 to 666, the domain is characterized as PASTA 4.
+At position 133 to 175, the domain is characterized as EGF-like 1.
+At position 287 to 328, the domain is characterized as EGF-like 2; calcium-binding.
+At position 44 to 291, the domain is characterized as Peptidase S1.
+At position 33 to 64, the domain is characterized as LRRNT.
+At position 145 to 198, the domain is characterized as LRRCT.
+At position 2 to 111, the domain is characterized as Bulb-type lectin 1.
+At position 117 to 222, the domain is characterized as Bulb-type lectin 2.
+At position 47 to 90, the domain is characterized as RPE1 insert.
+At position 11 to 305, the domain is characterized as Deacetylase sirtuin-type.
+At position 72 to 260, the domain is characterized as RNase H type-2.
+At position 14 to 135, the domain is characterized as MTTase N-terminal.
+At position 179 to 410, the domain is characterized as Radical SAM core.
+At position 412 to 480, the domain is characterized as TRAM.
+At position 13 to 168, the domain is characterized as N-acetyltransferase.
+At position 104 to 415, the domain is characterized as IF rod.
+At position 43 to 108, the domain is characterized as S4 RNA-binding.
+At position 341 to 583, the domain is characterized as NR LBD.
+At position 7 to 98, the domain is characterized as HIG1.
+At position 12 to 154, the domain is characterized as SprT-like.
+At position 33 to 102, the domain is characterized as Chitin-binding type R&R.
+At position 12 to 305, the domain is characterized as FERM.
+At position 34 to 227, the domain is characterized as TLC.
+At position 57 to 241, the domain is characterized as BPL/LPL catalytic.
+At position 41 to 71, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 50 to 149, the domain is characterized as HD.
+At position 393 to 454, the domain is characterized as TGS.
+At position 655 to 729, the domain is characterized as ACT.
+At position 41 to 229, the domain is characterized as GH11.
+At position 412 to 476, the domain is characterized as SAM 1.
+At position 486 to 548, the domain is characterized as SAM 2.
+At position 560 to 703, the domain is characterized as TIR.
+At position 4 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 37 to 115, the domain is characterized as Inhibitor I9.
+At position 122 to 600, the domain is characterized as Peptidase S8.
+At position 365 to 454, the domain is characterized as PA.
+At position 125 to 179, the domain is characterized as EamA.
+At position 187 to 239, the domain is characterized as HAMP.
+At position 247 to 461, the domain is characterized as Histidine kinase.
+At position 27 to 72, the domain is characterized as WAP.
+At position 185 to 321, the domain is characterized as DBB.
+At position 6 to 82, the domain is characterized as Cytochrome b5 heme-binding.
+At position 7 to 233, the domain is characterized as ThyX.
+At position 359 to 506, the domain is characterized as Helicase C-terminal.
+At position 209 to 271, the domain is characterized as t-SNARE coiled-coil homology.
+At position 1085 to 1388, the domain is characterized as Peptidase M60.
+At position 8 to 262, the domain is characterized as Protein kinase.
+At position 42 to 171, the domain is characterized as SCP.
+At position 207 to 240, the domain is characterized as ShKT.
+At position 150 to 259, the domain is characterized as AB hydrolase-1.
+At position 144 to 337, the domain is characterized as CheB-type methylesterase.
+At position 40 to 720, the domain is characterized as Myosin motor.
+At position 724 to 744, the domain is characterized as IQ 1.
+At position 745 to 770, the domain is characterized as IQ 2.
+At position 778 to 964, the domain is characterized as TH1.
+At position 1106 to 1165, the domain is characterized as SH3.
+At position 644 to 984, the domain is characterized as PUM-HD.
+At position 188 to 417, the domain is characterized as Sigma-54 factor interaction.
+At position 159 to 442, the domain is characterized as Dynamin-type G.
+At position 2 to 190, the domain is characterized as GMPS ATP-PPase.
+At position 39 to 140, the domain is characterized as HTH araC/xylS-type.
+At position 10 to 83, the domain is characterized as HTH HARE-type.
+At position 253 to 362, the domain is characterized as DEUBAD.
+At position 68 to 389, the domain is characterized as Peptidase A1.
+At position 13 to 135, the domain is characterized as MsrB.
+At position 8 to 225, the domain is characterized as ABC transporter.
+At position 40 to 230, the domain is characterized as RHD.
+At position 815 to 901, the domain is characterized as Death.
+At position 198 to 258, the domain is characterized as KH.
+At position 324 to 419, the domain is characterized as HD.
+At position 89 to 272, the domain is characterized as FAD-binding PCMH-type.
+At position 186 to 238, the domain is characterized as bZIP.
+At position 198 to 317, the domain is characterized as Ferric oxidoreductase.
+At position 346 to 451, the domain is characterized as FAD-binding FR-type.
+At position 13 to 288, the domain is characterized as tr-type G.
+At position 31 to 91, the domain is characterized as HTH iclR-type.
+At position 106 to 278, the domain is characterized as IclR-ED.
+At position 131 to 570, the domain is characterized as Urease.
+At position 170 to 434, the domain is characterized as MHD.
+At position 546 to 658, the domain is characterized as SMC hinge.
+At position 159 to 358, the domain is characterized as OBG-type G.
+At position 112 to 386, the domain is characterized as SET.
+At position 102 to 201, the domain is characterized as FAD-binding FR-type.
+At position 9 to 249, the domain is characterized as ABC transporter.
+At position 154 to 225, the domain is characterized as KRAB.
+At position 16 to 242, the domain is characterized as AB hydrolase-1.
+At position 225 to 303, the domain is characterized as RRM.
+At position 516 to 693, the domain is characterized as W2.
+At position 2 to 113, the domain is characterized as Response regulatory.
+At position 136 to 365, the domain is characterized as Sigma-54 factor interaction.
+At position 24 to 150, the domain is characterized as EamA 1.
+At position 194 to 323, the domain is characterized as EamA 2.
+At position 1 to 38, the domain is characterized as FHA-like.
+At position 142 to 247, the domain is characterized as HIT.
+At position 770 to 872, the domain is characterized as PH.
+At position 338 to 596, the domain is characterized as Protein kinase.
+At position 581 to 640, the domain is characterized as KH.
+At position 652 to 724, the domain is characterized as S1 motif.
+At position 47 to 273, the domain is characterized as Radical SAM core.
+At position 253 to 330, the domain is characterized as KH.
+At position 25 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 109 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 312 to 399, the domain is characterized as Ig-like C2-type 4.
+At position 408 to 506, the domain is characterized as Ig-like C2-type 5.
+At position 511 to 595, the domain is characterized as Ig-like C2-type 6.
+At position 600 to 684, the domain is characterized as Ig-like C2-type 7.
+At position 22 to 1047, the domain is characterized as Zinc-hook.
+At position 229 to 377, the domain is characterized as N-acetyltransferase.
+At position 119 to 316, the domain is characterized as ATP-grasp.
+At position 259 to 500, the domain is characterized as ABC transporter 2.
+At position 27 to 71, the domain is characterized as WAP.
+At position 106 to 264, the domain is characterized as Cupin type-1 1.
+At position 312 to 507, the domain is characterized as Cupin type-1 2.
+At position 218 to 445, the domain is characterized as Histidine kinase.
+At position 23 to 94, the domain is characterized as KH type-2.
+At position 27 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 151 to 216, the domain is characterized as HTH luxR-type.
+At position 22 to 136, the domain is characterized as Thioredoxin.
+At position 40 to 231, the domain is characterized as OTU.
+At position 105 to 286, the domain is characterized as Tyr recombinase.
+At position 6 to 153, the domain is characterized as N-acetyltransferase.
+At position 1648 to 1720, the domain is characterized as PAH 1.
+At position 1730 to 1801, the domain is characterized as PAH 2.
+At position 2167 to 2220, the domain is characterized as Myb-like.
+At position 59 to 164, the domain is characterized as Thioredoxin.
+At position 205 to 323, the domain is characterized as C-type lectin.
+At position 36 to 130, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 133 to 273, the domain is characterized as FAD-binding FR-type.
+At position 3 to 427, the domain is characterized as PTS EIIC type-1.
+At position 438 to 519, the domain is characterized as PTS EIIB type-1.
+At position 560 to 664, the domain is characterized as PTS EIIA type-1.
+At position 186 to 248, the domain is characterized as t-SNARE coiled-coil homology.
+At position 121 to 321, the domain is characterized as ATP-grasp.
+At position 35 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 85 to 142, the domain is characterized as Sushi 2.
+At position 147 to 205, the domain is characterized as Sushi 3.
+At position 206 to 268, the domain is characterized as Sushi 4.
+At position 13 to 266, the domain is characterized as Protein kinase.
+At position 565 to 678, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 679 to 792, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 895 to 973, the domain is characterized as POLO box.
+At position 93 to 166, the domain is characterized as PRC barrel.
+At position 178 to 321, the domain is characterized as FCP1 homology.
+At position 69 to 119, the domain is characterized as Sushi 1.
+At position 120 to 178, the domain is characterized as Sushi 2.
+At position 177 to 261, the domain is characterized as HYR.
+At position 262 to 321, the domain is characterized as Sushi 3.
+At position 101 to 298, the domain is characterized as ATP-grasp.
+At position 291 to 582, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 234, the domain is characterized as ABC transporter.
+At position 93 to 212, the domain is characterized as C-type lectin.
+At position 70 to 173, the domain is characterized as FAD-binding FR-type.
+At position 19 to 146, the domain is characterized as C-type lysozyme.
+At position 2 to 315, the domain is characterized as Asparaginase/glutaminase.
+At position 100 to 358, the domain is characterized as Protein kinase.
+At position 1 to 128, the domain is characterized as LBH.
+At position 53 to 269, the domain is characterized as Radical SAM core.
+At position 74 to 359, the domain is characterized as Protein kinase.
+At position 1 to 86, the domain is characterized as Core-binding (CB).
+At position 18 to 177, the domain is characterized as Thioredoxin.
+At position 31 to 205, the domain is characterized as SIS.
+At position 146 to 193, the domain is characterized as F-box.
+At position 921 to 938, the domain is characterized as WH2.
+At position 3 to 275, the domain is characterized as DegV.
+At position 8 to 160, the domain is characterized as Jacalin-type lectin.
+At position 112 to 267, the domain is characterized as CP-type G.
+At position 3 to 44, the domain is characterized as SpoVT-AbrB.
+At position 57 to 245, the domain is characterized as Reverse transcriptase.
+At position 460 to 590, the domain is characterized as RNase H type-1.
+At position 642 to 803, the domain is characterized as Integrase catalytic.
+At position 24 to 149, the domain is characterized as Plastocyanin-like 1.
+At position 161 to 303, the domain is characterized as Plastocyanin-like 2.
+At position 370 to 491, the domain is characterized as Plastocyanin-like 3.
+At position 30 to 166, the domain is characterized as MPN.
+At position 21 to 159, the domain is characterized as DAC.
+At position 22 to 147, the domain is characterized as Plastocyanin-like 1.
+At position 159 to 301, the domain is characterized as Plastocyanin-like 2.
+At position 368 to 490, the domain is characterized as Plastocyanin-like 3.
+At position 18 to 260, the domain is characterized as ABC transporter.
+At position 396 to 567, the domain is characterized as tr-type G.
+At position 426 to 495, the domain is characterized as bHLH.
+At position 132 to 166, the domain is characterized as SAP.
+At position 20 to 151, the domain is characterized as EamA 1.
+At position 216 to 324, the domain is characterized as EamA 2.
+At position 34 to 221, the domain is characterized as FAD-binding PCMH-type.
+At position 608 to 783, the domain is characterized as PCI.
+At position 23 to 210, the domain is characterized as B30.2/SPRY.
+At position 241 to 273, the domain is characterized as LisH.
+At position 279 to 336, the domain is characterized as CTLH.
+At position 37 to 317, the domain is characterized as Protein kinase.
+At position 1 to 84, the domain is characterized as FHA-like.
+At position 4 to 135, the domain is characterized as MSP.
+At position 683 to 763, the domain is characterized as ERCC4.
+At position 11 to 112, the domain is characterized as LOB.
+At position 277 to 335, the domain is characterized as RRM.
+At position 2213 to 2383, the domain is characterized as SPOC.
+At position 21 to 212, the domain is characterized as ABC transmembrane type-1.
+At position 62 to 462, the domain is characterized as Peptidase A1.
+At position 41 to 260, the domain is characterized as Radical SAM core.
+At position 24 to 98, the domain is characterized as Chitin-binding type R&R.
+At position 285 to 410, the domain is characterized as DOD-type homing endonuclease.
+At position 262 to 339, the domain is characterized as POU-specific.
+At position 96 to 154, the domain is characterized as S4 RNA-binding.
+At position 7 to 135, the domain is characterized as VOC 1.
+At position 160 to 328, the domain is characterized as VOC 2.
+At position 700 to 793, the domain is characterized as FDX-ACB.
+At position 19 to 122, the domain is characterized as Cystatin 1.
+At position 135 to 240, the domain is characterized as Cystatin 2.
+At position 280 to 358, the domain is characterized as PDZ 1.
+At position 745 to 827, the domain is characterized as PDZ 2.
+At position 860 to 930, the domain is characterized as PDZ 3.
+At position 46 to 92, the domain is characterized as Gla.
+At position 11 to 141, the domain is characterized as VOC 1.
+At position 151 to 303, the domain is characterized as VOC 2.
+At position 134 to 217, the domain is characterized as MtN3/slv 2.
+At position 31 to 74, the domain is characterized as P-type.
+At position 34 to 97, the domain is characterized as Kazal-like.
+At position 202 to 248, the domain is characterized as F-box.
+At position 144 to 406, the domain is characterized as Protein kinase.
+At position 448 to 484, the domain is characterized as EF-hand 1.
+At position 485 to 520, the domain is characterized as EF-hand 2.
+At position 521 to 560, the domain is characterized as EF-hand 3.
+At position 563 to 592, the domain is characterized as EF-hand 4.
+At position 78 to 252, the domain is characterized as PXA.
+At position 284 to 416, the domain is characterized as RGS.
+At position 518 to 638, the domain is characterized as PX.
+At position 3 to 148, the domain is characterized as Clp R.
+At position 30 to 290, the domain is characterized as Protein kinase.
+At position 953 to 1256, the domain is characterized as PKS/mFAS DH.
+At position 2464 to 2541, the domain is characterized as Carrier.
+At position 31 to 150, the domain is characterized as FZ.
+At position 68 to 179, the domain is characterized as Thioredoxin.
+At position 6 to 433, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 922 to 1242, the domain is characterized as PKS/mFAS DH.
+At position 2287 to 2364, the domain is characterized as Carrier.
+At position 434 to 565, the domain is characterized as Thioredoxin.
+At position 9 to 151, the domain is characterized as MABP.
+At position 215 to 265, the domain is characterized as UMA.
+At position 14 to 81, the domain is characterized as HMA.
+At position 481 to 542, the domain is characterized as LIM zinc-binding 1.
+At position 543 to 600, the domain is characterized as LIM zinc-binding 2.
+At position 601 to 671, the domain is characterized as LIM zinc-binding 3.
+At position 115 to 426, the domain is characterized as IF rod.
+At position 188 to 262, the domain is characterized as POU-specific.
+At position 153 to 317, the domain is characterized as N-acetyltransferase.
+At position 68 to 206, the domain is characterized as Flavodoxin-like.
+At position 240 to 454, the domain is characterized as FAD-binding FR-type.
+At position 412 to 482, the domain is characterized as TRAM.
+At position 127 to 242, the domain is characterized as C-type lectin.
+At position 87 to 202, the domain is characterized as C-type lectin.
+At position 23 to 77, the domain is characterized as bHLH.
+At position 16 to 230, the domain is characterized as ABC transporter.
+At position 2 to 196, the domain is characterized as UBC core.
+At position 13 to 120, the domain is characterized as VPS28 N-terminal.
+At position 124 to 220, the domain is characterized as VPS28 C-terminal.
+At position 138 to 350, the domain is characterized as ATP-grasp.
+At position 285 to 615, the domain is characterized as NR LBD.
+At position 55 to 468, the domain is characterized as USP.
+At position 4 to 75, the domain is characterized as Sm.
+At position 152 to 198, the domain is characterized as F-box.
+At position 66 to 259, the domain is characterized as ABC transmembrane type-1.
+At position 138 to 218, the domain is characterized as Ig-like V-type.
+At position 270 to 463, the domain is characterized as B30.2/SPRY.
+At position 9 to 154, the domain is characterized as Galectin.
+At position 9 to 147, the domain is characterized as DAC.
+At position 3 to 64, the domain is characterized as HTH asnC-type.
+At position 297 to 552, the domain is characterized as Protein kinase.
+At position 206 to 379, the domain is characterized as EngA-type G 2.
+At position 380 to 464, the domain is characterized as KH-like.
+At position 23 to 277, the domain is characterized as Protein kinase.
+At position 203 to 236, the domain is characterized as WW 1.
+At position 244 to 277, the domain is characterized as WW 2.
+At position 450 to 504, the domain is characterized as FF 1.
+At position 517 to 572, the domain is characterized as FF 2.
+At position 585 to 639, the domain is characterized as FF 3.
+At position 642 to 720, the domain is characterized as FF 4.
+At position 724 to 780, the domain is characterized as FF 5.
+At position 782 to 847, the domain is characterized as FF 6.
+At position 595 to 673, the domain is characterized as BRCT.
+At position 17 to 204, the domain is characterized as RNase H type-2.
+At position 143 to 318, the domain is characterized as Helicase ATP-binding.
+At position 332 to 502, the domain is characterized as Helicase C-terminal.
+At position 89 to 233, the domain is characterized as RDD.
+At position 24 to 371, the domain is characterized as DZF.
+At position 2 to 120, the domain is characterized as Chorismate mutase aroH-type.
+At position 45 to 95, the domain is characterized as KH 1.
+At position 129 to 182, the domain is characterized as KH 2.
+At position 293 to 357, the domain is characterized as KH 3.
+At position 142 to 221, the domain is characterized as RRM.
+At position 139 to 215, the domain is characterized as BCNT-C.
+At position 42 to 223, the domain is characterized as FAD-binding PCMH-type.
+At position 159 to 334, the domain is characterized as Helicase ATP-binding.
+At position 488 to 642, the domain is characterized as Helicase C-terminal.
+At position 229 to 346, the domain is characterized as PA.
+At position 265 to 402, the domain is characterized as MPN.
+At position 36 to 111, the domain is characterized as H15.
+At position 14 to 220, the domain is characterized as YjeF N-terminal.
+At position 69 to 339, the domain is characterized as PPM-type phosphatase.
+At position 613 to 691, the domain is characterized as BRCT.
+At position 1 to 124, the domain is characterized as PINc.
+At position 395 to 555, the domain is characterized as PA14.
+At position 239 to 299, the domain is characterized as SH3.
+At position 99 to 174, the domain is characterized as Smr.
+At position 6 to 78, the domain is characterized as Sm.
+At position 89 to 300, the domain is characterized as Lon N-terminal.
+At position 773 to 957, the domain is characterized as Lon proteolytic.
+At position 96 to 153, the domain is characterized as J.
+At position 419 to 534, the domain is characterized as Toprim.
+At position 442 to 505, the domain is characterized as SOCS box.
+At position 1 to 91, the domain is characterized as CARD.
+At position 185 to 376, the domain is characterized as CheB-type methylesterase.
+At position 249 to 495, the domain is characterized as ABC transporter 2.
+At position 25 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 338 to 573, the domain is characterized as ABC transporter.
+At position 43 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 133 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 322, the domain is characterized as Ig-like C2-type 3.
+At position 327 to 411, the domain is characterized as Ig-like C2-type 4.
+At position 417 to 504, the domain is characterized as Ig-like C2-type 5.
+At position 509 to 603, the domain is characterized as Ig-like C2-type 6.
+At position 610 to 708, the domain is characterized as Fibronectin type-III 1.
+At position 713 to 810, the domain is characterized as Fibronectin type-III 2.
+At position 815 to 910, the domain is characterized as Fibronectin type-III 3.
+At position 915 to 1006, the domain is characterized as Fibronectin type-III 4.
+At position 106 to 212, the domain is characterized as HTH APSES-type.
+At position 30 to 126, the domain is characterized as GOLD.
+At position 9 to 99, the domain is characterized as EH 1.
+At position 41 to 76, the domain is characterized as EF-hand 1.
+At position 138 to 226, the domain is characterized as EH 2.
+At position 22 to 290, the domain is characterized as Protein kinase.
+At position 185 to 248, the domain is characterized as bZIP.
+At position 491 to 639, the domain is characterized as Helicase C-terminal.
+At position 1000 to 1077, the domain is characterized as HTH OST-type 2.
+At position 1097 to 1171, the domain is characterized as HTH OST-type 3.
+At position 1173 to 1247, the domain is characterized as HTH OST-type 4.
+At position 1257 to 1332, the domain is characterized as HTH OST-type 5.
+At position 1333 to 1408, the domain is characterized as HTH OST-type 6.
+At position 1409 to 1484, the domain is characterized as HTH OST-type 7.
+At position 1486 to 1560, the domain is characterized as HTH OST-type 8.
+At position 356 to 415, the domain is characterized as LIM zinc-binding 1.
+At position 416 to 473, the domain is characterized as LIM zinc-binding 2.
+At position 474 to 533, the domain is characterized as LIM zinc-binding 3.
+At position 534 to 591, the domain is characterized as LIM zinc-binding 4.
+At position 135 to 177, the domain is characterized as EGF-like 1.
+At position 289 to 329, the domain is characterized as EGF-like 2; calcium-binding.
+At position 35 to 148, the domain is characterized as DOMON.
+At position 228 to 255, the domain is characterized as PLD phosphodiesterase 1.
+At position 406 to 433, the domain is characterized as PLD phosphodiesterase 2.
+At position 124 to 363, the domain is characterized as VWFA.
+At position 314 to 355, the domain is characterized as EGF-like 1.
+At position 356 to 396, the domain is characterized as EGF-like 2; calcium-binding.
+At position 397 to 437, the domain is characterized as EGF-like 3.
+At position 435 to 477, the domain is characterized as EGF-like 4.
+At position 741 to 781, the domain is characterized as EGF-like 5.
+At position 832 to 869, the domain is characterized as EGF-like 6.
+At position 870 to 911, the domain is characterized as EGF-like 7; calcium-binding.
+At position 912 to 952, the domain is characterized as EGF-like 8; calcium-binding.
+At position 971 to 1012, the domain is characterized as EGF-like 9.
+At position 20 to 176, the domain is characterized as UBC core.
+At position 300 to 339, the domain is characterized as LIM interaction domain (LID).
+At position 65 to 270, the domain is characterized as BURP.
+At position 21 to 131, the domain is characterized as sHSP.
+At position 14 to 142, the domain is characterized as RNase III.
+At position 170 to 235, the domain is characterized as DRBM.
+At position 98 to 172, the domain is characterized as PRC barrel.
+At position 97 to 165, the domain is characterized as POTRA.
+At position 21 to 306, the domain is characterized as FERM.
+At position 911 to 1182, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 138, the domain is characterized as Peptidase C39.
+At position 168 to 450, the domain is characterized as ABC transmembrane type-1.
+At position 484 to 717, the domain is characterized as ABC transporter.
+At position 52 to 323, the domain is characterized as GB1/RHD3-type G.
+At position 401 to 580, the domain is characterized as Helicase ATP-binding.
+At position 675 to 858, the domain is characterized as Helicase C-terminal.
+At position 153 to 570, the domain is characterized as Myotubularin phosphatase.
+At position 148 to 410, the domain is characterized as Protein kinase.
+At position 452 to 488, the domain is characterized as EF-hand 1.
+At position 489 to 524, the domain is characterized as EF-hand 2.
+At position 525 to 564, the domain is characterized as EF-hand 3.
+At position 567 to 596, the domain is characterized as EF-hand 4.
+At position 1 to 184, the domain is characterized as N-acetyltransferase.
+At position 1 to 157, the domain is characterized as Thioredoxin.
+At position 133 to 374, the domain is characterized as Rab-GAP TBC.
+At position 32 to 253, the domain is characterized as L-type lectin-like.
+At position 4 to 83, the domain is characterized as ACT.
+At position 4 to 143, the domain is characterized as SprT-like.
+At position 32 to 109, the domain is characterized as Death.
+At position 5 to 202, the domain is characterized as DPCK.
+At position 282 to 494, the domain is characterized as B30.2/SPRY.
+At position 31 to 155, the domain is characterized as AB hydrolase-1.
+At position 278 to 340, the domain is characterized as J.
+At position 608 to 758, the domain is characterized as MOSC.
+At position 422 to 435, the domain is characterized as CRIB.
+At position 801 to 1053, the domain is characterized as Protein kinase.
+At position 617 to 706, the domain is characterized as EH.
+At position 175 to 473, the domain is characterized as MHD.
+At position 204 to 242, the domain is characterized as LRRCT.
+At position 3 to 167, the domain is characterized as Thioredoxin.
+At position 1240 to 1355, the domain is characterized as Peptidase S74.
+At position 404 to 417, the domain is characterized as CRIB.
+At position 698 to 949, the domain is characterized as Protein kinase.
+At position 20 to 192, the domain is characterized as PITH.
+At position 136 to 344, the domain is characterized as ATP-grasp.
+At position 194 to 246, the domain is characterized as HAMP.
+At position 253 to 320, the domain is characterized as PAS.
+At position 371 to 589, the domain is characterized as Histidine kinase.
+At position 223 to 313, the domain is characterized as PA.
+At position 244 to 303, the domain is characterized as LIM zinc-binding.
+At position 28 to 41, the domain is characterized as CRIB.
+At position 44 to 168, the domain is characterized as VWFA 1.
+At position 613 to 738, the domain is characterized as VWFA 2.
+At position 833 to 957, the domain is characterized as VWFA 3.
+At position 91 to 320, the domain is characterized as TLDc.
+At position 9 to 98, the domain is characterized as MtN3/slv 1.
+At position 134 to 185, the domain is characterized as MtN3/slv 2.
+At position 16 to 67, the domain is characterized as bHLH.
+At position 117 to 181, the domain is characterized as PAS 1.
+At position 238 to 274, the domain is characterized as PAS 2.
+At position 1 to 109, the domain is characterized as Ig-like.
+At position 11 to 189, the domain is characterized as Guanylate kinase-like.
+At position 312 to 559, the domain is characterized as FAD-binding FR-type.
+At position 7 to 118, the domain is characterized as MTTase N-terminal.
+At position 142 to 371, the domain is characterized as Radical SAM core.
+At position 113 to 293, the domain is characterized as DH.
+At position 317 to 416, the domain is characterized as PH.
+At position 3 to 100, the domain is characterized as PTS EIIB type-2 1.
+At position 124 to 221, the domain is characterized as PTS EIIB type-2 2.
+At position 244 to 579, the domain is characterized as PTS EIIC type-2.
+At position 163 to 286, the domain is characterized as Fe2OG dioxygenase.
+At position 18 to 95, the domain is characterized as Cytochrome b5 heme-binding.
+At position 153 to 253, the domain is characterized as Fe2OG dioxygenase.
+At position 197 to 301, the domain is characterized as Fe2OG dioxygenase.
+At position 46 to 306, the domain is characterized as Protein kinase.
+At position 2 to 222, the domain is characterized as ABC transporter.
+At position 5 to 78, the domain is characterized as ACT.
+At position 218 to 374, the domain is characterized as TrmE-type G.
+At position 24 to 97, the domain is characterized as Ig-like.
+At position 148 to 176, the domain is characterized as ITAM.
+At position 5 to 246, the domain is characterized as ABC transporter.
+At position 29 to 217, the domain is characterized as GH11.
+At position 131 to 333, the domain is characterized as ATP-grasp.
+At position 27 to 257, the domain is characterized as GH16.
+At position 266 to 404, the domain is characterized as Ricin B-type lectin.
+At position 411 to 533, the domain is characterized as CBM6 1.
+At position 549 to 671, the domain is characterized as CBM6 2.
+At position 2 to 127, the domain is characterized as Thioredoxin.
+At position 250 to 335, the domain is characterized as PDZ.
+At position 424 to 498, the domain is characterized as DEP.
+At position 105 to 135, the domain is characterized as EF-hand 3.
+At position 136 to 171, the domain is characterized as EF-hand 4.
+At position 284 to 320, the domain is characterized as DFDF.
+At position 4 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 6 to 79, the domain is characterized as HTH OST-type 1.
+At position 378 to 452, the domain is characterized as HTH OST-type 3.
+At position 589 to 648, the domain is characterized as Tudor.
+At position 570 to 721, the domain is characterized as STAS.
+At position 295 to 566, the domain is characterized as Radical SAM core.
+At position 205 to 291, the domain is characterized as Ig-like C1-type.
+At position 6 to 282, the domain is characterized as tr-type G.
+At position 24 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 107 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 204 to 298, the domain is characterized as Ig-like C2-type 3.
+At position 299 to 397, the domain is characterized as Ig-like C2-type 4.
+At position 398 to 503, the domain is characterized as Ig-like C2-type 5.
+At position 580 to 913, the domain is characterized as Protein kinase.
+At position 76 to 256, the domain is characterized as FAD-binding PCMH-type.
+At position 162 to 242, the domain is characterized as PDZ 2.
+At position 6 to 214, the domain is characterized as Glutamine amidotransferase type-1.
+At position 14 to 75, the domain is characterized as HTH tetR-type.
+At position 16 to 151, the domain is characterized as VHS.
+At position 143 to 162, the domain is characterized as UIM.
+At position 196 to 255, the domain is characterized as SH3.
+At position 1 to 269, the domain is characterized as Deacetylase sirtuin-type.
+At position 669 to 903, the domain is characterized as NR LBD.
+At position 1 to 144, the domain is characterized as BAH.
+At position 145 to 256, the domain is characterized as ELM2.
+At position 263 to 315, the domain is characterized as SANT.
+At position 34 to 123, the domain is characterized as CTCK.
+At position 150 to 223, the domain is characterized as AWS.
+At position 225 to 342, the domain is characterized as SET.
+At position 349 to 365, the domain is characterized as Post-SET.
+At position 615 to 646, the domain is characterized as WW.
+At position 34 to 72, the domain is characterized as LRRNT.
+At position 275 to 460, the domain is characterized as GATase cobBQ-type.
+At position 15 to 204, the domain is characterized as Lon N-terminal.
+At position 595 to 776, the domain is characterized as Lon proteolytic.
+At position 263 to 317, the domain is characterized as PAP-associated.
+At position 283 to 486, the domain is characterized as B30.2/SPRY.
+At position 38 to 179, the domain is characterized as SLD.
+At position 135 to 200, the domain is characterized as S1 motif.
+At position 302 to 368, the domain is characterized as KH.
+At position 579 to 680, the domain is characterized as tRNA-binding.
+At position 19 to 210, the domain is characterized as Albumin 1.
+At position 404 to 602, the domain is characterized as Albumin 3.
+At position 11 to 78, the domain is characterized as HMA.
+At position 23 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 160 to 302, the domain is characterized as Plastocyanin-like 2.
+At position 369 to 489, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 434, the domain is characterized as SMP-LTD.
+At position 93 to 168, the domain is characterized as Lipoyl-binding.
+At position 139 to 189, the domain is characterized as DHHC.
+At position 24 to 139, the domain is characterized as Ig-like V-type.
+At position 145 to 237, the domain is characterized as Ig-like C2-type 1.
+At position 244 to 328, the domain is characterized as Ig-like C2-type 2.
+At position 91 to 179, the domain is characterized as Ig-like C1-type.
+At position 35 to 80, the domain is characterized as F-box.
+At position 709 to 966, the domain is characterized as Protein kinase.
+At position 5 to 156, the domain is characterized as NAC.
+At position 2 to 331, the domain is characterized as GH10.
+At position 30 to 138, the domain is characterized as C-type lectin.
+At position 632 to 681, the domain is characterized as GPS.
+At position 743 to 860, the domain is characterized as PLAT.
+At position 51 to 278, the domain is characterized as Radical SAM core.
+At position 34 to 355, the domain is characterized as G-alpha.
+At position 29 to 89, the domain is characterized as v-SNARE coiled-coil homology.
+At position 18 to 185, the domain is characterized as Era-type G.
+At position 216 to 293, the domain is characterized as KH type-2.
+At position 95 to 141, the domain is characterized as G-patch.
+At position 90 to 408, the domain is characterized as BRO1.
+At position 58 to 129, the domain is characterized as RRM 1.
+At position 131 to 209, the domain is characterized as RRM 2.
+At position 220 to 298, the domain is characterized as RRM 3.
+At position 389 to 449, the domain is characterized as PP1-binding.
+At position 43 to 121, the domain is characterized as RRM.
+At position 35 to 211, the domain is characterized as Helicase ATP-binding.
+At position 244 to 391, the domain is characterized as Helicase C-terminal.
+At position 229 to 314, the domain is characterized as Ig-like C2-type.
+At position 591 to 756, the domain is characterized as Helicase ATP-binding.
+At position 777 to 933, the domain is characterized as Helicase C-terminal.
+At position 94 to 407, the domain is characterized as IF rod.
+At position 16 to 458, the domain is characterized as Hexokinase 1.
+At position 464 to 906, the domain is characterized as Hexokinase 2.
+At position 47 to 119, the domain is characterized as KH type-2.
+At position 49 to 84, the domain is characterized as EF-hand 1.
+At position 85 to 119, the domain is characterized as EF-hand 2.
+At position 256 to 308, the domain is characterized as VWFC.
+At position 98 to 287, the domain is characterized as ABC transmembrane type-1.
+At position 29 to 146, the domain is characterized as Response regulatory.
+At position 311 to 503, the domain is characterized as PNPLA.
+At position 323 to 373, the domain is characterized as bHLH.
+At position 32 to 141, the domain is characterized as CUB.
+At position 143 to 239, the domain is characterized as LCCL.
+At position 20 to 70, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 98 to 184, the domain is characterized as PDZ 1.
+At position 193 to 279, the domain is characterized as PDZ 2.
+At position 421 to 501, the domain is characterized as PDZ 3.
+At position 536 to 606, the domain is characterized as SH3.
+At position 662 to 837, the domain is characterized as Guanylate kinase-like.
+At position 6 to 123, the domain is characterized as Calponin-homology (CH).
+At position 105 to 466, the domain is characterized as PTS EIIC type-1.
+At position 501 to 605, the domain is characterized as PTS EIIA type-1.
+At position 141 to 316, the domain is characterized as Helicase ATP-binding.
+At position 344 to 490, the domain is characterized as Helicase C-terminal.
+At position 2 to 171, the domain is characterized as Era-type G.
+At position 32 to 99, the domain is characterized as BTB.
+At position 134 to 233, the domain is characterized as BACK.
+At position 7 to 173, the domain is characterized as Era-type G.
+At position 196 to 280, the domain is characterized as KH type-2.
+At position 134 to 573, the domain is characterized as Urease.
+At position 39 to 90, the domain is characterized as LysM.
+At position 154 to 375, the domain is characterized as PE-PPE.
+At position 86 to 173, the domain is characterized as PB1.
+At position 30 to 84, the domain is characterized as FHA.
+At position 25 to 108, the domain is characterized as SWIB/MDM2.
+At position 224 to 276, the domain is characterized as HAMP.
+At position 291 to 510, the domain is characterized as Histidine kinase.
+At position 1 to 128, the domain is characterized as Plastocyanin-like.
+At position 491 to 645, the domain is characterized as Helicase C-terminal.
+At position 32 to 417, the domain is characterized as Helicase ATP-binding.
+At position 17 to 146, the domain is characterized as N-acetyltransferase.
+At position 18 to 136, the domain is characterized as MTTase N-terminal.
+At position 395 to 458, the domain is characterized as TRAM.
+At position 1184 to 1319, the domain is characterized as DOD-type homing endonuclease.
+At position 126 to 355, the domain is characterized as NR LBD.
+At position 57 to 116, the domain is characterized as SH3 1.
+At position 322 to 457, the domain is characterized as ZU5.
+At position 657 to 727, the domain is characterized as SH3 2.
+At position 114 to 177, the domain is characterized as LIM zinc-binding 1.
+At position 178 to 238, the domain is characterized as LIM zinc-binding 2.
+At position 483 to 546, the domain is characterized as LIM zinc-binding 3.
+At position 837 to 1038, the domain is characterized as Rho-GAP.
+At position 53 to 234, the domain is characterized as BPL/LPL catalytic.
+At position 101 to 174, the domain is characterized as PRC barrel.
+At position 25 to 266, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 238 to 313, the domain is characterized as MIT.
+At position 60 to 168, the domain is characterized as MTTase N-terminal.
+At position 196 to 427, the domain is characterized as Radical SAM core.
+At position 427 to 489, the domain is characterized as TRAM.
+At position 105 to 162, the domain is characterized as COS.
+At position 164 to 268, the domain is characterized as Fibronectin type-III.
+At position 281 to 476, the domain is characterized as B30.2/SPRY.
+At position 368 to 441, the domain is characterized as bHLH.
+At position 2 to 127, the domain is characterized as VOC 1.
+At position 141 to 276, the domain is characterized as VOC 2.
+At position 25 to 98, the domain is characterized as BTB.
+At position 23 to 194, the domain is characterized as EngB-type G.
+At position 2 to 209, the domain is characterized as Glutamine amidotransferase type-2.
+At position 210 to 523, the domain is characterized as Asparagine synthetase.
+At position 191 to 458, the domain is characterized as Protein kinase.
+At position 26 to 145, the domain is characterized as Bulb-type lectin.
+At position 282 to 318, the domain is characterized as EGF-like.
+At position 337 to 423, the domain is characterized as PAN.
+At position 501 to 786, the domain is characterized as Protein kinase.
+At position 2 to 118, the domain is characterized as PLAT.
+At position 119 to 674, the domain is characterized as Lipoxygenase.
+At position 6 to 88, the domain is characterized as Phosphagen kinase N-terminal.
+At position 116 to 353, the domain is characterized as Phosphagen kinase C-terminal.
+At position 109 to 348, the domain is characterized as NR LBD.
+At position 13 to 78, the domain is characterized as HTH IS21-type.
+At position 136 to 312, the domain is characterized as Integrase catalytic.
+At position 76 to 199, the domain is characterized as MSP.
+At position 4 to 411, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 65 to 100, the domain is characterized as EF-hand 1.
+At position 101 to 136, the domain is characterized as EF-hand 2.
+At position 146 to 181, the domain is characterized as EF-hand 3.
+At position 39 to 248, the domain is characterized as tr-type G.
+At position 52 to 111, the domain is characterized as CBS 1.
+At position 114 to 171, the domain is characterized as CBS 2.
+At position 1 to 25, the domain is characterized as Pentraxin (PTX).
+At position 4 to 132, the domain is characterized as RGS.
+At position 301 to 386, the domain is characterized as DIX.
+At position 7 to 283, the domain is characterized as YjeF C-terminal.
+At position 367 to 690, the domain is characterized as Protein kinase.
+At position 44 to 304, the domain is characterized as Protein kinase.
+At position 7 to 67, the domain is characterized as v-SNARE coiled-coil homology.
+At position 112 to 161, the domain is characterized as Myosin N-terminal SH3-like.
+At position 165 to 837, the domain is characterized as Myosin motor.
+At position 839 to 868, the domain is characterized as IQ 1.
+At position 862 to 891, the domain is characterized as IQ 2.
+At position 888 to 917, the domain is characterized as IQ 3.
+At position 911 to 940, the domain is characterized as IQ 4.
+At position 29 to 86, the domain is characterized as Tudor.
+At position 946 to 1022, the domain is characterized as Carrier 1.
+At position 2078 to 2154, the domain is characterized as Carrier 2.
+At position 13 to 130, the domain is characterized as Response regulatory.
+At position 954 to 1014, the domain is characterized as SH3.
+At position 104 to 148, the domain is characterized as bZIP.
+At position 175 to 390, the domain is characterized as DOG1.
+At position 229 to 292, the domain is characterized as bZIP.
+At position 217 to 400, the domain is characterized as GAF.
+At position 620 to 690, the domain is characterized as PAS 1.
+At position 750 to 824, the domain is characterized as PAS 2.
+At position 904 to 1124, the domain is characterized as Histidine kinase.
+At position 6 to 134, the domain is characterized as VOC 1.
+At position 161 to 320, the domain is characterized as VOC 2.
+At position 12 to 252, the domain is characterized as Protein kinase.
+At position 232 to 444, the domain is characterized as Helicase ATP-binding.
+At position 496 to 646, the domain is characterized as Helicase C-terminal.
+At position 1368 to 1656, the domain is characterized as Autotransporter.
+At position 119 to 138, the domain is characterized as HhH.
+At position 1 to 40, the domain is characterized as Fibronectin type-I 1.
+At position 45 to 88, the domain is characterized as Fibronectin type-I 2.
+At position 89 to 132, the domain is characterized as Fibronectin type-I 3.
+At position 134 to 178, the domain is characterized as Fibronectin type-I 4.
+At position 179 to 223, the domain is characterized as Fibronectin type-I 5.
+At position 256 to 295, the domain is characterized as Fibronectin type-I 6.
+At position 305 to 353, the domain is characterized as Fibronectin type-II 1.
+At position 365 to 413, the domain is characterized as Fibronectin type-II 2.
+At position 418 to 461, the domain is characterized as Fibronectin type-I 7.
+At position 466 to 508, the domain is characterized as Fibronectin type-I 8.
+At position 509 to 552, the domain is characterized as Fibronectin type-I 9.
+At position 560 to 653, the domain is characterized as Fibronectin type-III 1.
+At position 667 to 762, the domain is characterized as Fibronectin type-III 2.
+At position 763 to 852, the domain is characterized as Fibronectin type-III 3.
+At position 859 to 948, the domain is characterized as Fibronectin type-III 4.
+At position 949 to 1038, the domain is characterized as Fibronectin type-III 5.
+At position 1039 to 1125, the domain is characterized as Fibronectin type-III 6.
+At position 1126 to 1220, the domain is characterized as Fibronectin type-III 7.
+At position 1221 to 1309, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1310 to 1402, the domain is characterized as Fibronectin type-III 9.
+At position 1403 to 1490, the domain is characterized as Fibronectin type-III 10.
+At position 1491 to 1584, the domain is characterized as Fibronectin type-III 11.
+At position 1585 to 1676, the domain is characterized as Fibronectin type-III 12.
+At position 1677 to 1764, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1765 to 1858, the domain is characterized as Fibronectin type-III 14.
+At position 1859 to 1945, the domain is characterized as Fibronectin type-III 15.
+At position 1946 to 2036, the domain is characterized as Fibronectin type-III 16.
+At position 2144 to 2238, the domain is characterized as Fibronectin type-III 17.
+At position 2245 to 2289, the domain is characterized as Fibronectin type-I 10.
+At position 2290 to 2332, the domain is characterized as Fibronectin type-I 11.
+At position 2334 to 2374, the domain is characterized as Fibronectin type-I 12.
+At position 72 to 284, the domain is characterized as ABC transmembrane type-1.
+At position 110 to 619, the domain is characterized as Peptidase S8.
+At position 830 to 1172, the domain is characterized as PUM-HD.
+At position 107 to 312, the domain is characterized as ATP-grasp.
+At position 110 to 145, the domain is characterized as EF-hand.
+At position 607 to 666, the domain is characterized as KH.
+At position 678 to 747, the domain is characterized as S1 motif.
+At position 47 to 163, the domain is characterized as MRH 1.
+At position 172 to 320, the domain is characterized as MRH 2.
+At position 326 to 468, the domain is characterized as MRH 3.
+At position 473 to 619, the domain is characterized as MRH 4.
+At position 625 to 762, the domain is characterized as MRH 5.
+At position 765 to 924, the domain is characterized as MRH 6.
+At position 932 to 1079, the domain is characterized as MRH 7.
+At position 1082 to 1219, the domain is characterized as MRH 8.
+At position 1225 to 1363, the domain is characterized as MRH 9.
+At position 1367 to 1508, the domain is characterized as MRH 10.
+At position 1514 to 1648, the domain is characterized as MRH 11.
+At position 1650 to 1797, the domain is characterized as MRH 12.
+At position 1802 to 1989, the domain is characterized as Fibronectin type-II.
+At position 1992 to 2127, the domain is characterized as MRH 14.
+At position 2135 to 2280, the domain is characterized as MRH 15.
+At position 327 to 371, the domain is characterized as UBA.
+At position 72 to 158, the domain is characterized as Doublecortin 1.
+At position 197 to 280, the domain is characterized as Doublecortin 2.
+At position 411 to 668, the domain is characterized as Protein kinase.
+At position 39 to 244, the domain is characterized as uDENN.
+At position 263 to 399, the domain is characterized as cDENN.
+At position 401 to 581, the domain is characterized as dDENN.
+At position 772 to 932, the domain is characterized as RUN 1.
+At position 936 to 1044, the domain is characterized as PLAT.
+At position 1118 to 1267, the domain is characterized as RUN 2.
+At position 101 to 162, the domain is characterized as CBS 1.
+At position 185 to 243, the domain is characterized as CBS 2.
+At position 272 to 330, the domain is characterized as CBS 3.
+At position 335 to 391, the domain is characterized as CBS 4.
+At position 41 to 314, the domain is characterized as Septin-type G.
+At position 21 to 242, the domain is characterized as ABC transporter.
+At position 63 to 137, the domain is characterized as U-box.
+At position 89 to 156, the domain is characterized as PRC barrel.
+At position 42 to 124, the domain is characterized as SCAN box.
+At position 29 to 219, the domain is characterized as GH16.
+At position 1 to 55, the domain is characterized as PAS 1.
+At position 133 to 235, the domain is characterized as PAS 2.
+At position 44 to 227, the domain is characterized as PID.
+At position 370 to 461, the domain is characterized as SH2.
+At position 1 to 151, the domain is characterized as MGS-like.
+At position 269 to 397, the domain is characterized as MPN.
+At position 9 to 44, the domain is characterized as EF-hand 1.
+At position 118 to 234, the domain is characterized as Calponin-homology (CH) 1.
+At position 262 to 373, the domain is characterized as Calponin-homology (CH) 2.
+At position 392 to 501, the domain is characterized as Calponin-homology (CH) 3.
+At position 513 to 621, the domain is characterized as Calponin-homology (CH) 4.
+At position 20 to 262, the domain is characterized as Radical SAM core.
+At position 98 to 178, the domain is characterized as RRM 1.
+At position 231 to 315, the domain is characterized as RRM 2.
+At position 743 to 789, the domain is characterized as G-patch.
+At position 344 to 409, the domain is characterized as S4 RNA-binding.
+At position 89 to 275, the domain is characterized as DCUN1.
+At position 299 to 411, the domain is characterized as Cyclin N-terminal.
+At position 100 to 178, the domain is characterized as PRC barrel.
+At position 62 to 251, the domain is characterized as Peptidase M12A.
+At position 245 to 284, the domain is characterized as EGF-like.
+At position 9 to 252, the domain is characterized as ATP-grasp.
+At position 36 to 318, the domain is characterized as ABC transmembrane type-1.
+At position 352 to 585, the domain is characterized as ABC transporter.
+At position 31 to 224, the domain is characterized as Lon N-terminal.
+At position 613 to 790, the domain is characterized as Lon proteolytic.
+At position 120 to 344, the domain is characterized as ABC transmembrane type-1 1.
+At position 377 to 629, the domain is characterized as ABC transporter 1.
+At position 697 to 984, the domain is characterized as ABC transmembrane type-1 2.
+At position 1023 to 1269, the domain is characterized as ABC transporter 2.
+At position 26 to 130, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 521 to 634, the domain is characterized as SMC hinge.
+At position 81 to 115, the domain is characterized as EF-hand 2.
+At position 7 to 197, the domain is characterized as Glutamine amidotransferase type-1.
+At position 198 to 387, the domain is characterized as GMPS ATP-PPase.
+At position 54 to 149, the domain is characterized as GED.
+At position 167 to 274, the domain is characterized as Cadherin 1.
+At position 275 to 389, the domain is characterized as Cadherin 2.
+At position 390 to 504, the domain is characterized as Cadherin 3.
+At position 505 to 610, the domain is characterized as Cadherin 4.
+At position 611 to 721, the domain is characterized as Cadherin 5.
+At position 22 to 141, the domain is characterized as Bulb-type lectin.
+At position 277 to 313, the domain is characterized as EGF-like.
+At position 332 to 418, the domain is characterized as PAN.
+At position 488 to 773, the domain is characterized as Protein kinase.
+At position 23 to 291, the domain is characterized as GH18.
+At position 586 to 662, the domain is characterized as BRCT.
+At position 233 to 349, the domain is characterized as sHSP.
+At position 349 to 748, the domain is characterized as PIPK.
+At position 6 to 321, the domain is characterized as Hcy-binding.
+At position 29 to 143, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 211 to 325, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 832 to 897, the domain is characterized as HTH luxR-type.
+At position 2 to 202, the domain is characterized as CYTH.
+At position 218 to 433, the domain is characterized as CHAD.
+At position 141 to 450, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 6 to 52, the domain is characterized as F-box.
+At position 85 to 248, the domain is characterized as Tyr recombinase.
+At position 458 to 595, the domain is characterized as SIS 2.
+At position 13 to 320, the domain is characterized as IF rod.
+At position 28 to 69, the domain is characterized as Chitin-binding type-1 1.
+At position 70 to 112, the domain is characterized as Chitin-binding type-1 2.
+At position 113 to 155, the domain is characterized as Chitin-binding type-1 3.
+At position 156 to 198, the domain is characterized as Chitin-binding type-1 4.
+At position 62 to 225, the domain is characterized as SIS.
+At position 275 to 364, the domain is characterized as CS.
+At position 5 to 388, the domain is characterized as Helicase ATP-binding.
+At position 44 to 152, the domain is characterized as Rieske.
+At position 34 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 106 to 199, the domain is characterized as Ig-like C2-type 2.
+At position 207 to 294, the domain is characterized as Ig-like C2-type 3.
+At position 296 to 384, the domain is characterized as Ig-like C2-type 4.
+At position 398 to 483, the domain is characterized as Ig-like C2-type 5.
+At position 214 to 295, the domain is characterized as BCNT-C.
+At position 76 to 128, the domain is characterized as bHLH.
+At position 128 to 310, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 199, the domain is characterized as RNase H type-2.
+At position 141 to 374, the domain is characterized as Radical SAM core.
+At position 14 to 207, the domain is characterized as Lon N-terminal.
+At position 64 to 136, the domain is characterized as BTB.
+At position 63 to 135, the domain is characterized as Thyroglobulin type-1.
+At position 13 to 129, the domain is characterized as Response regulatory.
+At position 145 to 322, the domain is characterized as Helicase ATP-binding.
+At position 333 to 497, the domain is characterized as Helicase C-terminal.
+At position 1 to 288, the domain is characterized as SPX.
+At position 40 to 228, the domain is characterized as GH11.
+At position 22 to 120, the domain is characterized as MaoC-like.
+At position 13 to 239, the domain is characterized as Radical SAM core.
+At position 25 to 60, the domain is characterized as EF-hand 1.
+At position 95 to 130, the domain is characterized as EF-hand 2.
+At position 131 to 166, the domain is characterized as EF-hand 3.
+At position 17 to 138, the domain is characterized as Rhodanese 1.
+At position 168 to 281, the domain is characterized as Rhodanese 2.
+At position 36 to 196, the domain is characterized as SIS.
+At position 777 to 1054, the domain is characterized as Protein kinase.
+At position 36 to 87, the domain is characterized as LysM.
+At position 39 to 155, the domain is characterized as Plastocyanin-like 1.
+At position 165 to 323, the domain is characterized as Plastocyanin-like 2.
+At position 436 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 80 to 140, the domain is characterized as SH3.
+At position 218 to 279, the domain is characterized as KH 1.
+At position 281 to 351, the domain is characterized as KH 2.
+At position 210 to 434, the domain is characterized as Rab-GAP TBC.
+At position 58 to 166, the domain is characterized as sHSP.
+At position 98 to 354, the domain is characterized as Protein kinase.
+At position 355 to 430, the domain is characterized as AGC-kinase C-terminal.
+At position 3 to 198, the domain is characterized as DPCK.
+At position 1 to 140, the domain is characterized as MGS-like.
+At position 73 to 148, the domain is characterized as Carrier.
+At position 74 to 103, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 113 to 142, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 566 to 651, the domain is characterized as S1 motif.
+At position 654 to 743, the domain is characterized as BRCT 1.
+At position 808 to 911, the domain is characterized as BRCT 2.
+At position 210 to 489, the domain is characterized as Protein kinase.
+At position 96 to 285, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 295 to 537, the domain is characterized as Glutamine amidotransferase type-1.
+At position 78 to 163, the domain is characterized as PDZ.
+At position 920 to 1033, the domain is characterized as PH.
+At position 1140 to 1332, the domain is characterized as Rho-GAP.
+At position 1 to 85, the domain is characterized as HTH arsR-type.
+At position 494 to 549, the domain is characterized as Kazal-like.
+At position 13 to 204, the domain is characterized as DPCK.
+At position 22 to 101, the domain is characterized as U-box.
+At position 86 to 245, the domain is characterized as CP-type G.
+At position 126 to 292, the domain is characterized as JmjC.
+At position 275 to 338, the domain is characterized as bZIP.
+At position 538 to 879, the domain is characterized as Protein kinase.
+At position 48 to 79, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 124 to 157, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 126 to 197, the domain is characterized as POTRA.
+At position 41 to 139, the domain is characterized as Expansin-like EG45.
+At position 350 to 429, the domain is characterized as OCT.
+At position 944 to 1167, the domain is characterized as JmjC.
+At position 2 to 92, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 216 to 282, the domain is characterized as PAS.
+At position 339 to 534, the domain is characterized as Histidine kinase.
+At position 30 to 204, the domain is characterized as BPL/LPL catalytic.
+At position 437 to 498, the domain is characterized as LIM zinc-binding 1.
+At position 502 to 561, the domain is characterized as LIM zinc-binding 2.
+At position 562 to 631, the domain is characterized as LIM zinc-binding 3.
+At position 4 to 165, the domain is characterized as PCI.
+At position 1 to 112, the domain is characterized as OCIA.
+At position 214 to 299, the domain is characterized as KH.
+At position 340 to 432, the domain is characterized as HD.
+At position 87 to 339, the domain is characterized as Protein kinase.
+At position 269 to 446, the domain is characterized as B30.2/SPRY.
+At position 272 to 352, the domain is characterized as RRM 1.
+At position 432 to 512, the domain is characterized as RRM 2.
+At position 928 to 974, the domain is characterized as G-patch.
+At position 84 to 293, the domain is characterized as SMP-LTD.
+At position 7 to 144, the domain is characterized as SprT-like.
+At position 45 to 62, the domain is characterized as WH2.
+At position 207 to 505, the domain is characterized as Dynamin-type G.
+At position 780 to 872, the domain is characterized as GED.
+At position 20 to 380, the domain is characterized as GH18.
+At position 4 to 91, the domain is characterized as Acylphosphatase-like.
+At position 25 to 144, the domain is characterized as Rhodanese 1.
+At position 174 to 288, the domain is characterized as Rhodanese 2.
+At position 33 to 179, the domain is characterized as F5/8 type C.
+At position 214 to 346, the domain is characterized as Laminin G-like 1.
+At position 400 to 529, the domain is characterized as Laminin G-like 2.
+At position 551 to 588, the domain is characterized as EGF-like 1.
+At position 589 to 794, the domain is characterized as Fibrinogen C-terminal.
+At position 795 to 960, the domain is characterized as Laminin G-like 3.
+At position 960 to 999, the domain is characterized as EGF-like 2.
+At position 1048 to 1204, the domain is characterized as Laminin G-like 4.
+At position 539 to 780, the domain is characterized as Fibrinogen C-terminal.
+At position 614 to 715, the domain is characterized as tRNA-binding.
+At position 253 to 345, the domain is characterized as Enkurin.
+At position 282 to 485, the domain is characterized as B30.2/SPRY.
+At position 38 to 390, the domain is characterized as TTL.
+At position 107 to 178, the domain is characterized as S4 RNA-binding.
+At position 27 to 73, the domain is characterized as Gla.
+At position 23 to 150, the domain is characterized as EamA 1.
+At position 205 to 331, the domain is characterized as EamA 2.
+At position 112 to 302, the domain is characterized as ATP-grasp.
+At position 1642 to 1736, the domain is characterized as BRCT 1.
+At position 1756 to 1855, the domain is characterized as BRCT 2.
+At position 73 to 291, the domain is characterized as Radical SAM core.
+At position 305 to 559, the domain is characterized as Glutamine amidotransferase type-1.
+At position 114 to 351, the domain is characterized as Radical SAM core.
+At position 104 to 272, the domain is characterized as CP-type G.
+At position 24 to 83, the domain is characterized as LIM zinc-binding 1.
+At position 84 to 145, the domain is characterized as LIM zinc-binding 2.
+At position 161 to 247, the domain is characterized as PDZ.
+At position 314 to 572, the domain is characterized as Protein kinase.
+At position 97 to 214, the domain is characterized as Ferric oxidoreductase.
+At position 241 to 361, the domain is characterized as FAD-binding FR-type.
+At position 129 to 235, the domain is characterized as C-type lectin.
+At position 65 to 160, the domain is characterized as SH2 1.
+At position 358 to 452, the domain is characterized as SH2 2.
+At position 113 to 325, the domain is characterized as Radical SAM core.
+At position 137 to 212, the domain is characterized as HTH crp-type.
+At position 394 to 829, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1314 to 1619, the domain is characterized as PKS/mFAS DH.
+At position 1678 to 1752, the domain is characterized as Carrier 1.
+At position 1793 to 1870, the domain is characterized as Carrier 2.
+At position 15 to 181, the domain is characterized as PPIase cyclophilin-type.
+At position 62 to 349, the domain is characterized as PPM-type phosphatase.
+At position 462 to 658, the domain is characterized as FtsK.
+At position 36 to 289, the domain is characterized as GH16.
+At position 148 to 211, the domain is characterized as bZIP.
+At position 319 to 514, the domain is characterized as B30.2/SPRY.
+At position 79 to 186, the domain is characterized as C-type lectin.
+At position 46 to 312, the domain is characterized as Laminin N-terminal.
+At position 313 to 368, the domain is characterized as Laminin EGF-like 1.
+At position 369 to 431, the domain is characterized as Laminin EGF-like 2.
+At position 432 to 481, the domain is characterized as Laminin EGF-like 3.
+At position 533 to 725, the domain is characterized as NTR.
+At position 184 to 381, the domain is characterized as Peptidase M12B.
+At position 390 to 479, the domain is characterized as Disintegrin.
+At position 620 to 654, the domain is characterized as EGF-like.
+At position 34 to 91, the domain is characterized as bHLH.
+At position 110 to 143, the domain is characterized as Orange.
+At position 247 to 387, the domain is characterized as Helicase C-terminal.
+At position 312 to 591, the domain is characterized as Protein kinase.
+At position 32 to 315, the domain is characterized as ABC transmembrane type-1.
+At position 347 to 583, the domain is characterized as ABC transporter.
+At position 4 to 39, the domain is characterized as EF-hand 1.
+At position 227 to 353, the domain is characterized as OmpA-like.
+At position 31 to 192, the domain is characterized as N-acetyltransferase.
+At position 75 to 262, the domain is characterized as DCUN1.
+At position 227 to 325, the domain is characterized as HTH araC/xylS-type.
+At position 844 to 913, the domain is characterized as BTB.
+At position 18 to 274, the domain is characterized as Pterin-binding.
+At position 3 to 63, the domain is characterized as HTH tetR-type.
+At position 388 to 528, the domain is characterized as DOD-type homing endonuclease.
+At position 57 to 220, the domain is characterized as SIS.
+At position 87 to 213, the domain is characterized as GST C-terminal.
+At position 258 to 418, the domain is characterized as EF-1-gamma C-terminal.
+At position 129 to 376, the domain is characterized as ABC transporter 1.
+At position 472 to 748, the domain is characterized as ABC transmembrane type-2 1.
+At position 888 to 1141, the domain is characterized as ABC transporter 2.
+At position 1231 to 1504, the domain is characterized as ABC transmembrane type-2 2.
+At position 10 to 97, the domain is characterized as RH1.
+At position 294 to 359, the domain is characterized as RH2.
+At position 66 to 186, the domain is characterized as Plastocyanin-like 1.
+At position 196 to 351, the domain is characterized as Plastocyanin-like 2.
+At position 429 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 229, the domain is characterized as Deacetylase sirtuin-type.
+At position 21 to 195, the domain is characterized as EngB-type G.
+At position 25 to 253, the domain is characterized as Peptidase S1.
+At position 336 to 396, the domain is characterized as S4 RNA-binding.
+At position 82 to 337, the domain is characterized as Protein kinase.
+At position 513 to 595, the domain is characterized as POLO box 1.
+At position 614 to 700, the domain is characterized as POLO box 2.
+At position 1 to 110, the domain is characterized as MTTase N-terminal.
+At position 132 to 364, the domain is characterized as Radical SAM core.
+At position 366 to 427, the domain is characterized as TRAM.
+At position 1 to 179, the domain is characterized as TCTP.
+At position 641 to 719, the domain is characterized as BRCT.
+At position 15 to 100, the domain is characterized as GS beta-grasp.
+At position 107 to 473, the domain is characterized as GS catalytic.
+At position 33 to 309, the domain is characterized as GH16.
+At position 82 to 166, the domain is characterized as SAND.
+At position 50 to 278, the domain is characterized as BPL/LPL catalytic.
+At position 212 to 261, the domain is characterized as GPS.
+At position 352 to 486, the domain is characterized as PLAT.
+At position 24 to 82, the domain is characterized as Collagen-like 1.
+At position 84 to 132, the domain is characterized as Collagen-like 2.
+At position 134 to 193, the domain is characterized as Collagen-like 3.
+At position 197 to 333, the domain is characterized as C1q.
+At position 10 to 121, the domain is characterized as NTF2.
+At position 24 to 293, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 129 to 205, the domain is characterized as RRM.
+At position 249 to 323, the domain is characterized as POU-specific.
+At position 48 to 347, the domain is characterized as AB hydrolase-1.
+At position 50 to 124, the domain is characterized as Fibronectin type-III 1.
+At position 142 to 211, the domain is characterized as Fibronectin type-III 2.
+At position 246 to 306, the domain is characterized as Fibronectin type-III 3.
+At position 329 to 425, the domain is characterized as Fibronectin type-III 4.
+At position 435 to 531, the domain is characterized as Fibronectin type-III 5.
+At position 532 to 628, the domain is characterized as Fibronectin type-III 6.
+At position 631 to 724, the domain is characterized as Fibronectin type-III 7.
+At position 725 to 817, the domain is characterized as Fibronectin type-III 8.
+At position 938 to 1195, the domain is characterized as Tyrosine-protein phosphatase.
+At position 127 to 217, the domain is characterized as Fibronectin type-III 1.
+At position 219 to 318, the domain is characterized as Fibronectin type-III 2.
+At position 218 to 363, the domain is characterized as TrmE-type G.
+At position 99 to 284, the domain is characterized as ABC transmembrane type-1.
+At position 336 to 505, the domain is characterized as tr-type G.
+At position 252 to 496, the domain is characterized as ABC transporter 2.
+At position 4 to 79, the domain is characterized as KRAB.
+At position 333 to 587, the domain is characterized as Protein kinase.
+At position 300 to 476, the domain is characterized as Rab-GAP TBC.
+At position 235 to 290, the domain is characterized as bHLH.
+At position 1 to 228, the domain is characterized as tr-type G.
+At position 364 to 416, the domain is characterized as HAMP.
+At position 454 to 663, the domain is characterized as Histidine kinase.
+At position 302 to 477, the domain is characterized as Helicase ATP-binding.
+At position 520 to 694, the domain is characterized as Helicase C-terminal.
+At position 19 to 111, the domain is characterized as SANTA.
+At position 91 to 336, the domain is characterized as GB1/RHD3-type G.
+At position 235 to 449, the domain is characterized as Histidine kinase.
+At position 3 to 88, the domain is characterized as Acylphosphatase-like.
+At position 196 to 249, the domain is characterized as PDZ.
+At position 12 to 293, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 294 to 564, the domain is characterized as UvrD-like helicase C-terminal.
+At position 10 to 162, the domain is characterized as NAC.
+At position 58 to 247, the domain is characterized as RNase H type-2.
+At position 67 to 147, the domain is characterized as Cytochrome c 1.
+At position 177 to 255, the domain is characterized as Cytochrome c 2.
+At position 9 to 202, the domain is characterized as ABC transmembrane type-1.
+At position 8 to 245, the domain is characterized as ABC transporter 1.
+At position 255 to 500, the domain is characterized as ABC transporter 2.
+At position 61 to 214, the domain is characterized as N-acetyltransferase.
+At position 26 to 120, the domain is characterized as Ig-like C2-type.
+At position 128 to 221, the domain is characterized as Fibronectin type-III 1.
+At position 222 to 322, the domain is characterized as Fibronectin type-III 2.
+At position 327 to 417, the domain is characterized as Fibronectin type-III 3.
+At position 422 to 515, the domain is characterized as Fibronectin type-III 4.
+At position 517 to 611, the domain is characterized as Fibronectin type-III 5.
+At position 511 to 540, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 6 to 66, the domain is characterized as CSD.
+At position 132 to 383, the domain is characterized as Olfactomedin-like.
+At position 14 to 57, the domain is characterized as Peptidase M12B.
+At position 65 to 129, the domain is characterized as Disintegrin.
+At position 210 to 503, the domain is characterized as Protein kinase.
+At position 396 to 733, the domain is characterized as Kinesin motor.
+At position 73 to 109, the domain is characterized as EGF-like 1.
+At position 111 to 148, the domain is characterized as EGF-like 2.
+At position 150 to 188, the domain is characterized as EGF-like 3.
+At position 193 to 276, the domain is characterized as Kringle.
+At position 314 to 555, the domain is characterized as Peptidase S1.
+At position 40 to 75, the domain is characterized as EF-hand 2.
+At position 59 to 244, the domain is characterized as BPL/LPL catalytic.
+At position 21 to 70, the domain is characterized as Kazal-like.
+At position 18 to 117, the domain is characterized as Ig-like.
+At position 602 to 714, the domain is characterized as CNA-B 1.
+At position 715 to 824, the domain is characterized as CNA-B 2.
+At position 825 to 935, the domain is characterized as CNA-B 3.
+At position 36 to 99, the domain is characterized as S5 DRBM.
+At position 8 to 156, the domain is characterized as MGS-like.
+At position 8 to 86, the domain is characterized as KRAB.
+At position 63 to 214, the domain is characterized as Cupin type-1.
+At position 21 to 509, the domain is characterized as Sema.
+At position 861 to 955, the domain is characterized as IPT/TIG 1.
+At position 957 to 1041, the domain is characterized as IPT/TIG 2.
+At position 1044 to 1143, the domain is characterized as IPT/TIG 3.
+At position 1146 to 1232, the domain is characterized as IPT/TIG 4.
+At position 21 to 216, the domain is characterized as Rho-GAP.
+At position 37 to 156, the domain is characterized as C-type lectin.
+At position 607 to 942, the domain is characterized as HECT.
+At position 70 to 255, the domain is characterized as TR mART core.
+At position 1 to 131, the domain is characterized as CMP/dCMP-type deaminase.
+At position 33 to 305, the domain is characterized as EndoU.
+At position 599 to 702, the domain is characterized as tRNA-binding.
+At position 10 to 92, the domain is characterized as PTS EIIB type-1.
+At position 259 to 399, the domain is characterized as Flavodoxin-like.
+At position 120 to 431, the domain is characterized as IF rod.
+At position 37 to 216, the domain is characterized as FAD-binding PCMH-type.
+At position 156 to 198, the domain is characterized as CUE 1.
+At position 247 to 290, the domain is characterized as CUE 2.
+At position 504 to 672, the domain is characterized as Helicase ATP-binding.
+At position 853 to 1005, the domain is characterized as Helicase C-terminal.
+At position 5 to 125, the domain is characterized as Glycine radical.
+At position 82 to 150, the domain is characterized as POTRA.
+At position 7 to 123, the domain is characterized as Response regulatory.
+At position 231 to 298, the domain is characterized as PAS 1.
+At position 371 to 437, the domain is characterized as PAS 2.
+At position 445 to 488, the domain is characterized as PAC.
+At position 1 to 203, the domain is characterized as SMP-LTD.
+At position 217 to 386, the domain is characterized as PCI.
+At position 35 to 150, the domain is characterized as sHSP.
+At position 14 to 201, the domain is characterized as RNase H type-2.
+At position 226 to 317, the domain is characterized as RRM.
+At position 15 to 112, the domain is characterized as SCP2.
+At position 30 to 220, the domain is characterized as Cupin type-1 1.
+At position 284 to 433, the domain is characterized as Cupin type-1 2.
+At position 91 to 308, the domain is characterized as RNase H type-2.
+At position 214 to 336, the domain is characterized as SET.
+At position 8 to 284, the domain is characterized as tr-type G.
+At position 25 to 183, the domain is characterized as Helicase ATP-binding.
+At position 35 to 77, the domain is characterized as Chitin-binding type-1.
+At position 10 to 154, the domain is characterized as N-acetyltransferase 1.
+At position 156 to 305, the domain is characterized as N-acetyltransferase 2.
+At position 12 to 261, the domain is characterized as Radical SAM core.
+At position 31 to 266, the domain is characterized as ABC transporter.
+At position 412 to 461, the domain is characterized as bHLH.
+At position 708 to 772, the domain is characterized as SAM.
+At position 600 to 675, the domain is characterized as Carrier 1.
+At position 1168 to 1241, the domain is characterized as Carrier 2.
+At position 1236 to 1312, the domain is characterized as Carrier 3.
+At position 1143 to 1322, the domain is characterized as DOC.
+At position 151 to 253, the domain is characterized as PB1.
+At position 590 to 667, the domain is characterized as RRM 1.
+At position 666 to 743, the domain is characterized as RRM 2.
+At position 757 to 832, the domain is characterized as RRM 3.
+At position 874 to 946, the domain is characterized as RRM 4.
+At position 107 to 311, the domain is characterized as ATP-grasp.
+At position 70 to 317, the domain is characterized as Calpain catalytic.
+At position 329 to 403, the domain is characterized as HSA.
+At position 837 to 1002, the domain is characterized as Helicase ATP-binding.
+At position 1377 to 1527, the domain is characterized as Helicase C-terminal.
+At position 83 to 259, the domain is characterized as BPL/LPL catalytic.
+At position 106 to 296, the domain is characterized as Helicase ATP-binding.
+At position 335 to 498, the domain is characterized as Helicase C-terminal.
+At position 183 to 373, the domain is characterized as CheB-type methylesterase.
+At position 7 to 133, the domain is characterized as MATH.
+At position 16 to 130, the domain is characterized as MTTase N-terminal.
+At position 150 to 382, the domain is characterized as Radical SAM core.
+At position 385 to 455, the domain is characterized as TRAM.
+At position 147 to 425, the domain is characterized as Protein kinase.
+At position 132 to 571, the domain is characterized as Urease.
+At position 319 to 453, the domain is characterized as C-CAP/cofactor C-like.
+At position 67 to 168, the domain is characterized as Glutaredoxin.
+At position 137 to 370, the domain is characterized as Radical SAM core.
+At position 373 to 433, the domain is characterized as TRAM.
+At position 17 to 52, the domain is characterized as EF-hand 1.
+At position 53 to 88, the domain is characterized as EF-hand 2.
+At position 129 to 162, the domain is characterized as EF-hand 4.
+At position 1 to 263, the domain is characterized as CheR-type methyltransferase.
+At position 11 to 324, the domain is characterized as Kinesin motor.
+At position 19 to 215, the domain is characterized as Laminin G-like.
+At position 318 to 375, the domain is characterized as VWFC.
+At position 381 to 431, the domain is characterized as TSP type-1 1.
+At position 437 to 492, the domain is characterized as TSP type-1 2.
+At position 494 to 549, the domain is characterized as TSP type-1 3.
+At position 549 to 589, the domain is characterized as EGF-like 1.
+At position 648 to 692, the domain is characterized as EGF-like 2.
+At position 960 to 1172, the domain is characterized as TSP C-terminal.
+At position 22 to 271, the domain is characterized as ABC transporter.
+At position 24 to 139, the domain is characterized as Bulb-type lectin.
+At position 274 to 310, the domain is characterized as EGF-like; atypical.
+At position 321 to 407, the domain is characterized as PAN.
+At position 461 to 742, the domain is characterized as Protein kinase.
+At position 6 to 489, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 523 to 811, the domain is characterized as UvrD-like helicase C-terminal.
+At position 473 to 679, the domain is characterized as MCM.
+At position 177 to 352, the domain is characterized as CRAL-TRIO.
+At position 9 to 62, the domain is characterized as TIL.
+At position 27 to 108, the domain is characterized as UPAR/Ly6.
+At position 124 to 198, the domain is characterized as POU-specific.
+At position 15 to 96, the domain is characterized as Expansin-like CBD.
+At position 28 to 122, the domain is characterized as Ig-like 1.
+At position 127 to 214, the domain is characterized as Ig-like 2.
+At position 227 to 314, the domain is characterized as Ig-like 3.
+At position 319 to 403, the domain is characterized as Ig-like 4.
+At position 413 to 507, the domain is characterized as Fibronectin type-III 1.
+At position 509 to 605, the domain is characterized as Fibronectin type-III 2.
+At position 610 to 709, the domain is characterized as Fibronectin type-III 3.
+At position 716 to 809, the domain is characterized as Fibronectin type-III 4.
+At position 814 to 909, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 79, the domain is characterized as Carrier.
+At position 16 to 107, the domain is characterized as Chorismate mutase.
+At position 724 to 794, the domain is characterized as Bromo 1.
+At position 1120 to 1190, the domain is characterized as Bromo 2.
+At position 117 to 609, the domain is characterized as Lipoxygenase.
+At position 156 to 339, the domain is characterized as PID.
+At position 488 to 579, the domain is characterized as SH2.
+At position 222 to 282, the domain is characterized as HTH myb-type.
+At position 55 to 354, the domain is characterized as Calpain catalytic.
+At position 586 to 621, the domain is characterized as EF-hand 1.
+At position 623 to 651, the domain is characterized as EF-hand 2.
+At position 274 to 413, the domain is characterized as Helicase ATP-binding.
+At position 629 to 789, the domain is characterized as Helicase C-terminal.
+At position 817 to 912, the domain is characterized as Dicer dsRNA-binding fold.
+At position 1163 to 1296, the domain is characterized as PAZ.
+At position 1320 to 1498, the domain is characterized as RNase III 1.
+At position 1538 to 1686, the domain is characterized as RNase III 2.
+At position 1712 to 1775, the domain is characterized as DRBM 1.
+At position 1797 to 1872, the domain is characterized as DRBM 2.
+At position 39 to 129, the domain is characterized as RRM.
+At position 25 to 61, the domain is characterized as CBM1 1.
+At position 68 to 104, the domain is characterized as CBM1 2.
+At position 43 to 114, the domain is characterized as S4 RNA-binding.
+At position 545 to 608, the domain is characterized as SAM.
+At position 59 to 152, the domain is characterized as PH.
+At position 322 to 457, the domain is characterized as DAGKc.
+At position 823 to 862, the domain is characterized as Pentapeptide repeat.
+At position 28 to 143, the domain is characterized as Thioredoxin 1.
+At position 147 to 262, the domain is characterized as Thioredoxin 2.
+At position 210 to 391, the domain is characterized as PCI.
+At position 211 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 21 to 75, the domain is characterized as MIR 1.
+At position 83 to 138, the domain is characterized as MIR 2.
+At position 139 to 193, the domain is characterized as MIR 3.
+At position 435 to 489, the domain is characterized as HTH myb-type.
+At position 10 to 294, the domain is characterized as Pterin-binding.
+At position 61 to 169, the domain is characterized as FAD-binding FR-type.
+At position 12 to 93, the domain is characterized as RRM.
+At position 158 to 314, the domain is characterized as PPIase cyclophilin-type.
+At position 20 to 271, the domain is characterized as Protein kinase.
+At position 295 to 335, the domain is characterized as UBA.
+At position 137 to 212, the domain is characterized as RRM 1.
+At position 234 to 310, the domain is characterized as RRM 2.
+At position 32 to 189, the domain is characterized as PPIase cyclophilin-type.
+At position 175 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 552 to 693, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1163 to 1295, the domain is characterized as DOD-type homing endonuclease 2.
+At position 7 to 121, the domain is characterized as Response regulatory.
+At position 142 to 341, the domain is characterized as Sigma-54 factor interaction.
+At position 163 to 275, the domain is characterized as PINc.
+At position 289 to 350, the domain is characterized as TRAM.
+At position 79 to 179, the domain is characterized as Toprim.
+At position 218 to 284, the domain is characterized as J.
+At position 22 to 192, the domain is characterized as EngB-type G.
+At position 397 to 497, the domain is characterized as PFU.
+At position 586 to 856, the domain is characterized as PUL.
+At position 78 to 269, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 308, the domain is characterized as Protein kinase.
+At position 121 to 399, the domain is characterized as NB-ARC.
+At position 10 to 122, the domain is characterized as HotDog ACOT-type.
+At position 86 to 177, the domain is characterized as HTH La-type RNA-binding.
+At position 184 to 296, the domain is characterized as RRM.
+At position 427 to 485, the domain is characterized as SUZ-C.
+At position 244 to 415, the domain is characterized as W2.
+At position 67 to 102, the domain is characterized as EF-hand 1.
+At position 115 to 145, the domain is characterized as EF-hand 2.
+At position 39 to 217, the domain is characterized as Eph LBD.
+At position 339 to 451, the domain is characterized as Fibronectin type-III 1.
+At position 452 to 545, the domain is characterized as Fibronectin type-III 2.
+At position 633 to 896, the domain is characterized as Protein kinase.
+At position 925 to 989, the domain is characterized as SAM.
+At position 123 to 500, the domain is characterized as Protein kinase.
+At position 1 to 102, the domain is characterized as Thioredoxin.
+At position 69 to 261, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 96, the domain is characterized as EF-hand 2.
+At position 98 to 133, the domain is characterized as EF-hand 3.
+At position 134 to 169, the domain is characterized as EF-hand 4.
+At position 20 to 68, the domain is characterized as F-box.
+At position 84 to 178, the domain is characterized as PA.
+At position 106 to 283, the domain is characterized as Tyr recombinase.
+At position 39 to 62, the domain is characterized as IQ.
+At position 21 to 95, the domain is characterized as UPAR/Ly6.
+At position 42 to 272, the domain is characterized as ABC transporter.
+At position 493 to 702, the domain is characterized as MCM.
+At position 40 to 133, the domain is characterized as LCCL.
+At position 267 to 452, the domain is characterized as VWFA 1.
+At position 469 to 638, the domain is characterized as VWFA 2.
+At position 480 to 646, the domain is characterized as HNH Cas9-type.
+At position 42 to 162, the domain is characterized as Plastocyanin-like.
+At position 89 to 274, the domain is characterized as ATP-grasp.
+At position 11 to 97, the domain is characterized as Core-binding (CB).
+At position 118 to 298, the domain is characterized as Tyr recombinase.
+At position 239 to 483, the domain is characterized as CN hydrolase.
+At position 55 to 84, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 45 to 155, the domain is characterized as SRCR 1.
+At position 160 to 259, the domain is characterized as SRCR 2.
+At position 264 to 360, the domain is characterized as SRCR 3.
+At position 3 to 78, the domain is characterized as GIY-YIG.
+At position 443 to 502, the domain is characterized as Collagen-like 1.
+At position 527 to 586, the domain is characterized as Collagen-like 2.
+At position 614 to 731, the domain is characterized as C-type lectin.
+At position 44 to 94, the domain is characterized as bHLH.
+At position 102 to 225, the domain is characterized as MPN.
+At position 11 to 167, the domain is characterized as PPIase cyclophilin-type.
+At position 88 to 153, the domain is characterized as S4 RNA-binding.
+At position 52 to 112, the domain is characterized as v-SNARE coiled-coil homology.
+At position 104 to 172, the domain is characterized as FHA.
+At position 33 to 405, the domain is characterized as PIPK.
+At position 429 to 623, the domain is characterized as Thioredoxin.
+At position 124 to 156, the domain is characterized as EF-hand 4.
+At position 221 to 321, the domain is characterized as Rieske.
+At position 219 to 315, the domain is characterized as CRM 1.
+At position 421 to 518, the domain is characterized as CRM 2.
+At position 636 to 736, the domain is characterized as CRM 3.
+At position 7 to 125, the domain is characterized as Response regulatory.
+At position 72 to 167, the domain is characterized as Fibronectin type-III.
+At position 27 to 274, the domain is characterized as AB hydrolase-1.
+At position 18 to 169, the domain is characterized as Thioredoxin.
+At position 202 to 366, the domain is characterized as Hflx-type G.
+At position 67 to 195, the domain is characterized as Runt.
+At position 204 to 282, the domain is characterized as KH type-2.
+At position 10 to 280, the domain is characterized as F-BAR.
+At position 382 to 441, the domain is characterized as SH3.
+At position 1 to 378, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 30 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 91 to 123, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 124 to 153, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 158 to 189, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 177 to 361, the domain is characterized as Glutamine amidotransferase type-1.
+At position 22 to 214, the domain is characterized as Albumin 1.
+At position 215 to 407, the domain is characterized as Albumin 2.
+At position 408 to 605, the domain is characterized as Albumin 3.
+At position 16 to 97, the domain is characterized as GS beta-grasp.
+At position 103 to 443, the domain is characterized as GS catalytic.
+At position 7 to 122, the domain is characterized as MTTase N-terminal.
+At position 141 to 369, the domain is characterized as Radical SAM core.
+At position 57 to 106, the domain is characterized as HTH myb-type 2.
+At position 49 to 124, the domain is characterized as Rho RNA-BD.
+At position 51 to 300, the domain is characterized as GB1/RHD3-type G.
+At position 48 to 233, the domain is characterized as Helicase ATP-binding.
+At position 246 to 479, the domain is characterized as Helicase C-terminal.
+At position 42 to 200, the domain is characterized as PCI.
+At position 4 to 166, the domain is characterized as EngA-type G 1.
+At position 18 to 211, the domain is characterized as UmuC.
+At position 133 to 307, the domain is characterized as Helicase ATP-binding.
+At position 335 to 483, the domain is characterized as Helicase C-terminal.
+At position 597 to 675, the domain is characterized as BRCT.
+At position 1 to 98, the domain is characterized as Ig-like V-type.
+At position 99 to 176, the domain is characterized as Ig-like C2-type 1.
+At position 177 to 290, the domain is characterized as Ig-like C2-type 2.
+At position 291 to 347, the domain is characterized as Ig-like C2-type 3.
+At position 1213 to 1282, the domain is characterized as S1 motif.
+At position 1325 to 1431, the domain is characterized as SH2.
+At position 186 to 248, the domain is characterized as LIM zinc-binding.
+At position 723 to 874, the domain is characterized as bMERB.
+At position 23 to 101, the domain is characterized as POTRA.
+At position 21 to 111, the domain is characterized as Ig-like.
+At position 800 to 874, the domain is characterized as ACT 2.
+At position 1 to 137, the domain is characterized as SPX.
+At position 404 to 460, the domain is characterized as HTH myb-type.
+At position 61 to 96, the domain is characterized as EF-hand.
+At position 130 to 198, the domain is characterized as SAM.
+At position 4 to 226, the domain is characterized as Glutamine amidotransferase type-1.
+At position 138 to 197, the domain is characterized as TSP type-1.
+At position 82 to 299, the domain is characterized as Radical SAM core.
+At position 6 to 133, the domain is characterized as CMP/dCMP-type deaminase.
+At position 334 to 571, the domain is characterized as ABC transporter.
+At position 91 to 160, the domain is characterized as SH3.
+At position 691 to 764, the domain is characterized as BTB.
+At position 1 to 274, the domain is characterized as CheR-type methyltransferase.
+At position 198 to 304, the domain is characterized as RRM.
+At position 1 to 154, the domain is characterized as C2.
+At position 368 to 403, the domain is characterized as PLD phosphodiesterase 1.
+At position 713 to 740, the domain is characterized as PLD phosphodiesterase 2.
+At position 4 to 83, the domain is characterized as GIY-YIG.
+At position 147 to 207, the domain is characterized as TSP type-1.
+At position 56 to 202, the domain is characterized as Cupin type-1.
+At position 207 to 376, the domain is characterized as tr-type G.
+At position 167 to 227, the domain is characterized as v-SNARE coiled-coil homology.
+At position 218 to 412, the domain is characterized as Peptidase M12B.
+At position 420 to 470, the domain is characterized as Disintegrin.
+At position 341 to 510, the domain is characterized as tr-type G.
+At position 11 to 106, the domain is characterized as Fibronectin type-III.
+At position 37 to 138, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 228, the domain is characterized as Ig-like C2-type 2.
+At position 242 to 330, the domain is characterized as Ig-like C2-type 3.
+At position 336 to 425, the domain is characterized as Ig-like C2-type 4.
+At position 450 to 558, the domain is characterized as Fibronectin type-III 1.
+At position 566 to 661, the domain is characterized as Fibronectin type-III 2.
+At position 221 to 381, the domain is characterized as TrmE-type G.
+At position 10 to 60, the domain is characterized as CHCH.
+At position 60 to 315, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 14 to 90, the domain is characterized as PAS.
+At position 178 to 231, the domain is characterized as HAMP.
+At position 239 to 451, the domain is characterized as Histidine kinase.
+At position 9 to 67, the domain is characterized as CpcD-like.
+At position 104 to 228, the domain is characterized as FAD-binding FR-type.
+At position 67 to 105, the domain is characterized as LRRNT.
+At position 18 to 171, the domain is characterized as Helicase ATP-binding.
+At position 241 to 386, the domain is characterized as Helicase C-terminal.
+At position 418 to 476, the domain is characterized as CBS.
+At position 38 to 111, the domain is characterized as H15.
+At position 45 to 123, the domain is characterized as RRM.
+At position 713 to 973, the domain is characterized as Tyrosine-protein phosphatase.
+At position 138 to 173, the domain is characterized as EF-hand 4.
+At position 293 to 498, the domain is characterized as Peptidase M12B.
+At position 498 to 577, the domain is characterized as Disintegrin.
+At position 589 to 644, the domain is characterized as TSP type-1 1.
+At position 931 to 990, the domain is characterized as TSP type-1 2.
+At position 991 to 1049, the domain is characterized as TSP type-1 3.
+At position 1052 to 1116, the domain is characterized as TSP type-1 4.
+At position 1123 to 1178, the domain is characterized as TSP type-1 5.
+At position 1184 to 1221, the domain is characterized as PLAC.
+At position 568 to 731, the domain is characterized as Helicase ATP-binding.
+At position 753 to 933, the domain is characterized as Helicase C-terminal.
+At position 60 to 135, the domain is characterized as Carrier.
+At position 351 to 558, the domain is characterized as MCM.
+At position 348 to 531, the domain is characterized as MIF4G.
+At position 641 to 757, the domain is characterized as MI.
+At position 430 to 459, the domain is characterized as IQ.
+At position 618 to 698, the domain is characterized as BRCT.
+At position 140 to 369, the domain is characterized as Sigma-54 factor interaction.
+At position 18 to 134, the domain is characterized as Thioredoxin 1.
+At position 349 to 475, the domain is characterized as Thioredoxin 2.
+At position 36 to 289, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 15 to 148, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 76 to 249, the domain is characterized as Helicase ATP-binding.
+At position 261 to 422, the domain is characterized as Helicase C-terminal.
+At position 562 to 613, the domain is characterized as GRIP.
+At position 5 to 74, the domain is characterized as BTB.
+At position 6 to 244, the domain is characterized as Radical SAM core.
+At position 596 to 678, the domain is characterized as BRCT.
+At position 235 to 424, the domain is characterized as FAD-binding PCMH-type.
+At position 94 to 215, the domain is characterized as DOD-type homing endonuclease.
+At position 391 to 608, the domain is characterized as tr-type G.
+At position 44 to 273, the domain is characterized as Radical SAM core.
+At position 22 to 149, the domain is characterized as Rhodanese.
+At position 214 to 358, the domain is characterized as Tyrosine-protein phosphatase.
+At position 73 to 277, the domain is characterized as ABC transmembrane type-1.
+At position 182 to 282, the domain is characterized as PH.
+At position 41 to 114, the domain is characterized as U-box.
+At position 328 to 483, the domain is characterized as PPIase cyclophilin-type.
+At position 605 to 686, the domain is characterized as BRCT.
+At position 4 to 147, the domain is characterized as ADF-H.
+At position 562 to 667, the domain is characterized as tRNA-binding.
+At position 1 to 88, the domain is characterized as GST N-terminal.
+At position 6 to 123, the domain is characterized as Response regulatory.
+At position 163 to 228, the domain is characterized as HTH luxR-type.
+At position 1099 to 1216, the domain is characterized as SET.
+At position 1225 to 1241, the domain is characterized as Post-SET.
+At position 177 to 448, the domain is characterized as Peptidase M66.
+At position 97 to 172, the domain is characterized as Smr.
+At position 25 to 138, the domain is characterized as Ig-like C2-type.
+At position 1530 to 1718, the domain is characterized as PIK helical.
+At position 1808 to 2086, the domain is characterized as PI3K/PI4K catalytic.
+At position 1915 to 1944, the domain is characterized as IQ.
+At position 81 to 369, the domain is characterized as Protein kinase.
+At position 324 to 374, the domain is characterized as bHLH.
+At position 23 to 74, the domain is characterized as bHLH.
+At position 5 to 230, the domain is characterized as Radical SAM core.
+At position 21 to 110, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 154 to 184, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 43 to 136, the domain is characterized as Inhibitor I9.
+At position 146 to 448, the domain is characterized as Peptidase S8.
+At position 297 to 485, the domain is characterized as PCI.
+At position 20 to 93, the domain is characterized as S4 RNA-binding.
+At position 4 to 245, the domain is characterized as ABC transporter.
+At position 5 to 211, the domain is characterized as tr-type G.
+At position 11 to 277, the domain is characterized as tr-type G.
+At position 31 to 96, the domain is characterized as J.
+At position 6 to 121, the domain is characterized as MTTase N-terminal.
+At position 145 to 375, the domain is characterized as Radical SAM core.
+At position 378 to 445, the domain is characterized as TRAM.
+At position 52 to 107, the domain is characterized as bHLH.
+At position 142 to 175, the domain is characterized as Orange.
+At position 608 to 696, the domain is characterized as BRCT.
+At position 456 to 598, the domain is characterized as SIS 2.
+At position 104 to 153, the domain is characterized as Myosin N-terminal SH3-like.
+At position 157 to 829, the domain is characterized as Myosin motor.
+At position 831 to 860, the domain is characterized as IQ 1.
+At position 854 to 883, the domain is characterized as IQ 2.
+At position 903 to 932, the domain is characterized as IQ 3.
+At position 5 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 109 to 229, the domain is characterized as OTU.
+At position 371 to 430, the domain is characterized as SH3.
+At position 129 to 215, the domain is characterized as PB1.
+At position 5 to 75, the domain is characterized as J.
+At position 212 to 304, the domain is characterized as ARID.
+At position 407 to 501, the domain is characterized as REKLES.
+At position 29 to 205, the domain is characterized as FAD-binding PCMH-type.
+At position 381 to 503, the domain is characterized as C2.
+At position 592 to 872, the domain is characterized as Ras-GAP.
+At position 303 to 422, the domain is characterized as MATH.
+At position 1 to 246, the domain is characterized as Deacetylase sirtuin-type.
+At position 105 to 292, the domain is characterized as Tyr recombinase.
+At position 262 to 345, the domain is characterized as IPT/TIG.
+At position 15 to 125, the domain is characterized as MTTase N-terminal.
+At position 142 to 379, the domain is characterized as Radical SAM core.
+At position 379 to 447, the domain is characterized as TRAM.
+At position 41 to 76, the domain is characterized as EF-hand 2.
+At position 196 to 231, the domain is characterized as EF-hand 3.
+At position 233 to 268, the domain is characterized as EF-hand 4.
+At position 7 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 741 to 873, the domain is characterized as BAH 1.
+At position 1093 to 1527, the domain is characterized as SAM-dependent MTase C5-type.
+At position 66 to 176, the domain is characterized as Expansin-like EG45.
+At position 189 to 270, the domain is characterized as Expansin-like CBD.
+At position 17 to 140, the domain is characterized as CUB 1.
+At position 141 to 189, the domain is characterized as EGF-like; calcium-binding.
+At position 192 to 304, the domain is characterized as CUB 2.
+At position 306 to 372, the domain is characterized as Sushi 1.
+At position 373 to 448, the domain is characterized as Sushi 2.
+At position 463 to 703, the domain is characterized as Peptidase S1.
+At position 28 to 202, the domain is characterized as Laminin G-like 1.
+At position 198 to 235, the domain is characterized as EGF-like 1.
+At position 258 to 440, the domain is characterized as Laminin G-like 2.
+At position 447 to 639, the domain is characterized as Laminin G-like 3.
+At position 643 to 680, the domain is characterized as EGF-like 2.
+At position 685 to 857, the domain is characterized as Laminin G-like 4.
+At position 871 to 1046, the domain is characterized as Laminin G-like 5.
+At position 1049 to 1086, the domain is characterized as EGF-like 3.
+At position 1090 to 1290, the domain is characterized as Laminin G-like 6.
+At position 11 to 197, the domain is characterized as RNase H type-2.
+At position 47 to 141, the domain is characterized as UPAR/Ly6.
+At position 5 to 195, the domain is characterized as Flavodoxin-like.
+At position 236 to 328, the domain is characterized as RRM 1.
+At position 350 to 431, the domain is characterized as RRM 2.
+At position 14 to 168, the domain is characterized as UBC core.
+At position 214 to 314, the domain is characterized as Fe2OG dioxygenase.
+At position 188 to 501, the domain is characterized as IF rod.
+At position 71 to 207, the domain is characterized as RNase H type-1.
+At position 505 to 547, the domain is characterized as CAP-Gly 2.
+At position 33 to 441, the domain is characterized as SET.
+At position 245 to 474, the domain is characterized as Sigma-54 factor interaction.
+At position 19 to 80, the domain is characterized as HTH asnC-type.
+At position 24 to 414, the domain is characterized as Helicase ATP-binding.
+At position 426 to 591, the domain is characterized as Helicase C-terminal.
+At position 610 to 645, the domain is characterized as UVR.
+At position 104 to 165, the domain is characterized as J.
+At position 367 to 457, the domain is characterized as SEC63 1.
+At position 637 to 714, the domain is characterized as SEC63 2.
+At position 203 to 393, the domain is characterized as Peptidase M12B.
+At position 399 to 485, the domain is characterized as Disintegrin.
+At position 629 to 663, the domain is characterized as EGF-like.
+At position 247 to 439, the domain is characterized as GATase cobBQ-type.
+At position 31 to 523, the domain is characterized as Sema.
+At position 4 to 144, the domain is characterized as Tyrosine-protein phosphatase.
+At position 413 to 447, the domain is characterized as SAP.
+At position 35 to 68, the domain is characterized as LRRNT.
+At position 440 to 491, the domain is characterized as LRRCT.
+At position 495 to 594, the domain is characterized as Ig-like C2-type 1.
+At position 599 to 688, the domain is characterized as Ig-like C2-type 2.
+At position 693 to 779, the domain is characterized as Ig-like C2-type 3.
+At position 233 to 366, the domain is characterized as GGDEF.
+At position 30 to 168, the domain is characterized as MRH.
+At position 96 to 328, the domain is characterized as ABC transmembrane type-1.
+At position 6 to 64, the domain is characterized as TRAM.
+At position 688 to 717, the domain is characterized as IQ.
+At position 50 to 277, the domain is characterized as Radical SAM core.
+At position 374 to 807, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1294 to 1600, the domain is characterized as PKS/mFAS DH.
+At position 1649 to 1726, the domain is characterized as Carrier 1.
+At position 1764 to 1838, the domain is characterized as Carrier 2.
+At position 57 to 161, the domain is characterized as Core-binding (CB).
+At position 181 to 362, the domain is characterized as Tyr recombinase.
+At position 92 to 424, the domain is characterized as Asparaginase/glutaminase.
+At position 309 to 436, the domain is characterized as Ricin B-type lectin 1.
+At position 440 to 564, the domain is characterized as Ricin B-type lectin 2.
+At position 97 to 124, the domain is characterized as IQ.
+At position 250 to 417, the domain is characterized as W2.
+At position 233 to 327, the domain is characterized as PB1.
+At position 46 to 274, the domain is characterized as Radical SAM core.
+At position 593 to 694, the domain is characterized as tRNA-binding.
+At position 14 to 788, the domain is characterized as ABC transporter.
+At position 3 to 448, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 478 to 745, the domain is characterized as UvrD-like helicase C-terminal.
+At position 187 to 294, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 96 to 163, the domain is characterized as DRBM 1.
+At position 196 to 264, the domain is characterized as DRBM 2.
+At position 286 to 364, the domain is characterized as PUA.
+At position 54 to 155, the domain is characterized as LOB.
+At position 32 to 64, the domain is characterized as EGF-like 1.
+At position 67 to 109, the domain is characterized as EGF-like 2; calcium-binding.
+At position 110 to 151, the domain is characterized as EGF-like 3; calcium-binding.
+At position 294 to 325, the domain is characterized as EGF-like 4.
+At position 335 to 590, the domain is characterized as ZP.
+At position 9 to 261, the domain is characterized as Pyruvate carboxyltransferase.
+At position 60 to 263, the domain is characterized as ABC transmembrane type-1.
+At position 420 to 495, the domain is characterized as B5.
+At position 25 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 25 to 111, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 242 to 350, the domain is characterized as Ig-like C2-type 3.
+At position 12 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 211 to 403, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 111, the domain is characterized as Toprim.
+At position 103 to 259, the domain is characterized as CP-type G.
+At position 75 to 174, the domain is characterized as Mis18.
+At position 2 to 76, the domain is characterized as Ubiquitin-like 1.
+At position 77 to 155, the domain is characterized as Ubiquitin-like 2.
+At position 137 to 303, the domain is characterized as Integrase catalytic.
+At position 41 to 97, the domain is characterized as HTH cro/C1-type.
+At position 128 to 298, the domain is characterized as Era-type G.
+At position 329 to 406, the domain is characterized as KH type-2.
+At position 39 to 230, the domain is characterized as Helicase ATP-binding.
+At position 247 to 419, the domain is characterized as Helicase C-terminal.
+At position 627 to 788, the domain is characterized as SSD.
+At position 367 to 641, the domain is characterized as Protein kinase.
+At position 94 to 179, the domain is characterized as RRM.
+At position 781 to 898, the domain is characterized as SET.
+At position 904 to 920, the domain is characterized as Post-SET.
+At position 99 to 153, the domain is characterized as HTH cro/C1-type.
+At position 3 to 101, the domain is characterized as Glutaredoxin.
+At position 115 to 189, the domain is characterized as PRC barrel.
+At position 111 to 146, the domain is characterized as EF-hand.
+At position 139 to 203, the domain is characterized as S1 motif.
+At position 308 to 378, the domain is characterized as KH.
+At position 3 to 84, the domain is characterized as PDZ 1.
+At position 279 to 356, the domain is characterized as PDZ 2.
+At position 820 to 1211, the domain is characterized as FH2.
+At position 458 to 590, the domain is characterized as Ricin B-type lectin.
+At position 7 to 292, the domain is characterized as Protein kinase.
+At position 8 to 297, the domain is characterized as tr-type G.
+At position 96 to 273, the domain is characterized as uDENN.
+At position 299 to 476, the domain is characterized as cDENN.
+At position 478 to 600, the domain is characterized as dDENN.
+At position 389 to 428, the domain is characterized as UBA.
+At position 10 to 99, the domain is characterized as ACB.
+At position 33 to 110, the domain is characterized as CIDE-N.
+At position 120 to 184, the domain is characterized as PDZ.
+At position 2 to 79, the domain is characterized as GIY-YIG.
+At position 14 to 305, the domain is characterized as Protein kinase.
+At position 28 to 85, the domain is characterized as FHA.
+At position 14 to 195, the domain is characterized as tr-type G.
+At position 118 to 167, the domain is characterized as bHLH.
+At position 1 to 25, the domain is characterized as Peptidase S1.
+At position 61 to 93, the domain is characterized as LDL-receptor class A.
+At position 94 to 204, the domain is characterized as SRCR.
+At position 205 to 434, the domain is characterized as Peptidase S1.
+At position 4 to 90, the domain is characterized as BMC.
+At position 770 to 846, the domain is characterized as Carrier 1.
+At position 1845 to 1921, the domain is characterized as Carrier 2.
+At position 29 to 141, the domain is characterized as Ig-like V-type.
+At position 310 to 506, the domain is characterized as B30.2/SPRY.
+At position 135 to 396, the domain is characterized as NR LBD.
+At position 105 to 227, the domain is characterized as MPN.
+At position 133 to 364, the domain is characterized as SET.
+At position 36 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 154 to 253, the domain is characterized as SH2.
+At position 548 to 818, the domain is characterized as Ras-GEF.
+At position 77 to 177, the domain is characterized as Fe2OG dioxygenase.
+At position 19 to 72, the domain is characterized as Rubredoxin-like.
+At position 385 to 448, the domain is characterized as Thioredoxin.
+At position 98 to 358, the domain is characterized as ABC transporter.
+At position 449 to 659, the domain is characterized as ABC transmembrane type-2.
+At position 152 to 409, the domain is characterized as Protein kinase.
+At position 410 to 481, the domain is characterized as AGC-kinase C-terminal.
+At position 5 to 40, the domain is characterized as EF-hand 1.
+At position 45 to 90, the domain is characterized as EF-hand 2.
+At position 100 to 134, the domain is characterized as EF-hand 3.
+At position 379 to 484, the domain is characterized as PAZ.
+At position 649 to 950, the domain is characterized as Piwi.
+At position 28 to 242, the domain is characterized as MIF4G.
+At position 10 to 85, the domain is characterized as Carrier.
+At position 185 to 287, the domain is characterized as Fe2OG dioxygenase.
+At position 4 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 395, the domain is characterized as GMPS ATP-PPase.
+At position 5 to 195, the domain is characterized as HD Cas3-type.
+At position 52 to 334, the domain is characterized as FAE.
+At position 22 to 53, the domain is characterized as LRRNT.
+At position 423 to 475, the domain is characterized as LRRCT.
+At position 184 to 266, the domain is characterized as RRM 1.
+At position 291 to 368, the domain is characterized as RRM 2.
+At position 404 to 488, the domain is characterized as RRM 3.
+At position 383 to 611, the domain is characterized as START.
+At position 52 to 279, the domain is characterized as Radical SAM core.
+At position 5 to 149, the domain is characterized as PPPDE.
+At position 38 to 217, the domain is characterized as PCI.
+At position 1 to 55, the domain is characterized as LCN-type CS-alpha/beta.
+At position 34 to 270, the domain is characterized as Radical SAM core.
+At position 1058 to 1281, the domain is characterized as JmjC.
+At position 65 to 255, the domain is characterized as YrdC-like.
+At position 1 to 192, the domain is characterized as Glutamine amidotransferase type-1.
+At position 30 to 80, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 191 to 405, the domain is characterized as Galectin.
+At position 183 to 302, the domain is characterized as GST C-terminal.
+At position 21 to 78, the domain is characterized as bHLH.
+At position 68 to 502, the domain is characterized as USP.
+At position 383 to 560, the domain is characterized as Helicase ATP-binding.
+At position 617 to 766, the domain is characterized as Helicase C-terminal.
+At position 10 to 205, the domain is characterized as YjeF N-terminal.
+At position 210 to 473, the domain is characterized as YjeF C-terminal.
+At position 11 to 231, the domain is characterized as ABC transporter.
+At position 75 to 110, the domain is characterized as EF-hand 2.
+At position 111 to 143, the domain is characterized as EF-hand 3.
+At position 55 to 110, the domain is characterized as Tudor-knot.
+At position 174 to 447, the domain is characterized as MYST-type HAT.
+At position 1 to 60, the domain is characterized as MARVEL.
+At position 228 to 384, the domain is characterized as W2.
+At position 211 to 410, the domain is characterized as Peptidase M12A.
+At position 405 to 445, the domain is characterized as EGF-like.
+At position 455 to 571, the domain is characterized as CUB.
+At position 2 to 263, the domain is characterized as Protein kinase.
+At position 297 to 372, the domain is characterized as SAM.
+At position 96 to 167, the domain is characterized as SUI1.
+At position 2 to 111, the domain is characterized as CMP/dCMP-type deaminase.
+At position 24 to 145, the domain is characterized as Thioredoxin 1.
+At position 366 to 485, the domain is characterized as Thioredoxin 2.
+At position 20 to 120, the domain is characterized as PH.
+At position 152 to 248, the domain is characterized as SH2.
+At position 25 to 289, the domain is characterized as Protein kinase.
+At position 920 to 1207, the domain is characterized as CNH.
+At position 138 to 216, the domain is characterized as RRM.
+At position 402 to 479, the domain is characterized as ACT.
+At position 112 to 193, the domain is characterized as RRM 1.
+At position 268 to 329, the domain is characterized as RRM 2.
+At position 27 to 296, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 12 to 174, the domain is characterized as TIR.
+At position 211 to 474, the domain is characterized as NB-ARC.
+At position 83 to 199, the domain is characterized as RGS.
+At position 1 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 152 to 187, the domain is characterized as EF-hand 1.
+At position 257 to 292, the domain is characterized as EF-hand 2.
+At position 406 to 441, the domain is characterized as EF-hand 3.
+At position 476 to 511, the domain is characterized as EF-hand 4.
+At position 579 to 614, the domain is characterized as EF-hand 5.
+At position 37 to 115, the domain is characterized as RRM.
+At position 13 to 137, the domain is characterized as Arf-GAP.
+At position 458 to 665, the domain is characterized as MCM.
+At position 103 to 273, the domain is characterized as CP-type G.
+At position 493 to 632, the domain is characterized as Flavodoxin-like.
+At position 671 to 904, the domain is characterized as FAD-binding FR-type.
+At position 1 to 134, the domain is characterized as DAGKc.
+At position 442 to 522, the domain is characterized as HRDC.
+At position 1 to 278, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 272 to 590, the domain is characterized as UvrD-like helicase C-terminal.
+At position 220 to 321, the domain is characterized as PH.
+At position 312 to 430, the domain is characterized as C2.
+At position 484 to 676, the domain is characterized as Ras-GAP.
+At position 226 to 285, the domain is characterized as LIM zinc-binding 1.
+At position 286 to 343, the domain is characterized as LIM zinc-binding 2.
+At position 344 to 403, the domain is characterized as LIM zinc-binding 3.
+At position 404 to 461, the domain is characterized as LIM zinc-binding 4.
+At position 19 to 299, the domain is characterized as Protein kinase.
+At position 8 to 93, the domain is characterized as BRCT 1.
+At position 94 to 183, the domain is characterized as BRCT 2.
+At position 588 to 681, the domain is characterized as BRCT 3.
+At position 688 to 776, the domain is characterized as BRCT 4.
+At position 853 to 934, the domain is characterized as BRCT 5.
+At position 955 to 989, the domain is characterized as BRCT 6.
+At position 97 to 116, the domain is characterized as UIM.
+At position 162 to 650, the domain is characterized as USP.
+At position 110 to 186, the domain is characterized as DEP.
+At position 384 to 518, the domain is characterized as N-terminal Ras-GEF.
+At position 662 to 889, the domain is characterized as Ras-GEF.
+At position 29 to 138, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 214 to 328, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 93 to 343, the domain is characterized as Protein kinase.
+At position 31 to 134, the domain is characterized as Ig-like V-type.
+At position 159 to 244, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 350, the domain is characterized as Ig-like C2-type 2.
+At position 355 to 452, the domain is characterized as Ig-like C2-type 3.
+At position 623 to 658, the domain is characterized as EF-hand 1.
+At position 659 to 694, the domain is characterized as EF-hand 2.
+At position 14 to 206, the domain is characterized as RNase H type-2.
+At position 180 to 256, the domain is characterized as RRM.
+At position 40 to 154, the domain is characterized as TBDR plug.
+At position 159 to 624, the domain is characterized as TBDR beta-barrel.
+At position 165 to 475, the domain is characterized as Peptidase S8.
+At position 681 to 856, the domain is characterized as PCI.
+At position 40 to 142, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 177 to 221, the domain is characterized as LysM.
+At position 924 to 1002, the domain is characterized as BIG2.
+At position 1 to 143, the domain is characterized as HTH marR-type.
+At position 136 to 229, the domain is characterized as PpiC.
+At position 36 to 148, the domain is characterized as B12-binding.
+At position 173 to 408, the domain is characterized as Radical SAM core.
+At position 9 to 93, the domain is characterized as MtN3/slv 1.
+At position 128 to 210, the domain is characterized as MtN3/slv 2.
+At position 343 to 409, the domain is characterized as S4 RNA-binding.
+At position 50 to 244, the domain is characterized as Laminin G-like.
+At position 267 to 323, the domain is characterized as Collagen-like 1.
+At position 324 to 355, the domain is characterized as Collagen-like 2.
+At position 356 to 401, the domain is characterized as Collagen-like 3.
+At position 414 to 470, the domain is characterized as Collagen-like 4.
+At position 554 to 612, the domain is characterized as Collagen-like 5.
+At position 613 to 642, the domain is characterized as Collagen-like 6.
+At position 653 to 711, the domain is characterized as Collagen-like 7.
+At position 712 to 753, the domain is characterized as Collagen-like 8.
+At position 788 to 842, the domain is characterized as Collagen-like 9.
+At position 47 to 118, the domain is characterized as KRAB.
+At position 250 to 323, the domain is characterized as HTH CENPB-type.
+At position 353 to 567, the domain is characterized as DDE-1.
+At position 409 to 732, the domain is characterized as Kinesin motor.
+At position 58 to 303, the domain is characterized as Ferric oxidoreductase.
+At position 304 to 419, the domain is characterized as FAD-binding FR-type.
+At position 19 to 144, the domain is characterized as Bulb-type lectin.
+At position 280 to 330, the domain is characterized as EGF-like.
+At position 338 to 421, the domain is characterized as PAN.
+At position 515 to 800, the domain is characterized as Protein kinase.
+At position 65 to 245, the domain is characterized as Helicase ATP-binding.
+At position 506 to 662, the domain is characterized as Toprim.
+At position 274 to 377, the domain is characterized as CobW C-terminal.
+At position 197 to 257, the domain is characterized as KH.
+At position 323 to 418, the domain is characterized as HD.
+At position 29 to 110, the domain is characterized as UPAR/Ly6.
+At position 282 to 360, the domain is characterized as PUA.
+At position 70 to 282, the domain is characterized as ATLF-like 1.
+At position 609 to 804, the domain is characterized as ATLF-like 2.
+At position 5 to 89, the domain is characterized as S1-like.
+At position 1 to 163, the domain is characterized as PTS EIIB type-4.
+At position 122 to 328, the domain is characterized as ATP-grasp.
+At position 53 to 323, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 13 to 92, the domain is characterized as NAB.
+At position 696 to 775, the domain is characterized as BRCT 1.
+At position 954 to 1064, the domain is characterized as BRCT 2.
+At position 405 to 486, the domain is characterized as RCK C-terminal.
+At position 223 to 300, the domain is characterized as SWIB/MDM2.
+At position 333 to 384, the domain is characterized as HTH myb-type.
+At position 385 to 490, the domain is characterized as Myb-like.
+At position 18 to 98, the domain is characterized as PB1.
+At position 134 to 151, the domain is characterized as Pseudo-CRIB.
+At position 158 to 251, the domain is characterized as PDZ.
+At position 7 to 150, the domain is characterized as RNase H type-1.
+At position 386 to 544, the domain is characterized as FCP1 homology.
+At position 16 to 58, the domain is characterized as JmjN.
+At position 144 to 310, the domain is characterized as JmjC.
+At position 875 to 932, the domain is characterized as Tudor 1.
+At position 933 to 989, the domain is characterized as Tudor 2.
+At position 717 to 792, the domain is characterized as Smr.
+At position 257 to 451, the domain is characterized as GATase cobBQ-type.
+At position 144 to 456, the domain is characterized as NB-ARC.
+At position 373 to 439, the domain is characterized as S4 RNA-binding.
+At position 6 to 89, the domain is characterized as MtN3/slv 1.
+At position 124 to 207, the domain is characterized as MtN3/slv 2.
+At position 760 to 940, the domain is characterized as Flavodoxin-like.
+At position 995 to 1242, the domain is characterized as FAD-binding FR-type.
+At position 1 to 433, the domain is characterized as Helicase ATP-binding.
+At position 49 to 177, the domain is characterized as MPN.
+At position 558 to 683, the domain is characterized as DBINO.
+At position 808 to 980, the domain is characterized as Helicase ATP-binding.
+At position 1384 to 1544, the domain is characterized as Helicase C-terminal.
+At position 14 to 75, the domain is characterized as J.
+At position 26 to 97, the domain is characterized as KRAB.
+At position 1043 to 1296, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 84, the domain is characterized as Core-binding (CB).
+At position 100 to 274, the domain is characterized as Tyr recombinase.
+At position 87 to 165, the domain is characterized as RRM 1.
+At position 194 to 272, the domain is characterized as RRM 2.
+At position 1 to 161, the domain is characterized as PCI.
+At position 208 to 398, the domain is characterized as Peptidase M12B.
+At position 634 to 663, the domain is characterized as EGF-like.
+At position 339 to 482, the domain is characterized as RCK N-terminal.
+At position 212 to 610, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 26 to 225, the domain is characterized as DPCK.
+At position 8 to 67, the domain is characterized as SH3.
+At position 103 to 287, the domain is characterized as DH.
+At position 318 to 425, the domain is characterized as PH.
+At position 28 to 136, the domain is characterized as PH.
+At position 33 to 85, the domain is characterized as bHLH.
+At position 4 to 202, the domain is characterized as DPCK.
+At position 726 to 851, the domain is characterized as DBINO.
+At position 1010 to 1182, the domain is characterized as Helicase ATP-binding.
+At position 1583 to 1747, the domain is characterized as Helicase C-terminal.
+At position 19 to 177, the domain is characterized as CheW-like.
+At position 198 to 319, the domain is characterized as Response regulatory.
+At position 28 to 250, the domain is characterized as RNase H type-2.
+At position 540 to 710, the domain is characterized as tr-type G.
+At position 56 to 307, the domain is characterized as Protein kinase.
+At position 326 to 365, the domain is characterized as UBA.
+At position 748 to 797, the domain is characterized as KA1.
+At position 3 to 63, the domain is characterized as HTH tetR-type 1.
+At position 201 to 262, the domain is characterized as HTH tetR-type 2.
+At position 78 to 176, the domain is characterized as Fe2OG dioxygenase.
+At position 83 to 360, the domain is characterized as Protein kinase.
+At position 5 to 160, the domain is characterized as N-acetyltransferase.
+At position 50 to 157, the domain is characterized as Cadherin 1.
+At position 158 to 269, the domain is characterized as Cadherin 2.
+At position 270 to 389, the domain is characterized as Cadherin 3.
+At position 386 to 493, the domain is characterized as Cadherin 4.
+At position 321 to 694, the domain is characterized as GRAS.
+At position 26 to 413, the domain is characterized as Helicase ATP-binding.
+At position 625 to 660, the domain is characterized as UVR.
+At position 34 to 84, the domain is characterized as LIM zinc-binding 1.
+At position 93 to 147, the domain is characterized as LIM zinc-binding 2.
+At position 34 to 144, the domain is characterized as Ig-like V-type.
+At position 148 to 242, the domain is characterized as Link 1.
+At position 245 to 338, the domain is characterized as Link 2.
+At position 2 to 71, the domain is characterized as KH type-2.
+At position 13 to 82, the domain is characterized as J.
+At position 134 to 219, the domain is characterized as MtN3/slv 2.
+At position 18 to 125, the domain is characterized as Rhodanese 1.
+At position 154 to 274, the domain is characterized as Rhodanese 2.
+At position 25 to 297, the domain is characterized as CN hydrolase.
+At position 146 to 227, the domain is characterized as PDZ.
+At position 8 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 19 to 163, the domain is characterized as SprT-like.
+At position 164 to 332, the domain is characterized as Helicase ATP-binding.
+At position 473 to 627, the domain is characterized as Helicase C-terminal.
+At position 291 to 356, the domain is characterized as RH2.
+At position 126 to 216, the domain is characterized as Ig-like C1-type.
+At position 802 to 893, the domain is characterized as PKD.
+At position 23 to 86, the domain is characterized as S5 DRBM.
+At position 41 to 149, the domain is characterized as sHSP.
+At position 541 to 730, the domain is characterized as SEC7.
+At position 190 to 419, the domain is characterized as Sigma-54 factor interaction.
+At position 338 to 613, the domain is characterized as Protein kinase.
+At position 153 to 546, the domain is characterized as SAC.
+At position 712 to 778, the domain is characterized as SAM 1.
+At position 786 to 853, the domain is characterized as SAM 2.
+At position 952 to 1107, the domain is characterized as PID.
+At position 5 to 67, the domain is characterized as TRAM.
+At position 1 to 113, the domain is characterized as HTH marR-type.
+At position 74 to 132, the domain is characterized as TCP.
+At position 78 to 248, the domain is characterized as Helicase ATP-binding.
+At position 258 to 418, the domain is characterized as Helicase C-terminal.
+At position 152 to 365, the domain is characterized as Histidine kinase.
+At position 92 to 172, the domain is characterized as PUA.
+At position 24 to 194, the domain is characterized as Flo11 1.
+At position 332 to 502, the domain is characterized as Flo11 2.
+At position 61 to 166, the domain is characterized as Thioredoxin.
+At position 425 to 532, the domain is characterized as Rhodanese.
+At position 256 to 319, the domain is characterized as bZIP.
+At position 1 to 195, the domain is characterized as Protein kinase.
+At position 1 to 89, the domain is characterized as Pyrin.
+At position 344 to 511, the domain is characterized as tr-type G.
+At position 20 to 215, the domain is characterized as Rho-GAP.
+At position 54 to 145, the domain is characterized as RRM 1.
+At position 163 to 242, the domain is characterized as RRM 2.
+At position 313 to 385, the domain is characterized as RRM 3.
+At position 264 to 327, the domain is characterized as KH.
+At position 390 to 483, the domain is characterized as HD.
+At position 430 to 567, the domain is characterized as Thioredoxin.
+At position 114 to 275, the domain is characterized as TNase-like.
+At position 598 to 723, the domain is characterized as C2.
+At position 38 to 164, the domain is characterized as SCP.
+At position 200 to 233, the domain is characterized as ShKT.
+At position 59 to 128, the domain is characterized as SH3.
+At position 309 to 692, the domain is characterized as GRAS.
+At position 206 to 510, the domain is characterized as DOT1.
+At position 661 to 715, the domain is characterized as bHLH.
+At position 12 to 63, the domain is characterized as LIM zinc-binding 1.
+At position 72 to 124, the domain is characterized as LIM zinc-binding 2.
+At position 152 to 239, the domain is characterized as PDZ.
+At position 331 to 608, the domain is characterized as Protein kinase.
+At position 109 to 253, the domain is characterized as PA14.
+At position 216 to 375, the domain is characterized as TrmE-type G.
+At position 27 to 315, the domain is characterized as tr-type G.
+At position 222 to 403, the domain is characterized as PCI.
+At position 5 to 128, the domain is characterized as MsrB.
+At position 70 to 120, the domain is characterized as Sushi 1.
+At position 121 to 179, the domain is characterized as Sushi 2.
+At position 178 to 262, the domain is characterized as HYR.
+At position 263 to 322, the domain is characterized as Sushi 3.
+At position 349 to 446, the domain is characterized as Rhodanese.
+At position 77 to 162, the domain is characterized as PDZ.
+At position 906 to 1019, the domain is characterized as PH.
+At position 1126 to 1318, the domain is characterized as Rho-GAP.
+At position 403 to 604, the domain is characterized as Rho-GAP.
+At position 31 to 186, the domain is characterized as Helicase ATP-binding.
+At position 84 to 176, the domain is characterized as Ig-like C1-type.
+At position 249 to 442, the domain is characterized as B30.2/SPRY.
+At position 74 to 363, the domain is characterized as FAE.
+At position 45 to 312, the domain is characterized as Protein kinase.
+At position 381 to 486, the domain is characterized as PH.
+At position 37 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 4 to 183, the domain is characterized as Guanylate kinase-like.
+At position 14 to 100, the domain is characterized as Phosphagen kinase N-terminal.
+At position 127 to 369, the domain is characterized as Phosphagen kinase C-terminal.
+At position 273 to 408, the domain is characterized as Fido.
+At position 47 to 176, the domain is characterized as VOC.
+At position 490 to 526, the domain is characterized as CBM1.
+At position 31 to 61, the domain is characterized as LRRNT.
+At position 312 to 363, the domain is characterized as LRRCT.
+At position 20 to 277, the domain is characterized as Protein kinase.
+At position 79 to 315, the domain is characterized as Peptidase S1.
+At position 161 to 312, the domain is characterized as TRUD.
+At position 68 to 390, the domain is characterized as Asparaginase/glutaminase.
+At position 566 to 840, the domain is characterized as Protein kinase.
+At position 96 to 269, the domain is characterized as SET.
+At position 225 to 373, the domain is characterized as Exonuclease.
+At position 47 to 139, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 240, the domain is characterized as Ig-like C2-type 2.
+At position 250 to 334, the domain is characterized as Ig-like C2-type 3.
+At position 341 to 434, the domain is characterized as Fibronectin type-III 1.
+At position 439 to 535, the domain is characterized as Fibronectin type-III 2.
+At position 539 to 628, the domain is characterized as Fibronectin type-III 3.
+At position 633 to 748, the domain is characterized as Fibronectin type-III 4.
+At position 752 to 856, the domain is characterized as Fibronectin type-III 5.
+At position 857 to 956, the domain is characterized as Fibronectin type-III 6.
+At position 957 to 1053, the domain is characterized as Fibronectin type-III 7.
+At position 1058 to 1158, the domain is characterized as Fibronectin type-III 8.
+At position 1181 to 1287, the domain is characterized as Fibronectin type-III 9.
+At position 1647 to 1902, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1933 to 2192, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 928 to 958, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 41 to 155, the domain is characterized as CUB 1.
+At position 172 to 287, the domain is characterized as CUB 2.
+At position 291 to 327, the domain is characterized as LDL-receptor class A.
+At position 179 to 459, the domain is characterized as ABC transmembrane type-1 1.
+At position 562 to 783, the domain is characterized as ABC transporter 1.
+At position 858 to 1154, the domain is characterized as ABC transmembrane type-1 2.
+At position 1192 to 1426, the domain is characterized as ABC transporter 2.
+At position 395 to 602, the domain is characterized as MCM.
+At position 46 to 89, the domain is characterized as CUE.
+At position 1691 to 1770, the domain is characterized as Smr.
+At position 180 to 479, the domain is characterized as ABC transmembrane type-1 1.
+At position 514 to 750, the domain is characterized as ABC transporter 1.
+At position 837 to 1157, the domain is characterized as ABC transmembrane type-1 2.
+At position 1192 to 1428, the domain is characterized as ABC transporter 2.
+At position 205 to 424, the domain is characterized as ATP-grasp.
+At position 4 to 363, the domain is characterized as GH18.
+At position 10 to 90, the domain is characterized as Chromo.
+At position 249 to 542, the domain is characterized as MRG.
+At position 30 to 48, the domain is characterized as EF-hand 1.
+At position 129 to 164, the domain is characterized as EF-hand 4.
+At position 65 to 203, the domain is characterized as Flavodoxin-like.
+At position 236 to 450, the domain is characterized as FAD-binding FR-type.
+At position 6 to 253, the domain is characterized as ABC transporter 1.
+At position 327 to 572, the domain is characterized as ABC transporter 2.
+At position 97 to 211, the domain is characterized as NlpC/P60.
+At position 190 to 518, the domain is characterized as Protein kinase.
+At position 9 to 92, the domain is characterized as RRM.
+At position 169 to 356, the domain is characterized as CheB-type methylesterase.
+At position 37 to 84, the domain is characterized as F-box.
+At position 57 to 265, the domain is characterized as Rab-GAP TBC.
+At position 36 to 118, the domain is characterized as IGFBP N-terminal.
+At position 204 to 286, the domain is characterized as Thyroglobulin type-1.
+At position 113 to 188, the domain is characterized as MIT.
+At position 99 to 265, the domain is characterized as Helicase ATP-binding.
+At position 317 to 503, the domain is characterized as Helicase C-terminal.
+At position 901 to 962, the domain is characterized as Tudor.
+At position 22 to 99, the domain is characterized as Death.
+At position 145 to 279, the domain is characterized as TIR.
+At position 7 to 191, the domain is characterized as RNase H type-2.
+At position 1 to 244, the domain is characterized as tr-type G.
+At position 601 to 659, the domain is characterized as CBS 1.
+At position 713 to 777, the domain is characterized as CBS 2.
+At position 4 to 123, the domain is characterized as PINc.
+At position 27 to 99, the domain is characterized as Collagen-like.
+At position 131 to 247, the domain is characterized as C-type lectin.
+At position 6 to 164, the domain is characterized as Obg.
+At position 165 to 335, the domain is characterized as OBG-type G.
+At position 357 to 435, the domain is characterized as OCT.
+At position 10 to 173, the domain is characterized as Exonuclease.
+At position 32 to 134, the domain is characterized as Rieske.
+At position 162 to 435, the domain is characterized as ABC transporter 1.
+At position 513 to 725, the domain is characterized as ABC transmembrane type-2 1.
+At position 853 to 1105, the domain is characterized as ABC transporter 2.
+At position 1178 to 1392, the domain is characterized as ABC transmembrane type-2 2.
+At position 282 to 411, the domain is characterized as OTU.
+At position 430 to 449, the domain is characterized as UIM.
+At position 1 to 75, the domain is characterized as Ubiquitin-like.
+At position 99 to 274, the domain is characterized as WLM.
+At position 21 to 311, the domain is characterized as ABC transmembrane type-1.
+At position 345 to 579, the domain is characterized as ABC transporter.
+At position 56 to 121, the domain is characterized as NAC-A/B.
+At position 27 to 73, the domain is characterized as CHCH.
+At position 29 to 88, the domain is characterized as VWFC.
+At position 1028 to 1262, the domain is characterized as Fibrillar collagen NC1.
+At position 142 to 217, the domain is characterized as S4 RNA-binding.
+At position 130 to 383, the domain is characterized as ABC transporter 1.
+At position 488 to 715, the domain is characterized as ABC transmembrane type-2 1.
+At position 818 to 1062, the domain is characterized as ABC transporter 2.
+At position 1152 to 1386, the domain is characterized as ABC transmembrane type-2 2.
+At position 439 to 502, the domain is characterized as RRM 3.
+At position 138 to 208, the domain is characterized as FISNA.
+At position 218 to 534, the domain is characterized as NACHT.
+At position 60 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 276 to 445, the domain is characterized as tr-type G.
+At position 30 to 193, the domain is characterized as MAM.
+At position 195 to 280, the domain is characterized as Ig-like C2-type.
+At position 293 to 388, the domain is characterized as Fibronectin type-III 1.
+At position 391 to 487, the domain is characterized as Fibronectin type-III 2.
+At position 490 to 594, the domain is characterized as Fibronectin type-III 3.
+At position 595 to 688, the domain is characterized as Fibronectin type-III 4.
+At position 899 to 1159, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1191 to 1453, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 24 to 320, the domain is characterized as Protein kinase.
+At position 180 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 209 to 238, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 202 to 388, the domain is characterized as Glutamine amidotransferase type-1.
+At position 519 to 632, the domain is characterized as SMC hinge.
+At position 104 to 274, the domain is characterized as ATP-grasp.
+At position 67 to 249, the domain is characterized as IRG-type G.
+At position 73 to 331, the domain is characterized as Protein kinase.
+At position 374 to 408, the domain is characterized as EF-hand 1.
+At position 409 to 443, the domain is characterized as EF-hand 2; degenerate.
+At position 480 to 513, the domain is characterized as EF-hand 4.
+At position 165 to 335, the domain is characterized as Helicase ATP-binding.
+At position 345 to 505, the domain is characterized as Helicase C-terminal.
+At position 40 to 58, the domain is characterized as EF-hand 1.
+At position 13 to 135, the domain is characterized as CMP/dCMP-type deaminase.
+At position 125 to 303, the domain is characterized as SMP-LTD.
+At position 302 to 423, the domain is characterized as C2 1.
+At position 444 to 570, the domain is characterized as C2 2.
+At position 616 to 738, the domain is characterized as C2 3.
+At position 769 to 886, the domain is characterized as C2 4.
+At position 959 to 1081, the domain is characterized as C2 5.
+At position 11 to 93, the domain is characterized as PDZ 1.
+At position 187 to 264, the domain is characterized as PDZ 2.
+At position 369 to 435, the domain is characterized as PDZ 3.
+At position 464 to 538, the domain is characterized as SH3.
+At position 569 to 750, the domain is characterized as Guanylate kinase-like.
+At position 8 to 189, the domain is characterized as Tyr recombinase.
+At position 68 to 204, the domain is characterized as PLAT.
+At position 207 to 899, the domain is characterized as Lipoxygenase.
+At position 8 to 76, the domain is characterized as Ubiquitin-like.
+At position 601 to 679, the domain is characterized as BRCT.
+At position 16 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 325 to 545, the domain is characterized as Peptidase M12B.
+At position 546 to 633, the domain is characterized as Disintegrin.
+At position 634 to 686, the domain is characterized as TSP type-1 1.
+At position 915 to 975, the domain is characterized as TSP type-1 2.
+At position 976 to 1037, the domain is characterized as TSP type-1 3.
+At position 1039 to 1083, the domain is characterized as TSP type-1 4.
+At position 1087 to 1144, the domain is characterized as TSP type-1 5.
+At position 1160 to 1199, the domain is characterized as PLAC.
+At position 231 to 414, the domain is characterized as GAF.
+At position 629 to 699, the domain is characterized as PAS 1.
+At position 762 to 833, the domain is characterized as PAS 2.
+At position 913 to 1132, the domain is characterized as Histidine kinase.
+At position 40 to 712, the domain is characterized as PFL.
+At position 731 to 850, the domain is characterized as Glycine radical.
+At position 58 to 156, the domain is characterized as Rieske.
+At position 103 to 192, the domain is characterized as NID 1.
+At position 201 to 292, the domain is characterized as NID 2.
+At position 30 to 169, the domain is characterized as Ephrin RBD.
+At position 120 to 215, the domain is characterized as TAFH.
+At position 3 to 227, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 122, the domain is characterized as Calponin-homology (CH).
+At position 294 to 336, the domain is characterized as STI1.
+At position 47 to 194, the domain is characterized as Protein kinase.
+At position 18 to 59, the domain is characterized as F-box.
+At position 29 to 83, the domain is characterized as Cystatin.
+At position 25 to 282, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 19 to 210, the domain is characterized as ABC transmembrane type-1.
+At position 281 to 632, the domain is characterized as PDEase.
+At position 218 to 494, the domain is characterized as MYST-type HAT.
+At position 611 to 659, the domain is characterized as F-box.
+At position 17 to 94, the domain is characterized as Cytochrome b5 heme-binding.
+At position 62 to 84, the domain is characterized as GoLoco 1.
+At position 104 to 126, the domain is characterized as GoLoco 2.
+At position 132 to 155, the domain is characterized as GoLoco 3.
+At position 24 to 50, the domain is characterized as LRRNT.
+At position 180 to 233, the domain is characterized as LRRCT.
+At position 234 to 322, the domain is characterized as Ig-like C2-type 1.
+At position 330 to 414, the domain is characterized as Ig-like C2-type 2.
+At position 419 to 504, the domain is characterized as Ig-like C2-type 3.
+At position 507 to 596, the domain is characterized as Ig-like C2-type 4.
+At position 1393 to 1451, the domain is characterized as VWFC.
+At position 16 to 295, the domain is characterized as Protein kinase.
+At position 171 to 393, the domain is characterized as Histidine kinase.
+At position 199 to 265, the domain is characterized as KH.
+At position 31 to 147, the domain is characterized as SCP.
+At position 198 to 281, the domain is characterized as RCK C-terminal 1.
+At position 282 to 366, the domain is characterized as RCK C-terminal 2.
+At position 216 to 291, the domain is characterized as SPOR.
+At position 48 to 307, the domain is characterized as Pyruvate carboxyltransferase.
+At position 160 to 341, the domain is characterized as OBG-type G.
+At position 66 to 297, the domain is characterized as Helicase ATP-binding.
+At position 325 to 475, the domain is characterized as Helicase C-terminal.
+At position 193 to 486, the domain is characterized as Protein kinase.
+At position 1 to 234, the domain is characterized as Deacetylase sirtuin-type.
+At position 34 to 198, the domain is characterized as Thioredoxin.
+At position 207 to 430, the domain is characterized as SMP-LTD.
+At position 335 to 468, the domain is characterized as RanBD1.
+At position 118 to 197, the domain is characterized as RRM.
+At position 385 to 535, the domain is characterized as NTF2.
+At position 564 to 618, the domain is characterized as TAP-C.
+At position 14 to 125, the domain is characterized as MTTase N-terminal.
+At position 149 to 378, the domain is characterized as Radical SAM core.
+At position 381 to 452, the domain is characterized as TRAM.
+At position 46 to 313, the domain is characterized as Protein kinase.
+At position 38 to 154, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 238 to 357, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 157 to 349, the domain is characterized as CheB-type methylesterase.
+At position 99 to 678, the domain is characterized as RINT1/TIP20.
+At position 28 to 108, the domain is characterized as IGFBP N-terminal.
+At position 176 to 254, the domain is characterized as Thyroglobulin type-1.
+At position 5 to 243, the domain is characterized as ABC transporter 1.
+At position 293 to 525, the domain is characterized as ABC transporter 2.
+At position 46 to 230, the domain is characterized as Helicase ATP-binding.
+At position 243 to 477, the domain is characterized as Helicase C-terminal.
+At position 38 to 177, the domain is characterized as WIF.
+At position 178 to 210, the domain is characterized as EGF-like 1.
+At position 211 to 242, the domain is characterized as EGF-like 2.
+At position 243 to 271, the domain is characterized as EGF-like 3.
+At position 274 to 306, the domain is characterized as EGF-like 4.
+At position 307 to 338, the domain is characterized as EGF-like 5.
+At position 95 to 171, the domain is characterized as PRC barrel.
+At position 206 to 461, the domain is characterized as Fibrinogen C-terminal.
+At position 63 to 153, the domain is characterized as Rieske.
+At position 213 to 262, the domain is characterized as bHLH.
+At position 55 to 248, the domain is characterized as Helicase ATP-binding.
+At position 293 to 482, the domain is characterized as Helicase C-terminal.
+At position 20 to 66, the domain is characterized as F-box.
+At position 22 to 124, the domain is characterized as Ig-like V-type.
+At position 265 to 426, the domain is characterized as Flavodoxin-like.
+At position 174 to 260, the domain is characterized as Toprim.
+At position 5 to 46, the domain is characterized as SpoVT-AbrB 1.
+At position 75 to 118, the domain is characterized as SpoVT-AbrB 2.
+At position 360 to 450, the domain is characterized as Histidine kinase.
+At position 27 to 76, the domain is characterized as F-box.
+At position 1 to 154, the domain is characterized as MGS-like.
+At position 158 to 233, the domain is characterized as H15 1.
+At position 256 to 331, the domain is characterized as H15 2.
+At position 339 to 414, the domain is characterized as H15 3.
+At position 109 to 324, the domain is characterized as ATP-grasp.
+At position 14 to 186, the domain is characterized as N-acetyltransferase.
+At position 214 to 393, the domain is characterized as GAF.
+At position 608 to 679, the domain is characterized as PAS 1.
+At position 742 to 813, the domain is characterized as PAS 2.
+At position 893 to 1113, the domain is characterized as Histidine kinase.
+At position 581 to 662, the domain is characterized as BRCT.
+At position 21 to 195, the domain is characterized as Exonuclease.
+At position 290 to 423, the domain is characterized as C2 2.
+At position 25 to 171, the domain is characterized as Plastocyanin-like 1.
+At position 173 to 336, the domain is characterized as Plastocyanin-like 2.
+At position 382 to 501, the domain is characterized as Plastocyanin-like 3.
+At position 68 to 130, the domain is characterized as PWWP.
+At position 443 to 478, the domain is characterized as EF-hand.
+At position 234 to 330, the domain is characterized as BEN.
+At position 6 to 85, the domain is characterized as KRAB.
+At position 19 to 211, the domain is characterized as Albumin 1.
+At position 212 to 403, the domain is characterized as Albumin 2.
+At position 404 to 601, the domain is characterized as Albumin 3.
+At position 73 to 438, the domain is characterized as Peptidase A1.
+At position 37 to 107, the domain is characterized as HMA.
+At position 76 to 260, the domain is characterized as SMP-LBD.
+At position 268 to 389, the domain is characterized as C2.
+At position 24 to 80, the domain is characterized as Clip.
+At position 114 to 364, the domain is characterized as Peptidase S1.
+At position 437 to 486, the domain is characterized as bHLH.
+At position 36 to 148, the domain is characterized as CUB 1.
+At position 158 to 272, the domain is characterized as CUB 2.
+At position 341 to 460, the domain is characterized as NTR.
+At position 51 to 188, the domain is characterized as MPN.
+At position 31 to 269, the domain is characterized as Peptidase S1.
+At position 148 to 272, the domain is characterized as Fe2OG dioxygenase.
+At position 15 to 230, the domain is characterized as tr-type G.
+At position 4 to 172, the domain is characterized as Flavodoxin-like.
+At position 352 to 426, the domain is characterized as U-box.
+At position 70 to 159, the domain is characterized as Ig-like C2-type 1.
+At position 170 to 257, the domain is characterized as Ig-like C2-type 2.
+At position 91 to 115, the domain is characterized as EGF-like.
+At position 41 to 156, the domain is characterized as RGS.
+At position 2 to 224, the domain is characterized as Glutamine amidotransferase type-1.
+At position 56 to 134, the domain is characterized as RRM.
+At position 36 to 126, the domain is characterized as Ig-like C2-type.
+At position 200 to 332, the domain is characterized as FZ.
+At position 353 to 429, the domain is characterized as Kringle.
+At position 590 to 870, the domain is characterized as Protein kinase.
+At position 512 to 618, the domain is characterized as Calponin-homology (CH).
+At position 791 to 853, the domain is characterized as LIM zinc-binding.
+At position 1495 to 1661, the domain is characterized as bMERB.
+At position 135 to 254, the domain is characterized as OTU.
+At position 428 to 559, the domain is characterized as Plus3.
+At position 21 to 48, the domain is characterized as LRRNT.
+At position 571 to 620, the domain is characterized as LRRCT.
+At position 120 to 451, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 102, the domain is characterized as HPt.
+At position 233 to 488, the domain is characterized as Histidine kinase.
+At position 490 to 618, the domain is characterized as CheW-like.
+At position 107 to 318, the domain is characterized as ATP-grasp.
+At position 37 to 139, the domain is characterized as Ig-like V-type.
+At position 58 to 263, the domain is characterized as ABC transmembrane type-1 1.
+At position 333 to 528, the domain is characterized as ABC transmembrane type-1 2.
+At position 378 to 464, the domain is characterized as PDZ 3.
+At position 546 to 627, the domain is characterized as PDZ 4.
+At position 693 to 779, the domain is characterized as PDZ 5.
+At position 996 to 1077, the domain is characterized as PDZ 6.
+At position 1139 to 1231, the domain is characterized as PDZ 7.
+At position 1338 to 1421, the domain is characterized as PDZ 8.
+At position 1471 to 1552, the domain is characterized as PDZ 9.
+At position 1614 to 1697, the domain is characterized as PDZ 10.
+At position 1710 to 1792, the domain is characterized as PDZ 11.
+At position 1847 to 1933, the domain is characterized as PDZ 12.
+At position 1972 to 2055, the domain is characterized as PDZ 13.
+At position 239 to 312, the domain is characterized as RRM.
+At position 14 to 89, the domain is characterized as GIY-YIG.
+At position 270 to 418, the domain is characterized as MPN.
+At position 1 to 190, the domain is characterized as tr-type G.
+At position 165 to 352, the domain is characterized as Glutamine amidotransferase type-1.
+At position 15 to 218, the domain is characterized as YjeF N-terminal.
+At position 467 to 510, the domain is characterized as CUE.
+At position 23 to 345, the domain is characterized as G-alpha.
+At position 21 to 121, the domain is characterized as Ig-like.
+At position 89 to 150, the domain is characterized as SH3.
+At position 156 to 253, the domain is characterized as SH2.
+At position 278 to 531, the domain is characterized as Protein kinase.
+At position 6 to 150, the domain is characterized as Flavodoxin-like.
+At position 206 to 447, the domain is characterized as FAD-binding FR-type.
+At position 68 to 275, the domain is characterized as ABC transmembrane type-1.
+At position 65 to 244, the domain is characterized as FAD-binding PCMH-type.
+At position 777 to 861, the domain is characterized as PB1.
+At position 525 to 808, the domain is characterized as Protein kinase.
+At position 880 to 1010, the domain is characterized as Guanylate cyclase.
+At position 220 to 316, the domain is characterized as KRAB.
+At position 352 to 384, the domain is characterized as EGF-like 1.
+At position 387 to 422, the domain is characterized as EGF-like 2.
+At position 458 to 495, the domain is characterized as EGF-like 3.
+At position 79 to 331, the domain is characterized as Protein kinase.
+At position 500 to 578, the domain is characterized as POLO box 1.
+At position 598 to 682, the domain is characterized as POLO box 2.
+At position 1 to 196, the domain is characterized as N-acetyltransferase.
+At position 12 to 68, the domain is characterized as WHEP-TRS.
+At position 183 to 331, the domain is characterized as N-acetyltransferase.
+At position 533 to 832, the domain is characterized as Peptidase M60.
+At position 23 to 100, the domain is characterized as EMI.
+At position 94 to 129, the domain is characterized as EGF-like 1.
+At position 142 to 172, the domain is characterized as EGF-like 2.
+At position 314 to 344, the domain is characterized as EGF-like 6.
+At position 441 to 476, the domain is characterized as EGF-like 8.
+At position 484 to 519, the domain is characterized as EGF-like 9.
+At position 570 to 605, the domain is characterized as EGF-like 10.
+At position 613 to 650, the domain is characterized as EGF-like 11.
+At position 658 to 693, the domain is characterized as EGF-like 12.
+At position 706 to 736, the domain is characterized as EGF-like 13.
+At position 749 to 779, the domain is characterized as EGF-like 14.
+At position 787 to 822, the domain is characterized as EGF-like 15.
+At position 46 to 187, the domain is characterized as SCP.
+At position 4 to 68, the domain is characterized as HMA.
+At position 573 to 633, the domain is characterized as KH.
+At position 658 to 719, the domain is characterized as S1 motif.
+At position 8 to 71, the domain is characterized as S5 DRBM.
+At position 315 to 405, the domain is characterized as Fibronectin type-III 1.
+At position 406 to 488, the domain is characterized as Fibronectin type-III 2.
+At position 489 to 566, the domain is characterized as Fibronectin type-III 3.
+At position 568 to 643, the domain is characterized as Fibronectin type-III 4.
+At position 444 to 546, the domain is characterized as CBM20.
+At position 532 to 652, the domain is characterized as Ricin B-type lectin.
+At position 33 to 303, the domain is characterized as Deacetylase sirtuin-type.
+At position 17 to 202, the domain is characterized as Eph LBD.
+At position 323 to 432, the domain is characterized as Fibronectin type-III 1.
+At position 436 to 529, the domain is characterized as Fibronectin type-III 2.
+At position 615 to 899, the domain is characterized as Protein kinase.
+At position 907 to 971, the domain is characterized as SAM.
+At position 412 to 525, the domain is characterized as Toprim.
+At position 5 to 258, the domain is characterized as F-BAR.
+At position 406 to 468, the domain is characterized as SH3 1.
+At position 476 to 533, the domain is characterized as SH3 2.
+At position 109 to 144, the domain is characterized as EF-hand.
+At position 30 to 126, the domain is characterized as GS beta-grasp.
+At position 133 to 462, the domain is characterized as GS catalytic.
+At position 19 to 270, the domain is characterized as Pyruvate carboxyltransferase.
+At position 139 to 244, the domain is characterized as HTH LytTR-type.
+At position 31 to 359, the domain is characterized as G-alpha.
+At position 72 to 199, the domain is characterized as Thioredoxin.
+At position 243 to 292, the domain is characterized as bHLH.
+At position 1 to 236, the domain is characterized as Radical SAM core.
+At position 172 to 279, the domain is characterized as FAD-binding FR-type.
+At position 3 to 63, the domain is characterized as S4 RNA-binding.
+At position 54 to 364, the domain is characterized as ABC transmembrane type-1.
+At position 397 to 631, the domain is characterized as ABC transporter.
+At position 36 to 271, the domain is characterized as AB hydrolase-1.
+At position 1 to 185, the domain is characterized as KARI N-terminal Rossmann.
+At position 186 to 336, the domain is characterized as KARI C-terminal knotted.
+At position 1 to 91, the domain is characterized as NTR.
+At position 124 to 502, the domain is characterized as Myotubularin phosphatase.
+At position 14 to 98, the domain is characterized as YcgL.
+At position 159 to 228, the domain is characterized as DRBM.
+At position 33 to 82, the domain is characterized as Clip.
+At position 114 to 360, the domain is characterized as Peptidase S1.
+At position 6 to 115, the domain is characterized as Calponin-homology (CH).
+At position 31 to 69, the domain is characterized as EGF-like.
+At position 2 to 87, the domain is characterized as ACB.
+At position 45 to 210, the domain is characterized as Thioredoxin.
+At position 65 to 99, the domain is characterized as ShKT 1.
+At position 109 to 145, the domain is characterized as ShKT 2.
+At position 151 to 186, the domain is characterized as ShKT 3.
+At position 274 to 644, the domain is characterized as GRAS.
+At position 26 to 147, the domain is characterized as Avidin-like.
+At position 4 to 109, the domain is characterized as Gnk2-homologous.
+At position 1 to 143, the domain is characterized as PIK helical.
+At position 835 to 1106, the domain is characterized as PI3K/PI4K catalytic.
+At position 128 to 263, the domain is characterized as Fatty acid hydroxylase.
+At position 94 to 157, the domain is characterized as S5 DRBM.
+At position 699 to 995, the domain is characterized as Protein kinase.
+At position 73 to 150, the domain is characterized as POTRA.
+At position 60 to 200, the domain is characterized as SCP.
+At position 282 to 377, the domain is characterized as LCCL 1.
+At position 383 to 486, the domain is characterized as LCCL 2.
+At position 20 to 242, the domain is characterized as ABC transmembrane type-2.
+At position 47 to 275, the domain is characterized as ATP-grasp.
+At position 183 to 462, the domain is characterized as Protein kinase.
+At position 762 to 838, the domain is characterized as Carrier 1.
+At position 1553 to 1629, the domain is characterized as Carrier 2.
+At position 42 to 159, the domain is characterized as PX.
+At position 6 to 139, the domain is characterized as MPN.
+At position 630 to 884, the domain is characterized as Protein kinase.
+At position 23 to 117, the domain is characterized as HTH La-type RNA-binding.
+At position 120 to 198, the domain is characterized as RRM.
+At position 439 to 552, the domain is characterized as xRRM.
+At position 16 to 158, the domain is characterized as ENTH.
+At position 46 to 145, the domain is characterized as RRM.
+At position 73 to 202, the domain is characterized as SEC7.
+At position 260 to 377, the domain is characterized as PH.
+At position 4 to 223, the domain is characterized as ABC transporter.
+At position 17 to 118, the domain is characterized as RWD.
+At position 7 to 94, the domain is characterized as GLUE N-terminal.
+At position 97 to 129, the domain is characterized as GLUE C-terminal.
+At position 97 to 339, the domain is characterized as Radical SAM core.
+At position 21 to 85, the domain is characterized as NAC-A/B.
+At position 134 to 171, the domain is characterized as UBA.
+At position 152 to 408, the domain is characterized as ABC transporter 1.
+At position 846 to 1088, the domain is characterized as ABC transporter 2.
+At position 11 to 62, the domain is characterized as HTH psq-type.
+At position 77 to 149, the domain is characterized as HTH CENPB-type.
+At position 213 to 382, the domain is characterized as DDE-1.
+At position 70 to 143, the domain is characterized as PA.
+At position 61 to 121, the domain is characterized as Chromo.
+At position 157 to 399, the domain is characterized as Peptidase S1.
+At position 393 to 494, the domain is characterized as RWD.
+At position 35 to 422, the domain is characterized as Helicase ATP-binding.
+At position 268 to 346, the domain is characterized as PDZ 1.
+At position 756 to 826, the domain is characterized as PDZ 2.
+At position 93 to 173, the domain is characterized as PUA.
+At position 365 to 449, the domain is characterized as SWIB/MDM2.
+At position 473 to 546, the domain is characterized as SUI1.
+At position 56 to 301, the domain is characterized as Peptidase S6.
+At position 1106 to 1372, the domain is characterized as Autotransporter.
+At position 239 to 302, the domain is characterized as bZIP.
+At position 170 to 357, the domain is characterized as Helicase ATP-binding.
+At position 386 to 542, the domain is characterized as Helicase C-terminal.
+At position 11 to 91, the domain is characterized as Cytochrome b5 heme-binding.
+At position 485 to 654, the domain is characterized as tr-type G.
+At position 149 to 374, the domain is characterized as ATP-grasp.
+At position 9 to 253, the domain is characterized as ABC transporter.
+At position 9 to 247, the domain is characterized as ABC transporter 1.
+At position 256 to 496, the domain is characterized as ABC transporter 2.
+At position 121 to 228, the domain is characterized as Rieske.
+At position 28 to 130, the domain is characterized as Expansin-like EG45.
+At position 50 to 231, the domain is characterized as tr-type G.
+At position 380 to 487, the domain is characterized as SCP2.
+At position 63 to 169, the domain is characterized as Expansin-like EG45.
+At position 183 to 264, the domain is characterized as Expansin-like CBD.
+At position 104 to 444, the domain is characterized as Peptidase A1.
+At position 351 to 437, the domain is characterized as PPIase FKBP-type.
+At position 1 to 43, the domain is characterized as Chitin-binding type R&R.
+At position 11 to 143, the domain is characterized as ADF-H.
+At position 9 to 292, the domain is characterized as tr-type G.
+At position 103 to 400, the domain is characterized as ABC transmembrane type-1.
+At position 437 to 671, the domain is characterized as ABC transporter.
+At position 133 to 213, the domain is characterized as PDZ.
+At position 599 to 688, the domain is characterized as BRCT.
+At position 114 to 276, the domain is characterized as CP-type G.
+At position 2 to 25, the domain is characterized as Carrier.
+At position 586 to 644, the domain is characterized as CBS 1.
+At position 794 to 854, the domain is characterized as CBS 2.
+At position 55 to 133, the domain is characterized as RRM 1.
+At position 149 to 227, the domain is characterized as RRM 2.
+At position 180 to 286, the domain is characterized as Fe2OG dioxygenase.
+At position 660 to 724, the domain is characterized as J.
+At position 3 to 226, the domain is characterized as Glutamine amidotransferase type-1.
+At position 96 to 313, the domain is characterized as Radical SAM core.
+At position 1 to 123, the domain is characterized as C-type lysozyme.
+At position 1 to 48, the domain is characterized as IF rod.
+At position 88 to 150, the domain is characterized as S4 RNA-binding.
+At position 384 to 521, the domain is characterized as N-terminal Ras-GEF.
+At position 665 to 892, the domain is characterized as Ras-GEF.
+At position 18 to 115, the domain is characterized as SWIRM.
+At position 245 to 296, the domain is characterized as SANT.
+At position 9 to 207, the domain is characterized as Peptidase M12B.
+At position 215 to 301, the domain is characterized as Disintegrin.
+At position 28 to 258, the domain is characterized as Radical SAM core.
+At position 84 to 267, the domain is characterized as ABC transmembrane type-1.
+At position 167 to 281, the domain is characterized as SCP.
+At position 79 to 189, the domain is characterized as TBDR plug.
+At position 194 to 726, the domain is characterized as TBDR beta-barrel.
+At position 100 to 155, the domain is characterized as HTH myb-type 1.
+At position 156 to 206, the domain is characterized as HTH myb-type 2.
+At position 169 to 249, the domain is characterized as RRM Nup35-type.
+At position 88 to 169, the domain is characterized as Smr.
+At position 2 to 111, the domain is characterized as PH.
+At position 88 to 301, the domain is characterized as RNase H type-2.
+At position 266 to 329, the domain is characterized as bZIP.
+At position 2 to 101, the domain is characterized as FAD-binding FR-type.
+At position 240 to 409, the domain is characterized as tr-type G.
+At position 437 to 655, the domain is characterized as PPM-type phosphatase.
+At position 3 to 74, the domain is characterized as KRAB.
+At position 400 to 478, the domain is characterized as Disintegrin.
+At position 63 to 91, the domain is characterized as EF-hand 2.
+At position 189 to 371, the domain is characterized as Glutamine amidotransferase type-1.
+At position 55 to 119, the domain is characterized as Myb-like 1.
+At position 434 to 492, the domain is characterized as Myb-like 2.
+At position 58 to 215, the domain is characterized as CP-type G.
+At position 311 to 507, the domain is characterized as DH.
+At position 10 to 428, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 891 to 1178, the domain is characterized as PKS/mFAS DH.
+At position 2370 to 2452, the domain is characterized as Carrier.
+At position 157 to 231, the domain is characterized as RRM.
+At position 7 to 170, the domain is characterized as TIR.
+At position 88 to 779, the domain is characterized as Peptidase M13.
+At position 109 to 393, the domain is characterized as ABC transmembrane type-1.
+At position 470 to 708, the domain is characterized as ABC transporter.
+At position 214 to 246, the domain is characterized as LisH.
+At position 409 to 535, the domain is characterized as N-terminal Ras-GEF.
+At position 573 to 804, the domain is characterized as Ras-GEF.
+At position 582 to 617, the domain is characterized as EF-hand.
+At position 143 to 374, the domain is characterized as Radical SAM core.
+At position 377 to 441, the domain is characterized as TRAM.
+At position 895 to 959, the domain is characterized as HP.
+At position 205 to 400, the domain is characterized as Peptidase M12B.
+At position 545 to 620, the domain is characterized as Cytochrome b5 heme-binding.
+At position 660 to 772, the domain is characterized as FAD-binding FR-type.
+At position 7 to 137, the domain is characterized as ADF-H.
+At position 139 to 305, the domain is characterized as CRAL-TRIO.
+At position 37 to 217, the domain is characterized as BPL/LPL catalytic.
+At position 245 to 437, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 119, the domain is characterized as PH.
+At position 720 to 900, the domain is characterized as Rho-GAP.
+At position 278 to 367, the domain is characterized as Ig-like C2-type 1.
+At position 448 to 546, the domain is characterized as Ig-like C2-type 2.
+At position 1026 to 1110, the domain is characterized as Ig-like C2-type 3.
+At position 1160 to 1251, the domain is characterized as Ig-like C2-type 4.
+At position 1259 to 1349, the domain is characterized as Ig-like C2-type 5.
+At position 7 to 112, the domain is characterized as PH 1.
+At position 191 to 289, the domain is characterized as PH 2.
+At position 1 to 162, the domain is characterized as SPX.
+At position 3 to 65, the domain is characterized as TGS.
+At position 120 to 196, the domain is characterized as HTH crp-type.
+At position 63 to 321, the domain is characterized as Protein kinase.
+At position 364 to 399, the domain is characterized as EF-hand 1.
+At position 400 to 435, the domain is characterized as EF-hand 2.
+At position 436 to 471, the domain is characterized as EF-hand 3.
+At position 472 to 507, the domain is characterized as EF-hand 4.
+At position 47 to 262, the domain is characterized as Radical SAM core.
+At position 238 to 363, the domain is characterized as GAF.
+At position 363 to 580, the domain is characterized as Histidine kinase.
+At position 72 to 131, the domain is characterized as CBS 1.
+At position 137 to 194, the domain is characterized as CBS 2.
+At position 337 to 422, the domain is characterized as OCT.
+At position 15 to 90, the domain is characterized as RRM 1.
+At position 130 to 204, the domain is characterized as RRM 2.
+At position 101 to 286, the domain is characterized as ATP-grasp.
+At position 411 to 497, the domain is characterized as Fibronectin type-III.
+At position 3 to 151, the domain is characterized as Clp R.
+At position 169 to 243, the domain is characterized as Toprim.
+At position 410 to 485, the domain is characterized as B5.
+At position 712 to 805, the domain is characterized as FDX-ACB.
+At position 368 to 555, the domain is characterized as PID.
+At position 568 to 654, the domain is characterized as PDZ 1.
+At position 659 to 734, the domain is characterized as PDZ 2.
+At position 605 to 664, the domain is characterized as KH.
+At position 679 to 750, the domain is characterized as S1 motif.
+At position 121 to 260, the domain is characterized as SIS.
+At position 60 to 125, the domain is characterized as NAC-A/B.
+At position 158 to 203, the domain is characterized as UBA.
+At position 11 to 266, the domain is characterized as Protein kinase.
+At position 294 to 321, the domain is characterized as NAF.
+At position 43 to 86, the domain is characterized as CHCH.
+At position 3 to 169, the domain is characterized as FeoB-type G.
+At position 15 to 180, the domain is characterized as TIR.
+At position 201 to 445, the domain is characterized as NB-ARC.
+At position 252 to 446, the domain is characterized as PCI.
+At position 139 to 446, the domain is characterized as Peptidase A1.
+At position 700 to 771, the domain is characterized as PAS.
+At position 770 to 822, the domain is characterized as PAC.
+At position 837 to 1059, the domain is characterized as Histidine kinase.
+At position 1312 to 1492, the domain is characterized as Response regulatory 1.
+At position 1570 to 1692, the domain is characterized as Response regulatory 2.
+At position 141 to 260, the domain is characterized as C2 1.
+At position 272 to 405, the domain is characterized as C2 2.
+At position 65 to 259, the domain is characterized as FtsK 1.
+At position 359 to 545, the domain is characterized as FtsK 2.
+At position 354 to 433, the domain is characterized as Ubiquitin-like 1.
+At position 434 to 509, the domain is characterized as Ubiquitin-like 2.
+At position 56 to 240, the domain is characterized as EngB-type G.
+At position 43 to 322, the domain is characterized as GH10.
+At position 241 to 321, the domain is characterized as CobW C-terminal.
+At position 99 to 162, the domain is characterized as CBS 1.
+At position 164 to 223, the domain is characterized as CBS 2.
+At position 136 to 371, the domain is characterized as Radical SAM core.
+At position 372 to 433, the domain is characterized as TRAM.
+At position 22 to 186, the domain is characterized as Helicase ATP-binding.
+At position 338 to 516, the domain is characterized as Helicase C-terminal.
+At position 83 to 369, the domain is characterized as Protein kinase.
+At position 592 to 673, the domain is characterized as BRCT.
+At position 205 to 378, the domain is characterized as EngA-type G 2.
+At position 132 to 334, the domain is characterized as ATP-grasp.
+At position 90 to 283, the domain is characterized as SIS 1.
+At position 319 to 498, the domain is characterized as SIS 2.
+At position 38 to 66, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 75 to 104, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 20 to 136, the domain is characterized as Ig-like C2-type 1.
+At position 108 to 295, the domain is characterized as Tyr recombinase.
+At position 709 to 727, the domain is characterized as WH2 1.
+At position 739 to 756, the domain is characterized as WH2 2.
+At position 43 to 273, the domain is characterized as Radical SAM core.
+At position 1 to 78, the domain is characterized as Ubiquitin-like.
+At position 423 to 586, the domain is characterized as YDG.
+At position 12 to 81, the domain is characterized as BTB.
+At position 11 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 52 to 108, the domain is characterized as AWS.
+At position 110 to 227, the domain is characterized as SET.
+At position 234 to 250, the domain is characterized as Post-SET.
+At position 477 to 511, the domain is characterized as WW.
+At position 40 to 90, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 10 to 126, the domain is characterized as Arf-GAP.
+At position 20 to 111, the domain is characterized as UPAR/Ly6.
+At position 15 to 244, the domain is characterized as YjeF N-terminal.
+At position 19 to 211, the domain is characterized as NodB homology.
+At position 82 to 143, the domain is characterized as SH3.
+At position 149 to 246, the domain is characterized as SH2.
+At position 271 to 524, the domain is characterized as Protein kinase.
+At position 35 to 100, the domain is characterized as Sushi 1.
+At position 101 to 160, the domain is characterized as Sushi 2.
+At position 163 to 220, the domain is characterized as Sushi 3.
+At position 270 to 469, the domain is characterized as VWFA.
+At position 477 to 757, the domain is characterized as Peptidase S1.
+At position 393 to 552, the domain is characterized as N-acetyltransferase.
+At position 971 to 1137, the domain is characterized as PNPLA.
+At position 23 to 99, the domain is characterized as Ig-like.
+At position 160 to 187, the domain is characterized as ITAM.
+At position 136 to 311, the domain is characterized as Helicase ATP-binding.
+At position 326 to 486, the domain is characterized as Helicase C-terminal.
+At position 85 to 200, the domain is characterized as RGS.
+At position 39 to 162, the domain is characterized as PX.
+At position 47 to 212, the domain is characterized as BUB1 N-terminal.
+At position 705 to 1021, the domain is characterized as Protein kinase.
+At position 72 to 289, the domain is characterized as Radical SAM core.
+At position 129 to 349, the domain is characterized as Radical SAM core.
+At position 194 to 278, the domain is characterized as 5'-3' exonuclease.
+At position 38 to 252, the domain is characterized as PNPLA.
+At position 77 to 126, the domain is characterized as FHA.
+At position 56 to 283, the domain is characterized as Radical SAM core.
+At position 40 to 281, the domain is characterized as ABC transporter.
+At position 189 to 466, the domain is characterized as NB-ARC.
+At position 19 to 149, the domain is characterized as MATH.
+At position 188 to 255, the domain is characterized as BTB.
+At position 116 to 243, the domain is characterized as OmpA-like.
+At position 35 to 125, the domain is characterized as Plastocyanin-like.
+At position 120 to 427, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 9 to 196, the domain is characterized as RNase H type-2.
+At position 23 to 350, the domain is characterized as Kinesin motor.
+At position 24 to 297, the domain is characterized as CNH.
+At position 192 to 371, the domain is characterized as DH.
+At position 400 to 502, the domain is characterized as PH.
+At position 672 to 766, the domain is characterized as SH2.
+At position 788 to 847, the domain is characterized as SH3 2.
+At position 81 to 142, the domain is characterized as CBS 1.
+At position 175 to 231, the domain is characterized as CBS 2.
+At position 387 to 500, the domain is characterized as PAZ.
+At position 677 to 1001, the domain is characterized as Piwi.
+At position 577 to 652, the domain is characterized as PUA.
+At position 6 to 48, the domain is characterized as CARD.
+At position 351 to 411, the domain is characterized as S4 RNA-binding.
+At position 4 to 170, the domain is characterized as N-acetyltransferase.
+At position 290 to 540, the domain is characterized as Glutamine amidotransferase type-1.
+At position 275 to 361, the domain is characterized as PPIase FKBP-type.
+At position 39 to 112, the domain is characterized as H15.
+At position 199 to 345, the domain is characterized as Ricin B-type lectin.
+At position 1 to 400, the domain is characterized as SAM-dependent MTase C5-type.
+At position 234 to 320, the domain is characterized as RRM.
+At position 290 to 532, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 32, the domain is characterized as Peptidase S1.
+At position 51 to 246, the domain is characterized as Lon N-terminal.
+At position 633 to 815, the domain is characterized as Lon proteolytic.
+At position 4 to 291, the domain is characterized as Protein kinase.
+At position 4 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 207 to 404, the domain is characterized as GMPS ATP-PPase.
+At position 9 to 120, the domain is characterized as C-type lectin.
+At position 214 to 430, the domain is characterized as Rap-GAP.
+At position 512 to 824, the domain is characterized as CNH.
+At position 136 to 366, the domain is characterized as Sigma-54 factor interaction.
+At position 439 to 513, the domain is characterized as PAS.
+At position 34 to 110, the domain is characterized as Lipoyl-binding.
+At position 175 to 212, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 11 to 147, the domain is characterized as HTH marR-type.
+At position 2 to 374, the domain is characterized as Trm1 methyltransferase.
+At position 241 to 389, the domain is characterized as Helicase C-terminal.
+At position 55 to 160, the domain is characterized as HD.
+At position 668 to 743, the domain is characterized as ACT.
+At position 40 to 220, the domain is characterized as Helicase ATP-binding.
+At position 73 to 147, the domain is characterized as TFIIS N-terminal.
+At position 74 to 185, the domain is characterized as sHSP.
+At position 16 to 277, the domain is characterized as Protein kinase.
+At position 339 to 410, the domain is characterized as SAM.
+At position 110 to 195, the domain is characterized as PPIase FKBP-type.
+At position 11 to 239, the domain is characterized as PABS.
+At position 1 to 281, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 283 to 590, the domain is characterized as UvrD-like helicase C-terminal.
+At position 372 to 401, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 411 to 440, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 2 to 87, the domain is characterized as Acylphosphatase-like.
+At position 297 to 372, the domain is characterized as PUA.
+At position 103 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 314 to 441, the domain is characterized as Ricin B-type lectin 1.
+At position 445 to 568, the domain is characterized as Ricin B-type lectin 2.
+At position 630 to 665, the domain is characterized as UVR.
+At position 113 to 223, the domain is characterized as PH.
+At position 398 to 542, the domain is characterized as PI-PLC X-box.
+At position 585 to 701, the domain is characterized as PI-PLC Y-box.
+At position 701 to 830, the domain is characterized as C2.
+At position 90 to 164, the domain is characterized as PRC barrel.
+At position 16 to 278, the domain is characterized as Protein kinase.
+At position 5 to 119, the domain is characterized as VOC 1.
+At position 143 to 264, the domain is characterized as VOC 2.
+At position 20 to 168, the domain is characterized as MRH.
+At position 10 to 218, the domain is characterized as ABC transporter.
+At position 212 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 318 to 411, the domain is characterized as Ig-like C2-type 4.
+At position 414 to 508, the domain is characterized as Ig-like C2-type 5.
+At position 590 to 939, the domain is characterized as Protein kinase.
+At position 46 to 113, the domain is characterized as EamA.
+At position 40 to 154, the domain is characterized as sHSP.
+At position 29 to 234, the domain is characterized as HORMA.
+At position 928 to 1019, the domain is characterized as Fibronectin type-III 1.
+At position 1164 to 1257, the domain is characterized as Fibronectin type-III 2.
+At position 1255 to 1362, the domain is characterized as CBM20.
+At position 413 to 457, the domain is characterized as LysM.
+At position 8 to 276, the domain is characterized as tr-type G.
+At position 51 to 86, the domain is characterized as EF-hand 1.
+At position 87 to 122, the domain is characterized as EF-hand 2.
+At position 124 to 159, the domain is characterized as EF-hand 3.
+At position 160 to 195, the domain is characterized as EF-hand 4.
+At position 19 to 351, the domain is characterized as USP.
+At position 63 to 221, the domain is characterized as Thioredoxin.
+At position 279 to 356, the domain is characterized as RRM 1.
+At position 380 to 464, the domain is characterized as RRM 2.
+At position 2 to 143, the domain is characterized as RNase H type-1.
+At position 110 to 170, the domain is characterized as S4 RNA-binding 1.
+At position 189 to 251, the domain is characterized as S4 RNA-binding 2.
+At position 58 to 108, the domain is characterized as bHLH.
+At position 16 to 250, the domain is characterized as Glutamine amidotransferase type-1.
+At position 139 to 411, the domain is characterized as Septin-type G.
+At position 17 to 47, the domain is characterized as LRRNT.
+At position 221 to 282, the domain is characterized as LRRCT.
+At position 101 to 178, the domain is characterized as PRC barrel.
+At position 96 to 438, the domain is characterized as Peptidase A1.
+At position 131 to 214, the domain is characterized as MtN3/slv 2.
+At position 445 to 711, the domain is characterized as Protein kinase.
+At position 730 to 804, the domain is characterized as U-box.
+At position 5 to 175, the domain is characterized as Era-type G.
+At position 206 to 285, the domain is characterized as KH type-2.
+At position 6 to 149, the domain is characterized as MPN.
+At position 285 to 450, the domain is characterized as NIDO.
+At position 681 to 840, the domain is characterized as AMOP.
+At position 852 to 1088, the domain is characterized as VWFD.
+At position 1179 to 1238, the domain is characterized as Sushi.
+At position 23 to 816, the domain is characterized as Protein kinase.
+At position 817 to 860, the domain is characterized as AGC-kinase C-terminal.
+At position 204 to 584, the domain is characterized as GRAS.
+At position 7 to 157, the domain is characterized as Response regulatory.
+At position 273 to 377, the domain is characterized as RRM 1.
+At position 394 to 465, the domain is characterized as RRM 2.
+At position 108 to 209, the domain is characterized as Cytochrome c.
+At position 658 to 739, the domain is characterized as IPT/TIG.
+At position 22 to 114, the domain is characterized as Ig-like.
+At position 78 to 252, the domain is characterized as Helicase ATP-binding.
+At position 266 to 438, the domain is characterized as Helicase C-terminal.
+At position 157 to 307, the domain is characterized as Plastocyanin-like 2.
+At position 450 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 28 to 66, the domain is characterized as Kazal-like 1; atypical.
+At position 91 to 153, the domain is characterized as Kazal-like 2.
+At position 155 to 216, the domain is characterized as Kazal-like 3.
+At position 219 to 285, the domain is characterized as Kazal-like 4.
+At position 291 to 352, the domain is characterized as Kazal-like 5.
+At position 361 to 423, the domain is characterized as Kazal-like 6.
+At position 431 to 489, the domain is characterized as Kazal-like 7.
+At position 490 to 551, the domain is characterized as Kazal-like 8.
+At position 561 to 622, the domain is characterized as Kazal-like 9.
+At position 626 to 688, the domain is characterized as Kazal-like 10.
+At position 701 to 757, the domain is characterized as Kazal-like 11.
+At position 768 to 830, the domain is characterized as Kazal-like 12.
+At position 843 to 905, the domain is characterized as Kazal-like 13.
+At position 910 to 971, the domain is characterized as Kazal-like 14.
+At position 987 to 1048, the domain is characterized as Kazal-like 15.
+At position 18 to 53, the domain is characterized as QLQ.
+At position 90 to 134, the domain is characterized as WRC.
+At position 4 to 78, the domain is characterized as KRAB.
+At position 140 to 233, the domain is characterized as AB hydrolase-1.
+At position 121 to 180, the domain is characterized as CBS 1.
+At position 184 to 242, the domain is characterized as CBS 2.
+At position 44 to 261, the domain is characterized as Radical SAM core.
+At position 25 to 181, the domain is characterized as F5/8 type C.
+At position 527 to 785, the domain is characterized as Protein kinase.
+At position 367 to 440, the domain is characterized as ACT 1.
+At position 442 to 527, the domain is characterized as ACT 2.
+At position 122 to 293, the domain is characterized as Helicase ATP-binding.
+At position 304 to 477, the domain is characterized as Helicase C-terminal.
+At position 175 to 353, the domain is characterized as EngA-type G 2.
+At position 354 to 446, the domain is characterized as KH-like.
+At position 38 to 149, the domain is characterized as tRNA-binding.
+At position 47 to 212, the domain is characterized as Helicase ATP-binding.
+At position 340 to 494, the domain is characterized as Helicase C-terminal.
+At position 697 to 870, the domain is characterized as Macro.
+At position 930 to 1023, the domain is characterized as BRCT.
+At position 30 to 329, the domain is characterized as F5/8 type A 1.
+At position 30 to 193, the domain is characterized as Plastocyanin-like 1.
+At position 203 to 329, the domain is characterized as Plastocyanin-like 2.
+At position 348 to 683, the domain is characterized as F5/8 type A 2.
+At position 348 to 525, the domain is characterized as Plastocyanin-like 3.
+At position 535 to 683, the domain is characterized as Plastocyanin-like 4.
+At position 1616 to 1941, the domain is characterized as F5/8 type A 3.
+At position 1616 to 1785, the domain is characterized as Plastocyanin-like 5.
+At position 1795 to 1941, the domain is characterized as Plastocyanin-like 6.
+At position 1941 to 2095, the domain is characterized as F5/8 type C 1.
+At position 2100 to 2255, the domain is characterized as F5/8 type C 2.
+At position 124 to 212, the domain is characterized as Ig-like C1-type.
+At position 81 to 350, the domain is characterized as Protein kinase.
+At position 360 to 619, the domain is characterized as Protein kinase.
+At position 620 to 671, the domain is characterized as AGC-kinase C-terminal.
+At position 9 to 94, the domain is characterized as GIY-YIG.
+At position 5 to 120, the domain is characterized as VOC.
+At position 510 to 786, the domain is characterized as Protein kinase.
+At position 41 to 173, the domain is characterized as ADD.
+At position 1 to 221, the domain is characterized as Peptidase A1.
+At position 13 to 282, the domain is characterized as tr-type G.
+At position 273 to 323, the domain is characterized as SOCS box.
+At position 4 to 137, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 205 to 324, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 1 to 130, the domain is characterized as C2.
+At position 330 to 368, the domain is characterized as PLD phosphodiesterase 1.
+At position 658 to 685, the domain is characterized as PLD phosphodiesterase 2.
+At position 3 to 183, the domain is characterized as DHFR.
+At position 52 to 190, the domain is characterized as Fido.
+At position 233 to 284, the domain is characterized as LRRCT 1.
+At position 468 to 760, the domain is characterized as Protein kinase.
+At position 58 to 104, the domain is characterized as F-box.
+At position 165 to 361, the domain is characterized as CheB-type methylesterase.
+At position 24 to 356, the domain is characterized as FERM.
+At position 375 to 475, the domain is characterized as SH2; atypical.
+At position 521 to 781, the domain is characterized as Protein kinase 1.
+At position 822 to 1111, the domain is characterized as Protein kinase 2.
+At position 228 to 276, the domain is characterized as Fibronectin type-II 1.
+At position 286 to 334, the domain is characterized as Fibronectin type-II 2.
+At position 344 to 392, the domain is characterized as Fibronectin type-II 3.
+At position 16 to 74, the domain is characterized as TRAM.
+At position 129 to 315, the domain is characterized as CP-type G.
+At position 196 to 385, the domain is characterized as CheB-type methylesterase.
+At position 27 to 261, the domain is characterized as BAR.
+At position 305 to 365, the domain is characterized as SH3.
+At position 9 to 245, the domain is characterized as ABC transporter 1.
+At position 261 to 506, the domain is characterized as ABC transporter 2.
+At position 319 to 558, the domain is characterized as NR LBD.
+At position 521 to 777, the domain is characterized as ATP-grasp.
+At position 42 to 295, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 125 to 364, the domain is characterized as Radical SAM core.
+At position 90 to 381, the domain is characterized as Protein kinase.
+At position 199 to 390, the domain is characterized as GMPS ATP-PPase.
+At position 27 to 274, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 16 to 132, the domain is characterized as PX.
+At position 176 to 244, the domain is characterized as DRBM.
+At position 6 to 108, the domain is characterized as PINc.
+At position 187 to 220, the domain is characterized as WW.
+At position 90 to 142, the domain is characterized as bHLH.
+At position 220 to 375, the domain is characterized as TrmE-type G.
+At position 12 to 192, the domain is characterized as KARI N-terminal Rossmann.
+At position 193 to 338, the domain is characterized as KARI C-terminal knotted.
+At position 70 to 102, the domain is characterized as LisH.
+At position 222 to 322, the domain is characterized as Fe2OG dioxygenase.
+At position 29 to 102, the domain is characterized as Inhibitor I9.
+At position 98 to 604, the domain is characterized as Peptidase S8.
+At position 367 to 452, the domain is characterized as PA.
+At position 31 to 120, the domain is characterized as ATP-cone.
+At position 292 to 532, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 489, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 556 to 886, the domain is characterized as UvrD-like helicase C-terminal.
+At position 31 to 74, the domain is characterized as WAP.
+At position 17 to 124, the domain is characterized as Fibronectin type-III 1.
+At position 49 to 131, the domain is characterized as SCAN box.
+At position 205 to 289, the domain is characterized as KRAB.
+At position 355 to 405, the domain is characterized as bHLH.
+At position 111 to 142, the domain is characterized as EGF-like 1.
+At position 144 to 184, the domain is characterized as EGF-like 2; calcium-binding.
+At position 13 to 262, the domain is characterized as ABC transporter.
+At position 11 to 55, the domain is characterized as CHCH.
+At position 4 to 72, the domain is characterized as J.
+At position 136 to 369, the domain is characterized as Radical SAM core.
+At position 364 to 533, the domain is characterized as tr-type G.
+At position 125 to 371, the domain is characterized as NR LBD.
+At position 27 to 198, the domain is characterized as EngB-type G.
+At position 64 to 103, the domain is characterized as EGF-like 1; calcium-binding.
+At position 116 to 159, the domain is characterized as EGF-like 2; calcium-binding.
+At position 160 to 198, the domain is characterized as EGF-like 3; calcium-binding.
+At position 209 to 247, the domain is characterized as EGF-like 4; calcium-binding.
+At position 472 to 522, the domain is characterized as GPS.
+At position 95 to 154, the domain is characterized as Collagen-like 1.
+At position 158 to 271, the domain is characterized as Collagen-like 2.
+At position 52 to 161, the domain is characterized as Fibronectin type-III.
+At position 222 to 382, the domain is characterized as TrmE-type G.
+At position 680 to 855, the domain is characterized as Guanylate kinase-like.
+At position 1 to 149, the domain is characterized as SPX.
+At position 424 to 599, the domain is characterized as Rab-GAP TBC.
+At position 137 to 195, the domain is characterized as Collagen-like 1.
+At position 196 to 222, the domain is characterized as Collagen-like 2.
+At position 299 to 546, the domain is characterized as Olfactomedin-like.
+At position 118 to 350, the domain is characterized as ATP-grasp.
+At position 322 to 375, the domain is characterized as TSP type-1.
+At position 36 to 96, the domain is characterized as HTH tetR-type.
+At position 58 to 230, the domain is characterized as Phosphatase tensin-type.
+At position 234 to 530, the domain is characterized as C2 tensin-type.
+At position 196 to 382, the domain is characterized as Glutamine amidotransferase type-1.
+At position 25 to 144, the domain is characterized as Thioredoxin 1.
+At position 357 to 485, the domain is characterized as Thioredoxin 2.
+At position 52 to 167, the domain is characterized as Expansin-like EG45.
+At position 177 to 257, the domain is characterized as Expansin-like CBD.
+At position 223 to 484, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 11 to 234, the domain is characterized as ABC transporter.
+At position 277 to 355, the domain is characterized as Rhodanese.
+At position 2 to 26, the domain is characterized as Carrier.
+At position 15 to 97, the domain is characterized as GIY-YIG.
+At position 8 to 171, the domain is characterized as PPIase cyclophilin-type.
+At position 5 to 363, the domain is characterized as DZF.
+At position 510 to 576, the domain is characterized as DRBM 2.
+At position 229 to 264, the domain is characterized as EF-hand 1.
+At position 273 to 308, the domain is characterized as EF-hand 2.
+At position 395 to 551, the domain is characterized as Ferric oxidoreductase.
+At position 587 to 715, the domain is characterized as FAD-binding FR-type.
+At position 218 to 391, the domain is characterized as EngA-type G 2.
+At position 392 to 476, the domain is characterized as KH-like.
+At position 242 to 438, the domain is characterized as B30.2/SPRY.
+At position 134 to 570, the domain is characterized as Urease.
+At position 47 to 129, the domain is characterized as PDZ.
+At position 65 to 173, the domain is characterized as SH2.
+At position 197 to 366, the domain is characterized as PCI.
+At position 199 to 291, the domain is characterized as PpiC.
+At position 13 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 216 to 291, the domain is characterized as DEP.
+At position 496 to 634, the domain is characterized as N-terminal Ras-GEF.
+At position 772 to 1009, the domain is characterized as Ras-GEF.
+At position 36 to 393, the domain is characterized as PIPK.
+At position 135 to 237, the domain is characterized as BACK.
+At position 92 to 164, the domain is characterized as PRC barrel.
+At position 218 to 320, the domain is characterized as Fe2OG dioxygenase.
+At position 45 to 333, the domain is characterized as ABC transmembrane type-1 1.
+At position 368 to 604, the domain is characterized as ABC transporter 1.
+At position 705 to 992, the domain is characterized as ABC transmembrane type-1 2.
+At position 1027 to 1266, the domain is characterized as ABC transporter 2.
+At position 239 to 322, the domain is characterized as RRM 1.
+At position 359 to 437, the domain is characterized as RRM 2.
+At position 478 to 564, the domain is characterized as RRM 3.
+At position 313 to 410, the domain is characterized as RRM 1.
+At position 432 to 513, the domain is characterized as RRM 2.
+At position 76 to 380, the domain is characterized as Peptidase A1.
+At position 118 to 206, the domain is characterized as Rieske.
+At position 34 to 112, the domain is characterized as RRM.
+At position 139 to 348, the domain is characterized as ATP-grasp.
+At position 451 to 544, the domain is characterized as ELM2.
+At position 560 to 611, the domain is characterized as SANT.
+At position 194 to 235, the domain is characterized as CHCH.
+At position 1 to 141, the domain is characterized as B12-binding.
+At position 163 to 391, the domain is characterized as Radical SAM core.
+At position 1795 to 2003, the domain is characterized as Rap-GAP.
+At position 28 to 80, the domain is characterized as bHLH.
+At position 663 to 698, the domain is characterized as EF-hand.
+At position 135 to 570, the domain is characterized as Urease.
+At position 2199 to 2246, the domain is characterized as GRIP.
+At position 106 to 185, the domain is characterized as PDZ 1.
+At position 198 to 287, the domain is characterized as PDZ 2.
+At position 104 to 188, the domain is characterized as PDZ.
+At position 75 to 157, the domain is characterized as BRICHOS.
+At position 256 to 445, the domain is characterized as FAD-binding PCMH-type.
+At position 135 to 196, the domain is characterized as KRAB.
+At position 7 to 333, the domain is characterized as Transferrin-like 1.
+At position 345 to 670, the domain is characterized as Transferrin-like 2.
+At position 104 to 144, the domain is characterized as EGF-like.
+At position 644 to 737, the domain is characterized as Fe2OG dioxygenase.
+At position 396 to 849, the domain is characterized as FH2.
+At position 1124 to 1288, the domain is characterized as PNPLA.
+At position 3 to 132, the domain is characterized as Nudix hydrolase.
+At position 517 to 580, the domain is characterized as bZIP.
+At position 39 to 266, the domain is characterized as Radical SAM core.
+At position 220 to 465, the domain is characterized as CN hydrolase.
+At position 1 to 129, the domain is characterized as DAGKc.
+At position 109 to 421, the domain is characterized as IF rod.
+At position 27 to 160, the domain is characterized as FZ.
+At position 190 to 404, the domain is characterized as MurNAc-LAA.
+At position 11 to 180, the domain is characterized as Era-type G.
+At position 210 to 286, the domain is characterized as KH type-2.
+At position 125 to 176, the domain is characterized as SANT.
+At position 119 to 150, the domain is characterized as EF-hand 4.
+At position 29 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 78, the domain is characterized as BMV.
+At position 11 to 174, the domain is characterized as Era-type G.
+At position 205 to 273, the domain is characterized as KH type-2.
+At position 25 to 284, the domain is characterized as Protein kinase.
+At position 311 to 335, the domain is characterized as NAF.
+At position 3 to 149, the domain is characterized as bMERB.
+At position 29 to 134, the domain is characterized as Ig-like 1.
+At position 148 to 234, the domain is characterized as Ig-like 2.
+At position 237 to 327, the domain is characterized as Ig-like 3.
+At position 224 to 324, the domain is characterized as HD.
+At position 83 to 300, the domain is characterized as Radical SAM core.
+At position 588 to 689, the domain is characterized as tRNA-binding.
+At position 414 to 570, the domain is characterized as Exonuclease.
+At position 29 to 206, the domain is characterized as Eph LBD.
+At position 324 to 434, the domain is characterized as Fibronectin type-III 1.
+At position 435 to 530, the domain is characterized as Fibronectin type-III 2.
+At position 94 to 206, the domain is characterized as Ferric oxidoreductase.
+At position 230 to 355, the domain is characterized as FAD-binding FR-type.
+At position 614 to 649, the domain is characterized as UVR.
+At position 131 to 297, the domain is characterized as Helicase ATP-binding.
+At position 375 to 548, the domain is characterized as Helicase C-terminal.
+At position 639 to 742, the domain is characterized as tRNA-binding.
+At position 101 to 219, the domain is characterized as Ferric oxidoreductase.
+At position 250 to 388, the domain is characterized as FAD-binding FR-type.
+At position 26 to 76, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 288 to 366, the domain is characterized as TGS.
+At position 182 to 283, the domain is characterized as PpiC 1.
+At position 294 to 392, the domain is characterized as PpiC 2.
+At position 37 to 245, the domain is characterized as Alpha-carbonic anhydrase.
+At position 200 to 396, the domain is characterized as Peptidase M12B.
+At position 404 to 490, the domain is characterized as Disintegrin.
+At position 121 to 196, the domain is characterized as PDZ.
+At position 386 to 462, the domain is characterized as UBX.
+At position 64 to 99, the domain is characterized as EF-hand.
+At position 159 to 199, the domain is characterized as G-patch.
+At position 194 to 254, the domain is characterized as TSP type-1.
+At position 19 to 88, the domain is characterized as HTH HARE-type.
+At position 87 to 457, the domain is characterized as SAM-dependent MTase C5-type.
+At position 58 to 331, the domain is characterized as Septin-type G.
+At position 71 to 149, the domain is characterized as RRM 1.
+At position 151 to 233, the domain is characterized as RRM 2.
+At position 246 to 318, the domain is characterized as RRM 3.
+At position 94 to 393, the domain is characterized as AB hydrolase-1.
+At position 4 to 232, the domain is characterized as Peptidase M12B.
+At position 84 to 173, the domain is characterized as VPS37 C-terminal.
+At position 28 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 16 to 101, the domain is characterized as GS beta-grasp.
+At position 108 to 443, the domain is characterized as GS catalytic.
+At position 176 to 347, the domain is characterized as PCI.
+At position 106 to 185, the domain is characterized as PRC barrel.
+At position 130 to 157, the domain is characterized as KOW.
+At position 136 to 313, the domain is characterized as TNase-like.
+At position 472 to 680, the domain is characterized as NEL.
+At position 182 to 340, the domain is characterized as Cupin type-1 1.
+At position 386 to 566, the domain is characterized as Cupin type-1 2.
+At position 623 to 864, the domain is characterized as Fibrinogen C-terminal.
+At position 319 to 369, the domain is characterized as bHLH.
+At position 33 to 117, the domain is characterized as PNT.
+At position 202 to 280, the domain is characterized as RRM.
+At position 2 to 70, the domain is characterized as HTH gntR-type.
+At position 606 to 742, the domain is characterized as JmjC.
+At position 402 to 477, the domain is characterized as B5.
+At position 703 to 797, the domain is characterized as FDX-ACB.
+At position 1063 to 1301, the domain is characterized as Glutamine amidotransferase type-1.
+At position 30 to 159, the domain is characterized as CUB.
+At position 291 to 343, the domain is characterized as TSP type-1 1.
+At position 345 to 398, the domain is characterized as TSP type-1 2.
+At position 400 to 453, the domain is characterized as TSP type-1 3.
+At position 455 to 508, the domain is characterized as TSP type-1 4.
+At position 816 to 868, the domain is characterized as GPS.
+At position 28 to 203, the domain is characterized as BPL/LPL catalytic.
+At position 210 to 450, the domain is characterized as Asparagine synthetase.
+At position 394 to 552, the domain is characterized as SSD.
+At position 52 to 104, the domain is characterized as bHLH.
+At position 523 to 632, the domain is characterized as SMC hinge.
+At position 1 to 111, the domain is characterized as Calponin-homology (CH).
+At position 160 to 219, the domain is characterized as SH3.
+At position 241 to 421, the domain is characterized as DH.
+At position 443 to 548, the domain is characterized as PH.
+At position 99 to 137, the domain is characterized as LDL-receptor class A.
+At position 139 to 519, the domain is characterized as MACPF.
+At position 520 to 550, the domain is characterized as EGF-like.
+At position 580 to 670, the domain is characterized as SH2.
+At position 1 to 159, the domain is characterized as FAD-binding PCMH-type.
+At position 41 to 130, the domain is characterized as BTB.
+At position 124 to 163, the domain is characterized as Pentapeptide repeat 1.
+At position 169 to 208, the domain is characterized as Pentapeptide repeat 2.
+At position 93 to 217, the domain is characterized as AB hydrolase-1.
+At position 162 to 349, the domain is characterized as Helicase ATP-binding.
+At position 384 to 534, the domain is characterized as Helicase C-terminal.
+At position 22 to 115, the domain is characterized as B30.2/SPRY.
+At position 12 to 98, the domain is characterized as MtN3/slv 1.
+At position 134 to 218, the domain is characterized as MtN3/slv 2.
+At position 213 to 402, the domain is characterized as GMPS ATP-PPase.
+At position 44 to 454, the domain is characterized as GH18.
+At position 467 to 553, the domain is characterized as Fibronectin type-III 1.
+At position 562 to 647, the domain is characterized as Fibronectin type-III 2.
+At position 210 to 306, the domain is characterized as PH.
+At position 1 to 57, the domain is characterized as HTH lacI-type.
+At position 21 to 49, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 232 to 465, the domain is characterized as Peptidase S1.
+At position 23 to 101, the domain is characterized as KRAB.
+At position 1 to 97, the domain is characterized as C2 1.
+At position 672 to 796, the domain is characterized as C2 2.
+At position 1106 to 1249, the domain is characterized as MHD1.
+At position 1358 to 1525, the domain is characterized as MHD2.
+At position 1558 to 1685, the domain is characterized as C2 3.
+At position 22 to 101, the domain is characterized as GS beta-grasp.
+At position 108 to 354, the domain is characterized as GS catalytic.
+At position 10 to 84, the domain is characterized as U-box.
+At position 2 to 224, the domain is characterized as Glutamine amidotransferase type-2.
+At position 2 to 288, the domain is characterized as Glutamine amidotransferase type-2.
+At position 360 to 499, the domain is characterized as SIS 1.
+At position 531 to 672, the domain is characterized as SIS 2.
+At position 4 to 109, the domain is characterized as SSB.
+At position 281 to 557, the domain is characterized as Radical SAM core.
+At position 21 to 98, the domain is characterized as UPAR/Ly6.
+At position 15 to 145, the domain is characterized as DUSP.
+At position 317 to 916, the domain is characterized as USP.
+At position 92 to 135, the domain is characterized as LysM 2.
+At position 174 to 217, the domain is characterized as LysM 3.
+At position 240 to 283, the domain is characterized as LysM 4.
+At position 307 to 350, the domain is characterized as LysM 5.
+At position 370 to 488, the domain is characterized as NlpC/P60.
+At position 97 to 172, the domain is characterized as PRC barrel.
+At position 104 to 296, the domain is characterized as ATP-grasp.
+At position 35 to 140, the domain is characterized as Thioredoxin.
+At position 115 to 209, the domain is characterized as WSC.
+At position 7 to 149, the domain is characterized as Nudix hydrolase.
+At position 141 to 376, the domain is characterized as Radical SAM core.
+At position 96 to 131, the domain is characterized as EF-hand 1.
+At position 231 to 266, the domain is characterized as EF-hand 3.
+At position 276 to 311, the domain is characterized as EF-hand 4.
+At position 312 to 347, the domain is characterized as EF-hand 5.
+At position 258 to 292, the domain is characterized as ShKT.
+At position 298 to 383, the domain is characterized as Ig-like C2-type.
+At position 102 to 295, the domain is characterized as ATP-grasp.
+At position 6 to 90, the domain is characterized as Core-binding (CB).
+At position 111 to 290, the domain is characterized as Tyr recombinase.
+At position 93 to 425, the domain is characterized as Asparaginase/glutaminase.
+At position 2 to 171, the domain is characterized as Miro 1.
+At position 187 to 222, the domain is characterized as EF-hand 1.
+At position 307 to 342, the domain is characterized as EF-hand 2.
+At position 423 to 589, the domain is characterized as Miro 2.
+At position 431 to 583, the domain is characterized as Exonuclease.
+At position 6 to 101, the domain is characterized as SH2 1.
+At position 111 to 205, the domain is characterized as SH2 2.
+At position 227 to 645, the domain is characterized as Tyrosine-protein phosphatase.
+At position 320 to 379, the domain is characterized as COS.
+At position 381 to 484, the domain is characterized as Fibronectin type-III.
+At position 482 to 659, the domain is characterized as B30.2/SPRY.
+At position 465 to 513, the domain is characterized as Kazal-like.
+At position 147 to 282, the domain is characterized as Fatty acid hydroxylase.
+At position 80 to 339, the domain is characterized as Protein kinase 1.
+At position 340 to 409, the domain is characterized as AGC-kinase C-terminal.
+At position 435 to 692, the domain is characterized as Protein kinase 2.
+At position 27 to 155, the domain is characterized as FAS1 1.
+At position 167 to 321, the domain is characterized as FAS1 2.
+At position 329 to 470, the domain is characterized as FAS1 3.
+At position 474 to 622, the domain is characterized as FAS1 4.
+At position 1 to 97, the domain is characterized as STAS.
+At position 363 to 448, the domain is characterized as Death.
+At position 304 to 548, the domain is characterized as NR LBD.
+At position 123 to 306, the domain is characterized as Helicase ATP-binding.
+At position 340 to 523, the domain is characterized as Helicase C-terminal.
+At position 63 to 126, the domain is characterized as bZIP.
+At position 1339 to 1502, the domain is characterized as JmjC.
+At position 132 to 248, the domain is characterized as C-type lectin.
+At position 23 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 687 to 773, the domain is characterized as PDZ 5.
+At position 162 to 212, the domain is characterized as DHHC.
+At position 19 to 82, the domain is characterized as Sushi 1.
+At position 83 to 143, the domain is characterized as Sushi 2.
+At position 144 to 207, the domain is characterized as Sushi 3.
+At position 208 to 264, the domain is characterized as Sushi 4.
+At position 265 to 322, the domain is characterized as Sushi 5.
+At position 325 to 383, the domain is characterized as Sushi 6.
+At position 385 to 442, the domain is characterized as Sushi 7.
+At position 444 to 505, the domain is characterized as Sushi 8.
+At position 507 to 562, the domain is characterized as Sushi 9.
+At position 565 to 623, the domain is characterized as Sushi 10.
+At position 627 to 685, the domain is characterized as Sushi 11.
+At position 688 to 745, the domain is characterized as Sushi 12.
+At position 750 to 804, the domain is characterized as Sushi 13.
+At position 809 to 866, the domain is characterized as Sushi 14.
+At position 868 to 936, the domain is characterized as Sushi 15.
+At position 937 to 994, the domain is characterized as Sushi 16.
+At position 995 to 1053, the domain is characterized as Sushi 17.
+At position 1054 to 1111, the domain is characterized as Sushi 18.
+At position 1114 to 1172, the domain is characterized as Sushi 19.
+At position 1173 to 1235, the domain is characterized as Sushi 20.
+At position 23 to 92, the domain is characterized as Ubiquitin-like.
+At position 15 to 71, the domain is characterized as Sm.
+At position 13 to 137, the domain is characterized as MH1.
+At position 271 to 465, the domain is characterized as MH2.
+At position 36 to 305, the domain is characterized as Protein kinase.
+At position 346 to 381, the domain is characterized as EF-hand 1.
+At position 382 to 417, the domain is characterized as EF-hand 2.
+At position 418 to 453, the domain is characterized as EF-hand 3.
+At position 454 to 488, the domain is characterized as EF-hand 4.
+At position 164 to 243, the domain is characterized as PPIase FKBP-type.
+At position 141 to 222, the domain is characterized as KH.
+At position 291 to 354, the domain is characterized as MIR 1.
+At position 365 to 422, the domain is characterized as MIR 2.
+At position 426 to 486, the domain is characterized as MIR 3.
+At position 95 to 154, the domain is characterized as bHLH.
+At position 506 to 620, the domain is characterized as PH 1.
+At position 810 to 881, the domain is characterized as RBD.
+At position 890 to 976, the domain is characterized as PDZ.
+At position 1099 to 1293, the domain is characterized as DH.
+At position 1347 to 1478, the domain is characterized as PH 2.
+At position 248 to 439, the domain is characterized as GATase cobBQ-type.
+At position 9 to 145, the domain is characterized as C2 1.
+At position 184 to 307, the domain is characterized as C2 2.
+At position 338 to 471, the domain is characterized as C2 3.
+At position 112 to 298, the domain is characterized as ATP-grasp.
+At position 38 to 87, the domain is characterized as F-box.
+At position 1 to 54, the domain is characterized as bHLH.
+At position 1 to 125, the domain is characterized as MSP.
+At position 24 to 97, the domain is characterized as H15.
+At position 8 to 86, the domain is characterized as ACT.
+At position 80 to 190, the domain is characterized as PH.
+At position 281 to 470, the domain is characterized as Rho-GAP.
+At position 36 to 127, the domain is characterized as HTH La-type RNA-binding.
+At position 133 to 211, the domain is characterized as RRM.
+At position 425 to 538, the domain is characterized as xRRM.
+At position 59 to 118, the domain is characterized as Chromo.
+At position 14 to 155, the domain is characterized as CheW-like.
+At position 115 to 306, the domain is characterized as Rab-GAP TBC.
+At position 482 to 541, the domain is characterized as SH3.
+At position 557 to 720, the domain is characterized as RUN.
+At position 10 to 192, the domain is characterized as tr-type G.
+At position 151 to 343, the domain is characterized as CheB-type methylesterase.
+At position 1 to 115, the domain is characterized as C2 1.
+At position 124 to 247, the domain is characterized as C2 2.
+At position 291 to 513, the domain is characterized as VWFA.
+At position 318 to 358, the domain is characterized as UBA 2.
+At position 201 to 234, the domain is characterized as ShKT.
+At position 24 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 338 to 575, the domain is characterized as ABC transporter.
+At position 681 to 881, the domain is characterized as ATP-grasp 2.
+At position 964 to 1126, the domain is characterized as MGS-like.
+At position 102 to 301, the domain is characterized as MAGE.
+At position 3 to 106, the domain is characterized as Glutaredoxin.
+At position 33 to 186, the domain is characterized as SIS.
+At position 21 to 228, the domain is characterized as EngB-type G.
+At position 156 to 251, the domain is characterized as BRCT.
+At position 57 to 112, the domain is characterized as F-box.
+At position 436 to 497, the domain is characterized as SH3 3.
+At position 808 to 867, the domain is characterized as SH3 4.
+At position 365 to 533, the domain is characterized as tr-type G.
+At position 211 to 372, the domain is characterized as CP-type G.
+At position 32 to 108, the domain is characterized as ACT.
+At position 601 to 714, the domain is characterized as PI-PLC Y-box.
+At position 715 to 843, the domain is characterized as C2.
+At position 5 to 120, the domain is characterized as PINc.
+At position 5 to 225, the domain is characterized as tr-type G.
+At position 144 to 375, the domain is characterized as Radical SAM core.
+At position 378 to 446, the domain is characterized as TRAM.
+At position 84 to 399, the domain is characterized as IF rod.
+At position 117 to 326, the domain is characterized as TLC.
+At position 706 to 789, the domain is characterized as ACT 1.
+At position 816 to 896, the domain is characterized as ACT 2.
+At position 2 to 104, the domain is characterized as SSB.
+At position 19 to 115, the domain is characterized as Ig-like.
+At position 18 to 137, the domain is characterized as Peptidase C39.
+At position 44 to 281, the domain is characterized as Peptidase S1.
+At position 81 to 210, the domain is characterized as Thioredoxin.
+At position 318 to 395, the domain is characterized as Carrier.
+At position 8 to 249, the domain is characterized as ABC transporter.
+At position 19 to 249, the domain is characterized as ABC transporter.
+At position 296 to 369, the domain is characterized as RRM.
+At position 737 to 766, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 10 to 97, the domain is characterized as MtN3/slv 1.
+At position 133 to 212, the domain is characterized as MtN3/slv 2.
+At position 338 to 567, the domain is characterized as TLDc.
+At position 126 to 564, the domain is characterized as Urease.
+At position 144 to 380, the domain is characterized as Methyl-accepting transducer.
+At position 498 to 852, the domain is characterized as Reverse transcriptase.
+At position 133 to 387, the domain is characterized as ABC transporter 1.
+At position 829 to 1071, the domain is characterized as ABC transporter 2.
+At position 7 to 95, the domain is characterized as RH1.
+At position 500 to 571, the domain is characterized as RH2.
+At position 352 to 462, the domain is characterized as PAZ.
+At position 638 to 959, the domain is characterized as Piwi.
+At position 152 to 211, the domain is characterized as VWFC 1.
+At position 215 to 273, the domain is characterized as VWFC 2.
+At position 1213 to 1282, the domain is characterized as Sushi 1.
+At position 1283 to 1344, the domain is characterized as Sushi 2.
+At position 1345 to 1412, the domain is characterized as Sushi 3.
+At position 1413 to 1473, the domain is characterized as Sushi 4.
+At position 1476 to 1556, the domain is characterized as Sushi 5.
+At position 277 to 438, the domain is characterized as Helicase ATP-binding.
+At position 457 to 617, the domain is characterized as Helicase C-terminal.
+At position 58 to 88, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 99 to 128, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 62 to 167, the domain is characterized as THUMP.
+At position 25 to 259, the domain is characterized as Peptidase S1.
+At position 13 to 92, the domain is characterized as RRM.
+At position 91 to 126, the domain is characterized as EF-hand 2.
+At position 61 to 97, the domain is characterized as Tify 1.
+At position 228 to 264, the domain is characterized as Tify 2.
+At position 31 to 76, the domain is characterized as LRRNT.
+At position 241 to 330, the domain is characterized as LRRCT.
+At position 393 to 467, the domain is characterized as GW 1.
+At position 472 to 550, the domain is characterized as GW 2.
+At position 553 to 630, the domain is characterized as GW 3.
+At position 175 to 277, the domain is characterized as PpiC 1.
+At position 292 to 391, the domain is characterized as PpiC 2.
+At position 31 to 141, the domain is characterized as Ig-like V-type.
+At position 142 to 232, the domain is characterized as Ig-like C2-type.
+At position 42 to 117, the domain is characterized as Inhibitor I9.
+At position 128 to 400, the domain is characterized as Peptidase S8.
+At position 64 to 170, the domain is characterized as Calponin-homology (CH).
+At position 7 to 187, the domain is characterized as UmuC.
+At position 62 to 217, the domain is characterized as N-acetyltransferase.
+At position 338 to 500, the domain is characterized as PCI.
+At position 63 to 131, the domain is characterized as S1 motif.
+At position 139 to 197, the domain is characterized as KH.
+At position 93 to 139, the domain is characterized as S1 motif.
+At position 303 to 350, the domain is characterized as PAS.
+At position 454 to 587, the domain is characterized as GGDEF.
+At position 598 to 852, the domain is characterized as EAL.
+At position 141 to 246, the domain is characterized as POTRA 1.
+At position 247 to 364, the domain is characterized as POTRA 2.
+At position 365 to 448, the domain is characterized as POTRA 3.
+At position 56 to 162, the domain is characterized as sHSP.
+At position 179 to 266, the domain is characterized as Ras-associating.
+At position 313 to 422, the domain is characterized as PH.
+At position 94 to 167, the domain is characterized as PRC barrel.
+At position 1 to 69, the domain is characterized as MBD.
+At position 256 to 396, the domain is characterized as DOD-type homing endonuclease.
+At position 6 to 254, the domain is characterized as ABC transporter.
+At position 1 to 457, the domain is characterized as ADPK.
+At position 439 to 497, the domain is characterized as RAP.
+At position 97 to 496, the domain is characterized as Glutamine amidotransferase type-2.
+At position 10 to 271, the domain is characterized as Protein kinase.
+At position 344 to 410, the domain is characterized as PASTA 1.
+At position 411 to 477, the domain is characterized as PASTA 2.
+At position 478 to 545, the domain is characterized as PASTA 3.
+At position 32 to 140, the domain is characterized as Ig-like 1.
+At position 150 to 234, the domain is characterized as Ig-like 2.
+At position 242 to 324, the domain is characterized as Ig-like 3.
+At position 399 to 498, the domain is characterized as Ig-like 4.
+At position 500 to 592, the domain is characterized as Ig-like 5.
+At position 608 to 708, the domain is characterized as Fibronectin type-III.
+At position 550 to 763, the domain is characterized as FtsK.
+At position 113 to 148, the domain is characterized as Tify.
+At position 4 to 99, the domain is characterized as GRAM.
+At position 123 to 498, the domain is characterized as Myotubularin phosphatase.
+At position 167 to 241, the domain is characterized as Toprim.
+At position 61 to 115, the domain is characterized as J.
+At position 432 to 592, the domain is characterized as OTU.
+At position 7 to 246, the domain is characterized as ABC transporter 1.
+At position 263 to 508, the domain is characterized as ABC transporter 2.
+At position 10 to 157, the domain is characterized as SprT-like.
+At position 33 to 305, the domain is characterized as Septin-type G.
+At position 4 to 146, the domain is characterized as RNase H type-1.
+At position 6 to 196, the domain is characterized as UmuC.
+At position 4 to 103, the domain is characterized as SSB.
+At position 1 to 50, the domain is characterized as Peptidase S1.
+At position 96 to 167, the domain is characterized as KRAB.
+At position 66 to 250, the domain is characterized as RNase H type-2.
+At position 17 to 88, the domain is characterized as RRM.
+At position 242 to 394, the domain is characterized as GAF 1.
+At position 426 to 640, the domain is characterized as GAF 2.
+At position 670 to 993, the domain is characterized as PDEase.
+At position 73 to 243, the domain is characterized as Helicase ATP-binding.
+At position 254 to 415, the domain is characterized as Helicase C-terminal.
+At position 588 to 666, the domain is characterized as BRCT.
+At position 10 to 202, the domain is characterized as tr-type G.
+At position 248 to 501, the domain is characterized as CN hydrolase.
+At position 441 to 492, the domain is characterized as Rubredoxin-like.
+At position 37 to 194, the domain is characterized as SIS.
+At position 468 to 640, the domain is characterized as SSD.
+At position 560 to 665, the domain is characterized as tRNA-binding.
+At position 40 to 153, the domain is characterized as OmpA-like.
+At position 3 to 268, the domain is characterized as BAR.
+At position 277 to 375, the domain is characterized as PH.
+At position 486 to 635, the domain is characterized as PID.
+At position 1989 to 2106, the domain is characterized as C2.
+At position 44 to 315, the domain is characterized as Protein kinase.
+At position 121 to 172, the domain is characterized as Rubredoxin-like 2.
+At position 5 to 128, the domain is characterized as VOC.
+At position 111 to 306, the domain is characterized as ATP-grasp.
+At position 1 to 53, the domain is characterized as HTH myb-type 1.
+At position 54 to 108, the domain is characterized as HTH myb-type 2.
+At position 103 to 192, the domain is characterized as Ig-like C2-type.
+At position 1 to 47, the domain is characterized as Kazal-like 1.
+At position 48 to 95, the domain is characterized as Kazal-like 2.
+At position 96 to 143, the domain is characterized as Kazal-like 3.
+At position 144 to 194, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 346 to 499, the domain is characterized as N-acetyltransferase.
+At position 72 to 215, the domain is characterized as Flavodoxin-like.
+At position 277 to 511, the domain is characterized as FAD-binding FR-type.
+At position 173 to 484, the domain is characterized as IF rod.
+At position 629 to 718, the domain is characterized as EH.
+At position 8 to 174, the domain is characterized as UBC core.
+At position 5 to 117, the domain is characterized as MTTase N-terminal.
+At position 135 to 363, the domain is characterized as Radical SAM core.
+At position 366 to 437, the domain is characterized as TRAM.
+At position 841 to 1030, the domain is characterized as DH.
+At position 1059 to 1153, the domain is characterized as PH 1.
+At position 1302 to 1398, the domain is characterized as PH 2.
+At position 555 to 846, the domain is characterized as Protein kinase.
+At position 73 to 135, the domain is characterized as TGS.
+At position 30 to 227, the domain is characterized as BPL/LPL catalytic.
+At position 57 to 199, the domain is characterized as SCP.
+At position 76 to 342, the domain is characterized as Protein kinase.
+At position 343 to 413, the domain is characterized as AGC-kinase C-terminal.
+At position 1095 to 1214, the domain is characterized as PH.
+At position 1240 to 1513, the domain is characterized as CNH.
+At position 1583 to 1596, the domain is characterized as CRIB.
+At position 458 to 830, the domain is characterized as USP.
+At position 880 to 1052, the domain is characterized as Exonuclease.
+At position 7 to 67, the domain is characterized as Sm.
+At position 66 to 221, the domain is characterized as Flavodoxin-like.
+At position 277 to 538, the domain is characterized as FAD-binding FR-type.
+At position 31 to 49, the domain is characterized as EF-hand 1.
+At position 9 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 397, the domain is characterized as GMPS ATP-PPase.
+At position 65 to 143, the domain is characterized as RRM 1.
+At position 153 to 230, the domain is characterized as RRM 2.
+At position 246 to 323, the domain is characterized as RRM 3.
+At position 349 to 471, the domain is characterized as RRM 4.
+At position 676 to 753, the domain is characterized as PABC.
+At position 9 to 177, the domain is characterized as Era-type G.
+At position 200 to 284, the domain is characterized as KH type-2.
+At position 52 to 145, the domain is characterized as Rhodanese.
+At position 45 to 79, the domain is characterized as ShKT.
+At position 575 to 651, the domain is characterized as BRCT.
+At position 32 to 113, the domain is characterized as GST N-terminal.
+At position 118 to 241, the domain is characterized as GST C-terminal.
+At position 110 to 283, the domain is characterized as Helicase ATP-binding.
+At position 311 to 467, the domain is characterized as Helicase C-terminal.
+At position 437 to 485, the domain is characterized as LysM.
+At position 6 to 242, the domain is characterized as ABC transporter 1.
+At position 30 to 267, the domain is characterized as Peptidase S1.
+At position 42 to 129, the domain is characterized as RRM.
+At position 118 to 313, the domain is characterized as ATP-grasp.
+At position 11 to 64, the domain is characterized as HTH cro/C1-type.
+At position 5 to 121, the domain is characterized as Response regulatory.
+At position 26 to 63, the domain is characterized as EGF-like 1.
+At position 64 to 102, the domain is characterized as EGF-like 2.
+At position 105 to 143, the domain is characterized as EGF-like 3.
+At position 144 to 180, the domain is characterized as EGF-like 4.
+At position 182 to 219, the domain is characterized as EGF-like 5; calcium-binding.
+At position 221 to 258, the domain is characterized as EGF-like 6.
+At position 399 to 455, the domain is characterized as SH3.
+At position 129 to 455, the domain is characterized as SAC.
+At position 102 to 201, the domain is characterized as Cytochrome b5 heme-binding.
+At position 16 to 330, the domain is characterized as DOT1.
+At position 11 to 697, the domain is characterized as Myosin motor.
+At position 701 to 727, the domain is characterized as IQ 1.
+At position 723 to 750, the domain is characterized as IQ 2.
+At position 746 to 774, the domain is characterized as IQ 3.
+At position 861 to 1044, the domain is characterized as TH1.
+At position 22 to 101, the domain is characterized as GIY-YIG.
+At position 211 to 246, the domain is characterized as UVR.
+At position 21 to 303, the domain is characterized as Protein kinase.
+At position 16 to 282, the domain is characterized as Protein kinase.
+At position 332 to 1037, the domain is characterized as Myosin motor.
+At position 1036 to 1065, the domain is characterized as IQ 1.
+At position 1072 to 1101, the domain is characterized as IQ 2.
+At position 183 to 259, the domain is characterized as RRM.
+At position 136 to 185, the domain is characterized as bHLH.
+At position 27 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 118 to 211, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 315 to 409, the domain is characterized as Ig-like C2-type 4.
+At position 417 to 519, the domain is characterized as Ig-like C2-type 5.
+At position 595 to 970, the domain is characterized as Protein kinase.
+At position 207 to 297, the domain is characterized as Ig-like.
+At position 299 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 104, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 104 to 194, the domain is characterized as ACB.
+At position 51 to 178, the domain is characterized as TIR.
+At position 389 to 477, the domain is characterized as PPIase FKBP-type.
+At position 59 to 100, the domain is characterized as JmjN.
+At position 261 to 427, the domain is characterized as JmjC.
+At position 644 to 702, the domain is characterized as FYR N-terminal.
+At position 704 to 788, the domain is characterized as FYR C-terminal.
+At position 134 to 409, the domain is characterized as SMP-LTD.
+At position 57 to 189, the domain is characterized as FAS1.
+At position 352 to 600, the domain is characterized as NR LBD.
+At position 30 to 303, the domain is characterized as Pyruvate carboxyltransferase.
+At position 140 to 286, the domain is characterized as PA14.
+At position 491 to 643, the domain is characterized as Helicase C-terminal.
+At position 320 to 603, the domain is characterized as ABC transmembrane type-1 1.
+At position 635 to 859, the domain is characterized as ABC transporter 1.
+At position 977 to 1262, the domain is characterized as ABC transmembrane type-1 2.
+At position 1298 to 1532, the domain is characterized as ABC transporter 2.
+At position 8 to 131, the domain is characterized as MaoC-like.
+At position 41 to 144, the domain is characterized as FAD-binding FR-type.
+At position 49 to 237, the domain is characterized as BPL/LPL catalytic.
+At position 6 to 38, the domain is characterized as LisH.
+At position 40 to 92, the domain is characterized as CTLH.
+At position 207 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 1019 to 1082, the domain is characterized as SAM.
+At position 1105 to 1310, the domain is characterized as PARP catalytic.
+At position 79 to 249, the domain is characterized as Helicase ATP-binding.
+At position 260 to 421, the domain is characterized as Helicase C-terminal.
+At position 213 to 303, the domain is characterized as Death.
+At position 25 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 814 to 1095, the domain is characterized as Protein kinase.
+At position 8 to 70, the domain is characterized as 4Fe-4S Wbl-type.
+At position 7 to 82, the domain is characterized as GIY-YIG.
+At position 302 to 374, the domain is characterized as KH.
+At position 28 to 57, the domain is characterized as IQ.
+At position 658 to 1001, the domain is characterized as HECT.
+At position 206 to 448, the domain is characterized as FAD-binding FR-type.
+At position 57 to 139, the domain is characterized as Lipoyl-binding.
+At position 41 to 106, the domain is characterized as Death.
+At position 165 to 452, the domain is characterized as Protein kinase.
+At position 701 to 776, the domain is characterized as Smr.
+At position 2 to 80, the domain is characterized as PUA.
+At position 131 to 265, the domain is characterized as Fatty acid hydroxylase.
+At position 76 to 346, the domain is characterized as PPM-type phosphatase.
+At position 28 to 210, the domain is characterized as GH11.
+At position 131 to 409, the domain is characterized as ABC transmembrane type-1.
+At position 518 to 740, the domain is characterized as ABC transporter.
+At position 21 to 120, the domain is characterized as Ig-like V-type 1; required for binding to polymeric IgA and IgM.
+At position 135 to 237, the domain is characterized as Ig-like V-type 2.
+At position 245 to 351, the domain is characterized as Ig-like V-type 3.
+At position 352 to 457, the domain is characterized as Ig-like V-type 4.
+At position 463 to 563, the domain is characterized as Ig-like V-type 5.
+At position 261 to 495, the domain is characterized as NR LBD.
+At position 122 to 362, the domain is characterized as PABS.
+At position 8 to 132, the domain is characterized as PX.
+At position 277 to 305, the domain is characterized as MIT.
+At position 344 to 445, the domain is characterized as Protein kinase 1.
+At position 794 to 1056, the domain is characterized as Protein kinase 2.
+At position 22 to 383, the domain is characterized as GH18.
+At position 887 to 926, the domain is characterized as UBA.
+At position 289 to 341, the domain is characterized as bHLH.
+At position 35 to 93, the domain is characterized as 4Fe-4S.
+At position 22 to 112, the domain is characterized as Ig-like.
+At position 1 to 213, the domain is characterized as START.
+At position 1 to 294, the domain is characterized as BRO1.
+At position 109 to 187, the domain is characterized as Kringle 1.
+At position 214 to 292, the domain is characterized as Kringle 2.
+At position 367 to 621, the domain is characterized as Peptidase S1.
+At position 45 to 126, the domain is characterized as SCAN box.
+At position 202 to 292, the domain is characterized as KRAB.
+At position 45 to 188, the domain is characterized as SCP.
+At position 89 to 165, the domain is characterized as RRM.
+At position 429 to 551, the domain is characterized as Ricin B-type lectin.
+At position 25 to 413, the domain is characterized as Helicase ATP-binding.
+At position 629 to 664, the domain is characterized as UVR.
+At position 122 to 154, the domain is characterized as EF-hand 4.
+At position 140 to 269, the domain is characterized as PX.
+At position 299 to 523, the domain is characterized as BAR.
+At position 195 to 533, the domain is characterized as Protein kinase.
+At position 735 to 869, the domain is characterized as BAH 1.
+At position 909 to 1049, the domain is characterized as BAH 2.
+At position 221 to 479, the domain is characterized as Protein kinase.
+At position 152 to 249, the domain is characterized as HTH araC/xylS-type.
+At position 1 to 47, the domain is characterized as KRAB.
+At position 512 to 785, the domain is characterized as Protein kinase.
+At position 786 to 854, the domain is characterized as AGC-kinase C-terminal.
+At position 1104 to 1192, the domain is characterized as PDZ.
+At position 40 to 154, the domain is characterized as tRNA-binding.
+At position 407 to 482, the domain is characterized as B5.
+At position 704 to 797, the domain is characterized as FDX-ACB.
+At position 4 to 49, the domain is characterized as UBA-like.
+At position 55 to 245, the domain is characterized as DCUN1.
+At position 22 to 378, the domain is characterized as GH16.
+At position 40 to 265, the domain is characterized as GB1/RHD3-type G.
+At position 8 to 694, the domain is characterized as Myosin motor.
+At position 697 to 719, the domain is characterized as IQ 1.
+At position 720 to 742, the domain is characterized as IQ 2.
+At position 743 to 772, the domain is characterized as IQ 3.
+At position 858 to 1042, the domain is characterized as TH1.
+At position 88 to 139, the domain is characterized as HTH myb-type 1.
+At position 140 to 194, the domain is characterized as HTH myb-type 2.
+At position 571 to 832, the domain is characterized as Protein kinase.
+At position 835 to 963, the domain is characterized as KEN.
+At position 57 to 237, the domain is characterized as NodB homology.
+At position 74 to 271, the domain is characterized as TLC.
+At position 29 to 167, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 532 to 705, the domain is characterized as tr-type G.
+At position 1 to 128, the domain is characterized as N-acetyltransferase.
+At position 4 to 199, the domain is characterized as DPCK.
+At position 20 to 127, the domain is characterized as Ig-like.
+At position 162 to 414, the domain is characterized as NR LBD.
+At position 13 to 83, the domain is characterized as HTH iclR-type.
+At position 17 to 88, the domain is characterized as PAS.
+At position 92 to 144, the domain is characterized as PAC.
+At position 171 to 334, the domain is characterized as OBG-type G.
+At position 3 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 389, the domain is characterized as GMPS ATP-PPase.
+At position 127 to 398, the domain is characterized as Peptidase S8.
+At position 257 to 482, the domain is characterized as Lon N-terminal.
+At position 481 to 590, the domain is characterized as CULT.
+At position 3 to 332, the domain is characterized as SAM-dependent MTase C5-type.
+At position 129 to 233, the domain is characterized as sHSP.
+At position 793 to 972, the domain is characterized as DOC.
+At position 7 to 63, the domain is characterized as RabBD.
+At position 355 to 583, the domain is characterized as TLDc.
+At position 7 to 192, the domain is characterized as UmuC.
+At position 211 to 363, the domain is characterized as TrmE-type G.
+At position 13 to 76, the domain is characterized as CSD.
+At position 50 to 124, the domain is characterized as H15.
+At position 23 to 197, the domain is characterized as Exonuclease.
+At position 1 to 39, the domain is characterized as Cadherin 1.
+At position 40 to 145, the domain is characterized as Cadherin 2.
+At position 101 to 231, the domain is characterized as N-terminal Ras-GEF.
+At position 270 to 539, the domain is characterized as Ras-GEF.
+At position 684 to 771, the domain is characterized as Ras-associating.
+At position 2 to 133, the domain is characterized as HTH rrf2-type.
+At position 631 to 905, the domain is characterized as Protein kinase.
+At position 13 to 217, the domain is characterized as tr-type G.
+At position 66 to 148, the domain is characterized as Lipoyl-binding.
+At position 7 to 97, the domain is characterized as BRCT 1.
+At position 104 to 194, the domain is characterized as BRCT 2.
+At position 1090 to 1181, the domain is characterized as BRCT 3.
+At position 342 to 402, the domain is characterized as S4 RNA-binding.
+At position 304 to 401, the domain is characterized as RRM 1.
+At position 423 to 504, the domain is characterized as RRM 2.
+At position 2 to 62, the domain is characterized as S4 RNA-binding.
+At position 54 to 168, the domain is characterized as Expansin-like EG45.
+At position 178 to 257, the domain is characterized as Expansin-like CBD.
+At position 315 to 507, the domain is characterized as B30.2/SPRY.
+At position 402 to 610, the domain is characterized as Rab-GAP TBC.
+At position 31 to 211, the domain is characterized as Reticulon.
+At position 183 to 295, the domain is characterized as SPR.
+At position 49 to 145, the domain is characterized as Ig-like V-type.
+At position 212 to 232, the domain is characterized as ITAM.
+At position 4 to 332, the domain is characterized as HORMA.
+At position 233 to 337, the domain is characterized as HD.
+At position 18 to 136, the domain is characterized as Arf-GAP.
+At position 709 to 802, the domain is characterized as FDX-ACB.
+At position 160 to 348, the domain is characterized as OBG-type G.
+At position 101 to 348, the domain is characterized as Radical SAM core.
+At position 46 to 222, the domain is characterized as PCI.
+At position 1 to 95, the domain is characterized as Pyrin.
+At position 129 to 201, the domain is characterized as FISNA.
+At position 211 to 528, the domain is characterized as NACHT.
+At position 144 to 407, the domain is characterized as NR LBD.
+At position 32 to 90, the domain is characterized as VWFC.
+At position 1253 to 1487, the domain is characterized as Fibrillar collagen NC1.
+At position 162 to 475, the domain is characterized as IF rod.
+At position 45 to 231, the domain is characterized as tr-type G.
+At position 90 to 233, the domain is characterized as Clp R.
+At position 25 to 63, the domain is characterized as WAP; atypical.
+At position 33 to 356, the domain is characterized as G-alpha.
+At position 15 to 139, the domain is characterized as Toprim.
+At position 128 to 221, the domain is characterized as Rhodanese.
+At position 89 to 173, the domain is characterized as Thioredoxin.
+At position 317 to 498, the domain is characterized as PCI.
+At position 34 to 420, the domain is characterized as FERM.
+At position 439 to 544, the domain is characterized as SH2.
+At position 583 to 855, the domain is characterized as Protein kinase 1.
+At position 48 to 329, the domain is characterized as ABC transmembrane type-1.
+At position 360 to 595, the domain is characterized as ABC transporter.
+At position 43 to 440, the domain is characterized as Glutamine amidotransferase type-2.
+At position 165 to 355, the domain is characterized as CheB-type methylesterase.
+At position 133 to 285, the domain is characterized as Helicase ATP-binding.
+At position 317 to 463, the domain is characterized as Helicase C-terminal.
+At position 64 to 160, the domain is characterized as PA.
+At position 504 to 703, the domain is characterized as Helicase ATP-binding.
+At position 1003 to 1198, the domain is characterized as Helicase C-terminal.
+At position 145 to 191, the domain is characterized as F-box.
+At position 11 to 83, the domain is characterized as Sm.
+At position 106 to 517, the domain is characterized as PPM-type phosphatase.
+At position 4 to 73, the domain is characterized as J.
+At position 29 to 200, the domain is characterized as NAC.
+At position 260 to 335, the domain is characterized as PUA.
+At position 1 to 240, the domain is characterized as Protein kinase.
+At position 421 to 592, the domain is characterized as tr-type G.
+At position 1258 to 1492, the domain is characterized as Fibrillar collagen NC1.
+At position 35 to 129, the domain is characterized as PpiC.
+At position 38 to 273, the domain is characterized as AB hydrolase-1.
+At position 1260 to 1790, the domain is characterized as FAT.
+At position 1964 to 2279, the domain is characterized as PI3K/PI4K catalytic.
+At position 2348 to 2380, the domain is characterized as FATC.
+At position 269 to 396, the domain is characterized as Ricin B-type lectin 1.
+At position 400 to 520, the domain is characterized as Ricin B-type lectin 2.
+At position 649 to 698, the domain is characterized as PAP-associated 1.
+At position 1201 to 1254, the domain is characterized as PAP-associated 2.
+At position 1 to 58, the domain is characterized as HTH myb-type 1.
+At position 59 to 108, the domain is characterized as HTH myb-type 2.
+At position 5 to 273, the domain is characterized as YjeF C-terminal.
+At position 1724 to 1759, the domain is characterized as EF-hand.
+At position 38 to 288, the domain is characterized as PPM-type phosphatase.
+At position 933 to 1009, the domain is characterized as BRCT.
+At position 97 to 333, the domain is characterized as Radical SAM core.
+At position 107 to 210, the domain is characterized as PH.
+At position 290 to 351, the domain is characterized as SH3.
+At position 27 to 369, the domain is characterized as GH18.
+At position 96 to 160, the domain is characterized as S4 RNA-binding.
+At position 82 to 136, the domain is characterized as HTH cro/C1-type.
+At position 186 to 284, the domain is characterized as Cyclin N-terminal.
+At position 167 to 225, the domain is characterized as CBS.
+At position 738 to 880, the domain is characterized as Peptidase S59.
+At position 21 to 99, the domain is characterized as GIY-YIG.
+At position 151 to 396, the domain is characterized as Protein kinase.
+At position 99 to 410, the domain is characterized as IF rod.
+At position 177 to 346, the domain is characterized as PCI.
+At position 311 to 546, the domain is characterized as NR LBD.
+At position 213 to 414, the domain is characterized as Peptidase M12B.
+At position 421 to 508, the domain is characterized as Disintegrin.
+At position 657 to 685, the domain is characterized as EGF-like.
+At position 38 to 178, the domain is characterized as SLD.
+At position 65 to 245, the domain is characterized as FAD-binding PCMH-type.
+At position 55 to 108, the domain is characterized as bHLH.
+At position 1 to 80, the domain is characterized as MIB/HERC2 1.
+At position 149 to 227, the domain is characterized as MIB/HERC2 2.
+At position 12 to 207, the domain is characterized as B30.2/SPRY.
+At position 155 to 260, the domain is characterized as HIT.
+At position 92 to 158, the domain is characterized as S4 RNA-binding.
+At position 84 to 119, the domain is characterized as EF-hand 2.
+At position 167 to 202, the domain is characterized as EF-hand 4.
+At position 145 to 203, the domain is characterized as Sushi 3.
+At position 206 to 264, the domain is characterized as Sushi 4.
+At position 273 to 329, the domain is characterized as Sushi 5.
+At position 167 to 518, the domain is characterized as SAC.
+At position 593 to 760, the domain is characterized as hSac2.
+At position 63 to 339, the domain is characterized as Protein kinase.
+At position 90 to 162, the domain is characterized as MBD.
+At position 47 to 386, the domain is characterized as PORR.
+At position 561 to 730, the domain is characterized as C2 DOCK-type.
+At position 1633 to 2067, the domain is characterized as DOCKER.
+At position 273 to 457, the domain is characterized as DH.
+At position 489 to 601, the domain is characterized as PH.
+At position 612 to 673, the domain is characterized as SH3.
+At position 8 to 91, the domain is characterized as Toprim.
+At position 130 to 319, the domain is characterized as NR LBD.
+At position 299 to 373, the domain is characterized as HTH OST-type 3.
+At position 529 to 588, the domain is characterized as Tudor.
+At position 153 to 247, the domain is characterized as Rhodanese.
+At position 428 to 547, the domain is characterized as PH.
+At position 589 to 845, the domain is characterized as Protein kinase.
+At position 21 to 324, the domain is characterized as GH10.
+At position 824 to 860, the domain is characterized as CBM1.
+At position 138 to 210, the domain is characterized as HTH crp-type.
+At position 70 to 201, the domain is characterized as AB hydrolase-1.
+At position 2 to 162, the domain is characterized as DHFR.
+At position 1 to 491, the domain is characterized as SMP-LTD.
+At position 3 to 32, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 36 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 108 to 390, the domain is characterized as PPM-type phosphatase.
+At position 152 to 261, the domain is characterized as FAD-binding FR-type.
+At position 118 to 170, the domain is characterized as bHLH.
+At position 692 to 721, the domain is characterized as IQ.
+At position 100 to 152, the domain is characterized as SANT.
+At position 401 to 487, the domain is characterized as SWIRM.
+At position 279 to 406, the domain is characterized as Guanylate cyclase 1.
+At position 879 to 1023, the domain is characterized as Guanylate cyclase 2.
+At position 58 to 124, the domain is characterized as HMA 1.
+At position 143 to 209, the domain is characterized as HMA 2.
+At position 257 to 323, the domain is characterized as HMA 3.
+At position 359 to 425, the domain is characterized as HMA 4.
+At position 488 to 554, the domain is characterized as HMA 5.
+At position 564 to 630, the domain is characterized as HMA 6.
+At position 335 to 571, the domain is characterized as TLDc.
+At position 187 to 287, the domain is characterized as BEN.
+At position 725 to 802, the domain is characterized as KHA.
+At position 25 to 352, the domain is characterized as uDENN.
+At position 373 to 514, the domain is characterized as cDENN.
+At position 516 to 678, the domain is characterized as dDENN.
+At position 1490 to 1565, the domain is characterized as Death.
+At position 73 to 267, the domain is characterized as Macro.
+At position 116 to 628, the domain is characterized as Peptidase S8.
+At position 384 to 477, the domain is characterized as PA.
+At position 533 to 833, the domain is characterized as Protein kinase.
+At position 891 to 1021, the domain is characterized as Guanylate cyclase.
+At position 274 to 380, the domain is characterized as BEN.
+At position 243 to 412, the domain is characterized as PCI.
+At position 7 to 285, the domain is characterized as Helicase ATP-binding.
+At position 12 to 136, the domain is characterized as RWD.
+At position 29 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 186 to 260, the domain is characterized as Toprim.
+At position 7 to 69, the domain is characterized as SpoVT-AbrB 1.
+At position 98 to 141, the domain is characterized as SpoVT-AbrB 2.
+At position 262 to 487, the domain is characterized as Ku.
+At position 31 to 514, the domain is characterized as Sema.
+At position 576 to 665, the domain is characterized as Ig-like C2-type.
+At position 301 to 329, the domain is characterized as NAF.
+At position 1 to 368, the domain is characterized as PTS EIIC type-1.
+At position 34 to 61, the domain is characterized as LRRNT.
+At position 215 to 265, the domain is characterized as LRRCT 1.
+At position 271 to 307, the domain is characterized as LRRNT 2.
+At position 437 to 487, the domain is characterized as LRRCT 2.
+At position 496 to 532, the domain is characterized as LRRNT 3.
+At position 663 to 713, the domain is characterized as LRRCT 3.
+At position 716 to 752, the domain is characterized as LRRNT 4.
+At position 857 to 907, the domain is characterized as LRRCT 4.
+At position 918 to 953, the domain is characterized as EGF-like 1.
+At position 955 to 994, the domain is characterized as EGF-like 2.
+At position 996 to 1032, the domain is characterized as EGF-like 3.
+At position 1034 to 1072, the domain is characterized as EGF-like 4.
+At position 1074 to 1110, the domain is characterized as EGF-like 5.
+At position 1119 to 1155, the domain is characterized as EGF-like 6.
+At position 1158 to 1332, the domain is characterized as Laminin G-like.
+At position 1340 to 1365, the domain is characterized as EGF-like 7.
+At position 1368 to 1403, the domain is characterized as EGF-like 8.
+At position 1408 to 1444, the domain is characterized as EGF-like 9.
+At position 1449 to 1523, the domain is characterized as CTCK.
+At position 224 to 486, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 21 to 107, the domain is characterized as Core-binding (CB).
+At position 122 to 306, the domain is characterized as Tyr recombinase.
+At position 83 to 303, the domain is characterized as Radical SAM core.
+At position 43 to 154, the domain is characterized as sHSP.
+At position 266 to 444, the domain is characterized as TR mART core.
+At position 459 to 510, the domain is characterized as Collagen-like.
+At position 240 to 327, the domain is characterized as PKD.
+At position 14 to 46, the domain is characterized as LisH.
+At position 297 to 432, the domain is characterized as Fido.
+At position 1 to 73, the domain is characterized as KIND.
+At position 147 to 165, the domain is characterized as WH2 1.
+At position 211 to 228, the domain is characterized as WH2 2.
+At position 247 to 433, the domain is characterized as GATase cobBQ-type.
+At position 676 to 962, the domain is characterized as Protein kinase.
+At position 64 to 169, the domain is characterized as Expansin-like EG45.
+At position 179 to 258, the domain is characterized as Expansin-like CBD.
+At position 118 to 354, the domain is characterized as ATP-grasp.
+At position 883 to 976, the domain is characterized as BRCT 1.
+At position 1067 to 1174, the domain is characterized as BRCT 2.
+At position 163 to 298, the domain is characterized as Thioredoxin.
+At position 9 to 249, the domain is characterized as Protein kinase 1.
+At position 299 to 585, the domain is characterized as Protein kinase 2.
+At position 53 to 302, the domain is characterized as Peptidase S6.
+At position 1111 to 1377, the domain is characterized as Autotransporter.
+At position 26 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 510 to 800, the domain is characterized as UvrD-like helicase C-terminal.
+At position 241 to 436, the domain is characterized as Helicase ATP-binding.
+At position 460 to 606, the domain is characterized as Helicase C-terminal.
+At position 48 to 353, the domain is characterized as HAP1 N-terminal.
+At position 3 to 190, the domain is characterized as Prephenate dehydratase.
+At position 204 to 281, the domain is characterized as ACT.
+At position 9 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 110 to 205, the domain is characterized as Fibronectin type-III 1.
+At position 206 to 294, the domain is characterized as Fibronectin type-III 2.
+At position 566 to 666, the domain is characterized as Fibronectin type-III 3.
+At position 942 to 1037, the domain is characterized as Fibronectin type-III 4.
+At position 1038 to 1145, the domain is characterized as Fibronectin type-III 5.
+At position 1440 to 1548, the domain is characterized as Fibronectin type-III 6.
+At position 1549 to 1648, the domain is characterized as Fibronectin type-III 7.
+At position 1650 to 1743, the domain is characterized as Fibronectin type-III 8.
+At position 1744 to 1845, the domain is characterized as Fibronectin type-III 9.
+At position 1937 to 2210, the domain is characterized as Protein kinase.
+At position 159 to 435, the domain is characterized as Protein kinase.
+At position 76 to 322, the domain is characterized as ATP-grasp.
+At position 642 to 910, the domain is characterized as Autotransporter.
+At position 115 to 336, the domain is characterized as Radical SAM core.
+At position 250 to 449, the domain is characterized as Helicase ATP-binding.
+At position 515 to 668, the domain is characterized as Helicase C-terminal.
+At position 247 to 469, the domain is characterized as Helicase C-terminal.
+At position 1 to 30, the domain is characterized as Peptidase S1.
+At position 39 to 308, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 314 to 559, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 7 to 101, the domain is characterized as Sm.
+At position 179 to 287, the domain is characterized as Fe2OG dioxygenase.
+At position 2 to 168, the domain is characterized as Obg.
+At position 169 to 349, the domain is characterized as OBG-type G.
+At position 383 to 469, the domain is characterized as OCT.
+At position 66 to 260, the domain is characterized as Peptidase M12A.
+At position 264 to 433, the domain is characterized as MAM.
+At position 434 to 593, the domain is characterized as MATH.
+At position 670 to 710, the domain is characterized as EGF-like.
+At position 1 to 144, the domain is characterized as C2 1.
+At position 162 to 299, the domain is characterized as C2 2.
+At position 342 to 561, the domain is characterized as VWFA.
+At position 25 to 297, the domain is characterized as PPM-type phosphatase.
+At position 28 to 76, the domain is characterized as F-box.
+At position 149 to 246, the domain is characterized as HTH araC/xylS-type.
+At position 255 to 394, the domain is characterized as Flavodoxin-like.
+At position 241 to 405, the domain is characterized as Helicase C-terminal.
+At position 7 to 237, the domain is characterized as ThyX.
+At position 37 to 91, the domain is characterized as HTH cro/C1-type.
+At position 112 to 402, the domain is characterized as ABC transmembrane type-1 1.
+At position 437 to 682, the domain is characterized as ABC transporter 1.
+At position 780 to 1069, the domain is characterized as ABC transmembrane type-1 2.
+At position 1104 to 1342, the domain is characterized as ABC transporter 2.
+At position 522 to 634, the domain is characterized as SMC hinge.
+At position 2 to 119, the domain is characterized as Thioredoxin.
+At position 149 to 259, the domain is characterized as Fibronectin type-III.
+At position 31 to 126, the domain is characterized as EthD.
+At position 84 to 243, the domain is characterized as CRAL-TRIO.
+At position 303 to 574, the domain is characterized as Tyrosine-protein phosphatase.
+At position 41 to 118, the domain is characterized as Inhibitor I9.
+At position 124 to 608, the domain is characterized as Peptidase S8.
+At position 26 to 91, the domain is characterized as UPAR/Ly6.
+At position 1 to 113, the domain is characterized as WH1.
+At position 14 to 146, the domain is characterized as HTH marR-type.
+At position 612 to 689, the domain is characterized as BRCT.
+At position 478 to 635, the domain is characterized as CBM3.
+At position 2 to 197, the domain is characterized as DPCK.
+At position 87 to 391, the domain is characterized as Peptidase A1.
+At position 7 to 73, the domain is characterized as Ubiquitin-like.
+At position 930 to 1004, the domain is characterized as U-box.
+At position 181 to 427, the domain is characterized as NR LBD.
+At position 1 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 11 to 69, the domain is characterized as TRAM.
+At position 13 to 118, the domain is characterized as PAS 1.
+At position 151 to 305, the domain is characterized as GAF.
+At position 515 to 590, the domain is characterized as PAS 2.
+At position 34 to 261, the domain is characterized as TLC.
+At position 13 to 253, the domain is characterized as ABC transporter.
+At position 2 to 222, the domain is characterized as Glutamine amidotransferase type-2.
+At position 293 to 441, the domain is characterized as SIS 1.
+At position 471 to 616, the domain is characterized as SIS 2.
+At position 52 to 341, the domain is characterized as FAE.
+At position 101 to 583, the domain is characterized as Peptidase S8.
+At position 2 to 178, the domain is characterized as PRELI/MSF1.
+At position 297 to 474, the domain is characterized as CRAL-TRIO.
+At position 537 to 684, the domain is characterized as GOLD.
+At position 28 to 316, the domain is characterized as ABC transmembrane type-1.
+At position 350 to 581, the domain is characterized as ABC transporter.
+At position 213 to 347, the domain is characterized as Fe2OG dioxygenase.
+At position 38 to 100, the domain is characterized as TGS.
+At position 99 to 296, the domain is characterized as ATP-grasp.
+At position 14 to 222, the domain is characterized as AIG1-type G.
+At position 107 to 182, the domain is characterized as Smr.
+At position 54 to 89, the domain is characterized as Tify.
+At position 265 to 332, the domain is characterized as ACT.
+At position 5 to 101, the domain is characterized as Rieske.
+At position 20 to 109, the domain is characterized as Ig-like.
+At position 82 to 239, the domain is characterized as CRAL-TRIO.
+At position 327 to 445, the domain is characterized as MSP.
+At position 225 to 252, the domain is characterized as PLD phosphodiesterase 1.
+At position 403 to 430, the domain is characterized as PLD phosphodiesterase 2.
+At position 2 to 354, the domain is characterized as SPX.
+At position 608 to 799, the domain is characterized as EXS.
+At position 4 to 270, the domain is characterized as CN hydrolase.
+At position 55 to 107, the domain is characterized as bHLH.
+At position 596 to 674, the domain is characterized as Carrier.
+At position 35 to 343, the domain is characterized as GH18.
+At position 383 to 419, the domain is characterized as CBM1.
+At position 1 to 424, the domain is characterized as PTS EIIC type-1.
+At position 439 to 520, the domain is characterized as PTS EIIB type-1.
+At position 568 to 672, the domain is characterized as PTS EIIA type-1.
+At position 21 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 212 to 410, the domain is characterized as GMPS ATP-PPase.
+At position 163 to 333, the domain is characterized as Helicase ATP-binding.
+At position 478 to 642, the domain is characterized as Helicase C-terminal.
+At position 277 to 561, the domain is characterized as Protein kinase.
+At position 156 to 318, the domain is characterized as TRUD.
+At position 145 to 197, the domain is characterized as HTH psq-type 1.
+At position 334 to 386, the domain is characterized as HTH psq-type 2.
+At position 3 to 96, the domain is characterized as PTS EIIB type-2.
+At position 4 to 79, the domain is characterized as GIY-YIG.
+At position 78 to 388, the domain is characterized as AB hydrolase-1.
+At position 227 to 458, the domain is characterized as NR LBD.
+At position 211 to 464, the domain is characterized as ABC transporter.
+At position 540 to 793, the domain is characterized as ABC transmembrane type-2.
+At position 188 to 501, the domain is characterized as PPM-type phosphatase.
+At position 48 to 294, the domain is characterized as Radical SAM core.
+At position 412 to 529, the domain is characterized as SET.
+At position 84 to 208, the domain is characterized as GST C-terminal.
+At position 3 to 108, the domain is characterized as STAS.
+At position 36 to 260, the domain is characterized as AIG1-type G.
+At position 52 to 321, the domain is characterized as GB1/RHD3-type G.
+At position 7 to 39, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 46 to 75, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 70 to 320, the domain is characterized as ABC transporter 1.
+At position 345 to 568, the domain is characterized as ABC transporter 2.
+At position 154 to 304, the domain is characterized as GAF 1.
+At position 336 to 493, the domain is characterized as GAF 2.
+At position 526 to 850, the domain is characterized as PDEase.
+At position 68 to 97, the domain is characterized as IQ 1.
+At position 124 to 153, the domain is characterized as IQ 2.
+At position 176 to 232, the domain is characterized as CBS 1.
+At position 236 to 292, the domain is characterized as CBS 2.
+At position 30 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 561 to 727, the domain is characterized as C2 DOCK-type.
+At position 1678 to 2114, the domain is characterized as DOCKER.
+At position 119 to 298, the domain is characterized as SMP-LTD.
+At position 297 to 417, the domain is characterized as C2 1.
+At position 442 to 588, the domain is characterized as C2 2.
+At position 737 to 859, the domain is characterized as C2 3.
+At position 14 to 203, the domain is characterized as RNase H type-2.
+At position 178 to 245, the domain is characterized as R3H.
+At position 27 to 191, the domain is characterized as FAD-binding PCMH-type.
+At position 31 to 90, the domain is characterized as KID.
+At position 212 to 270, the domain is characterized as bZIP.
+At position 248 to 434, the domain is characterized as DH.
+At position 480 to 588, the domain is characterized as PH.
+At position 637 to 792, the domain is characterized as N-terminal Ras-GEF.
+At position 829 to 1066, the domain is characterized as Ras-GEF.
+At position 87 to 215, the domain is characterized as GST C-terminal.
+At position 256 to 416, the domain is characterized as EF-1-gamma C-terminal.
+At position 52 to 405, the domain is characterized as FH2.
+At position 8 to 121, the domain is characterized as NTF2.
+At position 14 to 130, the domain is characterized as I-type lysozyme.
+At position 61 to 209, the domain is characterized as Cupin type-1.
+At position 2 to 150, the domain is characterized as UBC core.
+At position 106 to 170, the domain is characterized as S4 RNA-binding.
+At position 333 to 507, the domain is characterized as Helicase ATP-binding.
+At position 537 to 714, the domain is characterized as Helicase C-terminal.
+At position 5 to 64, the domain is characterized as TRAM.
+At position 5 to 48, the domain is characterized as LEM-like.
+At position 109 to 153, the domain is characterized as LEM.
+At position 289 to 386, the domain is characterized as PH.
+At position 196 to 529, the domain is characterized as Peptidase S8.
+At position 535 to 662, the domain is characterized as P/Homo B.
+At position 2 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 445 to 614, the domain is characterized as tr-type G.
+At position 178 to 499, the domain is characterized as DOT1.
+At position 2 to 240, the domain is characterized as PPM-type phosphatase.
+At position 172 to 491, the domain is characterized as NACHT.
+At position 547 to 651, the domain is characterized as PTS EIIA type-1.
+At position 2 to 71, the domain is characterized as J.
+At position 210 to 226, the domain is characterized as UIM 1.
+At position 250 to 269, the domain is characterized as UIM 2.
+At position 257 to 320, the domain is characterized as Tudor 1.
+At position 347 to 403, the domain is characterized as Tudor 2.
+At position 594 to 665, the domain is characterized as MBD.
+At position 727 to 800, the domain is characterized as Pre-SET.
+At position 803 to 1266, the domain is characterized as SET.
+At position 1275 to 1291, the domain is characterized as Post-SET.
+At position 1 to 127, the domain is characterized as Jacalin-type lectin 1.
+At position 252 to 395, the domain is characterized as Jacalin-type lectin 2.
+At position 406 to 548, the domain is characterized as Jacalin-type lectin 3.
+At position 560 to 702, the domain is characterized as Jacalin-type lectin 4.
+At position 55 to 160, the domain is characterized as SUEL-type lectin.
+At position 145 to 189, the domain is characterized as LysM.
+At position 43 to 256, the domain is characterized as ThyX.
+At position 588 to 665, the domain is characterized as BRCT.
+At position 25 to 316, the domain is characterized as Protein kinase.
+At position 11 to 205, the domain is characterized as tr-type G.
+At position 251 to 409, the domain is characterized as EF-1-gamma C-terminal.
+At position 294 to 633, the domain is characterized as Kinesin motor.
+At position 909 to 1180, the domain is characterized as Tyrosine-protein phosphatase.
+At position 25 to 172, the domain is characterized as Nudix hydrolase.
+At position 331 to 575, the domain is characterized as Clu.
+At position 8 to 151, the domain is characterized as Nudix hydrolase.
+At position 104 to 284, the domain is characterized as Prephenate dehydratase.
+At position 558 to 617, the domain is characterized as KH.
+At position 627 to 695, the domain is characterized as S1 motif.
+At position 28 to 98, the domain is characterized as Chitin-binding type R&R.
+At position 20 to 167, the domain is characterized as CENP-V/GFA.
+At position 143 to 309, the domain is characterized as JmjC.
+At position 20 to 281, the domain is characterized as PPM-type phosphatase.
+At position 1025 to 1088, the domain is characterized as Pre-SET.
+At position 1091 to 1208, the domain is characterized as SET.
+At position 1217 to 1233, the domain is characterized as Post-SET.
+At position 29 to 106, the domain is characterized as GIY-YIG.
+At position 167 to 354, the domain is characterized as TRUD.
+At position 47 to 253, the domain is characterized as ABC transmembrane type-1.
+At position 117 to 325, the domain is characterized as ATP-grasp.
+At position 73 to 140, the domain is characterized as BTB.
+At position 175 to 277, the domain is characterized as BACK.
+At position 964 to 1127, the domain is characterized as MGS-like.
+At position 2 to 71, the domain is characterized as RRM.
+At position 11 to 107, the domain is characterized as C-type lectin.
+At position 4 to 260, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 267 to 503, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 142 to 364, the domain is characterized as Radical SAM core.
+At position 323 to 399, the domain is characterized as DEP.
+At position 1473 to 1796, the domain is characterized as PIPK.
+At position 260 to 506, the domain is characterized as ABC transporter 2.
+At position 427 to 510, the domain is characterized as PUA.
+At position 63 to 252, the domain is characterized as HD.
+At position 80 to 177, the domain is characterized as SWIRM.
+At position 310 to 362, the domain is characterized as SANT.
+At position 53 to 147, the domain is characterized as B12-binding N-terminal.
+At position 145 to 272, the domain is characterized as B12-binding.
+At position 27 to 261, the domain is characterized as NR LBD.
+At position 37 to 228, the domain is characterized as AB hydrolase-1.
+At position 215 to 427, the domain is characterized as SMP-LTD.
+At position 45 to 344, the domain is characterized as Calpain catalytic.
+At position 531 to 566, the domain is characterized as EF-hand 1.
+At position 575 to 610, the domain is characterized as EF-hand 2.
+At position 605 to 640, the domain is characterized as EF-hand 3.
+At position 670 to 703, the domain is characterized as EF-hand 4.
+At position 311 to 362, the domain is characterized as LRRCT.
+At position 9 to 191, the domain is characterized as UmuC.
+At position 27 to 162, the domain is characterized as MPN.
+At position 24 to 284, the domain is characterized as Protein kinase.
+At position 396 to 488, the domain is characterized as SH2.
+At position 435 to 567, the domain is characterized as Thioredoxin.
+At position 290 to 367, the domain is characterized as IPT/TIG.
+At position 333 to 538, the domain is characterized as MCM.
+At position 76 to 264, the domain is characterized as RNase H type-2.
+At position 72 to 284, the domain is characterized as TLC.
+At position 1714 to 1896, the domain is characterized as VWFA.
+At position 20 to 141, the domain is characterized as C-type lysozyme.
+At position 33 to 197, the domain is characterized as Helicase ATP-binding.
+At position 226 to 422, the domain is characterized as Helicase C-terminal.
+At position 33 to 134, the domain is characterized as BTB.
+At position 19 to 123, the domain is characterized as Ig-like V-type.
+At position 49 to 169, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 188 to 294, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 206 to 323, the domain is characterized as C2 2.
+At position 362 to 498, the domain is characterized as C2 3.
+At position 1146 to 1272, the domain is characterized as C2 4.
+At position 1320 to 1448, the domain is characterized as C2 5.
+At position 1571 to 1689, the domain is characterized as C2 6.
+At position 1805 to 1953, the domain is characterized as C2 7.
+At position 19 to 304, the domain is characterized as ABC transmembrane type-1.
+At position 337 to 572, the domain is characterized as ABC transporter.
+At position 125 to 320, the domain is characterized as ATP-grasp.
+At position 981 to 1246, the domain is characterized as Protein kinase.
+At position 1279 to 1444, the domain is characterized as KEN.
+At position 67 to 356, the domain is characterized as Protein kinase.
+At position 27 to 162, the domain is characterized as RanBD1.
+At position 341 to 397, the domain is characterized as S4 RNA-binding.
+At position 49 to 230, the domain is characterized as BPL/LPL catalytic.
+At position 415 to 581, the domain is characterized as Helicase ATP-binding.
+At position 717 to 884, the domain is characterized as Helicase C-terminal.
+At position 110 to 185, the domain is characterized as MIT.
+At position 198 to 304, the domain is characterized as Fe2OG dioxygenase.
+At position 162 to 189, the domain is characterized as PLD phosphodiesterase 1.
+At position 396 to 423, the domain is characterized as PLD phosphodiesterase 2.
+At position 111 to 254, the domain is characterized as N-acetyltransferase.
+At position 234 to 299, the domain is characterized as LIM zinc-binding 1.
+At position 300 to 359, the domain is characterized as LIM zinc-binding 2.
+At position 360 to 422, the domain is characterized as LIM zinc-binding 3.
+At position 77 to 122, the domain is characterized as LysM.
+At position 252 to 443, the domain is characterized as PCI.
+At position 6 to 144, the domain is characterized as SprT-like.
+At position 1284 to 1517, the domain is characterized as ABC transporter 2.
+At position 62 to 219, the domain is characterized as CP-type G.
+At position 45 to 479, the domain is characterized as GRAS.
+At position 62 to 262, the domain is characterized as TLC.
+At position 151 to 290, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 32 to 722, the domain is characterized as Peptidase M13.
+At position 41 to 171, the domain is characterized as C-type lectin.
+At position 43 to 128, the domain is characterized as Cytochrome b5 heme-binding.
+At position 6 to 85, the domain is characterized as GST N-terminal.
+At position 91 to 217, the domain is characterized as GST C-terminal.
+At position 755 to 1034, the domain is characterized as Autotransporter.
+At position 310 to 592, the domain is characterized as ABC transmembrane type-1 1.
+At position 625 to 849, the domain is characterized as ABC transporter 1.
+At position 966 to 1247, the domain is characterized as ABC transmembrane type-1 2.
+At position 1286 to 1518, the domain is characterized as ABC transporter 2.
+At position 261 to 468, the domain is characterized as Ku.
+At position 573 to 607, the domain is characterized as SAP.
+At position 95 to 161, the domain is characterized as S4 RNA-binding.
+At position 2 to 159, the domain is characterized as PCI.
+At position 43 to 75, the domain is characterized as EF-hand 2.
+At position 51 to 120, the domain is characterized as BTB.
+At position 159 to 259, the domain is characterized as BACK.
+At position 446 to 496, the domain is characterized as DHHC.
+At position 5 to 176, the domain is characterized as Era-type G.
+At position 207 to 286, the domain is characterized as KH type-2.
+At position 490 to 754, the domain is characterized as Protein kinase.
+At position 774 to 845, the domain is characterized as U-box.
+At position 10 to 131, the domain is characterized as MPN.
+At position 193 to 409, the domain is characterized as Helicase ATP-binding.
+At position 443 to 603, the domain is characterized as Helicase C-terminal.
+At position 19 to 331, the domain is characterized as GH18.
+At position 3 to 62, the domain is characterized as AFP-like.
+At position 8 to 76, the domain is characterized as HTH gntR-type.
+At position 31 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 32 to 385, the domain is characterized as G-alpha.
+At position 623 to 711, the domain is characterized as BRCT.
+At position 53 to 286, the domain is characterized as Radical SAM core.
+At position 410 to 458, the domain is characterized as LysM.
+At position 609 to 688, the domain is characterized as BRCT.
+At position 517 to 640, the domain is characterized as STAS.
+At position 163 to 407, the domain is characterized as NR LBD.
+At position 30 to 105, the domain is characterized as TFIIS N-terminal.
+At position 592 to 636, the domain is characterized as F-box.
+At position 758 to 841, the domain is characterized as BRCT.
+At position 10 to 215, the domain is characterized as tr-type G.
+At position 19 to 84, the domain is characterized as LCN-type CS-alpha/beta.
+At position 414 to 704, the domain is characterized as Protein kinase.
+At position 707 to 838, the domain is characterized as KEN.
+At position 65 to 183, the domain is characterized as Response regulatory.
+At position 442 to 484, the domain is characterized as CCT.
+At position 27 to 139, the domain is characterized as sHSP.
+At position 167 to 253, the domain is characterized as PPIase FKBP-type.
+At position 141 to 414, the domain is characterized as Septin-type G.
+At position 223 to 301, the domain is characterized as RRM.
+At position 53 to 406, the domain is characterized as IF rod.
+At position 459 to 575, the domain is characterized as LTD.
+At position 290 to 523, the domain is characterized as Glutamine amidotransferase type-1.
+At position 55 to 206, the domain is characterized as N-acetyltransferase.
+At position 69 to 115, the domain is characterized as G-patch.
+At position 144 to 204, the domain is characterized as TSP type-1.
+At position 317 to 478, the domain is characterized as 3'-5' exonuclease.
+At position 44 to 78, the domain is characterized as SAP.
+At position 163 to 215, the domain is characterized as bHLH.
+At position 437 to 781, the domain is characterized as Kinesin motor.
+At position 2 to 325, the domain is characterized as Hcy-binding.
+At position 356 to 617, the domain is characterized as Pterin-binding.
+At position 650 to 744, the domain is characterized as B12-binding N-terminal.
+At position 746 to 881, the domain is characterized as B12-binding.
+At position 897 to 1227, the domain is characterized as AdoMet activation.
+At position 55 to 114, the domain is characterized as SH3 1.
+At position 317 to 454, the domain is characterized as ZU5.
+At position 654 to 724, the domain is characterized as SH3 2.
+At position 71 to 184, the domain is characterized as SSB.
+At position 228 to 394, the domain is characterized as TrmE-type G.
+At position 17 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 32 to 356, the domain is characterized as SAM-dependent MTase C5-type.
+At position 182 to 272, the domain is characterized as SWIRM.
+At position 291 to 473, the domain is characterized as VWFA.
+At position 487 to 580, the domain is characterized as Cache.
+At position 54 to 308, the domain is characterized as ABC transporter.
+At position 67 to 185, the domain is characterized as MTTase N-terminal.
+At position 208 to 438, the domain is characterized as Radical SAM core.
+At position 441 to 504, the domain is characterized as TRAM.
+At position 756 to 814, the domain is characterized as SH3.
+At position 3 to 109, the domain is characterized as STAS.
+At position 29 to 292, the domain is characterized as Brix.
+At position 306 to 336, the domain is characterized as LRRCT.
+At position 5 to 169, the domain is characterized as Thioredoxin.
+At position 217 to 386, the domain is characterized as tr-type G.
+At position 42 to 127, the domain is characterized as ACB.
+At position 207 to 395, the domain is characterized as Glutamine amidotransferase type-1.
+At position 497 to 592, the domain is characterized as MRH.
+At position 32 to 239, the domain is characterized as GH11.
+At position 258 to 404, the domain is characterized as CBM-cenC.
+At position 434 to 513, the domain is characterized as Dockerin.
+At position 556 to 792, the domain is characterized as GH16.
+At position 3 to 153, the domain is characterized as PPIase cyclophilin-type.
+At position 601 to 702, the domain is characterized as tRNA-binding.
+At position 16 to 209, the domain is characterized as Lon N-terminal.
+At position 598 to 779, the domain is characterized as Lon proteolytic.
+At position 58 to 257, the domain is characterized as TNase-like.
+At position 99 to 149, the domain is characterized as DHHC.
+At position 313 to 398, the domain is characterized as SH3.
+At position 488 to 549, the domain is characterized as SH3.
+At position 561 to 700, the domain is characterized as PID.
+At position 556 to 656, the domain is characterized as tRNA-binding.
+At position 4 to 224, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 112, the domain is characterized as Longin.
+At position 127 to 187, the domain is characterized as v-SNARE coiled-coil homology.
+At position 40 to 217, the domain is characterized as Helicase ATP-binding.
+At position 241 to 388, the domain is characterized as Helicase C-terminal.
+At position 24 to 115, the domain is characterized as ABM.
+At position 133 to 202, the domain is characterized as COMM.
+At position 104 to 163, the domain is characterized as KID.
+At position 302 to 360, the domain is characterized as bZIP.
+At position 17 to 164, the domain is characterized as Thioredoxin.
+At position 87 to 182, the domain is characterized as POU-specific atypical.
+At position 14 to 191, the domain is characterized as Cyclin N-terminal.
+At position 570 to 670, the domain is characterized as tRNA-binding.
+At position 72 to 116, the domain is characterized as LysM.
+At position 19 to 252, the domain is characterized as ABC transporter.
+At position 225 to 346, the domain is characterized as Nop.
+At position 1687 to 1782, the domain is characterized as RAMA.
+At position 34 to 141, the domain is characterized as Ig-like V-type.
+At position 148 to 234, the domain is characterized as Ig-like C2-type.
+At position 301 to 524, the domain is characterized as TLDc.
+At position 62 to 198, the domain is characterized as HD.
+At position 4 to 161, the domain is characterized as Obg.
+At position 162 to 327, the domain is characterized as OBG-type G.
+At position 343 to 421, the domain is characterized as OCT.
+At position 117 to 195, the domain is characterized as RRM.
+At position 598 to 711, the domain is characterized as CNA-B 1.
+At position 712 to 822, the domain is characterized as CNA-B 2.
+At position 145 to 253, the domain is characterized as RRM.
+At position 179 to 231, the domain is characterized as KH.
+At position 165 to 251, the domain is characterized as PPIase FKBP-type 2.
+At position 68 to 353, the domain is characterized as tr-type G.
+At position 104 to 159, the domain is characterized as BSD 1.
+At position 180 to 232, the domain is characterized as BSD 2.
+At position 57 to 347, the domain is characterized as PPM-type phosphatase.
+At position 81 to 323, the domain is characterized as Peptidase S1.
+At position 32 to 186, the domain is characterized as F5/8 type C.
+At position 608 to 903, the domain is characterized as Protein kinase.
+At position 3 to 240, the domain is characterized as PABS.
+At position 11 to 212, the domain is characterized as YjeF N-terminal.
+At position 226 to 366, the domain is characterized as DM10 2.
+At position 428 to 535, the domain is characterized as DM10 3.
+At position 556 to 591, the domain is characterized as EF-hand 1.
+At position 631 to 666, the domain is characterized as EF-hand 2.
+At position 6 to 288, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 53 to 318, the domain is characterized as Protein kinase.
+At position 871 to 906, the domain is characterized as UVR.
+At position 139 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 238 to 320, the domain is characterized as Ig-like C2-type 2.
+At position 326 to 405, the domain is characterized as Ig-like C2-type 3.
+At position 411 to 507, the domain is characterized as Ig-like C2-type 4.
+At position 708 to 785, the domain is characterized as Ig-like C2-type 7.
+At position 799 to 894, the domain is characterized as Ig-like C2-type 8.
+At position 898 to 977, the domain is characterized as Ig-like C2-type 9.
+At position 984 to 1083, the domain is characterized as Ig-like C2-type 10.
+At position 1085 to 1165, the domain is characterized as Ig-like C2-type 11.
+At position 1176 to 1248, the domain is characterized as Ig-like C2-type 12.
+At position 1259 to 1341, the domain is characterized as Ig-like C2-type 13.
+At position 1350 to 1442, the domain is characterized as Ig-like C2-type 14.
+At position 1445 to 1528, the domain is characterized as Ig-like C2-type 15.
+At position 1536 to 1631, the domain is characterized as Ig-like C2-type 16.
+At position 13 to 99, the domain is characterized as Core-binding (CB).
+At position 127 to 305, the domain is characterized as Tyr recombinase.
+At position 697 to 755, the domain is characterized as bZIP.
+At position 37 to 242, the domain is characterized as BPL/LPL catalytic.
+At position 228 to 362, the domain is characterized as PADR1 zinc-binding.
+At position 387 to 478, the domain is characterized as BRCT.
+At position 544 to 640, the domain is characterized as WGR.
+At position 664 to 781, the domain is characterized as PARP alpha-helical.
+At position 790 to 1016, the domain is characterized as PARP catalytic.
+At position 381 to 814, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1302 to 1608, the domain is characterized as PKS/mFAS DH.
+At position 1671 to 1748, the domain is characterized as Carrier 1.
+At position 1775 to 1857, the domain is characterized as Carrier 2.
+At position 169 to 461, the domain is characterized as NB-ARC.
+At position 22 to 71, the domain is characterized as WAP 1.
+At position 72 to 125, the domain is characterized as WAP 2.
+At position 126 to 175, the domain is characterized as WAP 3.
+At position 283 to 340, the domain is characterized as KASH.
+At position 1313 to 1675, the domain is characterized as Protein kinase.
+At position 1 to 36, the domain is characterized as Peptidase S1.
+At position 4 to 36, the domain is characterized as ShKT.
+At position 38 to 206, the domain is characterized as Helicase ATP-binding.
+At position 213 to 367, the domain is characterized as Helicase C-terminal.
+At position 38 to 67, the domain is characterized as HhH.
+At position 230 to 427, the domain is characterized as Helicase ATP-binding.
+At position 483 to 642, the domain is characterized as Helicase C-terminal.
+At position 8 to 65, the domain is characterized as Kazal-like.
+At position 143 to 455, the domain is characterized as NB-ARC.
+At position 139 to 337, the domain is characterized as B30.2/SPRY.
+At position 30 to 63, the domain is characterized as WW 1.
+At position 71 to 104, the domain is characterized as WW 2.
+At position 191 to 245, the domain is characterized as FF 1.
+At position 257 to 313, the domain is characterized as FF 2.
+At position 326 to 385, the domain is characterized as FF 3.
+At position 403 to 465, the domain is characterized as FF 4.
+At position 470 to 521, the domain is characterized as FF 5.
+At position 544 to 601, the domain is characterized as FF 6.
+At position 89 to 231, the domain is characterized as Clp R.
+At position 506 to 541, the domain is characterized as UVR.
+At position 514 to 629, the domain is characterized as SMC hinge.
+At position 270 to 356, the domain is characterized as PpiC.
+At position 109 to 295, the domain is characterized as Tyr recombinase.
+At position 86 to 202, the domain is characterized as RGS.
+At position 777 to 931, the domain is characterized as Helicase C-terminal.
+At position 239 to 353, the domain is characterized as SEA 1.
+At position 897 to 1010, the domain is characterized as SEA 2.
+At position 1010 to 1051, the domain is characterized as EGF-like 1.
+At position 1052 to 1093, the domain is characterized as EGF-like 2.
+At position 68 to 349, the domain is characterized as tr-type G.
+At position 56 to 126, the domain is characterized as BTB.
+At position 28 to 71, the domain is characterized as CHCH.
+At position 211 to 402, the domain is characterized as Albumin 2.
+At position 403 to 601, the domain is characterized as Albumin 3.
+At position 7 to 64, the domain is characterized as HTH lysR-type.
+At position 173 to 208, the domain is characterized as QLQ.
+At position 436 to 508, the domain is characterized as HSA.
+At position 736 to 901, the domain is characterized as Helicase ATP-binding.
+At position 1054 to 1216, the domain is characterized as Helicase C-terminal.
+At position 1419 to 1489, the domain is characterized as Bromo.
+At position 10 to 367, the domain is characterized as Kinesin motor.
+At position 2 to 204, the domain is characterized as VWFA.
+At position 331 to 537, the domain is characterized as MCM.
+At position 71 to 337, the domain is characterized as Protein kinase.
+At position 338 to 408, the domain is characterized as AGC-kinase C-terminal.
+At position 947 to 1066, the domain is characterized as PH.
+At position 1092 to 1366, the domain is characterized as CNH.
+At position 1437 to 1450, the domain is characterized as CRIB.
+At position 35 to 291, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 32 to 143, the domain is characterized as HIT.
+At position 433 to 603, the domain is characterized as tr-type G.
+At position 127 to 317, the domain is characterized as Tyr recombinase.
+At position 48 to 218, the domain is characterized as MENTAL.
+At position 201 to 390, the domain is characterized as CheB-type methylesterase.
+At position 52 to 140, the domain is characterized as PPIase FKBP-type.
+At position 8 to 80, the domain is characterized as J.
+At position 509 to 622, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 623 to 736, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 809 to 887, the domain is characterized as POLO box.
+At position 346 to 425, the domain is characterized as HSA.
+At position 642 to 704, the domain is characterized as Myb-like.
+At position 29 to 147, the domain is characterized as Response regulatory.
+At position 443 to 485, the domain is characterized as CCT.
+At position 256 to 480, the domain is characterized as tr-type G.
+At position 175 to 226, the domain is characterized as F-box.
+At position 2 to 118, the domain is characterized as Thioredoxin.
+At position 14 to 268, the domain is characterized as Protein kinase.
+At position 386 to 505, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 506 to 613, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 675 to 755, the domain is characterized as POLO box.
+At position 42 to 142, the domain is characterized as Ig-like C2-type 1.
+At position 148 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 259 to 356, the domain is characterized as Fibronectin type-III 1.
+At position 358 to 453, the domain is characterized as Fibronectin type-III 2.
+At position 161 to 477, the domain is characterized as Protein kinase.
+At position 19 to 191, the domain is characterized as PITH.
+At position 374 to 437, the domain is characterized as TRAM.
+At position 172 to 248, the domain is characterized as Toprim.
+At position 198 to 272, the domain is characterized as RRM.
+At position 230 to 277, the domain is characterized as EGF-like 1.
+At position 278 to 319, the domain is characterized as EGF-like 2; calcium-binding.
+At position 404 to 677, the domain is characterized as Protein kinase.
+At position 5 to 59, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 27 to 54, the domain is characterized as LDL-receptor class A 1; truncated.
+At position 62 to 224, the domain is characterized as MAM 1.
+At position 229 to 269, the domain is characterized as LDL-receptor class A 2.
+At position 268 to 427, the domain is characterized as MAM 2.
+At position 454 to 491, the domain is characterized as LDL-receptor class A 3.
+At position 492 to 647, the domain is characterized as MAM 3.
+At position 654 to 813, the domain is characterized as MAM 4.
+At position 812 to 973, the domain is characterized as MAM 5.
+At position 972 to 1142, the domain is characterized as MAM 6.
+At position 109 to 342, the domain is characterized as Radical SAM core.
+At position 33 to 248, the domain is characterized as BPL/LPL catalytic.
+At position 72 to 291, the domain is characterized as Radical SAM core.
+At position 2250 to 2492, the domain is characterized as I/LWEQ.
+At position 5 to 92, the domain is characterized as J.
+At position 117 to 191, the domain is characterized as DPH-type MB.
+At position 1 to 71, the domain is characterized as GST N-terminal.
+At position 72 to 135, the domain is characterized as GST C-terminal.
+At position 435 to 477, the domain is characterized as Anaphylatoxin-like 1.
+At position 478 to 510, the domain is characterized as Anaphylatoxin-like 2.
+At position 511 to 543, the domain is characterized as Anaphylatoxin-like 3.
+At position 594 to 635, the domain is characterized as EGF-like 1; calcium-binding.
+At position 669 to 708, the domain is characterized as EGF-like 2.
+At position 709 to 755, the domain is characterized as EGF-like 3; calcium-binding.
+At position 756 to 800, the domain is characterized as EGF-like 4; calcium-binding.
+At position 801 to 846, the domain is characterized as EGF-like 5; calcium-binding.
+At position 847 to 894, the domain is characterized as EGF-like 6; calcium-binding.
+At position 895 to 937, the domain is characterized as EGF-like 7; calcium-binding.
+At position 938 to 979, the domain is characterized as EGF-like 8; calcium-binding.
+At position 980 to 1018, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1019 to 1061, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1062 to 1106, the domain is characterized as EGF-like 11; calcium-binding.
+At position 527 to 587, the domain is characterized as CBS 1.
+At position 617 to 674, the domain is characterized as CBS 2.
+At position 1 to 235, the domain is characterized as PABS.
+At position 62 to 127, the domain is characterized as NAC-A/B.
+At position 459 to 598, the domain is characterized as SIS 2.
+At position 10 to 69, the domain is characterized as CBS 1.
+At position 77 to 133, the domain is characterized as CBS 2.
+At position 817 to 1102, the domain is characterized as SMP-LTD.
+At position 375 to 566, the domain is characterized as PNPLA.
+At position 3 to 226, the domain is characterized as ABC transporter.
+At position 53 to 91, the domain is characterized as LRRNT.
+At position 26 to 291, the domain is characterized as Tyrosine-protein phosphatase.
+At position 551 to 609, the domain is characterized as CBS 1.
+At position 626 to 687, the domain is characterized as CBS 2.
+At position 94 to 285, the domain is characterized as ABC transmembrane type-1.
+At position 29 to 140, the domain is characterized as Thioredoxin.
+At position 91 to 137, the domain is characterized as F-box.
+At position 4 to 185, the domain is characterized as Guanylate kinase-like.
+At position 32 to 148, the domain is characterized as Ig-like V-type.
+At position 329 to 532, the domain is characterized as Protein kinase.
+At position 11 to 122, the domain is characterized as C-type lectin.
+At position 139 to 221, the domain is characterized as RRM.
+At position 605 to 695, the domain is characterized as PWI.
+At position 240 to 429, the domain is characterized as GATase cobBQ-type.
+At position 576 to 749, the domain is characterized as Helicase ATP-binding.
+At position 852 to 1021, the domain is characterized as Helicase C-terminal.
+At position 42 to 91, the domain is characterized as LysM 1.
+At position 270 to 320, the domain is characterized as LysM 2.
+At position 360 to 406, the domain is characterized as LysM 3.
+At position 228 to 241, the domain is characterized as CRIB.
+At position 567 to 818, the domain is characterized as Protein kinase.
+At position 28 to 139, the domain is characterized as Cupin type-1.
+At position 182 to 284, the domain is characterized as HPt.
+At position 350 to 418, the domain is characterized as S4 RNA-binding.
+At position 616 to 702, the domain is characterized as BRCT.
+At position 1 to 165, the domain is characterized as Plastocyanin-like 1.
+At position 166 to 330, the domain is characterized as Plastocyanin-like 2.
+At position 19 to 314, the domain is characterized as F-BAR.
+At position 481 to 671, the domain is characterized as Rho-GAP.
+At position 720 to 779, the domain is characterized as SH3.
+At position 292 to 524, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 278, the domain is characterized as YjeF C-terminal.
+At position 369 to 430, the domain is characterized as S4 RNA-binding.
+At position 82 to 294, the domain is characterized as CHASE.
+At position 362 to 651, the domain is characterized as Histidine kinase.
+At position 676 to 802, the domain is characterized as Response regulatory 1.
+At position 827 to 962, the domain is characterized as Response regulatory 2.
+At position 197 to 237, the domain is characterized as LRRCT.
+At position 7 to 229, the domain is characterized as ABC transporter.
+At position 274 to 309, the domain is characterized as CBM1.
+At position 573 to 675, the domain is characterized as tRNA-binding.
+At position 19 to 193, the domain is characterized as EngB-type G.
+At position 355 to 466, the domain is characterized as STAS.
+At position 27 to 81, the domain is characterized as TIL.
+At position 1 to 160, the domain is characterized as PPIase cyclophilin-type.
+At position 78 to 399, the domain is characterized as Peptidase A1.
+At position 21 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 242 to 348, the domain is characterized as Ig-like C2-type 3.
+At position 403 to 546, the domain is characterized as TIR.
+At position 107 to 158, the domain is characterized as bHLH.
+At position 73 to 400, the domain is characterized as Asparaginase/glutaminase.
+At position 55 to 98, the domain is characterized as CHCH.
+At position 8 to 44, the domain is characterized as EF-hand 1.
+At position 251 to 443, the domain is characterized as GATase cobBQ-type.
+At position 195 to 449, the domain is characterized as Protein kinase.
+At position 32 to 60, the domain is characterized as LRRNT.
+At position 359 to 406, the domain is characterized as LRRCT.
+At position 18 to 29, the domain is characterized as EF-hand.
+At position 408 to 577, the domain is characterized as tr-type G.
+At position 78 to 143, the domain is characterized as HTH luxR-type.
+At position 38 to 155, the domain is characterized as sHSP.
+At position 43 to 117, the domain is characterized as Carrier.
+At position 49 to 148, the domain is characterized as HD.
+At position 407 to 468, the domain is characterized as TGS.
+At position 674 to 749, the domain is characterized as ACT.
+At position 1 to 114, the domain is characterized as Toprim.
+At position 99 to 235, the domain is characterized as Fatty acid hydroxylase.
+At position 204 to 285, the domain is characterized as RRM.
+At position 1652 to 1739, the domain is characterized as BRCT 1.
+At position 1764 to 1863, the domain is characterized as BRCT 2.
+At position 306 to 366, the domain is characterized as CBS 1.
+At position 371 to 429, the domain is characterized as CBS 2.
+At position 221 to 448, the domain is characterized as CN hydrolase.
+At position 411 to 509, the domain is characterized as GTD-binding.
+At position 85 to 120, the domain is characterized as EF-hand 2.
+At position 130 to 155, the domain is characterized as EF-hand 3.
+At position 2 to 106, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 518 to 593, the domain is characterized as RRM.
+At position 1 to 145, the domain is characterized as Thioredoxin.
+At position 28 to 245, the domain is characterized as GB1/RHD3-type G.
+At position 45 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 103 to 271, the domain is characterized as CP-type G.
+At position 484 to 681, the domain is characterized as VWFA.
+At position 5 to 366, the domain is characterized as SAM-dependent MTase C5-type.
+At position 103 to 173, the domain is characterized as S4 RNA-binding.
+At position 4 to 80, the domain is characterized as Cytochrome b5 heme-binding.
+At position 1 to 106, the domain is characterized as Thioredoxin.
+At position 279 to 427, the domain is characterized as SIS 1.
+At position 454 to 594, the domain is characterized as SIS 2.
+At position 37 to 147, the domain is characterized as MTTase N-terminal.
+At position 165 to 402, the domain is characterized as Radical SAM core.
+At position 405 to 471, the domain is characterized as TRAM.
+At position 43 to 141, the domain is characterized as Rieske.
+At position 19 to 94, the domain is characterized as RRM.
+At position 203 to 285, the domain is characterized as Thyroglobulin type-1.
+At position 349 to 417, the domain is characterized as S4 RNA-binding.
+At position 23 to 149, the domain is characterized as C2.
+At position 23 to 264, the domain is characterized as tr-type G.
+At position 1 to 89, the domain is characterized as Peptidase S1.
+At position 81 to 297, the domain is characterized as YjeF N-terminal.
+At position 128 to 371, the domain is characterized as Radical SAM core.
+At position 245 to 495, the domain is characterized as CN hydrolase.
+At position 53 to 239, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 254, the domain is characterized as ABC transporter.
+At position 1 to 133, the domain is characterized as Jacalin-type lectin.
+At position 418 to 501, the domain is characterized as RRM 2.
+At position 321 to 373, the domain is characterized as bHLH.
+At position 46 to 216, the domain is characterized as Collagen-like.
+At position 273 to 371, the domain is characterized as C-type lectin.
+At position 40 to 152, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 499 to 658, the domain is characterized as Helicase ATP-binding.
+At position 679 to 835, the domain is characterized as Helicase C-terminal.
+At position 30 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 204, the domain is characterized as Ig-like C2-type 2.
+At position 219 to 298, the domain is characterized as Ig-like C2-type 3.
+At position 312 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 406 to 495, the domain is characterized as Ig-like C2-type 5.
+At position 500 to 589, the domain is characterized as Ig-like C2-type 6.
+At position 596 to 692, the domain is characterized as Fibronectin type-III 1.
+At position 697 to 793, the domain is characterized as Fibronectin type-III 2.
+At position 798 to 897, the domain is characterized as Fibronectin type-III 3.
+At position 901 to 995, the domain is characterized as Fibronectin type-III 4.
+At position 999 to 1098, the domain is characterized as Fibronectin type-III 5.
+At position 1103 to 1201, the domain is characterized as Fibronectin type-III 6.
+At position 1206 to 1303, the domain is characterized as Fibronectin type-III 7.
+At position 1307 to 1401, the domain is characterized as Fibronectin type-III 8.
+At position 1406 to 1503, the domain is characterized as Fibronectin type-III 9.
+At position 1508 to 1625, the domain is characterized as Fibronectin type-III 10.
+At position 1630 to 1726, the domain is characterized as Fibronectin type-III 11.
+At position 1730 to 1825, the domain is characterized as Fibronectin type-III 12.
+At position 1828 to 1930, the domain is characterized as Fibronectin type-III 13.
+At position 33 to 303, the domain is characterized as Alpha-carbonic anhydrase.
+At position 510 to 614, the domain is characterized as PH.
+At position 670 to 791, the domain is characterized as Arf-GAP.
+At position 27 to 272, the domain is characterized as PPM-type phosphatase.
+At position 13 to 218, the domain is characterized as DPCK.
+At position 148 to 238, the domain is characterized as RRM.
+At position 94 to 139, the domain is characterized as F-box.
+At position 74 to 381, the domain is characterized as AB hydrolase-1.
+At position 25 to 92, the domain is characterized as HMA.
+At position 1 to 167, the domain is characterized as NHR 1.
+At position 250 to 417, the domain is characterized as NHR 2.
+At position 450 to 616, the domain is characterized as NHR 3.
+At position 645 to 813, the domain is characterized as NHR 4.
+At position 841 to 1010, the domain is characterized as NHR 5.
+At position 1048 to 1211, the domain is characterized as NHR 6.
+At position 296 to 370, the domain is characterized as U-box.
+At position 7 to 273, the domain is characterized as CN hydrolase.
+At position 92 to 197, the domain is characterized as FAD-binding FR-type.
+At position 70 to 168, the domain is characterized as Plastocyanin-like.
+At position 114 to 290, the domain is characterized as NodB homology.
+At position 133 to 256, the domain is characterized as Nudix hydrolase.
+At position 1 to 123, the domain is characterized as Nudix hydrolase.
+At position 5 to 97, the domain is characterized as Acylphosphatase-like.
+At position 146 to 197, the domain is characterized as TSP type-1.
+At position 292 to 376, the domain is characterized as Ig-like C2-type.
+At position 10 to 74, the domain is characterized as Histone-fold.
+At position 4 to 397, the domain is characterized as BRO1.
+At position 73 to 133, the domain is characterized as CBS 1.
+At position 135 to 195, the domain is characterized as CBS 2.
+At position 155 to 279, the domain is characterized as FAD-binding FR-type.
+At position 23 to 201, the domain is characterized as Thioredoxin.
+At position 71 to 272, the domain is characterized as ABC transmembrane type-1.
+At position 17 to 269, the domain is characterized as Protein kinase.
+At position 92 to 214, the domain is characterized as MPN.
+At position 305 to 445, the domain is characterized as RanBD1.
+At position 85 to 391, the domain is characterized as Peptidase A1.
+At position 25 to 259, the domain is characterized as Alpha-carbonic anhydrase.
+At position 54 to 162, the domain is characterized as Expansin-like EG45.
+At position 175 to 256, the domain is characterized as Expansin-like CBD.
+At position 116 to 334, the domain is characterized as Radical SAM core.
+At position 3 to 141, the domain is characterized as DAC.
+At position 35 to 134, the domain is characterized as Cytochrome b5 heme-binding.
+At position 66 to 102, the domain is characterized as LRRNT.
+At position 386 to 434, the domain is characterized as GYF.
+At position 435 to 552, the domain is characterized as Toprim.
+At position 235 to 467, the domain is characterized as Peptidase S1.
+At position 59 to 306, the domain is characterized as Radical SAM core.
+At position 90 to 207, the domain is characterized as GST C-terminal.
+At position 215 to 370, the domain is characterized as TrmE-type G.
+At position 270 to 469, the domain is characterized as Rho-GAP.
+At position 115 to 376, the domain is characterized as NR LBD.
+At position 558 to 618, the domain is characterized as KH.
+At position 38 to 117, the domain is characterized as Inhibitor I9.
+At position 128 to 399, the domain is characterized as Peptidase S8.
+At position 26 to 78, the domain is characterized as Tudor-knot.
+At position 220 to 494, the domain is characterized as MYST-type HAT.
+At position 150 to 234, the domain is characterized as Ig-like C2-type 1.
+At position 236 to 332, the domain is characterized as Ig-like C2-type 2.
+At position 26 to 204, the domain is characterized as VWFA.
+At position 52 to 81, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 32 to 265, the domain is characterized as Alpha-carbonic anhydrase.
+At position 36 to 178, the domain is characterized as Thioredoxin.
+At position 125 to 239, the domain is characterized as Fe2OG dioxygenase.
+At position 251 to 291, the domain is characterized as ShKT.
+At position 274 to 352, the domain is characterized as PUA.
+At position 1 to 279, the domain is characterized as FERM.
+At position 2 to 124, the domain is characterized as PLAT.
+At position 125 to 676, the domain is characterized as Lipoxygenase.
+At position 10 to 168, the domain is characterized as YEATS.
+At position 1625 to 1697, the domain is characterized as RRM.
+At position 198 to 396, the domain is characterized as Peptidase M12B.
+At position 404 to 488, the domain is characterized as Disintegrin.
+At position 172 to 849, the domain is characterized as Peptidase M13.
+At position 71 to 107, the domain is characterized as EGF-like 1.
+At position 109 to 146, the domain is characterized as EGF-like 2.
+At position 148 to 186, the domain is characterized as EGF-like 3.
+At position 191 to 274, the domain is characterized as Kringle.
+At position 312 to 553, the domain is characterized as Peptidase S1.
+At position 235 to 310, the domain is characterized as MIT.
+At position 44 to 224, the domain is characterized as Macro.
+At position 329 to 483, the domain is characterized as CRAL-TRIO.
+At position 167 to 583, the domain is characterized as Protein kinase.
+At position 180 to 272, the domain is characterized as 5'-3' exonuclease.
+At position 312 to 468, the domain is characterized as 3'-5' exonuclease.
+At position 3 to 143, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 33 to 355, the domain is characterized as G-alpha.
+At position 220 to 401, the domain is characterized as PCI.
+At position 575 to 651, the domain is characterized as Carrier.
+At position 19 to 137, the domain is characterized as C2 1.
+At position 148 to 288, the domain is characterized as C2 2.
+At position 355 to 549, the domain is characterized as Ras-GAP.
+At position 603 to 704, the domain is characterized as PH.
+At position 26 to 72, the domain is characterized as G-patch.
+At position 26 to 103, the domain is characterized as CIDE-N.
+At position 22 to 211, the domain is characterized as RNase H type-2.
+At position 14 to 258, the domain is characterized as ABC transporter.
+At position 88 to 154, the domain is characterized as KH.
+At position 24 to 685, the domain is characterized as Vitellogenin.
+At position 1306 to 1475, the domain is characterized as VWFD.
+At position 101 to 276, the domain is characterized as Integrase catalytic.
+At position 779 to 917, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1051 to 1193, the domain is characterized as RNase H Ty1/copia-type.
+At position 108 to 315, the domain is characterized as ATP-grasp.
+At position 17 to 115, the domain is characterized as Rhodanese.
+At position 108 to 183, the domain is characterized as PRC barrel.
+At position 19 to 82, the domain is characterized as Histone-fold.
+At position 215 to 364, the domain is characterized as TrmE-type G.
+At position 4 to 109, the domain is characterized as PH.
+At position 105 to 210, the domain is characterized as IRS-type PTB.
+At position 1 to 409, the domain is characterized as Protein kinase 1.
+At position 1392 to 1462, the domain is characterized as Bromo 1.
+At position 1420 to 1865, the domain is characterized as Protein kinase 2.
+At position 1515 to 1585, the domain is characterized as Bromo 2.
+At position 25 to 228, the domain is characterized as AIG1-type G.
+At position 213 to 450, the domain is characterized as Peptidase S1.
+At position 588 to 766, the domain is characterized as Helicase ATP-binding.
+At position 793 to 943, the domain is characterized as Helicase C-terminal.
+At position 324 to 527, the domain is characterized as Helicase ATP-binding.
+At position 538 to 701, the domain is characterized as Helicase C-terminal.
+At position 23 to 123, the domain is characterized as LOB.
+At position 178 to 250, the domain is characterized as Cytochrome c.
+At position 54 to 151, the domain is characterized as BRICHOS.
+At position 193 to 228, the domain is characterized as EF-hand.
+At position 98 to 402, the domain is characterized as YjeF C-terminal.
+At position 5 to 98, the domain is characterized as Core-binding (CB).
+At position 122 to 281, the domain is characterized as Tyr recombinase.
+At position 11 to 100, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 141 to 171, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1206 to 1239, the domain is characterized as WW.
+At position 14 to 230, the domain is characterized as HD Cas3-type.
+At position 187 to 278, the domain is characterized as PI3K-RBD.
+At position 319 to 476, the domain is characterized as C2 PI3K-type.
+At position 496 to 673, the domain is characterized as PIK helical.
+At position 744 to 1026, the domain is characterized as PI3K/PI4K catalytic.
+At position 492 to 663, the domain is characterized as Helicase C-terminal.
+At position 234 to 444, the domain is characterized as Peptidase M12B.
+At position 453 to 541, the domain is characterized as Disintegrin.
+At position 542 to 597, the domain is characterized as TSP type-1 1.
+At position 848 to 904, the domain is characterized as TSP type-1 2.
+At position 34 to 379, the domain is characterized as GH18.
+At position 309 to 382, the domain is characterized as Ig-like C2-type 2.
+At position 538 to 839, the domain is characterized as Protein kinase.
+At position 184 to 359, the domain is characterized as EngA-type G 2.
+At position 360 to 444, the domain is characterized as KH-like.
+At position 98 to 177, the domain is characterized as PRC barrel.
+At position 17 to 174, the domain is characterized as Thioredoxin.
+At position 383 to 506, the domain is characterized as MsrB.
+At position 135 to 573, the domain is characterized as Urease.
+At position 78 to 177, the domain is characterized as AB hydrolase-1.
+At position 374 to 600, the domain is characterized as PARP catalytic.
+At position 11 to 236, the domain is characterized as Radical SAM core.
+At position 88 to 120, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 173 to 204, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 430 to 547, the domain is characterized as C2.
+At position 569 to 675, the domain is characterized as PH.
+At position 964 to 1095, the domain is characterized as MHD1.
+At position 29 to 450, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 966 to 1284, the domain is characterized as PKS/mFAS DH.
+At position 2485 to 2562, the domain is characterized as Carrier.
+At position 4 to 145, the domain is characterized as SLD.
+At position 364 to 695, the domain is characterized as Transferrin-like 2.
+At position 157 to 305, the domain is characterized as Plastocyanin-like 2.
+At position 375 to 488, the domain is characterized as Plastocyanin-like 3.
+At position 34 to 105, the domain is characterized as TB.
+At position 97 to 117, the domain is characterized as Follistatin-like 1.
+At position 111 to 167, the domain is characterized as Kazal-like 1.
+At position 168 to 191, the domain is characterized as Follistatin-like 2.
+At position 187 to 243, the domain is characterized as Kazal-like 2.
+At position 605 to 780, the domain is characterized as PCI.
+At position 600 to 678, the domain is characterized as Cytochrome c.
+At position 27 to 112, the domain is characterized as Ig-like V-type.
+At position 128 to 203, the domain is characterized as Ig-like C2-type.
+At position 225 to 327, the domain is characterized as Fe2OG dioxygenase.
+At position 118 to 170, the domain is characterized as FHA.
+At position 178 to 266, the domain is characterized as Rieske.
+At position 1 to 74, the domain is characterized as Sm.
+At position 1 to 190, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 231, the domain is characterized as ABC transporter.
+At position 98 to 355, the domain is characterized as Protein kinase.
+At position 356 to 431, the domain is characterized as AGC-kinase C-terminal.
+At position 90 to 209, the domain is characterized as Response regulatory.
+At position 83 to 297, the domain is characterized as Radical SAM core.
+At position 38 to 297, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 65 to 195, the domain is characterized as PX.
+At position 203 to 311, the domain is characterized as PH.
+At position 437 to 464, the domain is characterized as PLD phosphodiesterase 1.
+At position 751 to 778, the domain is characterized as PLD phosphodiesterase 2.
+At position 19 to 244, the domain is characterized as ABC transporter.
+At position 185 to 381, the domain is characterized as ATP-grasp 1.
+At position 743 to 955, the domain is characterized as ATP-grasp 2.
+At position 1027 to 1162, the domain is characterized as MGS-like.
+At position 118 to 192, the domain is characterized as POU-specific.
+At position 201 to 363, the domain is characterized as Hflx-type G.
+At position 596 to 691, the domain is characterized as Ig-like C2-type 1.
+At position 697 to 783, the domain is characterized as Ig-like C2-type 2.
+At position 870 to 1181, the domain is characterized as Protein kinase.
+At position 1 to 51, the domain is characterized as MADS-box.
+At position 18 to 88, the domain is characterized as HTH gntR-type.
+At position 63 to 177, the domain is characterized as sHSP.
+At position 422 to 596, the domain is characterized as tr-type G.
+At position 184 to 269, the domain is characterized as PNT.
+At position 19 to 235, the domain is characterized as Radical SAM core.
+At position 688 to 784, the domain is characterized as Zinc-hook.
+At position 4 to 475, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 515 to 816, the domain is characterized as UvrD-like helicase C-terminal.
+At position 48 to 287, the domain is characterized as Radical SAM core.
+At position 827 to 901, the domain is characterized as RRM.
+At position 4 to 89, the domain is characterized as Acylphosphatase-like.
+At position 36 to 304, the domain is characterized as GH18.
+At position 235 to 495, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 527 to 785, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 104 to 415, the domain is characterized as Peptidase A1.
+At position 154 to 301, the domain is characterized as C2 Aida-type.
+At position 18 to 79, the domain is characterized as HTH asnC-type.
+At position 35 to 103, the domain is characterized as BTB.
+At position 138 to 239, the domain is characterized as BACK.
+At position 168 to 224, the domain is characterized as CBS.
+At position 4 to 80, the domain is characterized as RRM 1.
+At position 114 to 191, the domain is characterized as RRM 2.
+At position 335 to 419, the domain is characterized as RRM 3.
+At position 487 to 597, the domain is characterized as RRM 4.
+At position 130 to 421, the domain is characterized as ABC transmembrane type-1.
+At position 456 to 692, the domain is characterized as ABC transporter.
+At position 1 to 108, the domain is characterized as NTR.
+At position 157 to 342, the domain is characterized as CheB-type methylesterase.
+At position 22 to 134, the domain is characterized as Ig-like V-type.
+At position 140 to 227, the domain is characterized as Ig-like C2-type.
+At position 2 to 167, the domain is characterized as Era-type G.
+At position 186 to 274, the domain is characterized as KH type-2.
+At position 18 to 234, the domain is characterized as tr-type G.
+At position 28 to 286, the domain is characterized as Protein kinase.
+At position 468 to 640, the domain is characterized as tr-type G.
+At position 81 to 161, the domain is characterized as RRM.
+At position 1887 to 1916, the domain is characterized as IQ.
+At position 4 to 153, the domain is characterized as UBC core.
+At position 112 to 212, the domain is characterized as HD.
+At position 470 to 505, the domain is characterized as EF-hand 1.
+At position 507 to 539, the domain is characterized as EF-hand 2.
+At position 328 to 474, the domain is characterized as SEFIR.
+At position 1 to 89, the domain is characterized as CS.
+At position 7 to 74, the domain is characterized as S4 RNA-binding.
+At position 1 to 232, the domain is characterized as ABC transporter.
+At position 183 to 405, the domain is characterized as Fibrinogen C-terminal.
+At position 418 to 440, the domain is characterized as Follistatin-like.
+At position 436 to 497, the domain is characterized as Kazal-like.
+At position 608 to 643, the domain is characterized as EF-hand.
+At position 2 to 214, the domain is characterized as ABC transporter.
+At position 26 to 127, the domain is characterized as PH.
+At position 127 to 441, the domain is characterized as IF rod.
+At position 19 to 245, the domain is characterized as Radical SAM core.
+At position 6 to 69, the domain is characterized as LCN-type CS-alpha/beta.
+At position 104 to 226, the domain is characterized as MPN.
+At position 126 to 307, the domain is characterized as FAD-binding PCMH-type.
+At position 485 to 559, the domain is characterized as PAS.
+At position 109 to 190, the domain is characterized as ELM2.
+At position 191 to 242, the domain is characterized as SANT 1.
+At position 497 to 548, the domain is characterized as SANT 2.
+At position 44 to 170, the domain is characterized as BAH.
+At position 951 to 1026, the domain is characterized as Carrier.
+At position 175 to 484, the domain is characterized as NACHT.
+At position 835 to 1118, the domain is characterized as FIIND.
+At position 1122 to 1211, the domain is characterized as CARD.
+At position 56 to 236, the domain is characterized as tr-type G.
+At position 113 to 159, the domain is characterized as F-box.
+At position 16 to 268, the domain is characterized as Protein kinase.
+At position 3 to 56, the domain is characterized as Kazal-like.
+At position 831 to 869, the domain is characterized as EGF-like 6.
+At position 972 to 1013, the domain is characterized as EGF-like 9.
+At position 31 to 100, the domain is characterized as Collagen-like.
+At position 134 to 247, the domain is characterized as C-type lectin.
+At position 325 to 348, the domain is characterized as Laminin EGF-like 1.
+At position 384 to 408, the domain is characterized as Laminin EGF-like 2.
+At position 13 to 184, the domain is characterized as Ku.
+At position 404 to 515, the domain is characterized as CBM2.
+At position 4 to 107, the domain is characterized as HIT.
+At position 21 to 154, the domain is characterized as MPN.
+At position 417 to 544, the domain is characterized as CUB.
+At position 32 to 320, the domain is characterized as tr-type G.
+At position 225 to 471, the domain is characterized as CN hydrolase.
+At position 189 to 364, the domain is characterized as EngA-type G 2.
+At position 365 to 449, the domain is characterized as KH-like.
+At position 153 to 183, the domain is characterized as ShKT.
+At position 124 to 329, the domain is characterized as ATP-grasp.
+At position 9 to 87, the domain is characterized as RRM.
+At position 97 to 168, the domain is characterized as SUI1.
+At position 51 to 97, the domain is characterized as EGF-like; atypical.
+At position 1 to 229, the domain is characterized as Peptidase S1.
+At position 9 to 161, the domain is characterized as NAC.
+At position 127 to 306, the domain is characterized as Helicase ATP-binding.
+At position 338 to 485, the domain is characterized as Helicase C-terminal.
+At position 3 to 473, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 500 to 782, the domain is characterized as UvrD-like helicase C-terminal.
+At position 208 to 373, the domain is characterized as Helicase ATP-binding.
+At position 506 to 657, the domain is characterized as Helicase C-terminal.
+At position 882 to 935, the domain is characterized as SANT 1.
+At position 988 to 1052, the domain is characterized as SANT 2.
+At position 5 to 141, the domain is characterized as SprT-like.
+At position 94 to 424, the domain is characterized as Asparaginase/glutaminase.
+At position 18 to 71, the domain is characterized as bHLH.
+At position 126 to 196, the domain is characterized as PAS.
+At position 11 to 474, the domain is characterized as Helicase ATP-binding.
+At position 475 to 629, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 64, the domain is characterized as PWWP.
+At position 16 to 82, the domain is characterized as HMA 1.
+At position 740 to 801, the domain is characterized as HMA 2.
+At position 3 to 72, the domain is characterized as RRM.
+At position 99 to 196, the domain is characterized as Cytochrome c 1.
+At position 219 to 305, the domain is characterized as Cytochrome c 2.
+At position 97 to 195, the domain is characterized as SSB.
+At position 1 to 182, the domain is characterized as Macro.
+At position 38 to 187, the domain is characterized as C-type lectin.
+At position 35 to 134, the domain is characterized as AB hydrolase-1.
+At position 3 to 70, the domain is characterized as S4 RNA-binding.
+At position 34 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 325 to 485, the domain is characterized as Helicase C-terminal.
+At position 1001 to 1041, the domain is characterized as HNH.
+At position 194 to 261, the domain is characterized as KH.
+At position 698 to 1202, the domain is characterized as USP.
+At position 150 to 389, the domain is characterized as VWFA.
+At position 97 to 240, the domain is characterized as Clp R.
+At position 222 to 283, the domain is characterized as CBS 1.
+At position 305 to 363, the domain is characterized as CBS 2.
+At position 380 to 440, the domain is characterized as CBS 3.
+At position 452 to 511, the domain is characterized as CBS 4.
+At position 10 to 91, the domain is characterized as ACT 1.
+At position 97 to 176, the domain is characterized as ACT 2.
+At position 97 to 420, the domain is characterized as PDEase.
+At position 275 to 356, the domain is characterized as PUA.
+At position 29 to 302, the domain is characterized as Septin-type G.
+At position 1018 to 1109, the domain is characterized as ARID.
+At position 125 to 157, the domain is characterized as LisH.
+At position 163 to 220, the domain is characterized as CTLH.
+At position 238 to 301, the domain is characterized as bZIP.
+At position 683 to 878, the domain is characterized as ATP-grasp 2.
+At position 945 to 1083, the domain is characterized as MGS-like.
+At position 260 to 379, the domain is characterized as C2 1.
+At position 415 to 550, the domain is characterized as C2 2.
+At position 61 to 162, the domain is characterized as SRCR 1.
+At position 191 to 305, the domain is characterized as SRCR 2.
+At position 329 to 428, the domain is characterized as SRCR 3.
+At position 438 to 546, the domain is characterized as SRCR 4.
+At position 1 to 52, the domain is characterized as HTH psq-type.
+At position 67 to 139, the domain is characterized as HTH CENPB-type.
+At position 168 to 385, the domain is characterized as DDE-1.
+At position 433 to 568, the domain is characterized as GGDEF.
+At position 125 to 184, the domain is characterized as SH3 1.
+At position 187 to 252, the domain is characterized as SH3 2.
+At position 382 to 443, the domain is characterized as SH3 3.
+At position 651 to 837, the domain is characterized as Lon proteolytic.
+At position 436 to 558, the domain is characterized as HD.
+At position 673 to 757, the domain is characterized as ACT 1.
+At position 785 to 852, the domain is characterized as ACT 2.
+At position 6 to 320, the domain is characterized as Asparaginase/glutaminase.
+At position 38 to 485, the domain is characterized as Biotin carboxylation.
+At position 157 to 355, the domain is characterized as ATP-grasp.
+At position 656 to 732, the domain is characterized as Biotinyl-binding.
+At position 27 to 199, the domain is characterized as BPL/LPL catalytic.
+At position 284 to 348, the domain is characterized as KH 3.
+At position 163 to 346, the domain is characterized as MIF4G.
+At position 38 to 359, the domain is characterized as AB hydrolase-1.
+At position 10 to 160, the domain is characterized as NAC.
+At position 78 to 268, the domain is characterized as Peptidase S1.
+At position 870 to 955, the domain is characterized as PDZ.
+At position 17 to 82, the domain is characterized as J.
+At position 193 to 378, the domain is characterized as Glutamine amidotransferase type-1.
+At position 25 to 288, the domain is characterized as GH16.
+At position 6 to 204, the domain is characterized as tr-type G.
+At position 39 to 93, the domain is characterized as TCP.
+At position 44 to 161, the domain is characterized as RabBD.
+At position 402 to 524, the domain is characterized as C2 1.
+At position 560 to 693, the domain is characterized as C2 2.
+At position 39 to 91, the domain is characterized as PISA.
+At position 33 to 290, the domain is characterized as AB hydrolase-1.
+At position 49 to 158, the domain is characterized as HIT.
+At position 402 to 612, the domain is characterized as Rab-GAP TBC.
+At position 27 to 98, the domain is characterized as KRAB.
+At position 151 to 255, the domain is characterized as HTH LytTR-type.
+At position 250 to 332, the domain is characterized as Toprim.
+At position 30 to 414, the domain is characterized as Helicase ATP-binding.
+At position 434 to 600, the domain is characterized as Helicase C-terminal.
+At position 39 to 87, the domain is characterized as F-box.
+At position 97 to 289, the domain is characterized as B30.2/SPRY.
+At position 315 to 379, the domain is characterized as PWWP.
+At position 457 to 516, the domain is characterized as FYR N-terminal.
+At position 520 to 604, the domain is characterized as FYR C-terminal.
+At position 919 to 1037, the domain is characterized as SET.
+At position 1043 to 1059, the domain is characterized as Post-SET.
+At position 11 to 292, the domain is characterized as Protein kinase.
+At position 1 to 133, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 361 to 439, the domain is characterized as EGF-like.
+At position 374 to 517, the domain is characterized as RCK N-terminal.
+At position 10 to 481, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 516 to 820, the domain is characterized as UvrD-like helicase C-terminal.
+At position 8 to 68, the domain is characterized as Sm.
+At position 401 to 1145, the domain is characterized as Myosin motor.
+At position 1147 to 1176, the domain is characterized as IQ.
+At position 1 to 102, the domain is characterized as Plastocyanin-like.
+At position 21 to 148, the domain is characterized as SCP.
+At position 184 to 216, the domain is characterized as ShKT.
+At position 2 to 145, the domain is characterized as UEV.
+At position 177 to 270, the domain is characterized as 5'-3' exonuclease.
+At position 302 to 465, the domain is characterized as 3'-5' exonuclease.
+At position 306 to 394, the domain is characterized as Saposin B-type.
+At position 26 to 130, the domain is characterized as CBM21.
+At position 541 to 619, the domain is characterized as Carrier.
+At position 326 to 856, the domain is characterized as USP.
+At position 654 to 695, the domain is characterized as UBA 1.
+At position 722 to 762, the domain is characterized as UBA 2.
+At position 199 to 394, the domain is characterized as Peptidase M12B.
+At position 96 to 284, the domain is characterized as RNase H type-2.
+At position 3 to 445, the domain is characterized as Hexokinase.
+At position 45 to 149, the domain is characterized as Gnk2-homologous 1.
+At position 170 to 269, the domain is characterized as Gnk2-homologous 2.
+At position 621 to 657, the domain is characterized as ShKT.
+At position 114 to 178, the domain is characterized as J.
+At position 517 to 790, the domain is characterized as Protein kinase.
+At position 31 to 175, the domain is characterized as F5/8 type C.
+At position 181 to 361, the domain is characterized as Laminin G-like 1.
+At position 368 to 545, the domain is characterized as Laminin G-like 2.
+At position 547 to 584, the domain is characterized as EGF-like 1.
+At position 585 to 792, the domain is characterized as Fibrinogen C-terminal.
+At position 959 to 997, the domain is characterized as EGF-like 2.
+At position 1019 to 1200, the domain is characterized as Laminin G-like 4.
+At position 37 to 188, the domain is characterized as CBM-cenC.
+At position 204 to 527, the domain is characterized as GH10.
+At position 903 to 966, the domain is characterized as SLH 1.
+At position 967 to 1025, the domain is characterized as SLH 2.
+At position 1028 to 1087, the domain is characterized as SLH 3.
+At position 30 to 226, the domain is characterized as VWFA 1.
+At position 227 to 267, the domain is characterized as EGF-like.
+At position 268 to 457, the domain is characterized as VWFA 2.
+At position 39 to 275, the domain is characterized as AB hydrolase-1.
+At position 41 to 70, the domain is characterized as PAS.
+At position 63 to 257, the domain is characterized as Peptidase M12A.
+At position 261 to 430, the domain is characterized as MAM.
+At position 431 to 586, the domain is characterized as MATH.
+At position 607 to 647, the domain is characterized as EGF-like.
+At position 564 to 623, the domain is characterized as KH.
+At position 633 to 707, the domain is characterized as S1 motif.
+At position 17 to 117, the domain is characterized as Rhodanese.
+At position 1 to 208, the domain is characterized as START.
+At position 717 to 763, the domain is characterized as F-box.
+At position 103 to 411, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 56 to 114, the domain is characterized as F-box.
+At position 76 to 177, the domain is characterized as SWIRM.
+At position 596 to 720, the domain is characterized as C2 2.
+At position 1025 to 1168, the domain is characterized as MHD1.
+At position 1275 to 1417, the domain is characterized as MHD2.
+At position 1450 to 1577, the domain is characterized as C2 3.
+At position 105 to 389, the domain is characterized as Protein kinase.
+At position 498 to 775, the domain is characterized as Protein kinase.
+At position 8 to 55, the domain is characterized as F-box.
+At position 212 to 238, the domain is characterized as PLD phosphodiesterase 1.
+At position 457 to 490, the domain is characterized as PLD phosphodiesterase 2.
+At position 1096 to 1215, the domain is characterized as PH.
+At position 1241 to 1515, the domain is characterized as CNH.
+At position 1585 to 1598, the domain is characterized as CRIB.
+At position 38 to 92, the domain is characterized as FHA.
+At position 45 to 100, the domain is characterized as HTH myb-type 1.
+At position 101 to 151, the domain is characterized as HTH myb-type 2.
+At position 59 to 123, the domain is characterized as CSD.
+At position 56 to 237, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 198, the domain is characterized as Lon N-terminal.
+At position 586 to 768, the domain is characterized as Lon proteolytic.
+At position 43 to 329, the domain is characterized as Protein kinase.
+At position 63 to 348, the domain is characterized as Protein kinase.
+At position 226 to 346, the domain is characterized as xRRM.
+At position 696 to 762, the domain is characterized as SAM 1.
+At position 770 to 837, the domain is characterized as SAM 2.
+At position 936 to 1091, the domain is characterized as PID.
+At position 28 to 293, the domain is characterized as Tyrosine-protein phosphatase.
+At position 207 to 280, the domain is characterized as S1 motif.
+At position 520 to 684, the domain is characterized as Helicase ATP-binding.
+At position 702 to 882, the domain is characterized as Helicase C-terminal.
+At position 8 to 208, the domain is characterized as DPCK.
+At position 2 to 101, the domain is characterized as SSB.
+At position 112 to 307, the domain is characterized as Peptidase M12A.
+At position 338 to 372, the domain is characterized as ShKT.
+At position 346 to 545, the domain is characterized as Helicase ATP-binding.
+At position 556 to 719, the domain is characterized as Helicase C-terminal.
+At position 187 to 295, the domain is characterized as SH2.
+At position 6 to 69, the domain is characterized as HTH asnC-type.
+At position 570 to 648, the domain is characterized as BRCT.
+At position 176 to 392, the domain is characterized as BURP.
+At position 121 to 183, the domain is characterized as CBS 1.
+At position 184 to 240, the domain is characterized as CBS 2.
+At position 106 to 491, the domain is characterized as GRAS.
+At position 21 to 202, the domain is characterized as N-acetyltransferase.
+At position 572 to 631, the domain is characterized as KH.
+At position 641 to 709, the domain is characterized as S1 motif.
+At position 7 to 72, the domain is characterized as S4 RNA-binding.
+At position 4 to 60, the domain is characterized as DPH-type MB.
+At position 21 to 81, the domain is characterized as Sushi 1.
+At position 82 to 139, the domain is characterized as Sushi 2.
+At position 140 to 202, the domain is characterized as Sushi 3.
+At position 203 to 262, the domain is characterized as Sushi 4.
+At position 274 to 337, the domain is characterized as bZIP.
+At position 2 to 26, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 27 to 55, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 42 to 171, the domain is characterized as PLAT.
+At position 174 to 866, the domain is characterized as Lipoxygenase.
+At position 160 to 483, the domain is characterized as NACHT.
+At position 667 to 694, the domain is characterized as LRRNT.
+At position 906 to 970, the domain is characterized as LRRCT.
+At position 41 to 148, the domain is characterized as HPt.
+At position 40 to 84, the domain is characterized as LysM.
+At position 14 to 257, the domain is characterized as CN hydrolase.
+At position 1 to 60, the domain is characterized as MADS-box.
+At position 293 to 565, the domain is characterized as Septin-type G.
+At position 15 to 179, the domain is characterized as UBC core.
+At position 433 to 549, the domain is characterized as Ricin B-type lectin.
+At position 3 to 330, the domain is characterized as Kinesin motor.
+At position 20 to 65, the domain is characterized as Gla.
+At position 42 to 270, the domain is characterized as Radical SAM core.
+At position 803 to 1074, the domain is characterized as Protein kinase.
+At position 390 to 750, the domain is characterized as Roc.
+At position 1356 to 1627, the domain is characterized as Protein kinase.
+At position 1821 to 1923, the domain is characterized as PH.
+At position 13 to 131, the domain is characterized as MTTase N-terminal.
+At position 154 to 385, the domain is characterized as Radical SAM core.
+At position 2 to 208, the domain is characterized as PH 1.
+At position 45 to 128, the domain is characterized as PDZ.
+At position 227 to 340, the domain is characterized as PH 2.
+At position 384 to 440, the domain is characterized as SU.
+At position 124 to 196, the domain is characterized as KRAB.
+At position 9 to 83, the domain is characterized as Carrier 1.
+At position 101 to 526, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 997 to 1267, the domain is characterized as PKS/mFAS DH.
+At position 1759 to 1836, the domain is characterized as Carrier 2.
+At position 158 to 265, the domain is characterized as PUA.
+At position 86 to 284, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 53 to 105, the domain is characterized as bHLH.
+At position 85 to 256, the domain is characterized as Tyrosine-protein phosphatase.
+At position 518 to 763, the domain is characterized as ABC transporter.
+At position 316 to 611, the domain is characterized as Calpain catalytic.
+At position 143 to 220, the domain is characterized as RRM.
+At position 28 to 339, the domain is characterized as Protein kinase.
+At position 129 to 294, the domain is characterized as TNase-like.
+At position 46 to 133, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 29 to 65, the domain is characterized as EGF-like.
+At position 72 to 153, the domain is characterized as Kringle.
+At position 181 to 426, the domain is characterized as Peptidase S1.
+At position 510 to 585, the domain is characterized as U-box.
+At position 11 to 332, the domain is characterized as ABC transporter.
+At position 66 to 238, the domain is characterized as Cupin type-1.
+At position 264 to 503, the domain is characterized as ABC transporter 2.
+At position 5 to 85, the domain is characterized as GST N-terminal.
+At position 92 to 219, the domain is characterized as GST C-terminal.
+At position 142 to 404, the domain is characterized as Protein kinase.
+At position 445 to 480, the domain is characterized as EF-hand 1.
+At position 481 to 516, the domain is characterized as EF-hand 2.
+At position 517 to 556, the domain is characterized as EF-hand 3.
+At position 557 to 586, the domain is characterized as EF-hand 4.
+At position 9 to 91, the domain is characterized as GIY-YIG.
+At position 483 to 803, the domain is characterized as Protein kinase.
+At position 876 to 1006, the domain is characterized as Guanylate cyclase.
+At position 190 to 346, the domain is characterized as GAF.
+At position 389 to 623, the domain is characterized as Histidine kinase.
+At position 180 to 354, the domain is characterized as CRAL-TRIO.
+At position 116 to 278, the domain is characterized as CP-type G.
+At position 36 to 114, the domain is characterized as IGFBP N-terminal.
+At position 105 to 159, the domain is characterized as Kazal-like.
+At position 390 to 472, the domain is characterized as PDZ.
+At position 193 to 461, the domain is characterized as SF4 helicase.
+At position 1 to 175, the domain is characterized as YrdC-like.
+At position 95 to 175, the domain is characterized as PRC barrel.
+At position 1 to 139, the domain is characterized as MGS-like.
+At position 97 to 175, the domain is characterized as PRC barrel.
+At position 317 to 369, the domain is characterized as bHLH.
+At position 140 to 247, the domain is characterized as C-type lectin.
+At position 173 to 211, the domain is characterized as EGF-like 1.
+At position 212 to 336, the domain is characterized as SEA.
+At position 322 to 361, the domain is characterized as EGF-like 2.
+At position 363 to 404, the domain is characterized as EGF-like 3.
+At position 559 to 635, the domain is characterized as Carrier.
+At position 2 to 116, the domain is characterized as Thioredoxin.
+At position 1 to 249, the domain is characterized as PABS.
+At position 4 to 64, the domain is characterized as LIM zinc-binding.
+At position 24 to 206, the domain is characterized as Plastocyanin-like 1.
+At position 218 to 366, the domain is characterized as Plastocyanin-like 2.
+At position 379 to 560, the domain is characterized as Plastocyanin-like 3.
+At position 570 to 718, the domain is characterized as Plastocyanin-like 4.
+At position 731 to 903, the domain is characterized as Plastocyanin-like 5.
+At position 911 to 1087, the domain is characterized as Plastocyanin-like 6.
+At position 1852 to 1881, the domain is characterized as IQ.
+At position 4 to 277, the domain is characterized as DegV.
+At position 282 to 526, the domain is characterized as Glutamine amidotransferase type-1.
+At position 217 to 378, the domain is characterized as TrmE-type G.
+At position 11 to 98, the domain is characterized as Acylphosphatase-like.
+At position 209 to 393, the domain is characterized as YrdC-like.
+At position 142 to 250, the domain is characterized as CBM21.
+At position 556 to 612, the domain is characterized as Myb-like.
+At position 185 to 256, the domain is characterized as SANT.
+At position 31 to 107, the domain is characterized as Chorismate mutase.
+At position 9 to 240, the domain is characterized as ATP-grasp.
+At position 94 to 188, the domain is characterized as BRICHOS.
+At position 1 to 414, the domain is characterized as KAP NTPase.
+At position 89 to 151, the domain is characterized as PA.
+At position 66 to 251, the domain is characterized as Tyrosine-protein phosphatase.
+At position 406 to 575, the domain is characterized as tr-type G.
+At position 12 to 130, the domain is characterized as Arf-GAP.
+At position 11 to 57, the domain is characterized as G-patch.
+At position 37 to 119, the domain is characterized as SCAN box.
+At position 95 to 266, the domain is characterized as Helicase ATP-binding.
+At position 277 to 437, the domain is characterized as Helicase C-terminal.
+At position 1 to 127, the domain is characterized as C2.
+At position 328 to 368, the domain is characterized as PLD phosphodiesterase 1.
+At position 112 to 350, the domain is characterized as Radical SAM core.
+At position 522 to 640, the domain is characterized as SMC hinge.
+At position 19 to 90, the domain is characterized as LCN-type CS-alpha/beta.
+At position 51 to 348, the domain is characterized as USP.
+At position 120 to 285, the domain is characterized as CRAL-TRIO.
+At position 174 to 218, the domain is characterized as DSL.
+At position 219 to 252, the domain is characterized as EGF-like 1.
+At position 256 to 283, the domain is characterized as EGF-like 2.
+At position 285 to 323, the domain is characterized as EGF-like 3.
+At position 325 to 361, the domain is characterized as EGF-like 4.
+At position 363 to 401, the domain is characterized as EGF-like 5.
+At position 403 to 439, the domain is characterized as EGF-like 6.
+At position 441 to 477, the domain is characterized as EGF-like 7.
+At position 481 to 519, the domain is characterized as EGF-like 8.
+At position 92 to 190, the domain is characterized as PRC barrel.
+At position 217 to 374, the domain is characterized as TrmE-type G.
+At position 60 to 252, the domain is characterized as Glutamine amidotransferase type-1.
+At position 253 to 461, the domain is characterized as GMPS ATP-PPase.
+At position 109 to 375, the domain is characterized as Protein kinase.
+At position 23 to 229, the domain is characterized as YjeF N-terminal.
+At position 4 to 248, the domain is characterized as CN hydrolase.
+At position 291 to 402, the domain is characterized as PAZ.
+At position 566 to 853, the domain is characterized as Piwi.
+At position 108 to 193, the domain is characterized as PDZ.
+At position 175 to 276, the domain is characterized as PpiC 1.
+At position 286 to 386, the domain is characterized as PpiC 2.
+At position 48 to 516, the domain is characterized as Sema.
+At position 518 to 569, the domain is characterized as PSI.
+At position 586 to 641, the domain is characterized as Ig-like C2-type.
+At position 610 to 774, the domain is characterized as PNPLA.
+At position 236 to 292, the domain is characterized as WHEP-TRS.
+At position 13 to 297, the domain is characterized as Protein kinase.
+At position 282 to 451, the domain is characterized as tr-type G.
+At position 14 to 105, the domain is characterized as FAD-binding FR-type.
+At position 211 to 364, the domain is characterized as TrmE-type G.
+At position 123 to 434, the domain is characterized as Protein kinase.
+At position 86 to 129, the domain is characterized as LysM 2.
+At position 150 to 193, the domain is characterized as LysM 3.
+At position 203 to 327, the domain is characterized as Peptidase C51.
+At position 12 to 30, the domain is characterized as PPIase cyclophilin-type.
+At position 48 to 495, the domain is characterized as Biotin carboxylation.
+At position 167 to 364, the domain is characterized as ATP-grasp.
+At position 649 to 724, the domain is characterized as Biotinyl-binding.
+At position 13 to 342, the domain is characterized as PTS EIIC type-2.
+At position 384 to 475, the domain is characterized as PTS EIIB type-2.
+At position 504 to 646, the domain is characterized as PTS EIIA type-2.
+At position 569 to 668, the domain is characterized as PilZ.
+At position 29 to 96, the domain is characterized as BTB.
+At position 131 to 238, the domain is characterized as BACK.
+At position 209 to 291, the domain is characterized as UBX.
+At position 11 to 63, the domain is characterized as bHLH.
+At position 60 to 106, the domain is characterized as G-patch.
+At position 211 to 440, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 66 to 178, the domain is characterized as Ig-like.
+At position 35 to 487, the domain is characterized as Hexokinase.
+At position 231 to 321, the domain is characterized as PA.
+At position 1 to 237, the domain is characterized as PTS EIIC type-4.
+At position 692 to 774, the domain is characterized as ACT 1.
+At position 14 to 104, the domain is characterized as Core-binding (CB).
+At position 125 to 311, the domain is characterized as Tyr recombinase.
+At position 431 to 684, the domain is characterized as Protein kinase.
+At position 6 to 227, the domain is characterized as ABC transporter.
+At position 203 to 379, the domain is characterized as PCI.
+At position 231 to 373, the domain is characterized as MPN.
+At position 124 to 288, the domain is characterized as JmjC.
+At position 103 to 168, the domain is characterized as BTB.
+At position 129 to 179, the domain is characterized as bHLH.
+At position 937 to 1075, the domain is characterized as MGS-like.
+At position 52 to 356, the domain is characterized as AB hydrolase-1.
+At position 6 to 127, the domain is characterized as MSP.
+At position 61 to 145, the domain is characterized as Cytochrome b5 heme-binding.
+At position 444 to 466, the domain is characterized as Follistatin-like.
+At position 462 to 523, the domain is characterized as Kazal-like.
+At position 634 to 669, the domain is characterized as EF-hand.
+At position 124 to 228, the domain is characterized as Ig-like C1-type.
+At position 531 to 689, the domain is characterized as STAS.
+At position 26 to 84, the domain is characterized as Chromo.
+At position 15 to 236, the domain is characterized as ABC transporter.
+At position 71 to 152, the domain is characterized as PDZ.
+At position 158 to 228, the domain is characterized as SH3.
+At position 282 to 451, the domain is characterized as Guanylate kinase-like.
+At position 3 to 327, the domain is characterized as Kinesin motor.
+At position 290 to 353, the domain is characterized as bZIP.
+At position 8 to 174, the domain is characterized as Era-type G.
+At position 197 to 282, the domain is characterized as KH type-2.
+At position 216 to 268, the domain is characterized as HAMP.
+At position 273 to 502, the domain is characterized as Methyl-accepting transducer.
+At position 689 to 929, the domain is characterized as VLIG-type G.
+At position 191 to 454, the domain is characterized as Protein kinase.
+At position 455 to 522, the domain is characterized as AGC-kinase C-terminal.
+At position 557 to 657, the domain is characterized as PH.
+At position 29 to 132, the domain is characterized as Ig-like V-type.
+At position 191 to 469, the domain is characterized as SF4 helicase.
+At position 21 to 139, the domain is characterized as C2 1.
+At position 171 to 293, the domain is characterized as C2 2.
+At position 326 to 453, the domain is characterized as C2 3.
+At position 755 to 960, the domain is characterized as PARP catalytic.
+At position 47 to 219, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 316 to 753, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 762 to 826, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 43 to 153, the domain is characterized as Rieske.
+At position 178 to 353, the domain is characterized as Macro.
+At position 398 to 623, the domain is characterized as Collagen IV NC1.
+At position 6 to 83, the domain is characterized as Core-binding (CB).
+At position 104 to 301, the domain is characterized as Tyr recombinase.
+At position 23 to 302, the domain is characterized as Protein kinase.
+At position 98 to 333, the domain is characterized as Radical SAM core.
+At position 10 to 268, the domain is characterized as Protein kinase.
+At position 8 to 200, the domain is characterized as DhaL.
+At position 7 to 136, the domain is characterized as ADF-H.
+At position 532 to 592, the domain is characterized as SH3.
+At position 12 to 208, the domain is characterized as ABC transmembrane type-1.
+At position 55 to 225, the domain is characterized as Helicase ATP-binding.
+At position 236 to 397, the domain is characterized as Helicase C-terminal.
+At position 21 to 104, the domain is characterized as IPT/TIG 1.
+At position 191 to 283, the domain is characterized as IPT/TIG 2.
+At position 50 to 173, the domain is characterized as GST C-terminal.
+At position 269 to 450, the domain is characterized as B30.2/SPRY.
+At position 50 to 135, the domain is characterized as ELM2.
+At position 136 to 187, the domain is characterized as SANT 1.
+At position 430 to 586, the domain is characterized as Exonuclease.
+At position 164 to 373, the domain is characterized as Helicase ATP-binding.
+At position 400 to 625, the domain is characterized as Helicase C-terminal.
+At position 76 to 111, the domain is characterized as QLQ.
+At position 144 to 188, the domain is characterized as WRC.
+At position 31 to 169, the domain is characterized as FZ.
+At position 169 to 410, the domain is characterized as NR LBD.
+At position 18 to 59, the domain is characterized as LRRNT.
+At position 93 to 168, the domain is characterized as PRC barrel.
+At position 10 to 75, the domain is characterized as Cytochrome b5 heme-binding.
+At position 243 to 452, the domain is characterized as Helicase ATP-binding.
+At position 494 to 640, the domain is characterized as Helicase C-terminal.
+At position 312 to 359, the domain is characterized as PAS.
+At position 558 to 893, the domain is characterized as PDEase.
+At position 4 to 238, the domain is characterized as PABS.
+At position 31 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 447 to 583, the domain is characterized as Histidine kinase.
+At position 1 to 106, the domain is characterized as HPt.
+At position 290 to 540, the domain is characterized as Histidine kinase.
+At position 542 to 678, the domain is characterized as CheW-like.
+At position 544 to 593, the domain is characterized as bHLH.
+At position 40 to 85, the domain is characterized as Gla.
+At position 123 to 164, the domain is characterized as EGF-like 2.
+At position 236 to 469, the domain is characterized as Peptidase S1.
+At position 295 to 369, the domain is characterized as HTH OST-type 3.
+At position 525 to 584, the domain is characterized as Tudor.
+At position 295 to 567, the domain is characterized as Septin-type G.
+At position 20 to 136, the domain is characterized as Thioredoxin 1.
+At position 626 to 705, the domain is characterized as BRCT.
+At position 121 to 509, the domain is characterized as Protein kinase.
+At position 161 to 247, the domain is characterized as PPIase FKBP-type.
+At position 91 to 124, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 133 to 169, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 177 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 44 to 97, the domain is characterized as bHLH.
+At position 115 to 193, the domain is characterized as PAS 1.
+At position 277 to 347, the domain is characterized as PAS 2.
+At position 348 to 392, the domain is characterized as PAC.
+At position 5 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 521 to 811, the domain is characterized as UvrD-like helicase C-terminal.
+At position 23 to 140, the domain is characterized as Ig-like C2-type 1.
+At position 130 to 234, the domain is characterized as Ig-like C2-type 2.
+At position 604 to 706, the domain is characterized as tRNA-binding.
+At position 4 to 187, the domain is characterized as tr-type G.
+At position 224 to 309, the domain is characterized as SCD.
+At position 1 to 111, the domain is characterized as Dynamin-type G.
+At position 1 to 34, the domain is characterized as FZ.
+At position 51 to 158, the domain is characterized as NTR.
+At position 11 to 89, the domain is characterized as GIY-YIG.
+At position 257 to 499, the domain is characterized as KaiC 2.
+At position 49 to 145, the domain is characterized as HD.
+At position 383 to 446, the domain is characterized as TGS.
+At position 623 to 696, the domain is characterized as ACT.
+At position 20 to 84, the domain is characterized as LCN-type CS-alpha/beta.
+At position 5 to 159, the domain is characterized as PPIase cyclophilin-type.
+At position 37 to 92, the domain is characterized as F-box.
+At position 36 to 302, the domain is characterized as Septin-type G.
+At position 16 to 175, the domain is characterized as NAC.
+At position 11 to 109, the domain is characterized as Glutaredoxin.
+At position 92 to 263, the domain is characterized as OTU.
+At position 28 to 277, the domain is characterized as AB hydrolase-1.
+At position 377 to 519, the domain is characterized as Jacalin-type lectin.
+At position 71 to 146, the domain is characterized as Sm.
+At position 230 to 402, the domain is characterized as PCI.
+At position 1962 to 2249, the domain is characterized as Autotransporter.
+At position 106 to 168, the domain is characterized as S4 RNA-binding.
+At position 137 to 334, the domain is characterized as ATP-grasp 1.
+At position 682 to 873, the domain is characterized as ATP-grasp 2.
+At position 955 to 1100, the domain is characterized as MGS-like.
+At position 29 to 87, the domain is characterized as 4Fe-4S.
+At position 101 to 130, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 131 to 160, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 40 to 263, the domain is characterized as ABC transporter.
+At position 2 to 78, the domain is characterized as Ubiquitin-like 1.
+At position 79 to 157, the domain is characterized as Ubiquitin-like 2.
+At position 136 to 228, the domain is characterized as WSC 1.
+At position 239 to 332, the domain is characterized as WSC 2.
+At position 176 to 349, the domain is characterized as EngA-type G 2.
+At position 350 to 434, the domain is characterized as KH-like.
+At position 67 to 378, the domain is characterized as IF rod.
+At position 107 to 295, the domain is characterized as ABC transmembrane type-1.
+At position 127 to 466, the domain is characterized as GS catalytic.
+At position 63 to 188, the domain is characterized as TBDR plug.
+At position 199 to 912, the domain is characterized as TBDR beta-barrel.
+At position 3 to 207, the domain is characterized as DPCK.
+At position 58 to 128, the domain is characterized as CSD.
+At position 192 to 510, the domain is characterized as IF rod.
+At position 41 to 291, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 29 to 129, the domain is characterized as Glutaredoxin.
+At position 93 to 153, the domain is characterized as S4 RNA-binding.
+At position 56 to 236, the domain is characterized as ABC transmembrane type-1.
+At position 327 to 520, the domain is characterized as Protein kinase.
+At position 1 to 117, the domain is characterized as HTH marR-type.
+At position 79 to 173, the domain is characterized as Toprim.
+At position 281 to 327, the domain is characterized as F-box.
+At position 91 to 243, the domain is characterized as Tyr recombinase.
+At position 38 to 315, the domain is characterized as tr-type G.
+At position 378 to 430, the domain is characterized as FBD.
+At position 269 to 370, the domain is characterized as Fibronectin type-III 1.
+At position 374 to 466, the domain is characterized as Fibronectin type-III 2.
+At position 470 to 563, the domain is characterized as Fibronectin type-III 3.
+At position 567 to 661, the domain is characterized as Fibronectin type-III 4.
+At position 665 to 758, the domain is characterized as Fibronectin type-III 5.
+At position 762 to 852, the domain is characterized as Fibronectin type-III 6.
+At position 864 to 951, the domain is characterized as Fibronectin type-III 7.
+At position 952 to 1045, the domain is characterized as Fibronectin type-III 8.
+At position 1046 to 1151, the domain is characterized as Fibronectin type-III 9.
+At position 191 to 377, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 227, the domain is characterized as tr-type G.
+At position 182 to 234, the domain is characterized as HAMP.
+At position 281 to 502, the domain is characterized as Histidine kinase.
+At position 658 to 777, the domain is characterized as Response regulatory.
+At position 814 to 907, the domain is characterized as HPt.
+At position 33 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 46 to 118, the domain is characterized as Bromo 1.
+At position 287 to 359, the domain is characterized as Bromo 2.
+At position 496 to 578, the domain is characterized as NET.
+At position 416 to 530, the domain is characterized as Toprim.
+At position 58 to 101, the domain is characterized as Chitin-binding type-1 1.
+At position 105 to 149, the domain is characterized as Chitin-binding type-1 2.
+At position 210 to 253, the domain is characterized as Chitin-binding type-1 3.
+At position 257 to 301, the domain is characterized as Chitin-binding type-1 4.
+At position 589 to 670, the domain is characterized as BRCT.
+At position 106 to 195, the domain is characterized as Histone-fold.
+At position 262 to 522, the domain is characterized as KaiC 2.
+At position 18 to 169, the domain is characterized as OCP N-terminal.
+At position 27 to 62, the domain is characterized as EF-hand 1.
+At position 115 to 150, the domain is characterized as EF-hand 2.
+At position 153 to 188, the domain is characterized as EF-hand 3.
+At position 223 to 310, the domain is characterized as PDZ 1.
+At position 318 to 405, the domain is characterized as PDZ 2.
+At position 466 to 547, the domain is characterized as PDZ 3.
+At position 581 to 651, the domain is characterized as SH3.
+At position 737 to 912, the domain is characterized as Guanylate kinase-like.
+At position 721 to 819, the domain is characterized as BRCT 1.
+At position 875 to 980, the domain is characterized as BRCT 2.
+At position 6 to 262, the domain is characterized as Pterin-binding.
+At position 247 to 306, the domain is characterized as OVATE.
+At position 4 to 256, the domain is characterized as Pyruvate carboxyltransferase.
+At position 4 to 192, the domain is characterized as Flavodoxin-like.
+At position 126 to 297, the domain is characterized as Tyrosine-protein phosphatase.
+At position 327 to 372, the domain is characterized as PSI.
+At position 280 to 420, the domain is characterized as SIS 1.
+At position 449 to 588, the domain is characterized as SIS 2.
+At position 455 to 654, the domain is characterized as FtsK.
+At position 16 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 340 to 575, the domain is characterized as ABC transporter.
+At position 40 to 106, the domain is characterized as Chitin-binding type R&R.
+At position 110 to 298, the domain is characterized as ATP-grasp.
+At position 6 to 58, the domain is characterized as F-box.
+At position 29 to 144, the domain is characterized as BAH.
+At position 1 to 114, the domain is characterized as C2 1.
+At position 247 to 370, the domain is characterized as C2 2.
+At position 458 to 493, the domain is characterized as EF-hand.
+At position 74 to 381, the domain is characterized as Peptidase A1.
+At position 163 to 191, the domain is characterized as IQ 1.
+At position 192 to 214, the domain is characterized as IQ 2.
+At position 1 to 312, the domain is characterized as Hcy-binding.
+At position 343 to 601, the domain is characterized as Pterin-binding.
+At position 635 to 728, the domain is characterized as B12-binding N-terminal.
+At position 729 to 866, the domain is characterized as B12-binding.
+At position 893 to 1192, the domain is characterized as AdoMet activation.
+At position 391 to 610, the domain is characterized as FtsK.
+At position 287 to 392, the domain is characterized as BEN.
+At position 12 to 141, the domain is characterized as EamA 1.
+At position 166 to 292, the domain is characterized as EamA 2.
+At position 2 to 67, the domain is characterized as Ubiquitin-like.
+At position 50 to 187, the domain is characterized as Thioredoxin.
+At position 398 to 662, the domain is characterized as Histidine kinase.
+At position 912 to 1044, the domain is characterized as Response regulatory.
+At position 16 to 126, the domain is characterized as MTTase N-terminal.
+At position 143 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 448, the domain is characterized as TRAM.
+At position 45 to 131, the domain is characterized as Phosphagen kinase N-terminal.
+At position 158 to 400, the domain is characterized as Phosphagen kinase C-terminal.
+At position 425 to 635, the domain is characterized as Rab-GAP TBC.
+At position 37 to 258, the domain is characterized as Cupin type-1 1.
+At position 412 to 558, the domain is characterized as Cupin type-1 2.
+At position 45 to 117, the domain is characterized as Bromo 1.
+At position 298 to 368, the domain is characterized as Bromo 2.
+At position 495 to 577, the domain is characterized as NET.
+At position 938 to 1149, the domain is characterized as JmjC.
+At position 188 to 266, the domain is characterized as RRM.
+At position 8 to 157, the domain is characterized as YEATS.
+At position 2 to 168, the domain is characterized as EngA-type G 1.
+At position 181 to 357, the domain is characterized as EngA-type G 2.
+At position 358 to 439, the domain is characterized as KH-like.
+At position 21 to 80, the domain is characterized as LCN-type CS-alpha/beta.
+At position 27 to 319, the domain is characterized as ABC transmembrane type-1 1.
+At position 357 to 603, the domain is characterized as ABC transporter 1.
+At position 717 to 1007, the domain is characterized as ABC transmembrane type-1 2.
+At position 1052 to 1287, the domain is characterized as ABC transporter 2.
+At position 28 to 373, the domain is characterized as FERM.
+At position 40 to 234, the domain is characterized as TLC.
+At position 274 to 444, the domain is characterized as TrmE-type G.
+At position 56 to 336, the domain is characterized as Protein kinase.
+At position 213 to 389, the domain is characterized as PCI.
+At position 249 to 436, the domain is characterized as GATase cobBQ-type.
+At position 26 to 141, the domain is characterized as MTTase N-terminal.
+At position 159 to 388, the domain is characterized as Radical SAM core.
+At position 391 to 453, the domain is characterized as TRAM.
+At position 141 to 212, the domain is characterized as RBD.
+At position 429 to 690, the domain is characterized as Protein kinase.
+At position 233 to 692, the domain is characterized as Trm1 methyltransferase.
+At position 1 to 224, the domain is characterized as RNase H type-2.
+At position 1 to 24, the domain is characterized as Peptidase M12B.
+At position 61 to 188, the domain is characterized as TBDR plug.
+At position 196 to 1046, the domain is characterized as TBDR beta-barrel.
+At position 472 to 600, the domain is characterized as NTR.
+At position 10 to 96, the domain is characterized as MtN3/slv 1.
+At position 132 to 216, the domain is characterized as MtN3/slv 2.
+At position 136 to 373, the domain is characterized as ABC transmembrane type-1.
+At position 505 to 727, the domain is characterized as ABC transporter.
+At position 1 to 203, the domain is characterized as Protein kinase.
+At position 39 to 184, the domain is characterized as EXPERA.
+At position 224 to 309, the domain is characterized as RWP-RK.
+At position 31 to 215, the domain is characterized as EngB-type G.
+At position 4 to 244, the domain is characterized as ABC transporter 1.
+At position 255 to 547, the domain is characterized as ABC transporter 2.
+At position 141 to 370, the domain is characterized as Sigma-54 factor interaction.
+At position 6 to 60, the domain is characterized as F-box.
+At position 43 to 106, the domain is characterized as bZIP.
+At position 109 to 142, the domain is characterized as KOW.
+At position 138 to 385, the domain is characterized as TLDc.
+At position 86 to 245, the domain is characterized as CRAL-TRIO.
+At position 632 to 706, the domain is characterized as S1 motif.
+At position 163 to 389, the domain is characterized as CHASE.
+At position 457 to 723, the domain is characterized as Histidine kinase.
+At position 746 to 865, the domain is characterized as Response regulatory 1.
+At position 891 to 1028, the domain is characterized as Response regulatory 2.
+At position 21 to 254, the domain is characterized as ABC transporter.
+At position 14 to 86, the domain is characterized as KRAB.
+At position 27 to 58, the domain is characterized as EGF-like 1.
+At position 62 to 89, the domain is characterized as EGF-like 2.
+At position 91 to 129, the domain is characterized as EGF-like 3.
+At position 131 to 172, the domain is characterized as EGF-like 4.
+At position 174 to 210, the domain is characterized as EGF-like 5; calcium-binding.
+At position 212 to 248, the domain is characterized as EGF-like 6; calcium-binding.
+At position 410 to 577, the domain is characterized as tr-type G.
+At position 11 to 246, the domain is characterized as PABS.
+At position 293 to 532, the domain is characterized as Glutamine amidotransferase type-1.
+At position 140 to 234, the domain is characterized as Rhodanese.
+At position 10 to 79, the domain is characterized as H15.
+At position 173 to 565, the domain is characterized as Kinesin motor.
+At position 12 to 40, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 128 to 159, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 161 to 190, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 34 to 157, the domain is characterized as RNase III.
+At position 185 to 256, the domain is characterized as DRBM.
+At position 81 to 370, the domain is characterized as FAE.
+At position 79 to 146, the domain is characterized as PUB.
+At position 2 to 27, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 28 to 55, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 61, the domain is characterized as Tudor-knot.
+At position 214 to 377, the domain is characterized as MRG.
+At position 343 to 392, the domain is characterized as bHLH.
+At position 8 to 69, the domain is characterized as SH3.
+At position 443 to 627, the domain is characterized as C2 DOCK-type.
+At position 1231 to 1642, the domain is characterized as DOCKER.
+At position 39 to 177, the domain is characterized as Thioredoxin.
+At position 434 to 482, the domain is characterized as LysM.
+At position 24 to 152, the domain is characterized as C-type lectin.
+At position 196 to 256, the domain is characterized as DDT 1.
+At position 341 to 396, the domain is characterized as DDT 2.
+At position 1883 to 1953, the domain is characterized as DDT 3.
+At position 1948 to 2014, the domain is characterized as DDT 4.
+At position 2047 to 2117, the domain is characterized as Bromo.
+At position 221 to 391, the domain is characterized as Helicase ATP-binding.
+At position 396 to 585, the domain is characterized as Helicase C-terminal.
+At position 18 to 83, the domain is characterized as HTH luxR-type.
+At position 98 to 350, the domain is characterized as EAL.
+At position 80 to 174, the domain is characterized as Toprim.
+At position 12 to 80, the domain is characterized as NAC-A/B.
+At position 403 to 475, the domain is characterized as PAS.
+At position 61 to 288, the domain is characterized as ATP-grasp.
+At position 211 to 372, the domain is characterized as TrmE-type G.
+At position 223 to 434, the domain is characterized as Helicase ATP-binding.
+At position 474 to 642, the domain is characterized as Helicase C-terminal.
+At position 81 to 182, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 20 to 217, the domain is characterized as PNPLA.
+At position 1407 to 1488, the domain is characterized as Carrier.
+At position 32 to 92, the domain is characterized as SH3.
+At position 94 to 191, the domain is characterized as SH2.
+At position 66 to 197, the domain is characterized as RNase H type-1.
+At position 56 to 126, the domain is characterized as POTRA.
+At position 2 to 185, the domain is characterized as GMPS ATP-PPase.
+At position 55 to 313, the domain is characterized as Protein kinase.
+At position 14 to 178, the domain is characterized as CP-type G.
+At position 37 to 162, the domain is characterized as Radical SAM core.
+At position 674 to 864, the domain is characterized as ATP-grasp 2.
+At position 933 to 1068, the domain is characterized as MGS-like.
+At position 149 to 316, the domain is characterized as Helicase ATP-binding.
+At position 327 to 495, the domain is characterized as Helicase C-terminal.
+At position 11 to 133, the domain is characterized as NTF2.
+At position 331 to 409, the domain is characterized as RRM.
+At position 38 to 194, the domain is characterized as NHR 1.
+At position 279 to 433, the domain is characterized as NHR 2.
+At position 7 to 245, the domain is characterized as ABC transporter.
+At position 38 to 149, the domain is characterized as Plastocyanin-like 1.
+At position 160 to 317, the domain is characterized as Plastocyanin-like 2.
+At position 421 to 556, the domain is characterized as Plastocyanin-like 3.
+At position 13 to 104, the domain is characterized as Core-binding (CB).
+At position 125 to 309, the domain is characterized as Tyr recombinase.
+At position 195 to 505, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 312 to 388, the domain is characterized as Toprim.
+At position 8 to 69, the domain is characterized as LCN-type CS-alpha/beta.
+At position 28 to 97, the domain is characterized as S4 RNA-binding.
+At position 178 to 466, the domain is characterized as Autotransporter.
+At position 2 to 156, the domain is characterized as DHFR.
+At position 164 to 199, the domain is characterized as EF-hand 1.
+At position 230 to 265, the domain is characterized as EF-hand 2.
+At position 54 to 201, the domain is characterized as DAC.
+At position 19 to 188, the domain is characterized as EngB-type G.
+At position 541 to 812, the domain is characterized as Protein kinase.
+At position 887 to 1017, the domain is characterized as Guanylate cyclase.
+At position 187 to 297, the domain is characterized as SCP.
+At position 3 to 223, the domain is characterized as tr-type G.
+At position 206 to 241, the domain is characterized as EF-hand.
+At position 322 to 464, the domain is characterized as PI-PLC X-box.
+At position 542 to 652, the domain is characterized as PI-PLC Y-box.
+At position 656 to 781, the domain is characterized as C2.
+At position 41 to 81, the domain is characterized as SCP.
+At position 8 to 286, the domain is characterized as tr-type G.
+At position 103 to 252, the domain is characterized as JmjC.
+At position 10 to 116, the domain is characterized as MaoC-like.
+At position 95 to 199, the domain is characterized as PH.
+At position 237 to 399, the domain is characterized as MyTH4.
+At position 404 to 757, the domain is characterized as FERM.
+At position 499 to 733, the domain is characterized as NR LBD.
+At position 191 to 359, the domain is characterized as PCI.
+At position 565 to 663, the domain is characterized as tRNA-binding.
+At position 178 to 294, the domain is characterized as Fe2OG dioxygenase.
+At position 34 to 464, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1403 to 1478, the domain is characterized as Carrier.
+At position 394 to 462, the domain is characterized as J.
+At position 242 to 304, the domain is characterized as t-SNARE coiled-coil homology.
+At position 71 to 173, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 271 to 332, the domain is characterized as SH3.
+At position 344 to 479, the domain is characterized as PID.
+At position 67 to 159, the domain is characterized as SUEL-type lectin 1.
+At position 168 to 260, the domain is characterized as SUEL-type lectin 2.
+At position 94 to 285, the domain is characterized as DH.
+At position 327 to 542, the domain is characterized as BAR.
+At position 581 to 644, the domain is characterized as SH3 1.
+At position 706 to 769, the domain is characterized as SH3 2.
+At position 12 to 247, the domain is characterized as ABC transporter.
+At position 5 to 248, the domain is characterized as ABC transporter.
+At position 65 to 91, the domain is characterized as EGF-like 1.
+At position 94 to 133, the domain is characterized as EGF-like 2; calcium-binding.
+At position 137 to 173, the domain is characterized as EGF-like 3.
+At position 174 to 212, the domain is characterized as EGF-like 4; calcium-binding.
+At position 219 to 259, the domain is characterized as EGF-like 5; calcium-binding.
+At position 400 to 546, the domain is characterized as MAM.
+At position 965 to 1039, the domain is characterized as Carrier.
+At position 9 to 155, the domain is characterized as UBC core.
+At position 26 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 99, the domain is characterized as BTB.
+At position 1 to 62, the domain is characterized as HTH lacI-type.
+At position 105 to 181, the domain is characterized as SH3b.
+At position 253 to 422, the domain is characterized as tr-type G.
+At position 145 to 349, the domain is characterized as ATP-grasp.
+At position 231 to 304, the domain is characterized as RRM 1.
+At position 310 to 389, the domain is characterized as RRM 2.
+At position 353 to 431, the domain is characterized as OCT.
+At position 108 to 369, the domain is characterized as Protein kinase.
+At position 591 to 667, the domain is characterized as BRCT.
+At position 120 to 234, the domain is characterized as SET.
+At position 55 to 132, the domain is characterized as RRM.
+At position 18 to 99, the domain is characterized as RRM 1.
+At position 106 to 186, the domain is characterized as RRM 2.
+At position 349 to 427, the domain is characterized as RRM 3.
+At position 521 to 627, the domain is characterized as Calponin-homology (CH).
+At position 772 to 834, the domain is characterized as LIM zinc-binding.
+At position 1816 to 1982, the domain is characterized as bMERB.
+At position 1 to 418, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 888 to 1165, the domain is characterized as PKS/mFAS DH.
+At position 1671 to 1746, the domain is characterized as Carrier.
+At position 83 to 205, the domain is characterized as FAD-binding FR-type.
+At position 58 to 121, the domain is characterized as Chitin-binding type R&R.
+At position 47 to 166, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 186 to 293, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 266 to 403, the domain is characterized as MPN.
+At position 37 to 143, the domain is characterized as Gnk2-homologous 1.
+At position 161 to 273, the domain is characterized as Gnk2-homologous 2.
+At position 171 to 545, the domain is characterized as GRAS.
+At position 239 to 273, the domain is characterized as SAP.
+At position 123 to 214, the domain is characterized as Fibronectin type-III.
+At position 45 to 152, the domain is characterized as Cadherin 1.
+At position 153 to 270, the domain is characterized as Cadherin 2.
+At position 283 to 400, the domain is characterized as Cadherin 3.
+At position 401 to 514, the domain is characterized as Cadherin 4.
+At position 515 to 621, the domain is characterized as Cadherin 5.
+At position 622 to 722, the domain is characterized as Cadherin 6.
+At position 724 to 824, the domain is characterized as Cadherin 7.
+At position 825 to 931, the domain is characterized as Cadherin 8.
+At position 932 to 1040, the domain is characterized as Cadherin 9.
+At position 1042 to 1149, the domain is characterized as Cadherin 10.
+At position 1150 to 1264, the domain is characterized as Cadherin 11.
+At position 12 to 69, the domain is characterized as S4 RNA-binding.
+At position 154 to 327, the domain is characterized as Helicase ATP-binding.
+At position 352 to 505, the domain is characterized as Helicase C-terminal.
+At position 172 to 471, the domain is characterized as SF4 helicase.
+At position 484 to 717, the domain is characterized as ABC transporter 1.
+At position 1293 to 1528, the domain is characterized as ABC transporter 2.
+At position 90 to 152, the domain is characterized as S1 motif.
+At position 64 to 139, the domain is characterized as Thyroglobulin type-1.
+At position 20 to 111, the domain is characterized as Ig-like C2-type 1.
+At position 126 to 211, the domain is characterized as Ig-like C2-type 2.
+At position 222 to 318, the domain is characterized as Ig-like C2-type 3.
+At position 381 to 536, the domain is characterized as TIR.
+At position 246 to 360, the domain is characterized as Nop.
+At position 13 to 105, the domain is characterized as ARID.
+At position 35 to 135, the domain is characterized as Gnk2-homologous 1.
+At position 137 to 236, the domain is characterized as Gnk2-homologous 2.
+At position 315 to 604, the domain is characterized as Protein kinase.
+At position 36 to 104, the domain is characterized as KH type-2.
+At position 1 to 40, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 46 to 86, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 87 to 129, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 46 to 284, the domain is characterized as ABC transmembrane type-2.
+At position 441 to 612, the domain is characterized as JmjC.
+At position 158 to 299, the domain is characterized as CMP/dCMP-type deaminase.
+At position 248 to 282, the domain is characterized as SAP.
+At position 132 to 267, the domain is characterized as Fatty acid hydroxylase.
+At position 24 to 101, the domain is characterized as Cytochrome b5 heme-binding.
+At position 6 to 297, the domain is characterized as YjeF C-terminal.
+At position 1 to 57, the domain is characterized as HTH myb-type 1.
+At position 7 to 172, the domain is characterized as uDENN.
+At position 191 to 324, the domain is characterized as cDENN.
+At position 326 to 427, the domain is characterized as dDENN.
+At position 871 to 957, the domain is characterized as GRAM.
+At position 1108 to 1584, the domain is characterized as Myotubularin phosphatase.
+At position 1743 to 1847, the domain is characterized as PH.
+At position 44 to 137, the domain is characterized as HTH La-type RNA-binding.
+At position 149 to 234, the domain is characterized as RRM.
+At position 259 to 386, the domain is characterized as xRRM.
+At position 27 to 302, the domain is characterized as GH18.
+At position 157 to 275, the domain is characterized as C2.
+At position 351 to 614, the domain is characterized as Protein kinase.
+At position 615 to 685, the domain is characterized as AGC-kinase C-terminal.
+At position 14 to 199, the domain is characterized as RNase H type-2.
+At position 1132 to 1233, the domain is characterized as Glutaredoxin.
+At position 24 to 137, the domain is characterized as Calponin-homology (CH).
+At position 62 to 108, the domain is characterized as G-patch.
+At position 214 to 438, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 84 to 170, the domain is characterized as K-box.
+At position 97 to 251, the domain is characterized as NHR 1.
+At position 359 to 514, the domain is characterized as NHR 2.
+At position 1 to 64, the domain is characterized as KRAB.
+At position 564 to 780, the domain is characterized as Laminin IV type B.
+At position 786 to 833, the domain is characterized as Laminin EGF-like 6.
+At position 834 to 879, the domain is characterized as Laminin EGF-like 7.
+At position 880 to 929, the domain is characterized as Laminin EGF-like 8.
+At position 930 to 988, the domain is characterized as Laminin EGF-like 9.
+At position 989 to 1040, the domain is characterized as Laminin EGF-like 10.
+At position 1041 to 1097, the domain is characterized as Laminin EGF-like 11.
+At position 1098 to 1145, the domain is characterized as Laminin EGF-like 12.
+At position 1146 to 1192, the domain is characterized as Laminin EGF-like 13.
+At position 482 to 719, the domain is characterized as PPM-type phosphatase.
+At position 2 to 187, the domain is characterized as UmuC.
+At position 25 to 313, the domain is characterized as ABC transmembrane type-1 1.
+At position 348 to 584, the domain is characterized as ABC transporter 1.
+At position 662 to 949, the domain is characterized as ABC transmembrane type-1 2.
+At position 984 to 1222, the domain is characterized as ABC transporter 2.
+At position 104 to 218, the domain is characterized as SET.
+At position 90 to 463, the domain is characterized as GBD/FH3.
+At position 544 to 620, the domain is characterized as FH1.
+At position 625 to 1025, the domain is characterized as FH2.
+At position 1048 to 1078, the domain is characterized as DAD.
+At position 459 to 509, the domain is characterized as DHHC.
+At position 62 to 125, the domain is characterized as S5 DRBM.
+At position 9 to 265, the domain is characterized as Protein kinase.
+At position 175 to 228, the domain is characterized as SOCS box.
+At position 225 to 345, the domain is characterized as Fe2OG dioxygenase.
+At position 214 to 293, the domain is characterized as UBX.
+At position 31 to 419, the domain is characterized as Helicase ATP-binding.
+At position 89 to 157, the domain is characterized as POTRA.
+At position 14 to 145, the domain is characterized as CMP/dCMP-type deaminase.
+At position 64 to 136, the domain is characterized as S4 RNA-binding.
+At position 100 to 387, the domain is characterized as tr-type G.
+At position 74 to 422, the domain is characterized as Peptidase A1.
+At position 38 to 139, the domain is characterized as Collagen-like.
+At position 143 to 279, the domain is characterized as C1q.
+At position 249 to 493, the domain is characterized as ABC transporter 2.
+At position 464 to 905, the domain is characterized as Hexokinase 2.
+At position 212 to 278, the domain is characterized as KH.
+At position 171 to 346, the domain is characterized as Helicase ATP-binding.
+At position 374 to 521, the domain is characterized as Helicase C-terminal.
+At position 49 to 141, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 184 to 214, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 4 to 477, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 512 to 810, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 109, the domain is characterized as IF rod.
+At position 9 to 152, the domain is characterized as PTS EIIA type-2.
+At position 448 to 596, the domain is characterized as GST C-terminal.
+At position 4 to 46, the domain is characterized as SpoVT-AbrB.
+At position 29 to 267, the domain is characterized as Peptidase S1.
+At position 52 to 270, the domain is characterized as Radical SAM core.
+At position 105 to 133, the domain is characterized as HhH.
+At position 1 to 127, the domain is characterized as N-acetyltransferase.
+At position 361 to 403, the domain is characterized as CCT.
+At position 4 to 95, the domain is characterized as CARD.
+At position 152 to 255, the domain is characterized as PA.
+At position 146 to 457, the domain is characterized as Peptidase S8.
+At position 49 to 295, the domain is characterized as AB hydrolase-1.
+At position 30 to 146, the domain is characterized as C2.
+At position 363 to 396, the domain is characterized as WW 1.
+At position 395 to 428, the domain is characterized as WW 2.
+At position 477 to 510, the domain is characterized as WW 3.
+At position 521 to 554, the domain is characterized as WW 4.
+At position 615 to 949, the domain is characterized as HECT.
+At position 181 to 210, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 48 to 347, the domain is characterized as Calpain catalytic.
+At position 530 to 565, the domain is characterized as EF-hand 1.
+At position 606 to 641, the domain is characterized as EF-hand 2.
+At position 671 to 705, the domain is characterized as EF-hand 3.
+At position 8 to 95, the domain is characterized as Ig-like C2-type 1.
+At position 157 to 259, the domain is characterized as Ig-like C2-type 2.
+At position 361 to 452, the domain is characterized as Ig-like C2-type 3.
+At position 452 to 546, the domain is characterized as Ig-like C2-type 4.
+At position 645 to 765, the domain is characterized as Ig-like C2-type 5.
+At position 774 to 870, the domain is characterized as Fibronectin type-III 1.
+At position 872 to 967, the domain is characterized as Fibronectin type-III 2.
+At position 971 to 1059, the domain is characterized as Ig-like C2-type 6.
+At position 1068 to 1163, the domain is characterized as Fibronectin type-III 3.
+At position 1181 to 1269, the domain is characterized as Ig-like C2-type 7.
+At position 104 to 279, the domain is characterized as Helicase ATP-binding.
+At position 306 to 457, the domain is characterized as Helicase C-terminal.
+At position 2 to 89, the domain is characterized as HPr.
+At position 54 to 151, the domain is characterized as Rieske.
+At position 1 to 134, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 181 to 327, the domain is characterized as OTU.
+At position 111 to 246, the domain is characterized as MRH 1.
+At position 342 to 469, the domain is characterized as MRH 2.
+At position 105 to 198, the domain is characterized as Integrase catalytic.
+At position 113 to 163, the domain is characterized as bHLH.
+At position 114 to 229, the domain is characterized as Ferric oxidoreductase.
+At position 254 to 410, the domain is characterized as FAD-binding FR-type.
+At position 132 to 193, the domain is characterized as KH 1.
+At position 223 to 284, the domain is characterized as KH 2.
+At position 54 to 122, the domain is characterized as POTRA.
+At position 44 to 223, the domain is characterized as Helicase ATP-binding.
+At position 240 to 402, the domain is characterized as Helicase C-terminal.
+At position 91 to 134, the domain is characterized as LysM 2.
+At position 158 to 201, the domain is characterized as LysM 3.
+At position 211 to 335, the domain is characterized as Peptidase C51.
+At position 613 to 830, the domain is characterized as Rap-GAP.
+At position 967 to 1045, the domain is characterized as PDZ.
+At position 172 to 220, the domain is characterized as LysM.
+At position 23 to 106, the domain is characterized as IGFBP N-terminal.
+At position 184 to 266, the domain is characterized as Thyroglobulin type-1.
+At position 45 to 106, the domain is characterized as Sushi 1.
+At position 107 to 170, the domain is characterized as Sushi 2.
+At position 171 to 236, the domain is characterized as Sushi 3.
+At position 14 to 270, the domain is characterized as Protein kinase.
+At position 280 to 348, the domain is characterized as MIT 1.
+At position 375 to 444, the domain is characterized as MIT 2.
+At position 27 to 483, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 512 to 800, the domain is characterized as UvrD-like helicase C-terminal.
+At position 579 to 649, the domain is characterized as Bromo.
+At position 929 to 1012, the domain is characterized as PWWP.
+At position 10 to 219, the domain is characterized as tr-type G.
+At position 44 to 248, the domain is characterized as Peptidase M12A.
+At position 110 to 160, the domain is characterized as bHLH.
+At position 580 to 651, the domain is characterized as PAS.
+At position 652 to 708, the domain is characterized as PAC.
+At position 726 to 948, the domain is characterized as Histidine kinase.
+At position 974 to 1095, the domain is characterized as Response regulatory.
+At position 1133 to 1228, the domain is characterized as HPt.
+At position 119 to 390, the domain is characterized as Protein kinase.
+At position 4 to 170, the domain is characterized as Thioredoxin.
+At position 18 to 247, the domain is characterized as Radical SAM core.
+At position 38 to 207, the domain is characterized as Helicase ATP-binding.
+At position 234 to 379, the domain is characterized as Helicase C-terminal.
+At position 169 to 340, the domain is characterized as OBG-type G.
+At position 20 to 127, the domain is characterized as Ig-like V-type.
+At position 81 to 203, the domain is characterized as FAD-binding FR-type.
+At position 39 to 187, the domain is characterized as Nudix hydrolase.
+At position 454 to 728, the domain is characterized as ZP.
+At position 20 to 132, the domain is characterized as Ig-like V-type 1.
+At position 137 to 250, the domain is characterized as Ig-like V-type 2.
+At position 106 to 297, the domain is characterized as Helicase ATP-binding.
+At position 329 to 493, the domain is characterized as Helicase C-terminal.
+At position 66 to 230, the domain is characterized as SIS.
+At position 44 to 159, the domain is characterized as Expansin-like EG45.
+At position 169 to 248, the domain is characterized as Expansin-like CBD.
+At position 9 to 80, the domain is characterized as KRAB.
+At position 37 to 93, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 211 to 482, the domain is characterized as MHD.
+At position 63 to 221, the domain is characterized as CP-type G.
+At position 215 to 488, the domain is characterized as USP.
+At position 23 to 366, the domain is characterized as GH18.
+At position 64 to 96, the domain is characterized as LisH.
+At position 97 to 154, the domain is characterized as CTLH.
+At position 188 to 375, the domain is characterized as Glutamine amidotransferase type-1.
+At position 225 to 497, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 477 to 759, the domain is characterized as Protein kinase.
+At position 26 to 338, the domain is characterized as Transferrin-like 1.
+At position 352 to 684, the domain is characterized as Transferrin-like 2.
+At position 709 to 784, the domain is characterized as Smr.
+At position 312 to 452, the domain is characterized as C-CAP/cofactor C-like.
+At position 304 to 435, the domain is characterized as C-CAP/cofactor C-like.
+At position 69 to 350, the domain is characterized as Protein kinase.
+At position 12 to 152, the domain is characterized as CheW-like.
+At position 57 to 80, the domain is characterized as EF-hand 2.
+At position 89 to 124, the domain is characterized as EF-hand 3.
+At position 130 to 159, the domain is characterized as EF-hand 4.
+At position 179 to 282, the domain is characterized as Fe2OG dioxygenase.
+At position 144 to 195, the domain is characterized as HTH myb-type 1.
+At position 196 to 251, the domain is characterized as HTH myb-type 2.
+At position 252 to 302, the domain is characterized as HTH myb-type 3.
+At position 427 to 647, the domain is characterized as Protein kinase.
+At position 495 to 1044, the domain is characterized as Protein kinase.
+At position 4 to 126, the domain is characterized as CMP/dCMP-type deaminase.
+At position 539 to 592, the domain is characterized as bHLH.
+At position 26 to 129, the domain is characterized as Ig-like V-type.
+At position 135 to 207, the domain is characterized as Ig-like C2-type.
+At position 14 to 104, the domain is characterized as BRCT 1.
+At position 105 to 196, the domain is characterized as BRCT 2.
+At position 311 to 399, the domain is characterized as BRCT 3.
+At position 654 to 744, the domain is characterized as BRCT 4.
+At position 767 to 872, the domain is characterized as BRCT 5.
+At position 4 to 152, the domain is characterized as MGS-like.
+At position 281 to 358, the domain is characterized as PUA.
+At position 116 to 222, the domain is characterized as HTH APSES-type.
+At position 71 to 114, the domain is characterized as LDL-receptor class A 1.
+At position 115 to 161, the domain is characterized as LDL-receptor class A 2; atypical.
+At position 162 to 203, the domain is characterized as LDL-receptor class A 3; atypical.
+At position 4 to 222, the domain is characterized as ABC transporter.
+At position 70 to 203, the domain is characterized as PH.
+At position 243 to 451, the domain is characterized as Rab-GAP TBC.
+At position 23 to 161, the domain is characterized as Ig-like V-type.
+At position 2 to 305, the domain is characterized as Glutamine amidotransferase type-2.
+At position 11 to 221, the domain is characterized as YjeF N-terminal.
+At position 248 to 416, the domain is characterized as Senescence.
+At position 279 to 356, the domain is characterized as PUA.
+At position 61 to 208, the domain is characterized as Nudix hydrolase.
+At position 235 to 279, the domain is characterized as DSL.
+At position 280 to 313, the domain is characterized as EGF-like 1.
+At position 311 to 345, the domain is characterized as EGF-like 2.
+At position 347 to 385, the domain is characterized as EGF-like 3.
+At position 387 to 485, the domain is characterized as EGF-like 4.
+At position 487 to 523, the domain is characterized as EGF-like 5; calcium-binding.
+At position 525 to 605, the domain is characterized as EGF-like 6; calcium-binding.
+At position 607 to 642, the domain is characterized as EGF-like 7; calcium-binding.
+At position 644 to 680, the domain is characterized as EGF-like 8; calcium-binding.
+At position 682 to 717, the domain is characterized as EGF-like 9.
+At position 719 to 793, the domain is characterized as EGF-like 10.
+At position 795 to 831, the domain is characterized as EGF-like 11; calcium-binding.
+At position 833 to 873, the domain is characterized as EGF-like 12.
+At position 875 to 911, the domain is characterized as EGF-like 13.
+At position 913 to 949, the domain is characterized as EGF-like 14; calcium-binding.
+At position 135 to 382, the domain is characterized as Radical SAM core.
+At position 384 to 452, the domain is characterized as TRAM.
+At position 670 to 699, the domain is characterized as CBM10.
+At position 859 to 962, the domain is characterized as CBM2.
+At position 18 to 207, the domain is characterized as RNase H type-2.
+At position 2 to 91, the domain is characterized as HPr.
+At position 688 to 830, the domain is characterized as PTS EIIA type-2.
+At position 125 to 271, the domain is characterized as N-acetyltransferase.
+At position 276 to 339, the domain is characterized as bZIP.
+At position 101 to 290, the domain is characterized as ABC transmembrane type-1.
+At position 347 to 457, the domain is characterized as Rhodanese.
+At position 31 to 239, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 205, the domain is characterized as SMP-LTD.
+At position 91 to 247, the domain is characterized as Flavodoxin-like.
+At position 341 to 580, the domain is characterized as Radical SAM core.
+At position 125 to 150, the domain is characterized as KOW.
+At position 12 to 269, the domain is characterized as Protein kinase.
+At position 474 to 553, the domain is characterized as PKD.
+At position 555 to 653, the domain is characterized as P/Homo B.
+At position 33 to 166, the domain is characterized as RUN.
+At position 168 to 259, the domain is characterized as PAZ.
+At position 419 to 694, the domain is characterized as Piwi.
+At position 4 to 139, the domain is characterized as MPN.
+At position 29 to 164, the domain is characterized as MPN.
+At position 39 to 71, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 165 to 340, the domain is characterized as Helicase ATP-binding.
+At position 497 to 654, the domain is characterized as Helicase C-terminal.
+At position 31 to 91, the domain is characterized as SH3.
+At position 93 to 190, the domain is characterized as SH2.
+At position 294 to 322, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 5 to 219, the domain is characterized as ABC transporter.
+At position 78 to 107, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 116 to 147, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 48 to 130, the domain is characterized as SCAN box.
+At position 76 to 111, the domain is characterized as EF-hand 2.
+At position 117 to 152, the domain is characterized as EF-hand 3.
+At position 215 to 401, the domain is characterized as Glutamine amidotransferase type-1.
+At position 548 to 740, the domain is characterized as ATP-grasp 1.
+At position 1090 to 1281, the domain is characterized as ATP-grasp 2.
+At position 1352 to 1496, the domain is characterized as MGS-like.
+At position 156 to 215, the domain is characterized as SH3 2.
+At position 490 to 673, the domain is characterized as Helicase ATP-binding 1.
+At position 684 to 921, the domain is characterized as Helicase C-terminal 1.
+At position 982 to 1286, the domain is characterized as SEC63 1.
+At position 1337 to 1512, the domain is characterized as Helicase ATP-binding 2.
+At position 1545 to 1753, the domain is characterized as Helicase C-terminal 2.
+At position 1812 to 2124, the domain is characterized as SEC63 2.
+At position 37 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 115 to 144, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 636 to 800, the domain is characterized as PCI.
+At position 38 to 227, the domain is characterized as RNase H type-2.
+At position 55 to 93, the domain is characterized as Collagen-like.
+At position 109 to 326, the domain is characterized as Fibrinogen C-terminal.
+At position 1683 to 1778, the domain is characterized as RAMA.
+At position 24 to 103, the domain is characterized as IGFBP N-terminal.
+At position 98 to 164, the domain is characterized as VWFC.
+At position 194 to 238, the domain is characterized as TSP type-1.
+At position 15 to 187, the domain is characterized as uDENN.
+At position 214 to 362, the domain is characterized as cDENN.
+At position 364 to 455, the domain is characterized as dDENN.
+At position 2 to 59, the domain is characterized as HTH lysR-type.
+At position 349 to 401, the domain is characterized as FBD.
+At position 4 to 196, the domain is characterized as HORMA.
+At position 5 to 101, the domain is characterized as Glutaredoxin.
+At position 47 to 129, the domain is characterized as Ig-like C2-type 1.
+At position 130 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 35 to 205, the domain is characterized as Helicase ATP-binding.
+At position 226 to 382, the domain is characterized as Helicase C-terminal.
+At position 9 to 138, the domain is characterized as VHS.
+At position 180 to 268, the domain is characterized as GAT.
+At position 954 to 972, the domain is characterized as WH2.
+At position 3 to 88, the domain is characterized as PB1.
+At position 550 to 595, the domain is characterized as UBA.
+At position 38 to 140, the domain is characterized as HPt.
+At position 48 to 95, the domain is characterized as F-box.
+At position 117 to 297, the domain is characterized as FBA.
+At position 314 to 592, the domain is characterized as ABC transporter 1.
+At position 612 to 941, the domain is characterized as ABC transporter 2.
+At position 454 to 493, the domain is characterized as Pentapeptide repeat 1.
+At position 504 to 543, the domain is characterized as Pentapeptide repeat 2.
+At position 132 to 417, the domain is characterized as Protein kinase.
+At position 14 to 113, the domain is characterized as EH 1.
+At position 47 to 82, the domain is characterized as EF-hand 1.
+At position 135 to 227, the domain is characterized as EH 2.
+At position 167 to 202, the domain is characterized as EF-hand 2.
+At position 276 to 311, the domain is characterized as EF-hand 3.
+At position 277 to 366, the domain is characterized as EH 3.
+At position 1338 to 1380, the domain is characterized as UBA.
+At position 10 to 51, the domain is characterized as JmjN.
+At position 75 to 165, the domain is characterized as ARID.
+At position 428 to 594, the domain is characterized as JmjC.
+At position 481 to 577, the domain is characterized as Fibronectin type-III.
+At position 566 to 777, the domain is characterized as ATP-grasp.
+At position 70 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 24 to 124, the domain is characterized as Phytocyanin.
+At position 47 to 353, the domain is characterized as Velvet.
+At position 72 to 182, the domain is characterized as Expansin-like EG45.
+At position 192 to 271, the domain is characterized as Expansin-like CBD.
+At position 1 to 87, the domain is characterized as Pyrin.
+At position 219 to 393, the domain is characterized as HIN-200.
+At position 185 to 258, the domain is characterized as SEP.
+At position 292 to 369, the domain is characterized as UBX.
+At position 199 to 374, the domain is characterized as EngA-type G 2.
+At position 375 to 461, the domain is characterized as KH-like.
+At position 27 to 111, the domain is characterized as BTB.
+At position 21 to 102, the domain is characterized as ACT.
+At position 309 to 401, the domain is characterized as ARID.
+At position 576 to 628, the domain is characterized as Tudor-knot.
+At position 1 to 66, the domain is characterized as HYR 1.
+At position 67 to 150, the domain is characterized as HYR 2.
+At position 151 to 234, the domain is characterized as HYR 3.
+At position 235 to 319, the domain is characterized as HYR 4.
+At position 320 to 403, the domain is characterized as HYR 5.
+At position 404 to 486, the domain is characterized as HYR 6.
+At position 487 to 530, the domain is characterized as HYR 7.
+At position 125 to 223, the domain is characterized as Ricin B-type lectin.
+At position 172 to 281, the domain is characterized as Fibronectin type-III 1.
+At position 392 to 486, the domain is characterized as Fibronectin type-III 2.
+At position 9 to 90, the domain is characterized as Cytochrome b5 heme-binding.
+At position 415 to 695, the domain is characterized as Protein kinase.
+At position 64 to 246, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 89, the domain is characterized as J.
+At position 93 to 400, the domain is characterized as Protein kinase.
+At position 12 to 141, the domain is characterized as CRESS-DNA virus Rep endonuclease.
+At position 368 to 640, the domain is characterized as Clu.
+At position 2 to 135, the domain is characterized as Toprim.
+At position 122 to 304, the domain is characterized as DH.
+At position 291 to 449, the domain is characterized as PH.
+At position 202 to 300, the domain is characterized as HTH araC/xylS-type.
+At position 325 to 364, the domain is characterized as LRRCT.
+At position 2 to 44, the domain is characterized as UBA-like.
+At position 198 to 217, the domain is characterized as UIM 1.
+At position 230 to 249, the domain is characterized as UIM 2.
+At position 482 to 560, the domain is characterized as UBX.
+At position 407 to 685, the domain is characterized as Rab-GAP TBC.
+At position 396 to 477, the domain is characterized as Disintegrin.
+At position 4 to 423, the domain is characterized as SAM-dependent MTase C5-type.
+At position 21 to 98, the domain is characterized as Ig-like C2-type 1.
+At position 99 to 182, the domain is characterized as Ig-like C2-type 2.
+At position 192 to 270, the domain is characterized as Ig-like C2-type 3.
+At position 284 to 369, the domain is characterized as Ig-like C2-type 4.
+At position 383 to 470, the domain is characterized as Ig-like C2-type 5.
+At position 476 to 563, the domain is characterized as Ig-like C2-type 6.
+At position 553 to 617, the domain is characterized as FHA.
+At position 182 to 322, the domain is characterized as Helicase ATP-binding.
+At position 341 to 506, the domain is characterized as Helicase C-terminal.
+At position 72 to 168, the domain is characterized as Fibronectin type-III.
+At position 283 to 498, the domain is characterized as B30.2/SPRY.
+At position 216 to 395, the domain is characterized as GAF.
+At position 610 to 681, the domain is characterized as PAS 1.
+At position 744 to 815, the domain is characterized as PAS 2.
+At position 895 to 1115, the domain is characterized as Histidine kinase.
+At position 5 to 88, the domain is characterized as Toprim.
+At position 50 to 137, the domain is characterized as ENT.
+At position 129 to 314, the domain is characterized as ATP-grasp.
+At position 354 to 420, the domain is characterized as S4 RNA-binding.
+At position 316 to 513, the domain is characterized as PCI.
+At position 51 to 132, the domain is characterized as Sm.
+At position 577 to 679, the domain is characterized as tRNA-binding.
+At position 24 to 100, the domain is characterized as Cytochrome b5 heme-binding.
+At position 39 to 170, the domain is characterized as Ig-like C2-type 1.
+At position 379 to 470, the domain is characterized as Fibronectin type-III 1.
+At position 587 to 678, the domain is characterized as Fibronectin type-III 2.
+At position 682 to 724, the domain is characterized as WR1.
+At position 827 to 914, the domain is characterized as Fibronectin type-III 3.
+At position 924 to 1020, the domain is characterized as Fibronectin type-III 4.
+At position 1116 to 1207, the domain is characterized as Ig-like C2-type 2.
+At position 1314 to 1406, the domain is characterized as Fibronectin type-III 5.
+At position 195 to 370, the domain is characterized as EngA-type G 2.
+At position 371 to 456, the domain is characterized as KH-like.
+At position 192 to 462, the domain is characterized as F-BAR.
+At position 671 to 886, the domain is characterized as Rho-GAP.
+At position 283 to 452, the domain is characterized as tr-type G.
+At position 96 to 172, the domain is characterized as PAS.
+At position 210 to 425, the domain is characterized as Histidine kinase.
+At position 103 to 183, the domain is characterized as RRM 1.
+At position 242 to 326, the domain is characterized as RRM 2.
+At position 766 to 812, the domain is characterized as G-patch.
+At position 115 to 305, the domain is characterized as ATP-grasp.
+At position 584 to 856, the domain is characterized as Protein kinase.
+At position 347 to 413, the domain is characterized as S4 RNA-binding.
+At position 38 to 214, the domain is characterized as Helicase ATP-binding.
+At position 230 to 393, the domain is characterized as Helicase C-terminal.
+At position 28 to 66, the domain is characterized as CHCH.
+At position 32 to 188, the domain is characterized as N-acetyltransferase.
+At position 14 to 304, the domain is characterized as Protein kinase.
+At position 99 to 164, the domain is characterized as J.
+At position 206 to 597, the domain is characterized as SEC63.
+At position 1883 to 1980, the domain is characterized as BEACH-type PH.
+At position 1992 to 2284, the domain is characterized as BEACH.
+At position 77 to 390, the domain is characterized as IF rod.
+At position 33 to 238, the domain is characterized as Cupin type-1 1.
+At position 313 to 462, the domain is characterized as Cupin type-1 2.
+At position 145 to 229, the domain is characterized as Bulb-type lectin 2.
+At position 13 to 256, the domain is characterized as ABC transporter.
+At position 7 to 227, the domain is characterized as ABC transporter.
+At position 41 to 271, the domain is characterized as Radical SAM core.
+At position 63 to 231, the domain is characterized as Helicase ATP-binding.
+At position 263 to 442, the domain is characterized as Helicase C-terminal.
+At position 23 to 212, the domain is characterized as RNase H type-2.
+At position 26 to 169, the domain is characterized as F5/8 type C.
+At position 204 to 356, the domain is characterized as Laminin G-like 1.
+At position 390 to 539, the domain is characterized as Laminin G-like 2.
+At position 545 to 577, the domain is characterized as EGF-like 1.
+At position 577 to 796, the domain is characterized as Fibrinogen C-terminal.
+At position 814 to 958, the domain is characterized as Laminin G-like 3.
+At position 1089 to 1251, the domain is characterized as Laminin G-like 4.
+At position 420 to 633, the domain is characterized as FtsK.
+At position 117 to 142, the domain is characterized as EF-hand 4.
+At position 10 to 100, the domain is characterized as RH1.
+At position 219 to 295, the domain is characterized as RH2.
+At position 913 to 1068, the domain is characterized as ZU5 1.
+At position 1070 to 1216, the domain is characterized as ZU5 2.
+At position 1403 to 1487, the domain is characterized as Death.
+At position 82 to 329, the domain is characterized as Deacetylase sirtuin-type.
+At position 1 to 33, the domain is characterized as EF-hand 1.
+At position 35 to 70, the domain is characterized as EF-hand 2.
+At position 49 to 358, the domain is characterized as AB hydrolase-1.
+At position 16 to 116, the domain is characterized as PilZ.
+At position 6 to 250, the domain is characterized as ABC transporter.
+At position 72 to 329, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 329 to 570, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 147 to 304, the domain is characterized as CRAL-TRIO.
+At position 3 to 113, the domain is characterized as MTTase N-terminal.
+At position 130 to 367, the domain is characterized as Radical SAM core.
+At position 6 to 147, the domain is characterized as Clp R.
+At position 99 to 128, the domain is characterized as KOW.
+At position 350 to 589, the domain is characterized as Histidine kinase.
+At position 615 to 732, the domain is characterized as Response regulatory.
+At position 1 to 56, the domain is characterized as HTH deoR-type.
+At position 19 to 84, the domain is characterized as J.
+At position 230 to 282, the domain is characterized as bHLH.
+At position 140 to 216, the domain is characterized as Toprim.
+At position 464 to 903, the domain is characterized as Hexokinase 2.
+At position 27 to 145, the domain is characterized as C2.
+At position 304 to 855, the domain is characterized as PLA2c.
+At position 145 to 459, the domain is characterized as IF rod.
+At position 11 to 132, the domain is characterized as C-type lectin.
+At position 49 to 178, the domain is characterized as MsrB.
+At position 65 to 189, the domain is characterized as OTU.
+At position 230 to 270, the domain is characterized as UBA-like.
+At position 399 to 433, the domain is characterized as SAP.
+At position 20 to 101, the domain is characterized as Lipoyl-binding.
+At position 2 to 116, the domain is characterized as MTTase N-terminal.
+At position 135 to 368, the domain is characterized as Radical SAM core.
+At position 371 to 437, the domain is characterized as TRAM.
+At position 20 to 171, the domain is characterized as MARVEL.
+At position 1 to 309, the domain is characterized as RanBD1.
+At position 143 to 372, the domain is characterized as Sigma-54 factor interaction.
+At position 2 to 45, the domain is characterized as WAP 1.
+At position 46 to 89, the domain is characterized as WAP 2.
+At position 90 to 132, the domain is characterized as WAP 3.
+At position 106 to 300, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 496 to 771, the domain is characterized as Protein kinase.
+At position 750 to 833, the domain is characterized as BRCT.
+At position 1 to 52, the domain is characterized as RRM 1.
+At position 60 to 139, the domain is characterized as RRM 2.
+At position 46 to 183, the domain is characterized as Nudix hydrolase.
+At position 209 to 434, the domain is characterized as MIF4G.
+At position 4 to 167, the domain is characterized as DHFR.
+At position 171 to 256, the domain is characterized as PPIase FKBP-type.
+At position 92 to 213, the domain is characterized as B12-binding.
+At position 342 to 443, the domain is characterized as Rhodanese.
+At position 123 to 504, the domain is characterized as Protein kinase.
+At position 19 to 97, the domain is characterized as GIY-YIG.
+At position 105 to 285, the domain is characterized as Prephenate dehydratase.
+At position 299 to 376, the domain is characterized as ACT.
+At position 91 to 259, the domain is characterized as TNase-like.
+At position 546 to 837, the domain is characterized as Protein kinase.
+At position 901 to 1031, the domain is characterized as Guanylate cyclase.
+At position 41 to 721, the domain is characterized as Myosin motor.
+At position 725 to 745, the domain is characterized as IQ 1.
+At position 746 to 771, the domain is characterized as IQ 2.
+At position 779 to 969, the domain is characterized as TH1.
+At position 1067 to 1125, the domain is characterized as SH3.
+At position 35 to 259, the domain is characterized as ABC transporter.
+At position 87 to 130, the domain is characterized as HTH myb-type 1.
+At position 131 to 186, the domain is characterized as HTH myb-type 2.
+At position 187 to 237, the domain is characterized as HTH myb-type 3.
+At position 137 to 231, the domain is characterized as BRICHOS.
+At position 44 to 321, the domain is characterized as tr-type G.
+At position 51 to 299, the domain is characterized as ABC transporter 1.
+At position 721 to 963, the domain is characterized as ABC transporter 2.
+At position 16 to 68, the domain is characterized as HTH myb-type 1.
+At position 69 to 123, the domain is characterized as HTH myb-type 2.
+At position 216 to 514, the domain is characterized as NR LBD.
+At position 2 to 89, the domain is characterized as RH1.
+At position 282 to 347, the domain is characterized as RH2.
+At position 1778 to 1887, the domain is characterized as PH.
+At position 132 to 369, the domain is characterized as Radical SAM core.
+At position 244 to 304, the domain is characterized as SH3.
+At position 611 to 672, the domain is characterized as SAM.
+At position 51 to 132, the domain is characterized as SCAN box.
+At position 218 to 291, the domain is characterized as KRAB.
+At position 4 to 86, the domain is characterized as PB1.
+At position 930 to 974, the domain is characterized as UBA.
+At position 60 to 281, the domain is characterized as Radical SAM core.
+At position 1 to 245, the domain is characterized as Deacetylase sirtuin-type.
+At position 27 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 26 to 321, the domain is characterized as Protein kinase.
+At position 40 to 159, the domain is characterized as Inhibitor I9.
+At position 164 to 709, the domain is characterized as Peptidase S8.
+At position 432 to 528, the domain is characterized as PA.
+At position 16 to 243, the domain is characterized as Peptidase S1.
+At position 362 to 427, the domain is characterized as S4 RNA-binding.
+At position 113 to 191, the domain is characterized as RRM.
+At position 94 to 314, the domain is characterized as SET.
+At position 46 to 113, the domain is characterized as BTB.
+At position 148 to 250, the domain is characterized as BACK.
+At position 358 to 633, the domain is characterized as Protein kinase.
+At position 9 to 124, the domain is characterized as VOC 1.
+At position 149 to 270, the domain is characterized as VOC 2.
+At position 152 to 196, the domain is characterized as CHCH.
+At position 408 to 687, the domain is characterized as Protein kinase.
+At position 427 to 583, the domain is characterized as Exonuclease.
+At position 69 to 217, the domain is characterized as HD.
+At position 29 to 77, the domain is characterized as WAP 1.
+At position 83 to 131, the domain is characterized as WAP 2.
+At position 25 to 80, the domain is characterized as LCN-type CS-alpha/beta.
+At position 418 to 489, the domain is characterized as MBD.
+At position 701 to 766, the domain is characterized as DDT.
+At position 1602 to 1672, the domain is characterized as Bromo.
+At position 344 to 616, the domain is characterized as Protein kinase.
+At position 28 to 133, the domain is characterized as Gnk2-homologous.
+At position 26 to 246, the domain is characterized as ABC transporter.
+At position 782 to 1354, the domain is characterized as GBD/FH3.
+At position 1956 to 2077, the domain is characterized as N-terminal Ras-GEF.
+At position 2112 to 2351, the domain is characterized as Ras-GEF.
+At position 98 to 148, the domain is characterized as F-box.
+At position 21 to 472, the domain is characterized as Sema.
+At position 474 to 523, the domain is characterized as PSI.
+At position 518 to 604, the domain is characterized as Ig-like.
+At position 238 to 313, the domain is characterized as PUA.
+At position 15 to 62, the domain is characterized as SpoVT-AbrB 1.
+At position 470 to 637, the domain is characterized as tr-type G.
+At position 9 to 204, the domain is characterized as Lon N-terminal.
+At position 596 to 777, the domain is characterized as Lon proteolytic.
+At position 40 to 225, the domain is characterized as Tyr recombinase.
+At position 238 to 431, the domain is characterized as GATase cobBQ-type.
+At position 11 to 198, the domain is characterized as RNase H type-2.
+At position 223 to 382, the domain is characterized as TrmE-type G.
+At position 10 to 454, the domain is characterized as Hexokinase.
+At position 24 to 312, the domain is characterized as Protein kinase.
+At position 14 to 207, the domain is characterized as HD Cas3-type.
+At position 274 to 480, the domain is characterized as Helicase ATP-binding.
+At position 47 to 152, the domain is characterized as FAD-binding FR-type.
+At position 179 to 366, the domain is characterized as Helicase ATP-binding.
+At position 397 to 584, the domain is characterized as Helicase C-terminal.
+At position 484 to 614, the domain is characterized as Ricin B-type lectin.
+At position 128 to 348, the domain is characterized as Radical SAM core.
+At position 109 to 209, the domain is characterized as S1 motif 1.
+At position 226 to 289, the domain is characterized as S1 motif 2.
+At position 306 to 376, the domain is characterized as S1 motif 3.
+At position 398 to 473, the domain is characterized as S1 motif 4.
+At position 490 to 559, the domain is characterized as S1 motif 5.
+At position 579 to 648, the domain is characterized as S1 motif 6.
+At position 666 to 739, the domain is characterized as S1 motif 7.
+At position 761 to 830, the domain is characterized as S1 motif 8.
+At position 866 to 942, the domain is characterized as S1 motif 9.
+At position 973 to 1044, the domain is characterized as S1 motif 10.
+At position 1053 to 1122, the domain is characterized as S1 motif 11.
+At position 1147 to 1216, the domain is characterized as S1 motif 12.
+At position 1236 to 1307, the domain is characterized as S1 motif 13.
+At position 346 to 407, the domain is characterized as S4 RNA-binding.
+At position 177 to 430, the domain is characterized as PI3K/PI4K catalytic.
+At position 250 to 448, the domain is characterized as GATase cobBQ-type.
+At position 551 to 580, the domain is characterized as IQ 1.
+At position 971 to 1000, the domain is characterized as IQ 2.
+At position 9 to 336, the domain is characterized as Kinesin motor.
+At position 40 to 114, the domain is characterized as U-box.
+At position 321 to 475, the domain is characterized as PPIase cyclophilin-type.
+At position 74 to 385, the domain is characterized as Peptidase A1.
+At position 65 to 181, the domain is characterized as RGS.
+At position 33 to 113, the domain is characterized as IGFBP N-terminal.
+At position 98 to 157, the domain is characterized as Kazal-like.
+At position 365 to 467, the domain is characterized as PDZ.
+At position 3 to 263, the domain is characterized as Pyruvate carboxyltransferase.
+At position 523 to 596, the domain is characterized as Biotinyl-binding.
+At position 39 to 328, the domain is characterized as Protein kinase.
+At position 99 to 336, the domain is characterized as Radical SAM core.
+At position 7 to 175, the domain is characterized as PPIase cyclophilin-type.
+At position 173 to 260, the domain is characterized as PPIase FKBP-type.
+At position 272 to 470, the domain is characterized as B30.2/SPRY.
+At position 706 to 896, the domain is characterized as ATP-grasp 2.
+At position 965 to 1106, the domain is characterized as MGS-like.
+At position 171 to 457, the domain is characterized as ABC transmembrane type-1.
+At position 492 to 731, the domain is characterized as ABC transporter.
+At position 24 to 201, the domain is characterized as Chitin-binding type-4.
+At position 437 to 478, the domain is characterized as Chitin-binding type-3.
+At position 1316 to 1639, the domain is characterized as PIPK.
+At position 15 to 98, the domain is characterized as GST N-terminal.
+At position 104 to 237, the domain is characterized as GST C-terminal.
+At position 362 to 434, the domain is characterized as PAS.
+At position 13 to 153, the domain is characterized as Nudix hydrolase.
+At position 43 to 291, the domain is characterized as Peptidase S1.
+At position 593 to 674, the domain is characterized as BRCT.
+At position 4 to 52, the domain is characterized as F-box.
+At position 13 to 202, the domain is characterized as RNase H type-2.
+At position 636 to 671, the domain is characterized as UVR.
+At position 9 to 296, the domain is characterized as tr-type G.
+At position 271 to 347, the domain is characterized as B5.
+At position 225 to 284, the domain is characterized as SH3.
+At position 22 to 131, the domain is characterized as Ig-like V-type.
+At position 300 to 451, the domain is characterized as Helicase C-terminal.
+At position 89 to 170, the domain is characterized as PUA.
+At position 362 to 447, the domain is characterized as SWIB/MDM2.
+At position 475 to 547, the domain is characterized as SUI1.
+At position 105 to 341, the domain is characterized as Radical SAM core.
+At position 2 to 248, the domain is characterized as Radical SAM core.
+At position 419 to 533, the domain is characterized as Toprim.
+At position 52 to 90, the domain is characterized as EGF-like 1; calcium-binding.
+At position 102 to 139, the domain is characterized as EGF-like 2; calcium-binding.
+At position 404 to 454, the domain is characterized as GPS.
+At position 38 to 161, the domain is characterized as Ricin B-type lectin.
+At position 238 to 355, the domain is characterized as C-type lectin 1.
+At position 385 to 502, the domain is characterized as C-type lectin 2.
+At position 522 to 643, the domain is characterized as C-type lectin 3.
+At position 673 to 797, the domain is characterized as C-type lectin 4.
+At position 819 to 938, the domain is characterized as C-type lectin 5.
+At position 965 to 1096, the domain is characterized as C-type lectin 6.
+At position 1121 to 1232, the domain is characterized as C-type lectin 7.
+At position 1257 to 1378, the domain is characterized as C-type lectin 8.
+At position 1 to 58, the domain is characterized as HTH tetR-type.
+At position 4 to 163, the domain is characterized as N-acetyltransferase.
+At position 52 to 108, the domain is characterized as Myb-like.
+At position 31 to 210, the domain is characterized as Helicase ATP-binding.
+At position 380 to 544, the domain is characterized as Helicase C-terminal.
+At position 559 to 645, the domain is characterized as Dicer dsRNA-binding fold.
+At position 805 to 935, the domain is characterized as PAZ.
+At position 962 to 1113, the domain is characterized as RNase III 1.
+At position 1149 to 1296, the domain is characterized as RNase III 2.
+At position 1315 to 1384, the domain is characterized as DRBM.
+At position 129 to 269, the domain is characterized as Fatty acid hydroxylase.
+At position 229 to 307, the domain is characterized as RRM 1.
+At position 319 to 398, the domain is characterized as RRM 2.
+At position 30 to 286, the domain is characterized as AB hydrolase-1.
+At position 136 to 510, the domain is characterized as GRAS.
+At position 12 to 130, the domain is characterized as NERD.
+At position 195 to 490, the domain is characterized as Protein kinase 1.
+At position 530 to 816, the domain is characterized as Protein kinase 2.
+At position 430 to 574, the domain is characterized as Thioredoxin.
+At position 1 to 94, the domain is characterized as TsaA-like.
+At position 1 to 45, the domain is characterized as SpoVT-AbrB.
+At position 1 to 232, the domain is characterized as SMP-LTD.
+At position 45 to 271, the domain is characterized as Radical SAM core.
+At position 100 to 135, the domain is characterized as EF-hand 3.
+At position 192 to 227, the domain is characterized as EF-hand 5.
+At position 235 to 271, the domain is characterized as EF-hand 6.
+At position 15 to 272, the domain is characterized as Pterin-binding.
+At position 642 to 723, the domain is characterized as S1 motif.
+At position 21 to 85, the domain is characterized as LCN-type CS-alpha/beta.
+At position 191 to 238, the domain is characterized as F-box.
+At position 135 to 281, the domain is characterized as RNase H type-1.
+At position 64 to 116, the domain is characterized as bHLH.
+At position 280 to 322, the domain is characterized as CCT.
+At position 1 to 185, the domain is characterized as Peptidase S1.
+At position 1379 to 1672, the domain is characterized as Autotransporter.
+At position 468 to 683, the domain is characterized as Histidine kinase.
+At position 722 to 835, the domain is characterized as Response regulatory.
+At position 1349 to 1901, the domain is characterized as FAT.
+At position 2005 to 2308, the domain is characterized as PI3K/PI4K catalytic.
+At position 2292 to 2324, the domain is characterized as FATC.
+At position 1 to 237, the domain is characterized as EAL.
+At position 320 to 394, the domain is characterized as ACT 1.
+At position 401 to 478, the domain is characterized as ACT 2.
+At position 289 to 352, the domain is characterized as LRRCT.
+At position 26 to 229, the domain is characterized as DHFR.
+At position 357 to 639, the domain is characterized as Protein kinase.
+At position 62 to 168, the domain is characterized as Expansin-like EG45.
+At position 181 to 262, the domain is characterized as Expansin-like CBD.
+At position 128 to 146, the domain is characterized as LRRCT.
+At position 303 to 395, the domain is characterized as CS.
+At position 27 to 267, the domain is characterized as Deacetylase sirtuin-type.
+At position 283 to 448, the domain is characterized as Helicase ATP-binding.
+At position 482 to 628, the domain is characterized as Helicase C-terminal.
+At position 5 to 242, the domain is characterized as ABC transporter.
+At position 36 to 113, the domain is characterized as GST N-terminal.
+At position 115 to 235, the domain is characterized as GST C-terminal.
+At position 40 to 182, the domain is characterized as RUN.
+At position 551 to 642, the domain is characterized as PH 1.
+At position 701 to 795, the domain is characterized as PH 2.
+At position 1 to 148, the domain is characterized as MGS-like.
+At position 79 to 267, the domain is characterized as BPL/LPL catalytic.
+At position 33 to 109, the domain is characterized as REM-1 1.
+At position 121 to 204, the domain is characterized as REM-1 2.
+At position 207 to 286, the domain is characterized as REM-1 3.
+At position 354 to 474, the domain is characterized as C2.
+At position 658 to 917, the domain is characterized as Protein kinase.
+At position 918 to 985, the domain is characterized as AGC-kinase C-terminal.
+At position 216 to 366, the domain is characterized as C-CAP/cofactor C-like.
+At position 3 to 188, the domain is characterized as UmuC.
+At position 57 to 280, the domain is characterized as Peptidase S1.
+At position 12 to 260, the domain is characterized as Pterin-binding.
+At position 88 to 406, the domain is characterized as FERM.
+At position 2205 to 2375, the domain is characterized as I/LWEQ.
+At position 1 to 21, the domain is characterized as PARP alpha-helical.
+At position 30 to 135, the domain is characterized as PARP catalytic.
+At position 160 to 329, the domain is characterized as OBG-type G.
+At position 355 to 433, the domain is characterized as OCT.
+At position 27 to 132, the domain is characterized as Thioredoxin.
+At position 364 to 446, the domain is characterized as PDZ.
+At position 55 to 167, the domain is characterized as Expansin-like EG45.
+At position 9 to 235, the domain is characterized as Radical SAM core.
+At position 3 to 106, the domain is characterized as PTS EIIB type-3.
+At position 28 to 206, the domain is characterized as Eph LBD.
+At position 588 to 671, the domain is characterized as BRCT.
+At position 594 to 700, the domain is characterized as tRNA-binding.
+At position 310 to 631, the domain is characterized as Protein kinase.
+At position 632 to 717, the domain is characterized as AGC-kinase C-terminal.
+At position 146 to 953, the domain is characterized as Myosin motor.
+At position 957 to 977, the domain is characterized as IQ 1.
+At position 979 to 1000, the domain is characterized as IQ 2.
+At position 1001 to 1023, the domain is characterized as IQ 3.
+At position 1024 to 1053, the domain is characterized as IQ 4.
+At position 1661 to 1846, the domain is characterized as Rho-GAP.
+At position 58 to 313, the domain is characterized as Protein kinase.
+At position 10 to 75, the domain is characterized as NAC-A/B.
+At position 120 to 159, the domain is characterized as UBA.
+At position 641 to 721, the domain is characterized as BRCT.
+At position 6 to 252, the domain is characterized as ABC transporter.
+At position 410 to 510, the domain is characterized as Tudor; atypical.
+At position 11 to 86, the domain is characterized as HTH HARE-type.
+At position 274 to 383, the domain is characterized as DEUBAD.
+At position 26 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 215 to 333, the domain is characterized as Nop.
+At position 37 to 172, the domain is characterized as Nudix hydrolase.
+At position 158 to 346, the domain is characterized as CP-type G.
+At position 144 to 253, the domain is characterized as CUB 1.
+At position 259 to 295, the domain is characterized as LDL-receptor class A 1.
+At position 301 to 414, the domain is characterized as CUB 2.
+At position 420 to 455, the domain is characterized as LDL-receptor class A 2.
+At position 461 to 579, the domain is characterized as FZ.
+At position 13 to 269, the domain is characterized as Protein kinase.
+At position 279 to 347, the domain is characterized as MIT 1.
+At position 374 to 442, the domain is characterized as MIT 2.
+At position 2 to 62, the domain is characterized as Kazal-like 1.
+At position 63 to 112, the domain is characterized as Kazal-like 2.
+At position 15 to 77, the domain is characterized as t-SNARE coiled-coil homology.
+At position 109 to 308, the domain is characterized as MAGE.
+At position 127 to 177, the domain is characterized as DHHC.
+At position 25 to 188, the domain is characterized as EngA-type G 1.
+At position 372 to 454, the domain is characterized as KH-like.
+At position 22 to 156, the domain is characterized as Nudix hydrolase.
+At position 1332 to 1492, the domain is characterized as NIDO.
+At position 1609 to 1804, the domain is characterized as VWFD.
+At position 2047 to 2086, the domain is characterized as EGF-like 1.
+At position 2256 to 2295, the domain is characterized as EGF-like 2.
+At position 62 to 116, the domain is characterized as bHLH.
+At position 2 to 99, the domain is characterized as FAD-binding FR-type.
+At position 30 to 213, the domain is characterized as DH.
+At position 254 to 455, the domain is characterized as BAR.
+At position 506 to 569, the domain is characterized as SH3 1.
+At position 603 to 666, the domain is characterized as SH3 2.
+At position 4 to 110, the domain is characterized as SSB.
+At position 52 to 230, the domain is characterized as FAD-binding PCMH-type.
+At position 453 to 508, the domain is characterized as Kazal-like.
+At position 93 to 152, the domain is characterized as Chromo 1.
+At position 332 to 396, the domain is characterized as Chromo 2; shadow subtype.
+At position 10 to 108, the domain is characterized as Rieske.
+At position 2 to 291, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 296 to 363, the domain is characterized as ACT.
+At position 111 to 151, the domain is characterized as CHCH.
+At position 24 to 500, the domain is characterized as Sema.
+At position 502 to 551, the domain is characterized as PSI.
+At position 555 to 636, the domain is characterized as Ig-like C2-type.
+At position 207 to 363, the domain is characterized as Helicase ATP-binding.
+At position 441 to 642, the domain is characterized as Helicase C-terminal.
+At position 97 to 171, the domain is characterized as PRC barrel.
+At position 259 to 294, the domain is characterized as DMA.
+At position 582 to 690, the domain is characterized as tRNA-binding.
+At position 19 to 205, the domain is characterized as Albumin 1.
+At position 206 to 398, the domain is characterized as Albumin 2.
+At position 402 to 600, the domain is characterized as Albumin 3.
+At position 356 to 435, the domain is characterized as ACT.
+At position 301 to 511, the domain is characterized as Ras-GAP.
+At position 565 to 672, the domain is characterized as PH.
+At position 6 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 35 to 131, the domain is characterized as Plastocyanin-like.
+At position 1 to 61, the domain is characterized as HTH myb-type.
+At position 100 to 296, the domain is characterized as Peptidase M12B.
+At position 304 to 390, the domain is characterized as Disintegrin.
+At position 22 to 78, the domain is characterized as F-box.
+At position 4 to 54, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 5 to 80, the domain is characterized as TFIIS N-terminal.
+At position 594 to 658, the domain is characterized as SH2.
+At position 898 to 1010, the domain is characterized as VRR-NUC.
+At position 23 to 305, the domain is characterized as Protein kinase.
+At position 27 to 124, the domain is characterized as Yippee.
+At position 1 to 242, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 18 to 97, the domain is characterized as GIY-YIG.
+At position 5 to 131, the domain is characterized as MATH.
+At position 10 to 409, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 969 to 1292, the domain is characterized as PKS/mFAS DH.
+At position 2527 to 2604, the domain is characterized as Carrier.
+At position 44 to 374, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 7 to 133, the domain is characterized as RabBD.
+At position 643 to 733, the domain is characterized as PDZ.
+At position 840 to 962, the domain is characterized as C2 1.
+At position 1417 to 1536, the domain is characterized as C2 2.
+At position 917 to 975, the domain is characterized as KASH.
+At position 391 to 464, the domain is characterized as bZIP.
+At position 15 to 98, the domain is characterized as PB1.
+At position 252 to 518, the domain is characterized as Protein kinase.
+At position 519 to 590, the domain is characterized as AGC-kinase C-terminal.
+At position 77 to 202, the domain is characterized as Nudix hydrolase.
+At position 132 to 182, the domain is characterized as DHHC.
+At position 161 to 190, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 644 to 686, the domain is characterized as CAP-Gly 3.
+At position 20 to 116, the domain is characterized as Ig-like.
+At position 6 to 65, the domain is characterized as SH3.
+At position 93 to 273, the domain is characterized as DH.
+At position 295 to 400, the domain is characterized as PH.
+At position 796 to 864, the domain is characterized as SAM.
+At position 576 to 850, the domain is characterized as Protein kinase.
+At position 359 to 460, the domain is characterized as Fibronectin type-III 1.
+At position 514 to 604, the domain is characterized as Fibronectin type-III 2.
+At position 606 to 716, the domain is characterized as Fibronectin type-III 3.
+At position 25 to 260, the domain is characterized as ABC transporter.
+At position 15 to 277, the domain is characterized as Pyruvate carboxyltransferase.
+At position 234 to 281, the domain is characterized as EGF-like 1.
+At position 282 to 328, the domain is characterized as EGF-like 2; calcium-binding.
+At position 409 to 692, the domain is characterized as Protein kinase.
+At position 12 to 265, the domain is characterized as ABC transporter.
+At position 1 to 137, the domain is characterized as B12-binding.
+At position 169 to 409, the domain is characterized as Radical SAM core.
+At position 797 to 885, the domain is characterized as PKD.
+At position 170 to 421, the domain is characterized as Protein kinase.
+At position 440 to 482, the domain is characterized as UBA.
+At position 1143 to 1192, the domain is characterized as KA1.
+At position 484 to 600, the domain is characterized as MaoC-like.
+At position 624 to 736, the domain is characterized as SCP2.
+At position 339 to 523, the domain is characterized as PCI.
+At position 213 to 386, the domain is characterized as EngA-type G 2.
+At position 387 to 471, the domain is characterized as KH-like.
+At position 21 to 349, the domain is characterized as Enoyl reductase (ER).
+At position 66 to 157, the domain is characterized as ABM.
+At position 14 to 197, the domain is characterized as HORMA.
+At position 375 to 514, the domain is characterized as SIS 1.
+At position 546 to 687, the domain is characterized as SIS 2.
+At position 41 to 69, the domain is characterized as EF-hand 1.
+At position 71 to 106, the domain is characterized as EF-hand 2.
+At position 88 to 161, the domain is characterized as J.
+At position 449 to 511, the domain is characterized as SANT 1.
+At position 549 to 604, the domain is characterized as SANT 2.
+At position 27 to 264, the domain is characterized as Peptidase S1.
+At position 1 to 70, the domain is characterized as Ubiquitin-like.
+At position 5 to 260, the domain is characterized as ABC transporter.
+At position 930 to 1065, the domain is characterized as MGS-like.
+At position 58 to 159, the domain is characterized as SRCR 1.
+At position 188 to 302, the domain is characterized as SRCR 2.
+At position 326 to 425, the domain is characterized as SRCR 3.
+At position 435 to 544, the domain is characterized as SRCR 4.
+At position 30 to 206, the domain is characterized as BPL/LPL catalytic.
+At position 7 to 204, the domain is characterized as tr-type G.
+At position 662 to 741, the domain is characterized as Carrier.
+At position 83 to 134, the domain is characterized as bHLH.
+At position 12 to 76, the domain is characterized as J.
+At position 309 to 419, the domain is characterized as SH2.
+At position 112 to 268, the domain is characterized as CP-type G.
+At position 557 to 717, the domain is characterized as SSD.
+At position 1 to 40, the domain is characterized as Biotin carboxylation.
+At position 13 to 27, the domain is characterized as ATP-grasp.
+At position 48 to 158, the domain is characterized as Cytochrome c 1.
+At position 201 to 346, the domain is characterized as Cytochrome c 2.
+At position 193 to 388, the domain is characterized as Peptidase M12B.
+At position 396 to 482, the domain is characterized as Disintegrin.
+At position 72 to 151, the domain is characterized as PDZ.
+At position 367 to 558, the domain is characterized as RGSL.
+At position 787 to 977, the domain is characterized as DH.
+At position 1019 to 1132, the domain is characterized as PH.
+At position 78 to 141, the domain is characterized as bZIP.
+At position 201 to 511, the domain is characterized as Protein kinase.
+At position 1 to 139, the domain is characterized as YEATS.
+At position 217 to 408, the domain is characterized as Helicase ATP-binding.
+At position 419 to 579, the domain is characterized as Helicase C-terminal.
+At position 1 to 703, the domain is characterized as GH81.
+At position 864 to 1009, the domain is characterized as TIR.
+At position 2 to 223, the domain is characterized as Radical SAM core.
+At position 27 to 165, the domain is characterized as Thioredoxin.
+At position 35 to 298, the domain is characterized as AB hydrolase-1.
+At position 75 to 110, the domain is characterized as EF-hand 1.
+At position 147 to 180, the domain is characterized as EF-hand 2.
+At position 9 to 304, the domain is characterized as Protein kinase.
+At position 7 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 194 to 469, the domain is characterized as Protein kinase.
+At position 493 to 644, the domain is characterized as Helicase C-terminal.
+At position 4 to 123, the domain is characterized as RabBD.
+At position 305 to 430, the domain is characterized as C2 1.
+At position 458 to 590, the domain is characterized as C2 2.
+At position 487 to 608, the domain is characterized as Cadherin 5.
+At position 13 to 124, the domain is characterized as MTTase N-terminal.
+At position 191 to 422, the domain is characterized as Radical SAM core.
+At position 424 to 497, the domain is characterized as TRAM.
+At position 25 to 333, the domain is characterized as Dynamin-type G.
+At position 670 to 757, the domain is characterized as GED.
+At position 2 to 90, the domain is characterized as N-acetyltransferase.
+At position 34 to 152, the domain is characterized as SCP.
+At position 4 to 228, the domain is characterized as Radical SAM core.
+At position 257 to 501, the domain is characterized as ABC transporter 2.
+At position 33 to 159, the domain is characterized as Thioredoxin.
+At position 399 to 506, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 35 to 86, the domain is characterized as HTH myb-type 1.
+At position 87 to 142, the domain is characterized as HTH myb-type 2.
+At position 143 to 193, the domain is characterized as HTH myb-type 3.
+At position 580 to 639, the domain is characterized as KH.
+At position 651 to 723, the domain is characterized as S1 motif.
+At position 202 to 344, the domain is characterized as GAF.
+At position 381 to 610, the domain is characterized as Sigma-54 factor interaction.
+At position 541 to 637, the domain is characterized as WGR.
+At position 661 to 778, the domain is characterized as PARP alpha-helical.
+At position 787 to 1013, the domain is characterized as PARP catalytic.
+At position 51 to 152, the domain is characterized as LOB.
+At position 1 to 230, the domain is characterized as ABC transporter.
+At position 33 to 104, the domain is characterized as KRAB.
+At position 34 to 105, the domain is characterized as KRAB 1.
+At position 124 to 195, the domain is characterized as KRAB 2.
+At position 100 to 319, the domain is characterized as Radical SAM core.
+At position 46 to 144, the domain is characterized as Plastocyanin-like 1.
+At position 190 to 292, the domain is characterized as Plastocyanin-like 2.
+At position 382 to 499, the domain is characterized as Plastocyanin-like 3.
+At position 248 to 362, the domain is characterized as PAZ.
+At position 541 to 848, the domain is characterized as Piwi.
+At position 55 to 130, the domain is characterized as Carrier.
+At position 2 to 255, the domain is characterized as ABC transporter.
+At position 665 to 694, the domain is characterized as IQ.
+At position 105 to 218, the domain is characterized as PX.
+At position 359 to 391, the domain is characterized as EGF-like.
+At position 38 to 148, the domain is characterized as tRNA-binding.
+At position 116 to 311, the domain is characterized as ATP-grasp.
+At position 112 to 191, the domain is characterized as RRM 2.
+At position 318 to 370, the domain is characterized as HAMP 1.
+At position 412 to 465, the domain is characterized as HAMP 2.
+At position 484 to 720, the domain is characterized as Methyl-accepting transducer.
+At position 20 to 91, the domain is characterized as KH type-2.
+At position 340 to 433, the domain is characterized as Fibronectin type-III.
+At position 337 to 435, the domain is characterized as Rhodanese.
+At position 277 to 438, the domain is characterized as Helicase C-terminal.
+At position 90 to 151, the domain is characterized as S4 RNA-binding.
+At position 153 to 345, the domain is characterized as CheB-type methylesterase.
+At position 11 to 65, the domain is characterized as HTH cro/C1-type.
+At position 25 to 247, the domain is characterized as Peptidase S1.
+At position 1175 to 1440, the domain is characterized as Protein kinase.
+At position 622 to 852, the domain is characterized as FAD-binding FR-type.
+At position 42 to 147, the domain is characterized as CUB.
+At position 161 to 397, the domain is characterized as Peptidase S1.
+At position 1 to 20, the domain is characterized as FZ.
+At position 24 to 63, the domain is characterized as EGF-like 1.
+At position 64 to 115, the domain is characterized as EGF-like 2.
+At position 118 to 155, the domain is characterized as EGF-like 3.
+At position 156 to 192, the domain is characterized as EGF-like 4.
+At position 194 to 232, the domain is characterized as EGF-like 5; calcium-binding.
+At position 234 to 274, the domain is characterized as EGF-like 6.
+At position 276 to 312, the domain is characterized as EGF-like 7; calcium-binding.
+At position 314 to 353, the domain is characterized as EGF-like 8; calcium-binding.
+At position 355 to 391, the domain is characterized as EGF-like 9; calcium-binding.
+At position 392 to 430, the domain is characterized as EGF-like 10.
+At position 432 to 473, the domain is characterized as EGF-like 11; calcium-binding.
+At position 475 to 511, the domain is characterized as EGF-like 12; calcium-binding.
+At position 513 to 549, the domain is characterized as EGF-like 13; calcium-binding.
+At position 551 to 587, the domain is characterized as EGF-like 14; calcium-binding.
+At position 589 to 625, the domain is characterized as EGF-like 15; calcium-binding.
+At position 626 to 659, the domain is characterized as EGF-like 16.
+At position 661 to 689, the domain is characterized as EGF-like 17.
+At position 691 to 727, the domain is characterized as EGF-like 18.
+At position 729 to 765, the domain is characterized as EGF-like 19.
+At position 767 to 803, the domain is characterized as EGF-like 20.
+At position 806 to 842, the domain is characterized as EGF-like 21.
+At position 844 to 880, the domain is characterized as EGF-like 22.
+At position 882 to 928, the domain is characterized as EGF-like 23.
+At position 930 to 966, the domain is characterized as EGF-like 24.
+At position 968 to 1004, the domain is characterized as EGF-like 25.
+At position 1006 to 1044, the domain is characterized as EGF-like 26.
+At position 1046 to 1085, the domain is characterized as EGF-like 27.
+At position 1087 to 1126, the domain is characterized as EGF-like 28.
+At position 1130 to 1171, the domain is characterized as EGF-like 29.
+At position 582 to 685, the domain is characterized as tRNA-binding.
+At position 8 to 250, the domain is characterized as ABC transporter 1.
+At position 295 to 523, the domain is characterized as ABC transporter 2.
+At position 216 to 399, the domain is characterized as GAF.
+At position 618 to 688, the domain is characterized as PAS 1.
+At position 748 to 822, the domain is characterized as PAS 2.
+At position 902 to 1122, the domain is characterized as Histidine kinase.
+At position 78 to 180, the domain is characterized as Ras-associating.
+At position 181 to 228, the domain is characterized as SARAH.
+At position 81 to 389, the domain is characterized as IF rod.
+At position 47 to 128, the domain is characterized as RRM 1.
+At position 135 to 215, the domain is characterized as RRM 2.
+At position 401 to 479, the domain is characterized as RRM 3.
+At position 9 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 200 to 392, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 147, the domain is characterized as N-acetyltransferase.
+At position 374 to 432, the domain is characterized as COS.
+At position 440 to 535, the domain is characterized as Fibronectin type-III.
+At position 533 to 702, the domain is characterized as B30.2/SPRY.
+At position 4 to 229, the domain is characterized as AB hydrolase-1.
+At position 24 to 103, the domain is characterized as GIY-YIG.
+At position 213 to 248, the domain is characterized as UVR.
+At position 7 to 183, the domain is characterized as UmuC.
+At position 83 to 171, the domain is characterized as Ig-like.
+At position 119 to 249, the domain is characterized as Fatty acid hydroxylase.
+At position 26 to 140, the domain is characterized as Ig-like V-type.
+At position 73 to 503, the domain is characterized as PPM-type phosphatase.
+At position 589 to 676, the domain is characterized as BRCT.
+At position 97 to 434, the domain is characterized as Asparaginase/glutaminase.
+At position 288 to 484, the domain is characterized as Helicase ATP-binding.
+At position 512 to 719, the domain is characterized as Helicase C-terminal.
+At position 108 to 277, the domain is characterized as Helicase ATP-binding.
+At position 305 to 466, the domain is characterized as Helicase C-terminal.
+At position 59 to 200, the domain is characterized as Cupin type-1 1.
+At position 236 to 377, the domain is characterized as Cupin type-1 2.
+At position 32 to 147, the domain is characterized as C-type lectin.
+At position 11 to 188, the domain is characterized as PBS-linker.
+At position 1 to 102, the domain is characterized as Cadherin 3.
+At position 103 to 208, the domain is characterized as Cadherin 4.
+At position 209 to 314, the domain is characterized as Cadherin 5.
+At position 7 to 320, the domain is characterized as Cbl-PTB.
+At position 70 to 102, the domain is characterized as ShKT 1.
+At position 113 to 149, the domain is characterized as ShKT 2.
+At position 155 to 190, the domain is characterized as ShKT 3.
+At position 76 to 234, the domain is characterized as TNase-like.
+At position 1 to 53, the domain is characterized as F-box.
+At position 276 to 326, the domain is characterized as FBD.
+At position 556 to 695, the domain is characterized as Tyrosine-protein phosphatase.
+At position 185 to 268, the domain is characterized as RRM.
+At position 32 to 168, the domain is characterized as Nudix hydrolase.
+At position 1 to 40, the domain is characterized as Ferritin-like diiron.
+At position 27 to 142, the domain is characterized as sHSP.
+At position 17 to 212, the domain is characterized as Lon N-terminal.
+At position 606 to 788, the domain is characterized as Lon proteolytic.
+At position 30 to 241, the domain is characterized as Pentraxin (PTX).
+At position 2 to 89, the domain is characterized as Core-binding (CB).
+At position 110 to 293, the domain is characterized as Tyr recombinase.
+At position 27 to 174, the domain is characterized as VOC.
+At position 4 to 86, the domain is characterized as BMC 1.
+At position 96 to 182, the domain is characterized as BMC 2.
+At position 37 to 110, the domain is characterized as U-box.
+At position 298 to 457, the domain is characterized as PPIase cyclophilin-type.
+At position 177 to 281, the domain is characterized as PB1.
+At position 293 to 536, the domain is characterized as Glutamine amidotransferase type-1.
+At position 507 to 665, the domain is characterized as OTU.
+At position 248 to 464, the domain is characterized as Rap-GAP.
+At position 116 to 307, the domain is characterized as Helicase ATP-binding.
+At position 341 to 503, the domain is characterized as Helicase C-terminal.
+At position 18 to 162, the domain is characterized as UEV.
+At position 292 to 360, the domain is characterized as SB.
+At position 967 to 1042, the domain is characterized as Carrier 1.
+At position 2003 to 2077, the domain is characterized as Carrier 2.
+At position 1 to 207, the domain is characterized as Protein kinase.
+At position 262 to 342, the domain is characterized as Toprim.
+At position 149 to 253, the domain is characterized as SH2.
+At position 268 to 521, the domain is characterized as Protein kinase.
+At position 256 to 516, the domain is characterized as Protein kinase.
+At position 15 to 163, the domain is characterized as TIR.
+At position 178 to 427, the domain is characterized as NB-ARC.
+At position 1238 to 1297, the domain is characterized as LIM zinc-binding.
+At position 145 to 212, the domain is characterized as GRAM 1.
+At position 285 to 353, the domain is characterized as GRAM 2.
+At position 504 to 691, the domain is characterized as Rab-GAP TBC.
+At position 79 to 254, the domain is characterized as Helicase ATP-binding.
+At position 266 to 427, the domain is characterized as Helicase C-terminal.
+At position 1 to 252, the domain is characterized as tr-type G.
+At position 426 to 455, the domain is characterized as EF-hand 1.
+At position 457 to 492, the domain is characterized as EF-hand 2.
+At position 493 to 528, the domain is characterized as EF-hand 3.
+At position 204 to 412, the domain is characterized as ATP-grasp.
+At position 159 to 351, the domain is characterized as Helicase ATP-binding.
+At position 377 to 536, the domain is characterized as Helicase C-terminal.
+At position 2 to 232, the domain is characterized as Glutamine amidotransferase type-1.
+At position 310 to 663, the domain is characterized as Kinesin motor.
+At position 225 to 381, the domain is characterized as TrmE-type G.
+At position 14 to 167, the domain is characterized as UBC core.
+At position 197 to 227, the domain is characterized as KOW.
+At position 22 to 81, the domain is characterized as PWWP.
+At position 34 to 177, the domain is characterized as SIS.
+At position 203 to 261, the domain is characterized as CBS 1.
+At position 269 to 321, the domain is characterized as CBS 2.
+At position 196 to 231, the domain is characterized as EF-hand.
+At position 2 to 130, the domain is characterized as C-type lysozyme.
+At position 34 to 297, the domain is characterized as Protein kinase.
+At position 88 to 207, the domain is characterized as GST C-terminal.
+At position 224 to 301, the domain is characterized as RRM 1.
+At position 325 to 405, the domain is characterized as RRM 2.
+At position 444 to 524, the domain is characterized as RRM 3.
+At position 1 to 51, the domain is characterized as PDZ.
+At position 224 to 380, the domain is characterized as TrmE-type G.
+At position 40 to 301, the domain is characterized as Protein kinase.
+At position 34 to 261, the domain is characterized as Peptidase S1.
+At position 21 to 75, the domain is characterized as Tudor-knot.
+At position 415 to 610, the domain is characterized as B30.2/SPRY.
+At position 1 to 91, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 91 to 130, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 229 to 285, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 49 to 210, the domain is characterized as C2 PI3K-type.
+At position 331 to 577, the domain is characterized as PIK helical.
+At position 666 to 1004, the domain is characterized as PI3K/PI4K catalytic.
+At position 103 to 268, the domain is characterized as Helicase ATP-binding.
+At position 293 to 473, the domain is characterized as Helicase C-terminal.
+At position 165 to 432, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 143 to 256, the domain is characterized as Gnk2-homologous 2.
+At position 35 to 149, the domain is characterized as sHSP.
+At position 192 to 268, the domain is characterized as UBX.
+At position 30 to 164, the domain is characterized as Ephrin RBD.
+At position 56 to 163, the domain is characterized as sHSP.
+At position 99 to 295, the domain is characterized as ABC transmembrane type-1.
+At position 601 to 682, the domain is characterized as BRCT.
+At position 91 to 181, the domain is characterized as K-box.
+At position 24 to 71, the domain is characterized as F-box.
+At position 106 to 474, the domain is characterized as GS catalytic.
+At position 529 to 604, the domain is characterized as Carrier 1.
+At position 624 to 1047, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 2009 to 2084, the domain is characterized as Carrier 2.
+At position 170 to 324, the domain is characterized as ELMO.
+At position 1 to 77, the domain is characterized as GIY-YIG.
+At position 28 to 71, the domain is characterized as LysM 1.
+At position 78 to 142, the domain is characterized as SH3b.
+At position 175 to 218, the domain is characterized as LysM 2.
+At position 297 to 341, the domain is characterized as LysM 3.
+At position 393 to 511, the domain is characterized as NlpC/P60.
+At position 7 to 82, the domain is characterized as Lipoyl-binding.
+At position 119 to 157, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 35 to 133, the domain is characterized as SRCR 1.
+At position 159 to 268, the domain is characterized as SRCR 2.
+At position 276 to 368, the domain is characterized as SRCR 3.
+At position 1 to 253, the domain is characterized as Deacetylase sirtuin-type.
+At position 600 to 701, the domain is characterized as tRNA-binding.
+At position 8 to 190, the domain is characterized as Jacalin-type lectin.
+At position 503 to 610, the domain is characterized as PTS EIIA type-1.
+At position 37 to 157, the domain is characterized as Ig-like V-type.
+At position 159 to 254, the domain is characterized as Link 1.
+At position 258 to 356, the domain is characterized as Link 2.
+At position 949 to 985, the domain is characterized as EGF-like 1.
+At position 987 to 1023, the domain is characterized as EGF-like 2; calcium-binding.
+At position 1025 to 1154, the domain is characterized as C-type lectin.
+At position 1154 to 1214, the domain is characterized as Sushi.
+At position 353 to 505, the domain is characterized as CBM3.
+At position 202 to 1083, the domain is characterized as USP.
+At position 589 to 776, the domain is characterized as Reticulon.
+At position 155 to 431, the domain is characterized as Velvet.
+At position 5 to 129, the domain is characterized as VOC 1.
+At position 150 to 266, the domain is characterized as VOC 2.
+At position 132 to 179, the domain is characterized as LRRCT.
+At position 215 to 244, the domain is characterized as IQ.
+At position 183 to 601, the domain is characterized as GRAS.
+At position 55 to 593, the domain is characterized as PLA2c.
+At position 135 to 261, the domain is characterized as N-acetyltransferase.
+At position 29 to 117, the domain is characterized as Ig-like C2-type.
+At position 171 to 199, the domain is characterized as ITAM.
+At position 598 to 798, the domain is characterized as FtsK.
+At position 90 to 383, the domain is characterized as Protein kinase.
+At position 384 to 453, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 194, the domain is characterized as SMP-LTD.
+At position 183 to 365, the domain is characterized as OTU.
+At position 256 to 335, the domain is characterized as G5.
+At position 44 to 162, the domain is characterized as Response regulatory.
+At position 574 to 616, the domain is characterized as CCT.
+At position 778 to 1133, the domain is characterized as G-alpha.
+At position 7 to 23, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 333 to 503, the domain is characterized as tr-type G.
+At position 40 to 159, the domain is characterized as tRNA-binding.
+At position 701 to 793, the domain is characterized as FDX-ACB.
+At position 230 to 320, the domain is characterized as PA.
+At position 5 to 234, the domain is characterized as ABC transporter.
+At position 51 to 110, the domain is characterized as VWFC.
+At position 1 to 188, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 259, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 263 to 509, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 38 to 380, the domain is characterized as G-alpha.
+At position 429 to 700, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 118 to 400, the domain is characterized as Calpain catalytic.
+At position 1 to 107, the domain is characterized as Barwin.
+At position 80 to 163, the domain is characterized as MEIS N-terminal.
+At position 1 to 70, the domain is characterized as Sm.
+At position 1 to 161, the domain is characterized as PPIase cyclophilin-type.
+At position 243 to 321, the domain is characterized as RRM.
+At position 3 to 244, the domain is characterized as CN hydrolase.
+At position 20 to 348, the domain is characterized as F5/8 type A 1.
+At position 20 to 198, the domain is characterized as Plastocyanin-like 1.
+At position 206 to 348, the domain is characterized as Plastocyanin-like 2.
+At position 399 to 730, the domain is characterized as F5/8 type A 2.
+At position 399 to 573, the domain is characterized as Plastocyanin-like 3.
+At position 583 to 730, the domain is characterized as Plastocyanin-like 4.
+At position 1713 to 2040, the domain is characterized as F5/8 type A 3.
+At position 1713 to 1877, the domain is characterized as Plastocyanin-like 5.
+At position 1887 to 2040, the domain is characterized as Plastocyanin-like 6.
+At position 2040 to 2188, the domain is characterized as F5/8 type C 1.
+At position 2193 to 2345, the domain is characterized as F5/8 type C 2.
+At position 78 to 144, the domain is characterized as DRBM 1.
+At position 231 to 298, the domain is characterized as DRBM 2.
+At position 370 to 707, the domain is characterized as A to I editase.
+At position 21 to 112, the domain is characterized as Ig-like.
+At position 50 to 330, the domain is characterized as GH10.
+At position 116 to 355, the domain is characterized as Radical SAM core.
+At position 3 to 89, the domain is characterized as Core-binding (CB).
+At position 110 to 297, the domain is characterized as Tyr recombinase.
+At position 199 to 417, the domain is characterized as Letm1 RBD.
+At position 179 to 350, the domain is characterized as PCI.
+At position 454 to 617, the domain is characterized as Helicase C-terminal.
+At position 652 to 687, the domain is characterized as UVR.
+At position 656 to 831, the domain is characterized as Integrase catalytic.
+At position 1353 to 1491, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1625 to 1767, the domain is characterized as RNase H Ty1/copia-type.
+At position 299 to 438, the domain is characterized as N-acetyltransferase.
+At position 1 to 82, the domain is characterized as Core-binding (CB).
+At position 103 to 285, the domain is characterized as Tyr recombinase.
+At position 3 to 239, the domain is characterized as ABC transporter.
+At position 104 to 305, the domain is characterized as ATP-grasp.
+At position 59 to 167, the domain is characterized as MTTase N-terminal.
+At position 195 to 426, the domain is characterized as Radical SAM core.
+At position 426 to 488, the domain is characterized as TRAM.
+At position 257 to 426, the domain is characterized as PCI.
+At position 133 to 399, the domain is characterized as Protein kinase.
+At position 399 to 460, the domain is characterized as SH3.
+At position 488 to 502, the domain is characterized as CRIB.
+At position 31 to 81, the domain is characterized as Myosin N-terminal SH3-like.
+At position 85 to 783, the domain is characterized as Myosin motor.
+At position 785 to 807, the domain is characterized as IQ.
+At position 27 to 79, the domain is characterized as F-box.
+At position 58 to 175, the domain is characterized as RGS.
+At position 190 to 455, the domain is characterized as Protein kinase.
+At position 456 to 521, the domain is characterized as AGC-kinase C-terminal.
+At position 4 to 227, the domain is characterized as tr-type G.
+At position 25 to 78, the domain is characterized as bHLH.
+At position 106 to 176, the domain is characterized as PAS.
+At position 19 to 73, the domain is characterized as HTH cro/C1-type.
+At position 4 to 53, the domain is characterized as F-box.
+At position 14 to 95, the domain is characterized as GIY-YIG.
+At position 16 to 98, the domain is characterized as Lipoyl-binding.
+At position 92 to 220, the domain is characterized as SEA.
+At position 233 to 346, the domain is characterized as CUB 1.
+At position 351 to 467, the domain is characterized as CUB 2.
+At position 469 to 505, the domain is characterized as LDL-receptor class A 1.
+At position 503 to 540, the domain is characterized as LDL-receptor class A 2.
+At position 544 to 581, the domain is characterized as LDL-receptor class A 3.
+At position 592 to 826, the domain is characterized as Peptidase S1.
+At position 21 to 253, the domain is characterized as AB hydrolase-1.
+At position 195 to 325, the domain is characterized as SRCR.
+At position 204 to 226, the domain is characterized as LDL-receptor class A.
+At position 326 to 559, the domain is characterized as Peptidase S1.
+At position 6 to 94, the domain is characterized as ACB.
+At position 22 to 72, the domain is characterized as WAP.
+At position 350 to 464, the domain is characterized as C2.
+At position 487 to 590, the domain is characterized as PH.
+At position 885 to 1056, the domain is characterized as MHD1.
+At position 82 to 178, the domain is characterized as Toprim.
+At position 5 to 72, the domain is characterized as J.
+At position 5 to 225, the domain is characterized as ABC transporter.
+At position 117 to 395, the domain is characterized as AB hydrolase-1.
+At position 58 to 113, the domain is characterized as TSP type-1 1.
+At position 115 to 152, the domain is characterized as LDL-receptor class A.
+At position 154 to 500, the domain is characterized as MACPF.
+At position 501 to 531, the domain is characterized as EGF-like.
+At position 542 to 588, the domain is characterized as TSP type-1 2.
+At position 60 to 341, the domain is characterized as Protein kinase.
+At position 697 to 777, the domain is characterized as ERCC4.
+At position 20 to 190, the domain is characterized as Phosphatase tensin-type.
+At position 195 to 350, the domain is characterized as C2 tensin-type.
+At position 412 to 582, the domain is characterized as tr-type G.
+At position 52 to 113, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 25 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 229 to 329, the domain is characterized as Ig-like C2-type 3.
+At position 386 to 541, the domain is characterized as TIR.
+At position 120 to 190, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 49 to 301, the domain is characterized as Cupin type-1 1.
+At position 360 to 509, the domain is characterized as Cupin type-1 2.
+At position 505 to 712, the domain is characterized as Protein kinase.
+At position 41 to 129, the domain is characterized as Ig-like C2-type 1.
+At position 136 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 243 to 332, the domain is characterized as Ig-like C2-type 3.
+At position 337 to 424, the domain is characterized as Ig-like C2-type 4.
+At position 430 to 517, the domain is characterized as Ig-like C2-type 5.
+At position 521 to 608, the domain is characterized as Ig-like C2-type 6.
+At position 625 to 720, the domain is characterized as Fibronectin type-III 1.
+At position 725 to 819, the domain is characterized as Fibronectin type-III 2.
+At position 824 to 926, the domain is characterized as Fibronectin type-III 3.
+At position 930 to 1026, the domain is characterized as Fibronectin type-III 4.
+At position 1040 to 1132, the domain is characterized as Fibronectin type-III 5.
+At position 260 to 464, the domain is characterized as Peptidase M12B.
+At position 474 to 554, the domain is characterized as Disintegrin.
+At position 555 to 610, the domain is characterized as TSP type-1 1.
+At position 848 to 906, the domain is characterized as TSP type-1 2.
+At position 908 to 968, the domain is characterized as TSP type-1 3.
+At position 969 to 1023, the domain is characterized as TSP type-1 4.
+At position 1053 to 1091, the domain is characterized as PLAC.
+At position 625 to 692, the domain is characterized as S1 motif.
+At position 423 to 681, the domain is characterized as Olfactomedin-like.
+At position 4 to 120, the domain is characterized as CMP/dCMP-type deaminase.
+At position 380 to 577, the domain is characterized as Rho-GAP.
+At position 987 to 1026, the domain is characterized as BESS.
+At position 1 to 125, the domain is characterized as Protein kinase.
+At position 3 to 191, the domain is characterized as DPCK.
+At position 18 to 319, the domain is characterized as Protein kinase.
+At position 47 to 169, the domain is characterized as MsrB.
+At position 96 to 174, the domain is characterized as PDZ.
+At position 4 to 181, the domain is characterized as tr-type G.
+At position 243 to 343, the domain is characterized as Cadherin 3.
+At position 344 to 448, the domain is characterized as Cadherin 4.
+At position 449 to 558, the domain is characterized as Cadherin 5.
+At position 566 to 671, the domain is characterized as Cadherin 6.
+At position 1 to 243, the domain is characterized as Peptidase S1.
+At position 75 to 248, the domain is characterized as Helicase ATP-binding.
+At position 142 to 355, the domain is characterized as ATP-grasp.
+At position 116 to 381, the domain is characterized as Protein kinase.
+At position 9 to 114, the domain is characterized as Thioredoxin.
+At position 57 to 161, the domain is characterized as FAD-binding FR-type.
+At position 16 to 85, the domain is characterized as Sm.
+At position 146 to 204, the domain is characterized as TRAM.
+At position 48 to 234, the domain is characterized as Radical SAM core.
+At position 67 to 180, the domain is characterized as sHSP.
+At position 19 to 66, the domain is characterized as F-box.
+At position 24 to 104, the domain is characterized as Chorismate mutase.
+At position 22 to 191, the domain is characterized as Flavodoxin-like.
+At position 131 to 189, the domain is characterized as HTH cro/C1-type.
+At position 28 to 197, the domain is characterized as EngA-type G 1.
+At position 225 to 401, the domain is characterized as EngA-type G 2.
+At position 402 to 486, the domain is characterized as KH-like.
+At position 348 to 425, the domain is characterized as OCT.
+At position 53 to 121, the domain is characterized as DRBM.
+At position 444 to 612, the domain is characterized as Helicase ATP-binding.
+At position 654 to 827, the domain is characterized as Helicase C-terminal.
+At position 248 to 477, the domain is characterized as Methyl-accepting transducer.
+At position 358 to 438, the domain is characterized as OCT.
+At position 339 to 411, the domain is characterized as HSA.
+At position 708 to 873, the domain is characterized as Helicase ATP-binding.
+At position 1247 to 1400, the domain is characterized as Helicase C-terminal.
+At position 31 to 353, the domain is characterized as Kinesin motor.
+At position 488 to 643, the domain is characterized as PPIase cyclophilin-type.
+At position 287 to 343, the domain is characterized as KARI C-terminal knotted 2.
+At position 701 to 784, the domain is characterized as BRCT.
+At position 159 to 235, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 363, the domain is characterized as Ig-like V-type 2.
+At position 364 to 452, the domain is characterized as Ig-like C2-type 2.
+At position 572 to 605, the domain is characterized as EF-hand 1.
+At position 602 to 637, the domain is characterized as EF-hand 2.
+At position 667 to 700, the domain is characterized as EF-hand 3.
+At position 637 to 656, the domain is characterized as WH2.
+At position 115 to 156, the domain is characterized as CHCH.
+At position 200 to 274, the domain is characterized as Toprim.
+At position 34 to 71, the domain is characterized as LRRNT.
+At position 201 to 255, the domain is characterized as LRRCT.
+At position 211 to 402, the domain is characterized as Helicase ATP-binding.
+At position 454 to 609, the domain is characterized as Helicase C-terminal.
+At position 139 to 204, the domain is characterized as HTH luxR-type.
+At position 49 to 84, the domain is characterized as EF-hand.
+At position 1 to 187, the domain is characterized as Glutamine amidotransferase type-1.
+At position 201 to 250, the domain is characterized as bHLH.
+At position 25 to 240, the domain is characterized as tr-type G.
+At position 52 to 239, the domain is characterized as Rho-GAP.
+At position 82 to 319, the domain is characterized as PABS.
+At position 91 to 242, the domain is characterized as CBM15.
+At position 245 to 596, the domain is characterized as GH10.
+At position 244 to 284, the domain is characterized as UBA.
+At position 123 to 505, the domain is characterized as Protein kinase.
+At position 435 to 597, the domain is characterized as Helicase C-terminal.
+At position 76 to 125, the domain is characterized as FHA.
+At position 347 to 483, the domain is characterized as JmjC.
+At position 723 to 1016, the domain is characterized as Protein kinase.
+At position 30 to 116, the domain is characterized as RRM.
+At position 318 to 857, the domain is characterized as USP.
+At position 635 to 676, the domain is characterized as UBA 1.
+At position 710 to 750, the domain is characterized as UBA 2.
+At position 193 to 373, the domain is characterized as CNNM transmembrane.
+At position 393 to 454, the domain is characterized as CBS 1.
+At position 461 to 527, the domain is characterized as CBS 2.
+At position 44 to 283, the domain is characterized as Laminin N-terminal.
+At position 284 to 339, the domain is characterized as Laminin EGF-like 1.
+At position 340 to 395, the domain is characterized as Laminin EGF-like 2.
+At position 396 to 442, the domain is characterized as Laminin EGF-like 3.
+At position 443 to 492, the domain is characterized as Laminin EGF-like 4.
+At position 493 to 502, the domain is characterized as Laminin EGF-like 5; first part.
+At position 512 to 687, the domain is characterized as Laminin IV type A.
+At position 688 to 721, the domain is characterized as Laminin EGF-like 5; second part.
+At position 722 to 770, the domain is characterized as Laminin EGF-like 6.
+At position 771 to 825, the domain is characterized as Laminin EGF-like 7.
+At position 826 to 881, the domain is characterized as Laminin EGF-like 8; nidogen-binding.
+At position 882 to 932, the domain is characterized as Laminin EGF-like 9.
+At position 933 to 980, the domain is characterized as Laminin EGF-like 10.
+At position 981 to 1028, the domain is characterized as Laminin EGF-like 11.
+At position 41 to 344, the domain is characterized as AB hydrolase-1.
+At position 602 to 684, the domain is characterized as BRCT.
+At position 151 to 528, the domain is characterized as PDEase.
+At position 293 to 390, the domain is characterized as Rieske.
+At position 197 to 252, the domain is characterized as KBD.
+At position 300 to 408, the domain is characterized as SPR.
+At position 419 to 501, the domain is characterized as G5 1.
+At position 547 to 629, the domain is characterized as G5 2.
+At position 675 to 757, the domain is characterized as G5 3.
+At position 803 to 885, the domain is characterized as G5 4.
+At position 931 to 1013, the domain is characterized as G5 5.
+At position 1059 to 1141, the domain is characterized as G5 6.
+At position 1187 to 1269, the domain is characterized as G5 7.
+At position 1315 to 1397, the domain is characterized as G5 8.
+At position 1443 to 1525, the domain is characterized as G5 9.
+At position 2 to 183, the domain is characterized as Prephenate dehydratase.
+At position 5 to 64, the domain is characterized as CSD.
+At position 18 to 91, the domain is characterized as H15.
+At position 236 to 288, the domain is characterized as CpcD-like.
+At position 1 to 379, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 29 to 137, the domain is characterized as Rieske.
+At position 34 to 146, the domain is characterized as C-type lectin.
+At position 21 to 128, the domain is characterized as PH.
+At position 42 to 293, the domain is characterized as Protein kinase.
+At position 608 to 655, the domain is characterized as SARAH.
+At position 351 to 414, the domain is characterized as S4 RNA-binding.
+At position 266 to 340, the domain is characterized as ACT 1.
+At position 346 to 412, the domain is characterized as ACT 2.
+At position 715 to 790, the domain is characterized as Smr.
+At position 39 to 85, the domain is characterized as F-box.
+At position 45 to 130, the domain is characterized as Inhibitor I9.
+At position 139 to 410, the domain is characterized as Peptidase S8.
+At position 392 to 574, the domain is characterized as RHD.
+At position 9 to 62, the domain is characterized as HTH cro/C1-type.
+At position 177 to 334, the domain is characterized as Tyrosine-protein phosphatase.
+At position 24 to 284, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 32 to 145, the domain is characterized as PX.
+At position 2 to 77, the domain is characterized as GST N-terminal.
+At position 86 to 217, the domain is characterized as GST C-terminal.
+At position 251 to 412, the domain is characterized as EF-1-gamma C-terminal.
+At position 68 to 162, the domain is characterized as SH2.
+At position 106 to 228, the domain is characterized as MPN.
+At position 120 to 340, the domain is characterized as Radical SAM core.
+At position 40 to 248, the domain is characterized as AIG1-type G.
+At position 21 to 321, the domain is characterized as Protein kinase.
+At position 98 to 166, the domain is characterized as PAS.
+At position 103 to 172, the domain is characterized as S4 RNA-binding.
+At position 673 to 849, the domain is characterized as PCI.
+At position 154 to 260, the domain is characterized as SPR.
+At position 45 to 123, the domain is characterized as RRM 1.
+At position 125 to 207, the domain is characterized as RRM 2.
+At position 220 to 292, the domain is characterized as RRM 3.
+At position 187 to 543, the domain is characterized as NB-ARC.
+At position 48 to 243, the domain is characterized as PBC.
+At position 215 to 375, the domain is characterized as TrmE-type G.
+At position 40 to 416, the domain is characterized as GBD/FH3.
+At position 518 to 594, the domain is characterized as FH1.
+At position 595 to 994, the domain is characterized as FH2.
+At position 1016 to 1048, the domain is characterized as DAD.
+At position 88 to 337, the domain is characterized as CN hydrolase.
+At position 30 to 302, the domain is characterized as Protein kinase.
+At position 15 to 109, the domain is characterized as HTH arsR-type.
+At position 6 to 77, the domain is characterized as KRAB.
+At position 131 to 296, the domain is characterized as TNase-like.
+At position 31 to 138, the domain is characterized as Rhodanese 1.
+At position 171 to 289, the domain is characterized as Rhodanese 2.
+At position 158 to 225, the domain is characterized as DRBM.
+At position 378 to 547, the domain is characterized as tr-type G.
+At position 97 to 360, the domain is characterized as Protein kinase.
+At position 361 to 431, the domain is characterized as AGC-kinase C-terminal.
+At position 1443 to 1563, the domain is characterized as PH.
+At position 1591 to 1881, the domain is characterized as CNH.
+At position 62 to 313, the domain is characterized as Protein kinase.
+At position 360 to 397, the domain is characterized as UBA.
+At position 187 to 272, the domain is characterized as Rieske.
+At position 587 to 715, the domain is characterized as B12-binding.
+At position 497 to 839, the domain is characterized as HECT.
+At position 324 to 560, the domain is characterized as NR LBD.
+At position 85 to 369, the domain is characterized as FERM.
+At position 2219 to 2460, the domain is characterized as I/LWEQ.
+At position 2553 to 2614, the domain is characterized as HP.
+At position 56 to 365, the domain is characterized as AB hydrolase-1.
+At position 1 to 102, the domain is characterized as Cystatin 1.
+At position 103 to 169, the domain is characterized as Cystatin 2.
+At position 31 to 69, the domain is characterized as LDL-receptor class A 1.
+At position 70 to 110, the domain is characterized as LDL-receptor class A 2.
+At position 111 to 151, the domain is characterized as LDL-receptor class A 3.
+At position 152 to 190, the domain is characterized as LDL-receptor class A 4.
+At position 191 to 231, the domain is characterized as LDL-receptor class A 5.
+At position 237 to 275, the domain is characterized as LDL-receptor class A 6.
+At position 276 to 314, the domain is characterized as LDL-receptor class A 7.
+At position 316 to 355, the domain is characterized as LDL-receptor class A 8.
+At position 356 to 391, the domain is characterized as EGF-like 1.
+At position 396 to 431, the domain is characterized as EGF-like 2; calcium-binding.
+At position 702 to 750, the domain is characterized as EGF-like 3.
+At position 73 to 408, the domain is characterized as Peptidase A1.
+At position 232 to 620, the domain is characterized as GBD/FH3.
+At position 740 to 972, the domain is characterized as FH1.
+At position 980 to 1391, the domain is characterized as FH2.
+At position 9 to 69, the domain is characterized as LIM zinc-binding 1.
+At position 105 to 165, the domain is characterized as LIM zinc-binding 2.
+At position 44 to 272, the domain is characterized as Radical SAM core.
+At position 1 to 120, the domain is characterized as Calponin-homology (CH).
+At position 193 to 371, the domain is characterized as DH.
+At position 576 to 642, the domain is characterized as SH3 1.
+At position 663 to 757, the domain is characterized as SH2.
+At position 806 to 867, the domain is characterized as SH3 2.
+At position 218 to 248, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 251 to 280, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 128 to 224, the domain is characterized as Ig-like.
+At position 232 to 314, the domain is characterized as Ig-like C2-type.
+At position 324 to 379, the domain is characterized as TSP type-1 1.
+At position 398 to 499, the domain is characterized as TSP type-1 2.
+At position 654 to 802, the domain is characterized as ZU5.
+At position 980 to 1067, the domain is characterized as Death.
+At position 55 to 91, the domain is characterized as F-box.
+At position 22 to 84, the domain is characterized as SH3b 1.
+At position 179 to 241, the domain is characterized as SH3b 2.
+At position 572 to 636, the domain is characterized as SH3b 3.
+At position 324 to 398, the domain is characterized as U-box.
+At position 51 to 158, the domain is characterized as RRM 1.
+At position 166 to 246, the domain is characterized as RRM 2.
+At position 317 to 395, the domain is characterized as RRM 3.
+At position 1 to 258, the domain is characterized as YjeF C-terminal.
+At position 158 to 275, the domain is characterized as C2 1.
+At position 287 to 422, the domain is characterized as C2 2.
+At position 28 to 155, the domain is characterized as PTB.
+At position 457 to 516, the domain is characterized as SH3.
+At position 477 to 679, the domain is characterized as FtsK 1.
+At position 855 to 1049, the domain is characterized as FtsK 2.
+At position 1158 to 1351, the domain is characterized as FtsK 3.
+At position 371 to 422, the domain is characterized as bHLH.
+At position 345 to 439, the domain is characterized as BRCT.
+At position 361 to 454, the domain is characterized as FDX-ACB.
+At position 36 to 130, the domain is characterized as Ig-like 1.
+At position 135 to 222, the domain is characterized as Ig-like 2.
+At position 235 to 322, the domain is characterized as Ig-like 3.
+At position 327 to 411, the domain is characterized as Ig-like 4.
+At position 421 to 515, the domain is characterized as Fibronectin type-III 1.
+At position 517 to 613, the domain is characterized as Fibronectin type-III 2.
+At position 618 to 717, the domain is characterized as Fibronectin type-III 3.
+At position 724 to 817, the domain is characterized as Fibronectin type-III 4.
+At position 822 to 917, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 256, the domain is characterized as SMP-LTD.
+At position 395 to 564, the domain is characterized as tr-type G.
+At position 6 to 53, the domain is characterized as F-box.
+At position 19 to 93, the domain is characterized as Rhodanese.
+At position 220 to 320, the domain is characterized as Rieske.
+At position 121 to 363, the domain is characterized as Radical SAM core.
+At position 33 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 69 to 115, the domain is characterized as F-box.
+At position 147 to 233, the domain is characterized as PKD.
+At position 97 to 149, the domain is characterized as bHLH.
+At position 186 to 638, the domain is characterized as DOCKER.
+At position 6 to 79, the domain is characterized as Sm.
+At position 43 to 407, the domain is characterized as GH18.
+At position 148 to 247, the domain is characterized as Fibronectin type-III.
+At position 215 to 365, the domain is characterized as TrmE-type G.
+At position 10 to 239, the domain is characterized as tr-type G.
+At position 370 to 435, the domain is characterized as TRAM.
+At position 445 to 719, the domain is characterized as PKS/mFAS DH.
+At position 1514 to 1589, the domain is characterized as Carrier.
+At position 23 to 93, the domain is characterized as PAS 1.
+At position 94 to 148, the domain is characterized as PAC.
+At position 151 to 217, the domain is characterized as PAS 2.
+At position 302 to 517, the domain is characterized as Histidine kinase.
+At position 122 to 343, the domain is characterized as Fibrinogen C-terminal.
+At position 52 to 154, the domain is characterized as Rhodanese.
+At position 147 to 368, the domain is characterized as Radical SAM core.
+At position 1724 to 1848, the domain is characterized as BRCT 1.
+At position 1864 to 1964, the domain is characterized as BRCT 2.
+At position 12 to 69, the domain is characterized as bHLH.
+At position 92 to 122, the domain is characterized as Orange.
+At position 43 to 311, the domain is characterized as Protein kinase.
+At position 83 to 148, the domain is characterized as Cytochrome b5 heme-binding.
+At position 256 to 328, the domain is characterized as HSA.
+At position 429 to 594, the domain is characterized as Helicase ATP-binding.
+At position 740 to 903, the domain is characterized as Helicase C-terminal.
+At position 1084 to 1154, the domain is characterized as Bromo.
+At position 46 to 117, the domain is characterized as KH type-2.
+At position 19 to 278, the domain is characterized as Protein kinase.
+At position 119 to 154, the domain is characterized as EF-hand.
+At position 2 to 236, the domain is characterized as PABS.
+At position 29 to 53, the domain is characterized as Chitin-binding type-1.
+At position 155 to 272, the domain is characterized as C2.
+At position 339 to 597, the domain is characterized as Protein kinase.
+At position 598 to 668, the domain is characterized as AGC-kinase C-terminal.
+At position 13 to 265, the domain is characterized as Pyruvate carboxyltransferase.
+At position 187 to 470, the domain is characterized as ABC transmembrane type-1.
+At position 503 to 742, the domain is characterized as ABC transporter.
+At position 604 to 694, the domain is characterized as BRCT.
+At position 593 to 681, the domain is characterized as EH 2.
+At position 625 to 660, the domain is characterized as EF-hand 3.
+At position 382 to 601, the domain is characterized as FtsK.
+At position 70 to 281, the domain is characterized as ABC transmembrane type-1.
+At position 699 to 880, the domain is characterized as Rho-GAP.
+At position 41 to 288, the domain is characterized as PPM-type phosphatase.
+At position 614 to 868, the domain is characterized as Protein kinase.
+At position 89 to 216, the domain is characterized as GST C-terminal.
+At position 4 to 84, the domain is characterized as GST N-terminal.
+At position 1 to 122, the domain is characterized as Plastocyanin-like 1.
+At position 134 to 300, the domain is characterized as Plastocyanin-like 2.
+At position 344 to 523, the domain is characterized as Plastocyanin-like 3.
+At position 205 to 574, the domain is characterized as GRAS.
+At position 26 to 85, the domain is characterized as CHORD 1.
+At position 169 to 228, the domain is characterized as CHORD 2.
+At position 65 to 97, the domain is characterized as EF-hand 2.
+At position 3 to 150, the domain is characterized as N-acetyltransferase.
+At position 27 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 729 to 813, the domain is characterized as BRCT.
+At position 1 to 78, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 78 to 117, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 215 to 271, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 10 to 94, the domain is characterized as MtN3/slv 1.
+At position 127 to 212, the domain is characterized as MtN3/slv 2.
+At position 63 to 98, the domain is characterized as EF-hand.
+At position 45 to 347, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 11 to 75, the domain is characterized as Histone-fold.
+At position 131 to 384, the domain is characterized as SMP-LTD.
+At position 3 to 72, the domain is characterized as J.
+At position 2 to 85, the domain is characterized as GST N-terminal.
+At position 90 to 215, the domain is characterized as GST C-terminal.
+At position 342 to 432, the domain is characterized as IPT/TIG.
+At position 220 to 377, the domain is characterized as TrmE-type G.
+At position 79 to 119, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 138 to 165, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 181 to 211, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 257 to 313, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 48 to 180, the domain is characterized as RUN.
+At position 26 to 162, the domain is characterized as SprT-like.
+At position 488 to 637, the domain is characterized as PID.
+At position 29 to 267, the domain is characterized as PABS.
+At position 1 to 48, the domain is characterized as Kazal-like.
+At position 14 to 202, the domain is characterized as BPL/LPL catalytic.
+At position 7 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1 to 175, the domain is characterized as Helicase ATP-binding.
+At position 232 to 381, the domain is characterized as Helicase C-terminal.
+At position 62 to 225, the domain is characterized as PPIase cyclophilin-type.
+At position 356 to 414, the domain is characterized as S4 RNA-binding.
+At position 26 to 164, the domain is characterized as RanBD1.
+At position 157 to 203, the domain is characterized as LysM 1.
+At position 245 to 291, the domain is characterized as LysM 2.
+At position 325 to 371, the domain is characterized as LysM 3.
+At position 409 to 455, the domain is characterized as LysM 4.
+At position 341 to 611, the domain is characterized as Protein kinase.
+At position 178 to 214, the domain is characterized as DFDF.
+At position 76 to 185, the domain is characterized as CBM20.
+At position 46 to 115, the domain is characterized as POTRA.
+At position 142 to 239, the domain is characterized as PpiC.
+At position 110 to 160, the domain is characterized as Myosin N-terminal SH3-like.
+At position 164 to 830, the domain is characterized as Myosin motor.
+At position 832 to 861, the domain is characterized as IQ 1.
+At position 855 to 884, the domain is characterized as IQ 2.
+At position 891 to 920, the domain is characterized as IQ 3.
+At position 151 to 239, the domain is characterized as PB1.
+At position 18 to 149, the domain is characterized as EamA 1.
+At position 171 to 296, the domain is characterized as EamA 2.
+At position 115 to 167, the domain is characterized as bHLH.
+At position 372 to 401, the domain is characterized as IQ.
+At position 7 to 231, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 143, the domain is characterized as Jacalin-type lectin.
+At position 27 to 157, the domain is characterized as FZ.
+At position 186 to 329, the domain is characterized as FCP1 homology.
+At position 400 to 450, the domain is characterized as DHHC.
+At position 312 to 589, the domain is characterized as ABC transporter 1.
+At position 609 to 938, the domain is characterized as ABC transporter 2.
+At position 1 to 198, the domain is characterized as MAGE.
+At position 77 to 157, the domain is characterized as GS beta-grasp.
+At position 161 to 430, the domain is characterized as GS catalytic.
+At position 62 to 278, the domain is characterized as Radical SAM core.
+At position 10 to 244, the domain is characterized as ABC transporter.
+At position 83 to 181, the domain is characterized as Toprim.
+At position 99 to 246, the domain is characterized as MDFI.
+At position 24 to 129, the domain is characterized as Ig-like V-type 1.
+At position 139 to 242, the domain is characterized as Ig-like V-type 2.
+At position 244 to 330, the domain is characterized as Ig-like C2-type 1.
+At position 335 to 424, the domain is characterized as Ig-like C2-type 2.
+At position 430 to 510, the domain is characterized as Ig-like C2-type 3.
+At position 55 to 86, the domain is characterized as PQ-loop 1.
+At position 214 to 245, the domain is characterized as PQ-loop 2.
+At position 52 to 111, the domain is characterized as Collagen-like.
+At position 112 to 329, the domain is characterized as Fibrinogen C-terminal.
+At position 310 to 445, the domain is characterized as GGDEF.
+At position 22 to 301, the domain is characterized as Protein kinase.
+At position 360 to 526, the domain is characterized as Helicase ATP-binding.
+At position 540 to 735, the domain is characterized as Helicase C-terminal.
+At position 574 to 593, the domain is characterized as WH2.
+At position 9 to 215, the domain is characterized as YjeF N-terminal.
+At position 226 to 508, the domain is characterized as YjeF C-terminal.
+At position 547 to 758, the domain is characterized as Histidine kinase.
+At position 417 to 631, the domain is characterized as BURP.
+At position 11 to 291, the domain is characterized as Protein kinase.
+At position 1 to 107, the domain is characterized as Thioredoxin.
+At position 25 to 148, the domain is characterized as Response regulatory.
+At position 366 to 459, the domain is characterized as Zinc-hook.
+At position 141 to 346, the domain is characterized as ATP-grasp.
+At position 67 to 175, the domain is characterized as PRD 1.
+At position 176 to 284, the domain is characterized as PRD 2.
+At position 28 to 131, the domain is characterized as Gnk2-homologous 1.
+At position 143 to 250, the domain is characterized as Gnk2-homologous 2.
+At position 348 to 619, the domain is characterized as Protein kinase.
+At position 80 to 224, the domain is characterized as Flavodoxin-like.
+At position 279 to 521, the domain is characterized as FAD-binding FR-type.
+At position 33 to 106, the domain is characterized as TB.
+At position 97 to 120, the domain is characterized as Follistatin-like 1.
+At position 103 to 169, the domain is characterized as Kazal-like 1.
+At position 189 to 244, the domain is characterized as Kazal-like 2.
+At position 247 to 271, the domain is characterized as Follistatin-like 3.
+At position 267 to 321, the domain is characterized as Kazal-like 3.
+At position 5 to 185, the domain is characterized as Guanylate kinase-like.
+At position 8 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 79 to 184, the domain is characterized as AB hydrolase-1.
+At position 127 to 417, the domain is characterized as ABC transmembrane type-1.
+At position 472 to 747, the domain is characterized as ABC transporter.
+At position 411 to 674, the domain is characterized as Protein kinase 2.
+At position 538 to 676, the domain is characterized as Flavodoxin-like.
+At position 729 to 969, the domain is characterized as FAD-binding FR-type.
+At position 21 to 132, the domain is characterized as PH.
+At position 23 to 80, the domain is characterized as bHLH.
+At position 109 to 180, the domain is characterized as PAS.
+At position 257 to 388, the domain is characterized as MPN.
+At position 94 to 182, the domain is characterized as BRCT 2.
+At position 664 to 756, the domain is characterized as BRCT 3.
+At position 763 to 851, the domain is characterized as BRCT 4.
+At position 25 to 252, the domain is characterized as Peptidase S1.
+At position 8 to 465, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 965 to 1261, the domain is characterized as PKS/mFAS DH.
+At position 2416 to 2494, the domain is characterized as Carrier.
+At position 45 to 144, the domain is characterized as HD.
+At position 386 to 447, the domain is characterized as TGS.
+At position 628 to 702, the domain is characterized as ACT.
+At position 404 to 822, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1298 to 1618, the domain is characterized as PKS/mFAS DH.
+At position 1658 to 1733, the domain is characterized as Carrier.
+At position 8 to 148, the domain is characterized as CheW-like.
+At position 109 to 137, the domain is characterized as IQ 1.
+At position 138 to 160, the domain is characterized as IQ 2.
+At position 40 to 326, the domain is characterized as Protein kinase.
+At position 13 to 162, the domain is characterized as Cupin type-1.
+At position 29 to 100, the domain is characterized as BTB.
+At position 205 to 476, the domain is characterized as NPH3.
+At position 5 to 215, the domain is characterized as tr-type G.
+At position 196 to 262, the domain is characterized as J.
+At position 100 to 210, the domain is characterized as OCEL.
+At position 119 to 170, the domain is characterized as LIM zinc-binding 2.
+At position 448 to 547, the domain is characterized as CBM2.
+At position 29 to 79, the domain is characterized as Myosin N-terminal SH3-like.
+At position 83 to 775, the domain is characterized as Myosin motor.
+At position 778 to 805, the domain is characterized as IQ.
+At position 22 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 8 to 163, the domain is characterized as Thioredoxin.
+At position 8 to 87, the domain is characterized as GST N-terminal.
+At position 92 to 215, the domain is characterized as GST C-terminal.
+At position 64 to 325, the domain is characterized as Protein kinase.
+At position 199 to 464, the domain is characterized as ABC transporter 1.
+At position 532 to 748, the domain is characterized as ABC transporter 2.
+At position 510 to 598, the domain is characterized as ABM.
+At position 1 to 43, the domain is characterized as Gla.
+At position 177 to 312, the domain is characterized as GAF.
+At position 341 to 670, the domain is characterized as PDEase.
+At position 322 to 356, the domain is characterized as EGF-like 1; incomplete.
+At position 357 to 397, the domain is characterized as EGF-like 2; calcium-binding.
+At position 398 to 438, the domain is characterized as EGF-like 3.
+At position 436 to 478, the domain is characterized as EGF-like 4.
+At position 743 to 783, the domain is characterized as EGF-like 5.
+At position 835 to 873, the domain is characterized as EGF-like 6.
+At position 874 to 915, the domain is characterized as EGF-like 7; calcium-binding.
+At position 916 to 956, the domain is characterized as EGF-like 8; calcium-binding.
+At position 975 to 1016, the domain is characterized as EGF-like 9.
+At position 6 to 248, the domain is characterized as ABC transporter.
+At position 175 to 347, the domain is characterized as Phosphatase tensin-type.
+At position 352 to 478, the domain is characterized as C2 tensin-type.
+At position 1616 to 1725, the domain is characterized as SH2.
+At position 1751 to 1885, the domain is characterized as PTB.
+At position 218 to 295, the domain is characterized as UBX.
+At position 553 to 628, the domain is characterized as PUA.
+At position 162 to 390, the domain is characterized as Peptidase M12B.
+At position 251 to 449, the domain is characterized as GATase cobBQ-type.
+At position 159 to 258, the domain is characterized as RRM 1.
+At position 266 to 348, the domain is characterized as RRM 2.
+At position 9 to 185, the domain is characterized as TIR.
+At position 201 to 255, the domain is characterized as KASH.
+At position 17 to 182, the domain is characterized as CP-type G.
+At position 7 to 88, the domain is characterized as RRM 1.
+At position 94 to 174, the domain is characterized as RRM 2.
+At position 367 to 445, the domain is characterized as RRM 3.
+At position 115 to 241, the domain is characterized as MRH.
+At position 16 to 195, the domain is characterized as Guanylate kinase-like.
+At position 88 to 215, the domain is characterized as C-type lysozyme.
+At position 524 to 823, the domain is characterized as Peptidase M60.
+At position 1 to 65, the domain is characterized as HMA.
+At position 80 to 250, the domain is characterized as Helicase ATP-binding.
+At position 260 to 420, the domain is characterized as Helicase C-terminal.
+At position 5 to 139, the domain is characterized as UBC core.
+At position 72 to 256, the domain is characterized as RNase H type-2.
+At position 281 to 450, the domain is characterized as tr-type G.
+At position 543 to 618, the domain is characterized as Cytochrome b5 heme-binding.
+At position 661 to 774, the domain is characterized as FAD-binding FR-type.
+At position 116 to 274, the domain is characterized as CP-type G.
+At position 67 to 168, the domain is characterized as CBM20.
+At position 1 to 117, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 360, the domain is characterized as Kinesin motor.
+At position 23 to 211, the domain is characterized as EngB-type G.
+At position 120 to 326, the domain is characterized as ATP-grasp.
+At position 43 to 112, the domain is characterized as J.
+At position 36 to 211, the domain is characterized as BPL/LPL catalytic.
+At position 398 to 470, the domain is characterized as B5.
+At position 703 to 795, the domain is characterized as FDX-ACB.
+At position 94 to 170, the domain is characterized as BTB.
+At position 205 to 307, the domain is characterized as BACK.
+At position 75 to 180, the domain is characterized as Thioredoxin.
+At position 211 to 492, the domain is characterized as FERM.
+At position 401 to 575, the domain is characterized as tr-type G.
+At position 7 to 86, the domain is characterized as RRM 1.
+At position 151 to 225, the domain is characterized as RRM 2.
+At position 188 to 407, the domain is characterized as MurNAc-LAA.
+At position 209 to 379, the domain is characterized as Helicase ATP-binding.
+At position 469 to 639, the domain is characterized as Helicase C-terminal.
+At position 278 to 408, the domain is characterized as GGDEF.
+At position 63 to 160, the domain is characterized as PH.
+At position 568 to 719, the domain is characterized as STAS.
+At position 144 to 274, the domain is characterized as Fatty acid hydroxylase.
+At position 18 to 111, the domain is characterized as BRCT 1.
+At position 136 to 161, the domain is characterized as BRCT 2.
+At position 1 to 185, the domain is characterized as Glutamine amidotransferase type-1.
+At position 186 to 376, the domain is characterized as GMPS ATP-PPase.
+At position 134 to 418, the domain is characterized as Protein kinase.
+At position 153 to 219, the domain is characterized as KH.
+At position 4 to 145, the domain is characterized as RNase H type-1.
+At position 11 to 109, the domain is characterized as PTS EIIA type-3.
+At position 492 to 641, the domain is characterized as uDENN.
+At position 663 to 796, the domain is characterized as cDENN.
+At position 798 to 888, the domain is characterized as dDENN.
+At position 158 to 324, the domain is characterized as OBG-type G.
+At position 336 to 414, the domain is characterized as OCT.
+At position 5 to 67, the domain is characterized as IBB.
+At position 31 to 131, the domain is characterized as Glutaredoxin.
+At position 171 to 268, the domain is characterized as HTH araC/xylS-type.
+At position 10 to 263, the domain is characterized as Protein kinase.
+At position 374 to 491, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 492 to 595, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 662 to 745, the domain is characterized as POLO box.
+At position 1855 to 1918, the domain is characterized as SAM.
+At position 186 to 284, the domain is characterized as HTH araC/xylS-type.
+At position 459 to 489, the domain is characterized as KASH.
+At position 36 to 81, the domain is characterized as EGF-like 1; atypical.
+At position 123 to 163, the domain is characterized as EGF-like 2; calcium-binding.
+At position 164 to 202, the domain is characterized as EGF-like 3; calcium-binding.
+At position 203 to 242, the domain is characterized as EGF-like 4; calcium-binding.
+At position 243 to 282, the domain is characterized as EGF-like 5; calcium-binding.
+At position 283 to 328, the domain is characterized as EGF-like 6; calcium-binding.
+At position 7 to 67, the domain is characterized as LIM zinc-binding 1.
+At position 68 to 127, the domain is characterized as LIM zinc-binding 2.
+At position 128 to 186, the domain is characterized as LIM zinc-binding 3.
+At position 85 to 320, the domain is characterized as UmuC.
+At position 244 to 412, the domain is characterized as TLDc.
+At position 252 to 340, the domain is characterized as ABM.
+At position 23 to 91, the domain is characterized as HTH gntR-type.
+At position 12 to 112, the domain is characterized as SSB.
+At position 84 to 262, the domain is characterized as FAD-binding PCMH-type.
+At position 183 to 341, the domain is characterized as Cupin type-1 1.
+At position 387 to 564, the domain is characterized as Cupin type-1 2.
+At position 158 to 245, the domain is characterized as PB1.
+At position 29 to 159, the domain is characterized as EamA 1.
+At position 208 to 337, the domain is characterized as EamA 2.
+At position 243 to 475, the domain is characterized as START.
+At position 117 to 288, the domain is characterized as MRG.
+At position 112 to 187, the domain is characterized as PRC barrel.
+At position 5 to 60, the domain is characterized as bHLH.
+At position 303 to 355, the domain is characterized as HAMP 1.
+At position 397 to 450, the domain is characterized as HAMP 2.
+At position 469 to 705, the domain is characterized as Methyl-accepting transducer.
+At position 136 to 440, the domain is characterized as NB-ARC.
+At position 216 to 379, the domain is characterized as W2.
+At position 37 to 100, the domain is characterized as S5 DRBM.
+At position 29 to 159, the domain is characterized as Bulb-type lectin.
+At position 356 to 433, the domain is characterized as PAN.
+At position 177 to 477, the domain is characterized as Protein kinase.
+At position 478 to 555, the domain is characterized as AGC-kinase C-terminal.
+At position 72 to 162, the domain is characterized as PB1.
+At position 46 to 122, the domain is characterized as Ubiquitin-like.
+At position 138 to 219, the domain is characterized as BAG.
+At position 1 to 134, the domain is characterized as PX.
+At position 29 to 73, the domain is characterized as P-type 1.
+At position 79 to 122, the domain is characterized as P-type 2.
+At position 24 to 273, the domain is characterized as Peptidase S1 1.
+At position 294 to 525, the domain is characterized as Peptidase S1 2.
+At position 822 to 907, the domain is characterized as SUEL-type lectin.
+At position 1 to 168, the domain is characterized as PPIase cyclophilin-type.
+At position 244 to 322, the domain is characterized as RRM.
+At position 44 to 193, the domain is characterized as Tyrosine-protein phosphatase.
+At position 71 to 344, the domain is characterized as Pyruvate carboxyltransferase.
+At position 183 to 264, the domain is characterized as RRM Nup35-type.
+At position 1 to 454, the domain is characterized as SMP-LTD.
+At position 543 to 629, the domain is characterized as GED.
+At position 3 to 31, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 36 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 23 to 48, the domain is characterized as EF-hand 1.
+At position 89 to 323, the domain is characterized as Radical SAM core.
+At position 199 to 387, the domain is characterized as GMPS ATP-PPase.
+At position 64 to 126, the domain is characterized as TGS.
+At position 909 to 1064, the domain is characterized as ZU5 1.
+At position 1066 to 1212, the domain is characterized as ZU5 2.
+At position 1399 to 1483, the domain is characterized as Death.
+At position 114 to 143, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 153 to 182, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 95 to 173, the domain is characterized as RRM.
+At position 1 to 56, the domain is characterized as IRS-type PTB.
+At position 162 to 372, the domain is characterized as CP-type G.
+At position 416 to 490, the domain is characterized as RRM 3.
+At position 498 to 586, the domain is characterized as RRM 4.
+At position 315 to 491, the domain is characterized as PCI.
+At position 1 to 284, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 279 to 583, the domain is characterized as UvrD-like helicase C-terminal.
+At position 31 to 292, the domain is characterized as Deacetylase sirtuin-type.
+At position 304 to 540, the domain is characterized as MHD.
+At position 1545 to 1603, the domain is characterized as Prospero-type homeo.
+At position 1604 to 1703, the domain is characterized as Prospero.
+At position 13 to 254, the domain is characterized as ABC transporter.
+At position 207 to 268, the domain is characterized as KH.
+At position 188 to 266, the domain is characterized as RRM 2.
+At position 111 to 146, the domain is characterized as EF-hand 2.
+At position 152 to 187, the domain is characterized as EF-hand 3.
+At position 3 to 124, the domain is characterized as PINc.
+At position 34 to 81, the domain is characterized as KH.
+At position 23 to 314, the domain is characterized as Protein kinase.
+At position 108 to 398, the domain is characterized as Radical SAM core.
+At position 422 to 573, the domain is characterized as N-acetyltransferase.
+At position 373 to 614, the domain is characterized as Histidine kinase.
+At position 779 to 921, the domain is characterized as Response regulatory.
+At position 53 to 112, the domain is characterized as Collagen-like.
+At position 155 to 271, the domain is characterized as C-type lectin.
+At position 146 to 433, the domain is characterized as NR LBD.
+At position 43 to 262, the domain is characterized as Radical SAM core.
+At position 61 to 137, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 204 to 266, the domain is characterized as t-SNARE coiled-coil homology.
+At position 9 to 85, the domain is characterized as GIY-YIG.
+At position 23 to 220, the domain is characterized as tr-type G.
+At position 1 to 58, the domain is characterized as Kazal-like.
+At position 57 to 197, the domain is characterized as Nudix hydrolase.
+At position 268 to 303, the domain is characterized as EF-hand 1.
+At position 312 to 347, the domain is characterized as EF-hand 2.
+At position 431 to 587, the domain is characterized as Ferric oxidoreductase.
+At position 626 to 748, the domain is characterized as FAD-binding FR-type.
+At position 21 to 213, the domain is characterized as NodB homology.
+At position 1 to 109, the domain is characterized as PX.
+At position 115 to 206, the domain is characterized as Ras-associating.
+At position 80 to 123, the domain is characterized as SpoVT-AbrB 2.
+At position 101 to 298, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 14 to 185, the domain is characterized as Phosphatase tensin-type.
+At position 190 to 350, the domain is characterized as C2 tensin-type.
+At position 608 to 948, the domain is characterized as PUM-HD.
+At position 44 to 106, the domain is characterized as Ig-like V-type.
+At position 126 to 223, the domain is characterized as Ig-like C2-type 1.
+At position 236 to 310, the domain is characterized as Ig-like C2-type 2.
+At position 182 to 249, the domain is characterized as BTB.
+At position 35 to 338, the domain is characterized as GH10.
+At position 1 to 255, the domain is characterized as IF rod.
+At position 21 to 223, the domain is characterized as GH16.
+At position 406 to 480, the domain is characterized as B5.
+At position 11 to 225, the domain is characterized as ABC transporter.
+At position 60 to 105, the domain is characterized as CWF21.
+At position 8 to 136, the domain is characterized as VOC 1.
+At position 150 to 263, the domain is characterized as VOC 2.
+At position 161 to 243, the domain is characterized as Expansin-like CBD.
+At position 260 to 509, the domain is characterized as ABC transporter 2.
+At position 8 to 249, the domain is characterized as ABC transporter 1.
+At position 261 to 499, the domain is characterized as ABC transporter 2.
+At position 1445 to 1535, the domain is characterized as PDZ.
+At position 282 to 400, the domain is characterized as Nop.
+At position 1 to 62, the domain is characterized as HMA.
+At position 562 to 650, the domain is characterized as Ig-like.
+At position 49 to 306, the domain is characterized as GB1/RHD3-type G.
+At position 110 to 232, the domain is characterized as MPN.
+At position 14 to 266, the domain is characterized as Pyruvate carboxyltransferase.
+At position 178 to 372, the domain is characterized as Helicase ATP-binding.
+At position 405 to 605, the domain is characterized as Helicase C-terminal.
+At position 71 to 377, the domain is characterized as Peptidase A1.
+At position 17 to 141, the domain is characterized as EamA 1.
+At position 183 to 288, the domain is characterized as EamA 2.
+At position 109 to 189, the domain is characterized as ACT 1.
+At position 224 to 294, the domain is characterized as ACT 2.
+At position 39 to 205, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 252, the domain is characterized as Deacetylase sirtuin-type.
+At position 145 to 239, the domain is characterized as Rhodanese.
+At position 116 to 146, the domain is characterized as EF-hand 2.
+At position 1 to 180, the domain is characterized as PBS-linker.
+At position 220 to 273, the domain is characterized as CpcD-like.
+At position 1 to 439, the domain is characterized as SMP-LTD.
+At position 273 to 448, the domain is characterized as DH.
+At position 92 to 165, the domain is characterized as PRC barrel.
+At position 30 to 136, the domain is characterized as Ig-like C2-type 1.
+At position 160 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 240 to 335, the domain is characterized as Ig-like C2-type 3.
+At position 340 to 421, the domain is characterized as Ig-like C2-type 4.
+At position 430 to 566, the domain is characterized as Ig-like C2-type 5.
+At position 569 to 684, the domain is characterized as Ig-like C2-type 6.
+At position 691 to 777, the domain is characterized as Ig-like C2-type 7.
+At position 858 to 1185, the domain is characterized as Protein kinase.
+At position 66 to 127, the domain is characterized as FHA.
+At position 170 to 436, the domain is characterized as Protein kinase.
+At position 186 to 376, the domain is characterized as Helicase ATP-binding.
+At position 745 to 870, the domain is characterized as C2.
+At position 217 to 379, the domain is characterized as TrmE-type G.
+At position 89 to 162, the domain is characterized as PAS 1.
+At position 163 to 217, the domain is characterized as PAC 1.
+At position 375 to 448, the domain is characterized as PAS 2.
+At position 449 to 503, the domain is characterized as PAC 2.
+At position 576 to 863, the domain is characterized as Protein kinase.
+At position 703 to 968, the domain is characterized as Autotransporter.
+At position 355 to 418, the domain is characterized as bZIP.
+At position 1 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 139 to 169, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 165 to 305, the domain is characterized as PPC.
+At position 17 to 262, the domain is characterized as tr-type G.
+At position 248 to 435, the domain is characterized as GATase cobBQ-type.
+At position 844 to 958, the domain is characterized as VRR-NUC.
+At position 2 to 108, the domain is characterized as Thioredoxin.
+At position 51 to 187, the domain is characterized as MPN.
+At position 59 to 173, the domain is characterized as Response regulatory.
+At position 197 to 269, the domain is characterized as HTH LytTR-type.
+At position 1 to 69, the domain is characterized as J.
+At position 23 to 141, the domain is characterized as Ig-like V-type 1.
+At position 161 to 233, the domain is characterized as Ig-like C1-type 2.
+At position 1 to 227, the domain is characterized as IMD.
+At position 274 to 337, the domain is characterized as SH3.
+At position 26 to 75, the domain is characterized as F-box.
+At position 124 to 214, the domain is characterized as Rhodanese.
+At position 92 to 167, the domain is characterized as Lipoyl-binding.
+At position 22 to 97, the domain is characterized as ACT.
+At position 101 to 397, the domain is characterized as PI3K/PI4K catalytic.
+At position 2 to 282, the domain is characterized as FERM.
+At position 17 to 137, the domain is characterized as CBM6.
+At position 153 to 455, the domain is characterized as GH26.
+At position 365 to 535, the domain is characterized as tr-type G.
+At position 23 to 304, the domain is characterized as Protein kinase.
+At position 324 to 406, the domain is characterized as RRM.
+At position 1 to 49, the domain is characterized as POU-specific.
+At position 62 to 167, the domain is characterized as PRD 1.
+At position 168 to 276, the domain is characterized as PRD 2.
+At position 147 to 460, the domain is characterized as NB-ARC.
+At position 8 to 65, the domain is characterized as Tudor-knot.
+At position 227 to 504, the domain is characterized as MYST-type HAT.
+At position 23 to 281, the domain is characterized as SET.
+At position 157 to 324, the domain is characterized as OBG-type G.
+At position 338 to 416, the domain is characterized as OCT.
+At position 178 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 5 to 87, the domain is characterized as PTS EIIB type-1.
+At position 130 to 484, the domain is characterized as PTS EIIC type-1.
+At position 226 to 274, the domain is characterized as F-box.
+At position 496 to 618, the domain is characterized as HD.
+At position 737 to 821, the domain is characterized as ACT 1.
+At position 848 to 929, the domain is characterized as ACT 2.
+At position 49 to 104, the domain is characterized as bHLH.
+At position 122 to 158, the domain is characterized as Orange.
+At position 2 to 93, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 98 to 197, the domain is characterized as FAD-binding FR-type.
+At position 221 to 256, the domain is characterized as EF-hand 1.
+At position 265 to 300, the domain is characterized as EF-hand 2.
+At position 383 to 540, the domain is characterized as Ferric oxidoreductase.
+At position 575 to 703, the domain is characterized as FAD-binding FR-type.
+At position 25 to 223, the domain is characterized as RNase H type-2.
+At position 464 to 660, the domain is characterized as FtsK.
+At position 110 to 306, the domain is characterized as ATP-grasp.
+At position 289 to 428, the domain is characterized as SIS 1.
+At position 461 to 606, the domain is characterized as SIS 2.
+At position 258 to 355, the domain is characterized as Fe2OG dioxygenase.
+At position 4 to 431, the domain is characterized as SAM-dependent MTase C5-type.
+At position 363 to 646, the domain is characterized as Protein kinase.
+At position 128 to 178, the domain is characterized as DHHC.
+At position 25 to 147, the domain is characterized as MsrB.
+At position 12 to 341, the domain is characterized as PTS EIIC type-2.
+At position 374 to 469, the domain is characterized as PTS EIIB type-2.
+At position 488 to 630, the domain is characterized as PTS EIIA type-2.
+At position 92 to 151, the domain is characterized as S4 RNA-binding.
+At position 35 to 154, the domain is characterized as Ig-like V-type.
+At position 156 to 251, the domain is characterized as Link 1.
+At position 256 to 353, the domain is characterized as Link 2.
+At position 622 to 658, the domain is characterized as EGF-like.
+At position 658 to 786, the domain is characterized as C-type lectin.
+At position 789 to 849, the domain is characterized as Sushi.
+At position 93 to 172, the domain is characterized as PRC barrel.
+At position 8 to 43, the domain is characterized as NB-ARC.
+At position 152 to 392, the domain is characterized as NR LBD.
+At position 10 to 254, the domain is characterized as ABC transporter.
+At position 29 to 160, the domain is characterized as C-type lectin.
+At position 153 to 243, the domain is characterized as TonB C-terminal.
+At position 158 to 208, the domain is characterized as LRRCT.
+At position 21 to 144, the domain is characterized as Ig-like V-type 1.
+At position 145 to 271, the domain is characterized as Ig-like V-type 2.
+At position 277 to 360, the domain is characterized as Ig-like C2-type 1.
+At position 367 to 464, the domain is characterized as Ig-like C2-type 2.
+At position 94 to 147, the domain is characterized as ClpX-type ZB.
+At position 2 to 205, the domain is characterized as ABC transporter.
+At position 29 to 137, the domain is characterized as Rhodanese.
+At position 4 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 394, the domain is characterized as GMPS ATP-PPase.
+At position 180 to 229, the domain is characterized as Collagen-like.
+At position 304 to 471, the domain is characterized as Helicase ATP-binding.
+At position 575 to 735, the domain is characterized as Helicase C-terminal.
+At position 8 to 339, the domain is characterized as Kinesin motor.
+At position 159 to 335, the domain is characterized as OBG-type G.
+At position 323 to 396, the domain is characterized as SAM.
+At position 27 to 132, the domain is characterized as Gnk2-homologous 1.
+At position 142 to 252, the domain is characterized as Gnk2-homologous 2.
+At position 345 to 626, the domain is characterized as Protein kinase.
+At position 125 to 492, the domain is characterized as Protein kinase.
+At position 2 to 185, the domain is characterized as tr-type G.
+At position 7 to 330, the domain is characterized as SAM-dependent MTase C5-type.
+At position 5 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 82 to 181, the domain is characterized as Toprim.
+At position 114 to 215, the domain is characterized as Ig-like C1-type.
+At position 151 to 256, the domain is characterized as Fe2OG dioxygenase.
+At position 30 to 74, the domain is characterized as CHCH.
+At position 55 to 405, the domain is characterized as IF rod.
+At position 273 to 349, the domain is characterized as B5.
+At position 2 to 136, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 393 to 647, the domain is characterized as Tyrosine-protein phosphatase.
+At position 682 to 831, the domain is characterized as Flavodoxin-like.
+At position 17 to 253, the domain is characterized as tr-type G.
+At position 5 to 254, the domain is characterized as Deacetylase sirtuin-type.
+At position 26 to 139, the domain is characterized as Expansin-like EG45.
+At position 467 to 757, the domain is characterized as Protein kinase.
+At position 34 to 201, the domain is characterized as N-acetyltransferase.
+At position 15 to 78, the domain is characterized as HMA.
+At position 226 to 327, the domain is characterized as HD.
+At position 14 to 244, the domain is characterized as Phosphagen kinase C-terminal.
+At position 86 to 379, the domain is characterized as ABC transmembrane type-1 1.
+At position 412 to 647, the domain is characterized as ABC transporter 1.
+At position 835 to 1123, the domain is characterized as ABC transmembrane type-1 2.
+At position 1158 to 1395, the domain is characterized as ABC transporter 2.
+At position 25 to 57, the domain is characterized as LRRNT.
+At position 21 to 149, the domain is characterized as Plastocyanin-like.
+At position 63 to 253, the domain is characterized as TR mART core.
+At position 292 to 481, the domain is characterized as B30.2/SPRY.
+At position 131 to 324, the domain is characterized as ATP-grasp 1.
+At position 663 to 854, the domain is characterized as ATP-grasp 2.
+At position 920 to 1056, the domain is characterized as MGS-like.
+At position 8 to 130, the domain is characterized as Arf-GAP.
+At position 486 to 706, the domain is characterized as Histidine kinase.
+At position 731 to 846, the domain is characterized as Response regulatory.
+At position 446 to 615, the domain is characterized as tr-type G.
+At position 92 to 160, the domain is characterized as POTRA.
+At position 301 to 513, the domain is characterized as PCI.
+At position 451 to 651, the domain is characterized as PAW.
+At position 30 to 205, the domain is characterized as BPL/LPL catalytic.
+At position 115 to 325, the domain is characterized as Alpha-type protein kinase.
+At position 488 to 577, the domain is characterized as Ig-like C2-type 6.
+At position 491 to 724, the domain is characterized as ABC transporter 1.
+At position 1309 to 1544, the domain is characterized as ABC transporter 2.
+At position 98 to 126, the domain is characterized as HhH.
+At position 110 to 349, the domain is characterized as Radical SAM core.
+At position 889 to 929, the domain is characterized as LDL-receptor class A 1.
+At position 929 to 956, the domain is characterized as LDL-receptor class A 2; truncated.
+At position 955 to 1006, the domain is characterized as LDL-receptor class A 3.
+At position 1145 to 1383, the domain is characterized as Peptidase S1 1.
+At position 1394 to 1432, the domain is characterized as LDL-receptor class A 4.
+At position 1713 to 1743, the domain is characterized as LDL-receptor class A 5; truncated.
+At position 1745 to 1775, the domain is characterized as LDL-receptor class A 6; truncated.
+At position 1774 to 1813, the domain is characterized as LDL-receptor class A 7.
+At position 2027 to 2301, the domain is characterized as Peptidase S1 2.
+At position 2308 to 2346, the domain is characterized as LDL-receptor class A 8.
+At position 2349 to 2389, the domain is characterized as LDL-receptor class A 9.
+At position 2387 to 2419, the domain is characterized as LDL-receptor class A 10; truncated.
+At position 2419 to 2459, the domain is characterized as LDL-receptor class A 11.
+At position 1 to 108, the domain is characterized as C2 1.
+At position 251 to 371, the domain is characterized as C2 2.
+At position 411 to 536, the domain is characterized as C2 3.
+At position 579 to 704, the domain is characterized as C2 4.
+At position 83 to 192, the domain is characterized as PH.
+At position 143 to 222, the domain is characterized as Death.
+At position 35 to 282, the domain is characterized as PPM-type phosphatase.
+At position 11 to 127, the domain is characterized as Arf-GAP.
+At position 62 to 201, the domain is characterized as SCP.
+At position 287 to 382, the domain is characterized as LCCL 1.
+At position 388 to 491, the domain is characterized as LCCL 2.
+At position 5 to 55, the domain is characterized as CHCH.
+At position 97 to 271, the domain is characterized as Thioredoxin.
+At position 120 to 304, the domain is characterized as ATP-grasp.
+At position 15 to 277, the domain is characterized as Radical SAM core.
+At position 79 to 237, the domain is characterized as Flavodoxin-like.
+At position 400 to 644, the domain is characterized as Radical SAM core.
+At position 196 to 368, the domain is characterized as EngA-type G 2.
+At position 35 to 136, the domain is characterized as Plastocyanin-like.
+At position 363 to 413, the domain is characterized as DHHC.
+At position 217 to 276, the domain is characterized as SH3 1.
+At position 277 to 334, the domain is characterized as SH3 2.
+At position 330 to 411, the domain is characterized as PAN.
+At position 64 to 239, the domain is characterized as Helicase ATP-binding.
+At position 381 to 548, the domain is characterized as Helicase C-terminal.
+At position 122 to 325, the domain is characterized as FAD-binding PCMH-type.
+At position 148 to 247, the domain is characterized as SH2.
+At position 543 to 813, the domain is characterized as Ras-GEF.
+At position 13 to 68, the domain is characterized as bHLH.
+At position 83 to 116, the domain is characterized as Orange.
+At position 103 to 181, the domain is characterized as PRC barrel.
+At position 1 to 29, the domain is characterized as ShKT.
+At position 1 to 180, the domain is characterized as Macro.
+At position 211 to 284, the domain is characterized as RRM 1.
+At position 295 to 368, the domain is characterized as RRM 2.
+At position 319 to 438, the domain is characterized as Toprim.
+At position 165 to 446, the domain is characterized as Protein kinase.
+At position 209 to 338, the domain is characterized as EamA.
+At position 1 to 152, the domain is characterized as TCTP.
+At position 41 to 168, the domain is characterized as ALOG.
+At position 274 to 345, the domain is characterized as PUA.
+At position 11 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 241 to 419, the domain is characterized as FAD-binding PCMH-type.
+At position 719 to 776, the domain is characterized as CBS 2.
+At position 21 to 135, the domain is characterized as Response regulatory.
+At position 14 to 68, the domain is characterized as SMP 1.
+At position 136 to 192, the domain is characterized as SMP 2.
+At position 201 to 260, the domain is characterized as SMP 3.
+At position 5 to 166, the domain is characterized as Thioredoxin.
+At position 135 to 437, the domain is characterized as NB-ARC.
+At position 137 to 199, the domain is characterized as t-SNARE coiled-coil homology.
+At position 305 to 329, the domain is characterized as NAF.
+At position 5 to 137, the domain is characterized as ADF-H.
+At position 4 to 617, the domain is characterized as Protein kinase.
+At position 427 to 712, the domain is characterized as Protein kinase.
+At position 242 to 305, the domain is characterized as bZIP.
+At position 144 to 210, the domain is characterized as J.
+At position 103 to 199, the domain is characterized as PB1.
+At position 22 to 148, the domain is characterized as MPN.
+At position 57 to 259, the domain is characterized as TLC.
+At position 104 to 157, the domain is characterized as KASH.
+At position 17 to 188, the domain is characterized as Glutamine amidotransferase type-1.
+At position 13 to 199, the domain is characterized as CRAL-TRIO.
+At position 226 to 412, the domain is characterized as Rho-GAP.
+At position 1 to 153, the domain is characterized as PPIase cyclophilin-type.
+At position 16 to 71, the domain is characterized as bHLH.
+At position 59 to 96, the domain is characterized as LRRNT.
+At position 630 to 764, the domain is characterized as C2.
+At position 37 to 71, the domain is characterized as LDL-receptor class A 1.
+At position 69 to 113, the domain is characterized as LDL-receptor class A 2.
+At position 209 to 244, the domain is characterized as EF-hand 1.
+At position 245 to 290, the domain is characterized as EF-hand 2.
+At position 406 to 507, the domain is characterized as MRH.
+At position 22 to 102, the domain is characterized as IGFBP N-terminal.
+At position 188 to 262, the domain is characterized as Thyroglobulin type-1.
+At position 85 to 137, the domain is characterized as Kazal-like 1.
+At position 176 to 229, the domain is characterized as Kazal-like 2.
+At position 261 to 301, the domain is characterized as EGF-like.
+At position 113 to 189, the domain is characterized as PRC barrel.
+At position 86 to 198, the domain is characterized as Ferric oxidoreductase.
+At position 225 to 348, the domain is characterized as FAD-binding FR-type.
+At position 59 to 291, the domain is characterized as Helicase ATP-binding.
+At position 330 to 507, the domain is characterized as Helicase C-terminal.
+At position 38 to 175, the domain is characterized as Thioredoxin.
+At position 8 to 112, the domain is characterized as MaoC-like.
+At position 45 to 352, the domain is characterized as AB hydrolase-1.
+At position 373 to 430, the domain is characterized as CBS 1.
+At position 434 to 487, the domain is characterized as CBS 2.
+At position 265 to 401, the domain is characterized as Flavodoxin-like.
+At position 78 to 138, the domain is characterized as SH3.
+At position 144 to 241, the domain is characterized as SH2.
+At position 262 to 515, the domain is characterized as Protein kinase.
+At position 56 to 272, the domain is characterized as Radical SAM core.
+At position 37 to 150, the domain is characterized as DOMON.
+At position 80 to 372, the domain is characterized as ABC transmembrane type-1 1.
+At position 405 to 706, the domain is characterized as ABC transporter 1.
+At position 777 to 1063, the domain is characterized as ABC transmembrane type-1 2.
+At position 1096 to 1333, the domain is characterized as ABC transporter 2.
+At position 80 to 342, the domain is characterized as Protein kinase.
+At position 133 to 162, the domain is characterized as IQ.
+At position 515 to 708, the domain is characterized as SEC7.
+At position 772 to 864, the domain is characterized as PH.
+At position 132 to 569, the domain is characterized as Urease.
+At position 710 to 802, the domain is characterized as FDX-ACB.
+At position 3 to 68, the domain is characterized as SH3 1.
+At position 69 to 132, the domain is characterized as SH3 2.
+At position 353 to 415, the domain is characterized as SH3 3.
+At position 13 to 145, the domain is characterized as B12-binding.
+At position 188 to 402, the domain is characterized as Radical SAM core.
+At position 32 to 127, the domain is characterized as CTCK.
+At position 14 to 217, the domain is characterized as Cytochrome b561.
+At position 32 to 99, the domain is characterized as KH 1.
+At position 130 to 196, the domain is characterized as KH 2.
+At position 406 to 473, the domain is characterized as KH 3.
+At position 30 to 88, the domain is characterized as Chromo 1.
+At position 1386 to 1943, the domain is characterized as FAT.
+At position 2052 to 2370, the domain is characterized as PI3K/PI4K catalytic.
+At position 2354 to 2386, the domain is characterized as FATC.
+At position 1 to 260, the domain is characterized as F-BAR.
+At position 292 to 372, the domain is characterized as REM-1.
+At position 437 to 496, the domain is characterized as SH3.
+At position 8 to 133, the domain is characterized as CMP/dCMP-type deaminase.
+At position 141 to 332, the domain is characterized as Rho-GAP.
+At position 141 to 277, the domain is characterized as LTD.
+At position 393 to 488, the domain is characterized as SH2.
+At position 57 to 161, the domain is characterized as Calponin-homology (CH) 1.
+At position 176 to 281, the domain is characterized as Calponin-homology (CH) 2.
+At position 2218 to 2328, the domain is characterized as PH.
+At position 9 to 55, the domain is characterized as SpoVT-AbrB 1.
+At position 37 to 321, the domain is characterized as Protein kinase.
+At position 8 to 291, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 292 to 565, the domain is characterized as UvrD-like helicase C-terminal.
+At position 66 to 127, the domain is characterized as SH3 2.
+At position 146 to 205, the domain is characterized as SH3 3.
+At position 244 to 303, the domain is characterized as SH3 4.
+At position 783 to 970, the domain is characterized as DH.
+At position 1011 to 1220, the domain is characterized as BAR.
+At position 1288 to 1351, the domain is characterized as SH3 5.
+At position 1516 to 1579, the domain is characterized as SH3 6.
+At position 11 to 274, the domain is characterized as Protein kinase.
+At position 356 to 422, the domain is characterized as PASTA 1.
+At position 423 to 490, the domain is characterized as PASTA 2.
+At position 491 to 557, the domain is characterized as PASTA 3.
+At position 558 to 626, the domain is characterized as PASTA 4.
+At position 185 to 270, the domain is characterized as Rieske.
+At position 364 to 794, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1254 to 1573, the domain is characterized as PKS/mFAS DH.
+At position 1616 to 1693, the domain is characterized as Carrier.
+At position 88 to 224, the domain is characterized as GST C-terminal.
+At position 253 to 336, the domain is characterized as IPT/TIG.
+At position 97 to 408, the domain is characterized as IF rod.
+At position 110 to 177, the domain is characterized as GRAM.
+At position 1 to 119, the domain is characterized as MGS-like.
+At position 32 to 285, the domain is characterized as Pyruvate carboxyltransferase.
+At position 14 to 197, the domain is characterized as RNase H type-2.
+At position 139 to 245, the domain is characterized as PpiC.
+At position 39 to 90, the domain is characterized as sHSP.
+At position 530 to 584, the domain is characterized as LRRCT.
+At position 636 to 779, the domain is characterized as TIR.
+At position 15 to 241, the domain is characterized as AB hydrolase-1.
+At position 33 to 402, the domain is characterized as Protein kinase.
+At position 1025 to 1154, the domain is characterized as MATH 1.
+At position 1172 to 1291, the domain is characterized as MATH 2.
+At position 1 to 60, the domain is characterized as LCN-type CS-alpha/beta.
+At position 243 to 496, the domain is characterized as ABC transporter 2.
+At position 31 to 82, the domain is characterized as FHA.
+At position 351 to 403, the domain is characterized as SAM.
+At position 147 to 306, the domain is characterized as JmjC.
+At position 73 to 186, the domain is characterized as Thioredoxin.
+At position 148 to 260, the domain is characterized as CENP-V/GFA.
+At position 51 to 222, the domain is characterized as VWFA 1.
+At position 296 to 333, the domain is characterized as EGF-like 1.
+At position 343 to 517, the domain is characterized as VWFA 2.
+At position 531 to 705, the domain is characterized as VWFA 3.
+At position 712 to 748, the domain is characterized as EGF-like 2.
+At position 290 to 529, the domain is characterized as Glutamine amidotransferase type-1.
+At position 18 to 188, the domain is characterized as N-acetyltransferase.
+At position 445 to 518, the domain is characterized as PAS.
+At position 115 to 662, the domain is characterized as Lipoxygenase.
+At position 46 to 95, the domain is characterized as PSI.
+At position 146 to 384, the domain is characterized as VWFA.
+At position 595 to 675, the domain is characterized as PB1.
+At position 25 to 255, the domain is characterized as Peptidase S1.
+At position 205 to 469, the domain is characterized as NR LBD.
+At position 24 to 687, the domain is characterized as Vitellogenin.
+At position 1308 to 1477, the domain is characterized as VWFD.
+At position 236 to 453, the domain is characterized as FAD-binding FR-type.
+At position 26 to 157, the domain is characterized as Nudix hydrolase.
+At position 47 to 117, the domain is characterized as HTH iclR-type.
+At position 1 to 71, the domain is characterized as LITAF.
+At position 15 to 94, the domain is characterized as GIY-YIG.
+At position 208 to 261, the domain is characterized as CVC.
+At position 48 to 211, the domain is characterized as PPIase cyclophilin-type.
+At position 761 to 821, the domain is characterized as RAP.
+At position 147 to 315, the domain is characterized as Helicase ATP-binding.
+At position 490 to 651, the domain is characterized as Helicase C-terminal.
+At position 50 to 479, the domain is characterized as IF rod.
+At position 439 to 749, the domain is characterized as NACHT.
+At position 460 to 638, the domain is characterized as Helicase ATP-binding.
+At position 665 to 813, the domain is characterized as Helicase C-terminal.
+At position 12 to 129, the domain is characterized as PINc.
+At position 12 to 258, the domain is characterized as Protein kinase.
+At position 41 to 715, the domain is characterized as Myosin motor.
+At position 740 to 765, the domain is characterized as IQ 2.
+At position 773 to 962, the domain is characterized as TH1.
+At position 1075 to 1134, the domain is characterized as SH3.
+At position 199 to 535, the domain is characterized as Kinesin motor.
+At position 21 to 176, the domain is characterized as N-acetyltransferase 1.
+At position 191 to 354, the domain is characterized as N-acetyltransferase 2.
+At position 589 to 692, the domain is characterized as tRNA-binding.
+At position 369 to 696, the domain is characterized as HECT.
+At position 22 to 85, the domain is characterized as PAS.
+At position 7 to 184, the domain is characterized as Miro 1.
+At position 200 to 235, the domain is characterized as EF-hand 1.
+At position 320 to 355, the domain is characterized as EF-hand 2.
+At position 436 to 601, the domain is characterized as Miro 2.
+At position 33 to 132, the domain is characterized as Cadherin 1.
+At position 156 to 241, the domain is characterized as Cadherin 2.
+At position 242 to 349, the domain is characterized as Cadherin 3.
+At position 350 to 454, the domain is characterized as Cadherin 4.
+At position 580 to 677, the domain is characterized as Cadherin 6.
+At position 79 to 289, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 352, the domain is characterized as Protein kinase.
+At position 25 to 284, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 399 to 568, the domain is characterized as tr-type G.
+At position 45 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 160 to 619, the domain is characterized as TBDR beta-barrel.
+At position 179 to 354, the domain is characterized as EngA-type G 2.
+At position 355 to 438, the domain is characterized as KH-like.
+At position 38 to 77, the domain is characterized as Pentapeptide repeat 1.
+At position 78 to 117, the domain is characterized as Pentapeptide repeat 2.
+At position 118 to 157, the domain is characterized as Pentapeptide repeat 3.
+At position 296 to 371, the domain is characterized as PUA.
+At position 107 to 399, the domain is characterized as ABC transmembrane type-1.
+At position 478 to 704, the domain is characterized as ABC transporter.
+At position 144 to 180, the domain is characterized as EGF-like 1.
+At position 182 to 218, the domain is characterized as EGF-like 2; calcium-binding.
+At position 220 to 256, the domain is characterized as EGF-like 3; calcium-binding.
+At position 258 to 298, the domain is characterized as EGF-like 4.
+At position 300 to 336, the domain is characterized as EGF-like 5; calcium-binding.
+At position 338 to 374, the domain is characterized as EGF-like 6.
+At position 376 to 413, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1018 to 1054, the domain is characterized as EGF-like 8.
+At position 1059 to 1266, the domain is characterized as Laminin G-like 1.
+At position 1309 to 1346, the domain is characterized as EGF-like 9.
+At position 1353 to 1549, the domain is characterized as Laminin G-like 2.
+At position 1545 to 1581, the domain is characterized as EGF-like 10.
+At position 1583 to 1621, the domain is characterized as EGF-like 11.
+At position 1692 to 1879, the domain is characterized as Laminin G-like 3.
+At position 1875 to 1912, the domain is characterized as EGF-like 12.
+At position 1913 to 1946, the domain is characterized as EGF-like 13.
+At position 1952 to 2166, the domain is characterized as Laminin G-like 4.
+At position 28 to 282, the domain is characterized as Protein kinase.
+At position 340 to 364, the domain is characterized as NAF.
+At position 26 to 166, the domain is characterized as MARVEL.
+At position 77 to 253, the domain is characterized as IRG-type G.
+At position 189 to 407, the domain is characterized as Radical SAM core.
+At position 300 to 495, the domain is characterized as Histidine kinase.
+At position 48 to 130, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 242 to 329, the domain is characterized as Ig-like C2-type 3.
+At position 337 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 408 to 486, the domain is characterized as Ig-like C2-type 5.
+At position 491 to 568, the domain is characterized as Ig-like C2-type 6.
+At position 573 to 662, the domain is characterized as Ig-like C2-type 7.
+At position 666 to 739, the domain is characterized as Ig-like C2-type 8.
+At position 746 to 830, the domain is characterized as Ig-like C2-type 9.
+At position 734 to 994, the domain is characterized as Tyrosine-protein phosphatase.
+At position 48 to 150, the domain is characterized as Collagen-like.
+At position 154 to 290, the domain is characterized as C1q.
+At position 16 to 87, the domain is characterized as RRM.
+At position 103 to 301, the domain is characterized as ATP-grasp.
+At position 5 to 76, the domain is characterized as Sm.
+At position 12 to 326, the domain is characterized as Hcy-binding.
+At position 506 to 648, the domain is characterized as Flavodoxin-like.
+At position 688 to 932, the domain is characterized as FAD-binding FR-type.
+At position 35 to 92, the domain is characterized as bHLH.
+At position 111 to 144, the domain is characterized as Orange.
+At position 230 to 331, the domain is characterized as HD.
+At position 46 to 138, the domain is characterized as DEP.
+At position 7 to 193, the domain is characterized as Flavodoxin-like.
+At position 47 to 274, the domain is characterized as Peptidase S1.
+At position 86 to 783, the domain is characterized as Myosin motor.
+At position 786 to 815, the domain is characterized as IQ.
+At position 452 to 688, the domain is characterized as ABC transporter.
+At position 87 to 115, the domain is characterized as IQ 1.
+At position 116 to 138, the domain is characterized as IQ 2.
+At position 139 to 164, the domain is characterized as IQ 3.
+At position 168 to 244, the domain is characterized as Toprim.
+At position 2 to 57, the domain is characterized as HTH myb-type 1.
+At position 58 to 102, the domain is characterized as HTH myb-type 2.
+At position 40 to 150, the domain is characterized as tRNA-binding.
+At position 28 to 87, the domain is characterized as Chromo.
+At position 16 to 311, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 24 to 256, the domain is characterized as Radical SAM core.
+At position 107 to 381, the domain is characterized as SET.
+At position 1 to 101, the domain is characterized as Hcy-binding.
+At position 365 to 482, the domain is characterized as FZ.
+At position 522 to 704, the domain is characterized as Laminin G-like.
+At position 823 to 878, the domain is characterized as Collagen-like 1.
+At position 953 to 1007, the domain is characterized as Collagen-like 2.
+At position 1008 to 1041, the domain is characterized as Collagen-like 3.
+At position 1066 to 1117, the domain is characterized as Collagen-like 4.
+At position 1118 to 1147, the domain is characterized as Collagen-like 5.
+At position 1162 to 1202, the domain is characterized as Collagen-like 6.
+At position 1216 to 1264, the domain is characterized as Collagen-like 7.
+At position 450 to 646, the domain is characterized as FtsK.
+At position 110 to 204, the domain is characterized as Ig-like C1-type.
+At position 40 to 221, the domain is characterized as tr-type G.
+At position 134 to 389, the domain is characterized as Protein kinase.
+At position 390 to 460, the domain is characterized as AGC-kinase C-terminal.
+At position 11 to 81, the domain is characterized as J.
+At position 1 to 99, the domain is characterized as C2 1.
+At position 152 to 265, the domain is characterized as C2 2.
+At position 308 to 425, the domain is characterized as C2 3.
+At position 1057 to 1188, the domain is characterized as C2 4.
+At position 1213 to 1346, the domain is characterized as C2 5.
+At position 1467 to 1587, the domain is characterized as C2 6.
+At position 1705 to 1853, the domain is characterized as C2 7.
+At position 271 to 491, the domain is characterized as Fibrinogen C-terminal.
+At position 62 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 146 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 39 to 113, the domain is characterized as KH type-2.
+At position 38 to 161, the domain is characterized as Ig-like V-type 1.
+At position 162 to 256, the domain is characterized as Ig-like V-type 2.
+At position 35 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 145 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 236 to 315, the domain is characterized as Ig-like C2-type 3.
+At position 328 to 403, the domain is characterized as Ig-like C2-type 4.
+At position 424 to 493, the domain is characterized as Ig-like C2-type 5.
+At position 499 to 590, the domain is characterized as Ig-like C2-type 6.
+At position 20 to 270, the domain is characterized as Protein kinase.
+At position 81 to 170, the domain is characterized as NID 1.
+At position 183 to 266, the domain is characterized as NID 2.
+At position 15 to 205, the domain is characterized as DPCK.
+At position 204 to 362, the domain is characterized as SUN.
+At position 76 to 139, the domain is characterized as bZIP.
+At position 61 to 238, the domain is characterized as TR mART core.
+At position 2 to 103, the domain is characterized as Calponin-homology (CH).
+At position 173 to 247, the domain is characterized as EB1 C-terminal.
+At position 362 to 422, the domain is characterized as LIM zinc-binding 3.
+At position 292 to 466, the domain is characterized as Helicase ATP-binding.
+At position 645 to 801, the domain is characterized as Helicase C-terminal.
+At position 32 to 102, the domain is characterized as Chitin-binding type R&R.
+At position 6 to 77, the domain is characterized as RRM.
+At position 514 to 573, the domain is characterized as DDT.
+At position 696 to 765, the domain is characterized as HTH HARE-type.
+At position 4 to 63, the domain is characterized as CHORD 1.
+At position 140 to 199, the domain is characterized as CHORD 2.
+At position 210 to 301, the domain is characterized as CS.
+At position 85 to 178, the domain is characterized as K-box.
+At position 52 to 281, the domain is characterized as Radical SAM core.
+At position 128 to 418, the domain is characterized as ABC transmembrane type-1.
+At position 453 to 689, the domain is characterized as ABC transporter.
+At position 276 to 335, the domain is characterized as SH3.
+At position 12 to 306, the domain is characterized as Protein kinase.
+At position 400 to 435, the domain is characterized as EF-hand 1.
+At position 436 to 471, the domain is characterized as EF-hand 2.
+At position 478 to 513, the domain is characterized as EF-hand 3.
+At position 308 to 507, the domain is characterized as Peptidase M12A.
+At position 510 to 546, the domain is characterized as ShKT.
+At position 358 to 507, the domain is characterized as MATH.
+At position 130 to 182, the domain is characterized as Kazal-like.
+At position 310 to 376, the domain is characterized as Thyroglobulin type-1.
+At position 19 to 91, the domain is characterized as S1-like.
+At position 35 to 114, the domain is characterized as PAS.
+At position 118 to 158, the domain is characterized as PAC.
+At position 196 to 242, the domain is characterized as F-box.
+At position 469 to 586, the domain is characterized as MaoC-like.
+At position 11 to 81, the domain is characterized as MBD.
+At position 1385 to 1447, the domain is characterized as PWWP.
+At position 152 to 238, the domain is characterized as RRM.
+At position 29 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 115 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 308, the domain is characterized as Ig-like C2-type 3.
+At position 401 to 482, the domain is characterized as Ig-like C2-type 5.
+At position 572 to 665, the domain is characterized as Ig-like C2-type 6.
+At position 662 to 756, the domain is characterized as Ig-like C2-type 7.
+At position 761 to 853, the domain is characterized as Ig-like C2-type 8.
+At position 857 to 942, the domain is characterized as Ig-like C2-type 9.
+At position 949 to 1044, the domain is characterized as Ig-like C2-type 10.
+At position 1049 to 1134, the domain is characterized as Ig-like C2-type 11.
+At position 1145 to 1226, the domain is characterized as Ig-like C2-type 12.
+At position 502 to 759, the domain is characterized as Olfactomedin-like.
+At position 3 to 106, the domain is characterized as HIT.
+At position 214 to 518, the domain is characterized as Protein kinase.
+At position 519 to 598, the domain is characterized as AGC-kinase C-terminal.
+At position 1558 to 1667, the domain is characterized as MaoC-like.
+At position 44 to 228, the domain is characterized as tr-type G.
+At position 620 to 922, the domain is characterized as Autotransporter.
+At position 254 to 337, the domain is characterized as IPT/TIG.
+At position 358 to 636, the domain is characterized as Protein kinase.
+At position 2004 to 2225, the domain is characterized as Histidine kinase.
+At position 2340 to 2466, the domain is characterized as Response regulatory.
+At position 20 to 162, the domain is characterized as RNase H type-1.
+At position 222 to 459, the domain is characterized as NR LBD.
+At position 45 to 277, the domain is characterized as ABC transporter.
+At position 316 to 585, the domain is characterized as ABC transporter 1.
+At position 605 to 937, the domain is characterized as ABC transporter 2.
+At position 414 to 584, the domain is characterized as tr-type G.
+At position 293 to 426, the domain is characterized as GGDEF.
+At position 435 to 689, the domain is characterized as EAL.
+At position 18 to 52, the domain is characterized as SAP.
+At position 6 to 90, the domain is characterized as Phosphagen kinase N-terminal.
+At position 118 to 355, the domain is characterized as Phosphagen kinase C-terminal.
+At position 34 to 153, the domain is characterized as FZ.
+At position 25 to 115, the domain is characterized as Ig-like.
+At position 336 to 428, the domain is characterized as PH.
+At position 451 to 574, the domain is characterized as Arf-GAP.
+At position 1082 to 1144, the domain is characterized as SH3.
+At position 6 to 86, the domain is characterized as GST N-terminal.
+At position 91 to 218, the domain is characterized as GST C-terminal.
+At position 7 to 120, the domain is characterized as Response regulatory.
+At position 97 to 147, the domain is characterized as DHHC.
+At position 3 to 241, the domain is characterized as ABC transporter.
+At position 228 to 442, the domain is characterized as Helicase ATP-binding.
+At position 482 to 650, the domain is characterized as Helicase C-terminal.
+At position 237 to 310, the domain is characterized as RRM 1.
+At position 316 to 395, the domain is characterized as RRM 2.
+At position 200 to 416, the domain is characterized as Rap-GAP.
+At position 498 to 812, the domain is characterized as CNH.
+At position 106 to 446, the domain is characterized as USP.
+At position 495 to 598, the domain is characterized as DUSP 1.
+At position 613 to 715, the domain is characterized as DUSP 2.
+At position 738 to 862, the domain is characterized as DUSP 3.
+At position 961 to 1037, the domain is characterized as Ubiquitin-like.
+At position 219 to 407, the domain is characterized as Glutamine amidotransferase type-1.
+At position 19 to 96, the domain is characterized as RRM.
+At position 4 to 72, the domain is characterized as HTH gntR-type.
+At position 196 to 392, the domain is characterized as Peptidase M12B.
+At position 400 to 486, the domain is characterized as Disintegrin.
+At position 1030 to 1229, the domain is characterized as PH.
+At position 46 to 104, the domain is characterized as TCP.
+At position 17 to 101, the domain is characterized as GST N-terminal.
+At position 106 to 233, the domain is characterized as GST C-terminal.
+At position 69 to 200, the domain is characterized as HD.
+At position 237 to 338, the domain is characterized as HD.
+At position 155 to 228, the domain is characterized as HTH crp-type.
+At position 66 to 129, the domain is characterized as S5 DRBM.
+At position 87 to 258, the domain is characterized as Helicase ATP-binding.
+At position 282 to 430, the domain is characterized as Helicase C-terminal.
+At position 123 to 245, the domain is characterized as C2 2.
+At position 285 to 505, the domain is characterized as VWFA.
+At position 41 to 253, the domain is characterized as Bin3-type SAM.
+At position 620 to 709, the domain is characterized as BRCT.
+At position 39 to 92, the domain is characterized as WAP.
+At position 126 to 177, the domain is characterized as Kazal-like.
+At position 210 to 303, the domain is characterized as Ig-like C2-type.
+At position 328 to 378, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 386 to 436, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 445 to 566, the domain is characterized as NTR.
+At position 269 to 344, the domain is characterized as B5.
+At position 35 to 176, the domain is characterized as GAF.
+At position 205 to 432, the domain is characterized as Sigma-54 factor interaction.
+At position 2 to 135, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 12 to 149, the domain is characterized as N-acetyltransferase 1.
+At position 165 to 308, the domain is characterized as N-acetyltransferase 2.
+At position 341 to 407, the domain is characterized as S4 RNA-binding.
+At position 1 to 197, the domain is characterized as MAGE.
+At position 95 to 227, the domain is characterized as Fe2OG dioxygenase.
+At position 158 to 326, the domain is characterized as OBG-type G.
+At position 341 to 419, the domain is characterized as OCT.
+At position 160 to 204, the domain is characterized as CHCH.
+At position 30 to 141, the domain is characterized as MTTase N-terminal.
+At position 165 to 394, the domain is characterized as Radical SAM core.
+At position 397 to 463, the domain is characterized as TRAM.
+At position 7 to 278, the domain is characterized as CN hydrolase.
+At position 175 to 220, the domain is characterized as UBA.
+At position 555 to 722, the domain is characterized as Helicase ATP-binding.
+At position 832 to 1012, the domain is characterized as Helicase C-terminal.
+At position 40 to 147, the domain is characterized as Cadherin 1.
+At position 148 to 265, the domain is characterized as Cadherin 2.
+At position 278 to 395, the domain is characterized as Cadherin 3.
+At position 396 to 509, the domain is characterized as Cadherin 4.
+At position 510 to 616, the domain is characterized as Cadherin 5.
+At position 617 to 717, the domain is characterized as Cadherin 6.
+At position 719 to 819, the domain is characterized as Cadherin 7.
+At position 820 to 926, the domain is characterized as Cadherin 8.
+At position 927 to 1035, the domain is characterized as Cadherin 9.
+At position 1037 to 1144, the domain is characterized as Cadherin 10.
+At position 1145 to 1259, the domain is characterized as Cadherin 11.
+At position 29 to 65, the domain is characterized as LRRNT.
+At position 167 to 217, the domain is characterized as LRRCT.
+At position 8 to 135, the domain is characterized as MATH.
+At position 23 to 219, the domain is characterized as EngB-type G.
+At position 3 to 188, the domain is characterized as Glutamine amidotransferase type-1.
+At position 54 to 158, the domain is characterized as Calponin-homology (CH) 1.
+At position 173 to 278, the domain is characterized as Calponin-homology (CH) 2.
+At position 257 to 452, the domain is characterized as PCI.
+At position 4 to 87, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 473 to 566, the domain is characterized as SH2.
+At position 1531 to 1673, the domain is characterized as VPS9.
+At position 1689 to 1777, the domain is characterized as Ras-associating.
+At position 36 to 163, the domain is characterized as C-type lysozyme.
+At position 193 to 474, the domain is characterized as FERM.
+At position 35 to 72, the domain is characterized as Myb-like.
+At position 28 to 157, the domain is characterized as Nudix hydrolase.
+At position 74 to 292, the domain is characterized as Radical SAM core.
+At position 65 to 153, the domain is characterized as PPIase FKBP-type 1.
+At position 181 to 271, the domain is characterized as PPIase FKBP-type 2.
+At position 299 to 393, the domain is characterized as PPIase FKBP-type 3.
+At position 1 to 250, the domain is characterized as IMD.
+At position 375 to 438, the domain is characterized as SH3.
+At position 34 to 149, the domain is characterized as SCP.
+At position 15 to 101, the domain is characterized as Acylphosphatase-like.
+At position 34 to 216, the domain is characterized as BPL/LPL catalytic.
+At position 117 to 250, the domain is characterized as TIR.
+At position 44 to 230, the domain is characterized as Peptidase M12A.
+At position 224 to 263, the domain is characterized as EGF-like.
+At position 1 to 56, the domain is characterized as Ubiquitin-like 1.
+At position 57 to 132, the domain is characterized as Ubiquitin-like 2.
+At position 23 to 83, the domain is characterized as v-SNARE coiled-coil homology.
+At position 84 to 275, the domain is characterized as Rab-GAP TBC.
+At position 408 to 585, the domain is characterized as TLDc.
+At position 42 to 144, the domain is characterized as Ig-like C2-type 1.
+At position 160 to 244, the domain is characterized as Ig-like C2-type 2.
+At position 146 to 346, the domain is characterized as Peptidase M12A.
+At position 348 to 460, the domain is characterized as CUB 1.
+At position 461 to 573, the domain is characterized as CUB 2.
+At position 573 to 614, the domain is characterized as EGF-like 1; calcium-binding.
+At position 617 to 729, the domain is characterized as CUB 3.
+At position 729 to 769, the domain is characterized as EGF-like 2; calcium-binding.
+At position 773 to 885, the domain is characterized as CUB 4.
+At position 886 to 1002, the domain is characterized as CUB 5.
+At position 103 to 138, the domain is characterized as EF-hand 1.
+At position 148 to 183, the domain is characterized as EF-hand 2.
+At position 181 to 502, the domain is characterized as DOT1.
+At position 51 to 117, the domain is characterized as HMA 1.
+At position 133 to 199, the domain is characterized as HMA 2.
+At position 207 to 273, the domain is characterized as HMA 3.
+At position 313 to 480, the domain is characterized as Helicase ATP-binding.
+At position 649 to 810, the domain is characterized as Helicase C-terminal.
+At position 24 to 266, the domain is characterized as ABC transporter.
+At position 149 to 245, the domain is characterized as RRM 1.
+At position 249 to 325, the domain is characterized as RRM 2.
+At position 400 to 479, the domain is characterized as RRM 3.
+At position 217 to 366, the domain is characterized as TrmE-type G.
+At position 552 to 728, the domain is characterized as tr-type G.
+At position 18 to 93, the domain is characterized as S1-like.
+At position 85 to 345, the domain is characterized as Protein kinase.
+At position 462 to 553, the domain is characterized as PH.
+At position 298 to 542, the domain is characterized as B30.2/SPRY.
+At position 180 to 437, the domain is characterized as Protein kinase.
+At position 438 to 515, the domain is characterized as AGC-kinase C-terminal.
+At position 28 to 217, the domain is characterized as RNase H type-2.
+At position 35 to 162, the domain is characterized as Thioredoxin.
+At position 4 to 129, the domain is characterized as Galectin.
+At position 199 to 255, the domain is characterized as SSD.
+At position 3 to 325, the domain is characterized as Kinesin motor.
+At position 61 to 220, the domain is characterized as N-acetyltransferase.
+At position 797 to 974, the domain is characterized as Helicase ATP-binding.
+At position 1031 to 1180, the domain is characterized as Helicase C-terminal.
+At position 81 to 376, the domain is characterized as AB hydrolase-1.
+At position 208 to 271, the domain is characterized as bZIP.
+At position 31 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 218, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 317, the domain is characterized as Ig-like C2-type 3.
+At position 309 to 407, the domain is characterized as Ig-like C2-type 4.
+At position 412 to 497, the domain is characterized as Ig-like C2-type 5.
+At position 503 to 586, the domain is characterized as Ig-like C2-type 6.
+At position 578 to 680, the domain is characterized as Ig-like C2-type 7.
+At position 796 to 1066, the domain is characterized as Protein kinase; inactive.
+At position 318 to 381, the domain is characterized as MIR 1.
+At position 392 to 449, the domain is characterized as MIR 2.
+At position 453 to 513, the domain is characterized as MIR 3.
+At position 349 to 640, the domain is characterized as Protein kinase.
+At position 443 to 612, the domain is characterized as tr-type G.
+At position 1 to 94, the domain is characterized as PTS EIIB type-2.
+At position 27 to 215, the domain is characterized as ABC transmembrane type-1.
+At position 128 to 312, the domain is characterized as Helicase ATP-binding.
+At position 323 to 483, the domain is characterized as Helicase C-terminal.
+At position 14 to 25, the domain is characterized as Peptidase M12B.
+At position 21 to 233, the domain is characterized as Radical SAM core.
+At position 21 to 116, the domain is characterized as Cystatin.
+At position 634 to 714, the domain is characterized as BRCT.
+At position 121 to 358, the domain is characterized as Radical SAM core.
+At position 87 to 185, the domain is characterized as HTH araC/xylS-type.
+At position 868 to 1013, the domain is characterized as TIR.
+At position 411 to 519, the domain is characterized as Fe2OG dioxygenase.
+At position 782 to 893, the domain is characterized as MaoC-like.
+At position 557 to 620, the domain is characterized as bZIP.
+At position 33 to 265, the domain is characterized as GB1/RHD3-type G.
+At position 314 to 375, the domain is characterized as TRAM.
+At position 557 to 671, the domain is characterized as Fe2OG dioxygenase.
+At position 95 to 226, the domain is characterized as Nudix hydrolase.
+At position 98 to 325, the domain is characterized as Radical SAM core.
+At position 133 to 240, the domain is characterized as Fibronectin type-III 1.
+At position 339 to 436, the domain is characterized as Fibronectin type-III 2.
+At position 106 to 201, the domain is characterized as PTS EIIB type-2 2.
+At position 224 to 556, the domain is characterized as PTS EIIC type-2.
+At position 96 to 179, the domain is characterized as MEIS N-terminal.
+At position 38 to 76, the domain is characterized as EGF-like 1.
+At position 77 to 127, the domain is characterized as EGF-like 2; calcium-binding.
+At position 289 to 338, the domain is characterized as GPS.
+At position 450 to 755, the domain is characterized as USP.
+At position 808 to 976, the domain is characterized as Exonuclease.
+At position 472 to 535, the domain is characterized as SAM 1.
+At position 541 to 605, the domain is characterized as SAM 2.
+At position 206 to 402, the domain is characterized as Peptidase M12B.
+At position 410 to 496, the domain is characterized as Disintegrin.
+At position 628 to 660, the domain is characterized as EGF-like.
+At position 34 to 188, the domain is characterized as Tyrosine-protein phosphatase.
+At position 100 to 128, the domain is characterized as EGF-like.
+At position 131 to 247, the domain is characterized as CUB.
+At position 702 to 747, the domain is characterized as PSI 1.
+At position 754 to 793, the domain is characterized as PSI 2.
+At position 794 to 918, the domain is characterized as C-type lectin.
+At position 931 to 982, the domain is characterized as PSI 3.
+At position 985 to 1060, the domain is characterized as PSI 4.
+At position 1062 to 1107, the domain is characterized as Laminin EGF-like 1.
+At position 1108 to 1156, the domain is characterized as Laminin EGF-like 2.
+At position 113 to 305, the domain is characterized as CP-type G.
+At position 104 to 400, the domain is characterized as Protein kinase.
+At position 147 to 344, the domain is characterized as Histidine kinase.
+At position 159 to 324, the domain is characterized as OBG-type G.
+At position 3 to 125, the domain is characterized as ApaG.
+At position 806 to 876, the domain is characterized as SAM.
+At position 3 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 308, the domain is characterized as Fe2OG dioxygenase.
+At position 101 to 255, the domain is characterized as UBC core.
+At position 31 to 121, the domain is characterized as PPIase FKBP-type.
+At position 597 to 772, the domain is characterized as PCI.
+At position 5 to 67, the domain is characterized as HTH IS21-type.
+At position 113 to 287, the domain is characterized as Integrase catalytic.
+At position 8 to 76, the domain is characterized as KRAB.
+At position 20 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 336 to 572, the domain is characterized as ABC transporter.
+At position 2 to 30, the domain is characterized as ACB.
+At position 40 to 118, the domain is characterized as KH; atypical.
+At position 28 to 350, the domain is characterized as G-alpha.
+At position 164 to 230, the domain is characterized as GRAM.
+At position 403 to 576, the domain is characterized as VASt.
+At position 124 to 294, the domain is characterized as Helicase ATP-binding.
+At position 305 to 473, the domain is characterized as Helicase C-terminal.
+At position 366 to 388, the domain is characterized as WH2.
+At position 107 to 301, the domain is characterized as B30.2/SPRY.
+At position 23 to 225, the domain is characterized as YjeF N-terminal.
+At position 234 to 501, the domain is characterized as YjeF C-terminal.
+At position 13 to 103, the domain is characterized as SUEL-type lectin.
+At position 11 to 72, the domain is characterized as BTB.
+At position 102 to 259, the domain is characterized as CP-type G.
+At position 4 to 143, the domain is characterized as Jacalin-type lectin.
+At position 116 to 194, the domain is characterized as RRM 1.
+At position 196 to 278, the domain is characterized as RRM 2.
+At position 292 to 368, the domain is characterized as RRM 3.
+At position 133 to 237, the domain is characterized as BACK.
+At position 238 to 331, the domain is characterized as Fibronectin type-III 1.
+At position 329 to 427, the domain is characterized as Ig-like.
+At position 537 to 632, the domain is characterized as Fibronectin type-III 2.
+At position 637 to 729, the domain is characterized as Fibronectin type-III 3.
+At position 738 to 832, the domain is characterized as Fibronectin type-III 4.
+At position 26 to 86, the domain is characterized as Kazal-like.
+At position 116 to 148, the domain is characterized as LisH.
+At position 155 to 212, the domain is characterized as CTLH.
+At position 18 to 233, the domain is characterized as tr-type G.
+At position 87 to 201, the domain is characterized as GST C-terminal.
+At position 48 to 185, the domain is characterized as SLD.
+At position 222 to 395, the domain is characterized as EngA-type G 2.
+At position 396 to 480, the domain is characterized as KH-like.
+At position 141 to 206, the domain is characterized as HTH luxR-type.
+At position 7 to 55, the domain is characterized as RPE1 insert.
+At position 98 to 314, the domain is characterized as Radical SAM core.
+At position 37 to 199, the domain is characterized as SIS.
+At position 147 to 330, the domain is characterized as Rho-GAP.
+At position 30 to 118, the domain is characterized as PINc.
+At position 122 to 207, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 311, the domain is characterized as Ig-like C2-type 3.
+At position 316 to 400, the domain is characterized as Ig-like C2-type 4.
+At position 406 to 493, the domain is characterized as Ig-like C2-type 5.
+At position 497 to 586, the domain is characterized as Ig-like C2-type 6.
+At position 599 to 697, the domain is characterized as Fibronectin type-III 1.
+At position 702 to 799, the domain is characterized as Fibronectin type-III 2.
+At position 804 to 899, the domain is characterized as Fibronectin type-III 3.
+At position 900 to 995, the domain is characterized as Fibronectin type-III 4.
+At position 17 to 105, the domain is characterized as PDZ 1.
+At position 96 to 287, the domain is characterized as Guanylate kinase-like.
+At position 359 to 392, the domain is characterized as WW 2.
+At position 464 to 546, the domain is characterized as PDZ 2.
+At position 635 to 713, the domain is characterized as PDZ 3.
+At position 833 to 915, the domain is characterized as PDZ 4.
+At position 990 to 1074, the domain is characterized as PDZ 5.
+At position 1132 to 1214, the domain is characterized as PDZ 6.
+At position 206 to 269, the domain is characterized as KH.
+At position 332 to 425, the domain is characterized as HD.
+At position 146 to 248, the domain is characterized as PB1.
+At position 80 to 275, the domain is characterized as tr-type G.
+At position 102 to 217, the domain is characterized as PilZ.
+At position 33 to 126, the domain is characterized as Fibronectin type-III 1.
+At position 103 to 203, the domain is characterized as Fibronectin type-III 2.
+At position 207 to 302, the domain is characterized as Fibronectin type-III 3.
+At position 307 to 402, the domain is characterized as Fibronectin type-III 4.
+At position 1543 to 1637, the domain is characterized as Fibronectin type-III 5.
+At position 86 to 163, the domain is characterized as Cytochrome b5 heme-binding.
+At position 189 to 559, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 7 to 129, the domain is characterized as C2 1.
+At position 168 to 301, the domain is characterized as C2 2.
+At position 745 to 872, the domain is characterized as C2 3.
+At position 920 to 1043, the domain is characterized as C2 4.
+At position 1231 to 1350, the domain is characterized as C2 5.
+At position 1476 to 1625, the domain is characterized as C2 6.
+At position 72 to 135, the domain is characterized as bZIP.
+At position 8 to 68, the domain is characterized as TRAM.
+At position 170 to 293, the domain is characterized as MsrB.
+At position 115 to 334, the domain is characterized as Radical SAM core.
+At position 39 to 323, the domain is characterized as Protein kinase.
+At position 28 to 244, the domain is characterized as BAR.
+At position 591 to 694, the domain is characterized as tRNA-binding.
+At position 209 to 228, the domain is characterized as UIM 1.
+At position 236 to 255, the domain is characterized as UIM 2.
+At position 11 to 251, the domain is characterized as ABC transporter 1.
+At position 319 to 552, the domain is characterized as ABC transporter 2.
+At position 143 to 290, the domain is characterized as DAGKc.
+At position 71 to 232, the domain is characterized as Thioredoxin.
+At position 665 to 747, the domain is characterized as PB1.
+At position 1 to 114, the domain is characterized as OCIA.
+At position 247 to 346, the domain is characterized as Cadherin 3.
+At position 351 to 450, the domain is characterized as Cadherin 4.
+At position 455 to 560, the domain is characterized as Cadherin 5.
+At position 567 to 670, the domain is characterized as Cadherin 6.
+At position 110 to 316, the domain is characterized as ATP-grasp.
+At position 14 to 116, the domain is characterized as RWD.
+At position 3 to 113, the domain is characterized as STAS.
+At position 8 to 284, the domain is characterized as Pyruvate carboxyltransferase.
+At position 212 to 271, the domain is characterized as HTH myb-type.
+At position 152 to 215, the domain is characterized as S5 DRBM.
+At position 187 to 413, the domain is characterized as Histidine kinase.
+At position 564 to 681, the domain is characterized as Response regulatory.
+At position 34 to 93, the domain is characterized as KID.
+At position 357 to 544, the domain is characterized as DH.
+At position 504 to 659, the domain is characterized as HNH Cas9-type.
+At position 28 to 223, the domain is characterized as Lon N-terminal.
+At position 610 to 791, the domain is characterized as Lon proteolytic.
+At position 448 to 619, the domain is characterized as tr-type G.
+At position 61 to 249, the domain is characterized as tr-type G.
+At position 6 to 75, the domain is characterized as NAC-A/B.
+At position 149 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 235 to 331, the domain is characterized as Ig-like C2-type 2.
+At position 41 to 123, the domain is characterized as Thioredoxin.
+At position 64 to 278, the domain is characterized as Radical SAM core.
+At position 182 to 383, the domain is characterized as ABC transmembrane type-2.
+At position 492 to 727, the domain is characterized as ABC transporter 1.
+At position 47 to 137, the domain is characterized as ATP-cone.
+At position 74 to 116, the domain is characterized as CUE.
+At position 105 to 201, the domain is characterized as BRICHOS.
+At position 542 to 664, the domain is characterized as STAS.
+At position 1 to 171, the domain is characterized as TCTP.
+At position 339 to 414, the domain is characterized as RRM.
+At position 144 to 267, the domain is characterized as VWFA.
+At position 42 to 107, the domain is characterized as J.
+At position 56 to 89, the domain is characterized as KOW.
+At position 23 to 278, the domain is characterized as Protein kinase.
+At position 308 to 332, the domain is characterized as NAF.
+At position 8 to 297, the domain is characterized as RHD.
+At position 70 to 145, the domain is characterized as Thyroglobulin type-1.
+At position 64 to 227, the domain is characterized as Laminin G-like.
+At position 271 to 332, the domain is characterized as VWFC 1.
+At position 434 to 475, the domain is characterized as EGF-like 1; calcium-binding.
+At position 476 to 516, the domain is characterized as EGF-like 2; calcium-binding.
+At position 517 to 547, the domain is characterized as EGF-like 3.
+At position 549 to 587, the domain is characterized as EGF-like 4; calcium-binding.
+At position 596 to 631, the domain is characterized as EGF-like 5; calcium-binding.
+At position 692 to 750, the domain is characterized as VWFC 2.
+At position 15 to 129, the domain is characterized as Response regulatory.
+At position 135 to 196, the domain is characterized as ANTAR.
+At position 84 to 160, the domain is characterized as RBD.
+At position 479 to 744, the domain is characterized as Protein kinase.
+At position 9 to 315, the domain is characterized as YjeF C-terminal.
+At position 9 to 243, the domain is characterized as ATP-grasp.
+At position 1224 to 1388, the domain is characterized as PNPLA.
+At position 108 to 218, the domain is characterized as Expansin-like EG45.
+At position 228 to 307, the domain is characterized as Expansin-like CBD.
+At position 42 to 365, the domain is characterized as ABC transmembrane type-1.
+At position 185 to 476, the domain is characterized as Deacetylase sirtuin-type.
+At position 154 to 361, the domain is characterized as ATP-grasp.
+At position 24 to 111, the domain is characterized as Ig-like C1-type.
+At position 36 to 91, the domain is characterized as FHA.
+At position 277 to 351, the domain is characterized as PUA.
+At position 122 to 166, the domain is characterized as DSL.
+At position 171 to 216, the domain is characterized as EGF-like 1.
+At position 229 to 266, the domain is characterized as EGF-like 2.
+At position 7 to 251, the domain is characterized as ABC transporter.
+At position 80 to 178, the domain is characterized as SSB.
+At position 4 to 77, the domain is characterized as KRAB.
+At position 67 to 300, the domain is characterized as AB hydrolase-1.
+At position 147 to 197, the domain is characterized as bHLH.
+At position 134 to 219, the domain is characterized as RRM 1.
+At position 265 to 350, the domain is characterized as RRM 2.
+At position 12 to 59, the domain is characterized as F-box.
+At position 52 to 332, the domain is characterized as Protein kinase.
+At position 47 to 152, the domain is characterized as BMC circularly permuted 1.
+At position 154 to 262, the domain is characterized as BMC circularly permuted 2.
+At position 172 to 207, the domain is characterized as EF-hand 2.
+At position 297 to 332, the domain is characterized as EF-hand 3.
+At position 403 to 438, the domain is characterized as EF-hand 4.
+At position 439 to 474, the domain is characterized as EF-hand 5.
+At position 504 to 539, the domain is characterized as EF-hand 6.
+At position 634 to 669, the domain is characterized as EF-hand 7.
+At position 741 to 776, the domain is characterized as EF-hand 8.
+At position 847 to 882, the domain is characterized as EF-hand 9.
+At position 883 to 918, the domain is characterized as EF-hand 10.
+At position 964 to 999, the domain is characterized as EF-hand 11.
+At position 1069 to 1104, the domain is characterized as EF-hand 12.
+At position 1176 to 1211, the domain is characterized as EF-hand 13.
+At position 1212 to 1247, the domain is characterized as EF-hand 14.
+At position 1359 to 1394, the domain is characterized as EF-hand 15.
+At position 1434 to 1469, the domain is characterized as EF-hand 16.
+At position 1470 to 1501, the domain is characterized as EF-hand 17.
+At position 30 to 312, the domain is characterized as ABC transmembrane type-1.
+At position 344 to 580, the domain is characterized as ABC transporter.
+At position 109 to 301, the domain is characterized as ATP-grasp.
+At position 249 to 451, the domain is characterized as GATase cobBQ-type.
+At position 301 to 535, the domain is characterized as ABC transporter 2.
+At position 134 to 204, the domain is characterized as HTH crp-type.
+At position 97 to 270, the domain is characterized as CRAL-TRIO.
+At position 25 to 123, the domain is characterized as AB hydrolase-1.
+At position 41 to 109, the domain is characterized as Importin N-terminal.
+At position 50 to 392, the domain is characterized as Kinesin motor.
+At position 159 to 359, the domain is characterized as OBG-type G.
+At position 3 to 474, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 518 to 809, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 126, the domain is characterized as MGS-like.
+At position 220 to 269, the domain is characterized as bHLH.
+At position 605 to 822, the domain is characterized as Rap-GAP.
+At position 960 to 1024, the domain is characterized as PDZ.
+At position 481 to 605, the domain is characterized as Ricin B-type lectin.
+At position 191 to 383, the domain is characterized as CheB-type methylesterase.
+At position 1 to 93, the domain is characterized as FAD-binding FR-type.
+At position 219 to 304, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 41 to 396, the domain is characterized as YcaO.
+At position 72 to 123, the domain is characterized as bHLH.
+At position 166 to 239, the domain is characterized as RRM 1.
+At position 251 to 324, the domain is characterized as RRM 2.
+At position 135 to 207, the domain is characterized as FISNA.
+At position 217 to 533, the domain is characterized as NACHT.
+At position 359 to 410, the domain is characterized as FBD.
+At position 225 to 330, the domain is characterized as PilZ.
+At position 25 to 72, the domain is characterized as WAP 1.
+At position 74 to 118, the domain is characterized as WAP 2.
+At position 41 to 237, the domain is characterized as Lon N-terminal.
+At position 625 to 805, the domain is characterized as Lon proteolytic.
+At position 34 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 500 to 560, the domain is characterized as PWWP.
+At position 17 to 83, the domain is characterized as HMA.
+At position 29 to 312, the domain is characterized as FERM.
+At position 510 to 582, the domain is characterized as PDZ.
+At position 646 to 901, the domain is characterized as Tyrosine-protein phosphatase.
+At position 355 to 414, the domain is characterized as Sushi 1.
+At position 416 to 527, the domain is characterized as CUB 1.
+At position 530 to 591, the domain is characterized as Sushi 2.
+At position 593 to 704, the domain is characterized as CUB 2.
+At position 708 to 767, the domain is characterized as Sushi 3.
+At position 769 to 832, the domain is characterized as Sushi 4.
+At position 836 to 897, the domain is characterized as Sushi 5.
+At position 3 to 171, the domain is characterized as Era-type G.
+At position 202 to 279, the domain is characterized as KH type-2.
+At position 56 to 226, the domain is characterized as Helicase ATP-binding.
+At position 58 to 161, the domain is characterized as FAD-binding FR-type.
+At position 219 to 372, the domain is characterized as TrmE-type G.
+At position 29 to 104, the domain is characterized as Cytochrome c 1.
+At position 116 to 206, the domain is characterized as Cytochrome c 2.
+At position 125 to 309, the domain is characterized as ATP-grasp.
+At position 103 to 389, the domain is characterized as tr-type G.
+At position 4 to 80, the domain is characterized as Carrier.
+At position 50 to 159, the domain is characterized as PDZ.
+At position 931 to 1040, the domain is characterized as PH.
+At position 1147 to 1339, the domain is characterized as Rho-GAP.
+At position 188 to 295, the domain is characterized as HD.
+At position 41 to 137, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 244 to 332, the domain is characterized as Ig-like C2-type 3.
+At position 521 to 603, the domain is characterized as Ig-like C2-type 6.
+At position 630 to 725, the domain is characterized as Fibronectin type-III 1.
+At position 727 to 823, the domain is characterized as Fibronectin type-III 2.
+At position 827 to 923, the domain is characterized as Fibronectin type-III 3.
+At position 1007 to 1099, the domain is characterized as Fibronectin type-III 4.
+At position 249 to 324, the domain is characterized as Cytochrome b5 heme-binding.
+At position 361 to 473, the domain is characterized as FAD-binding FR-type.
+At position 991 to 1119, the domain is characterized as RGS.
+At position 1949 to 2208, the domain is characterized as Protein kinase.
+At position 123 to 274, the domain is characterized as N-acetyltransferase.
+At position 191 to 380, the domain is characterized as Helicase ATP-binding.
+At position 391 to 551, the domain is characterized as Helicase C-terminal.
+At position 39 to 280, the domain is characterized as ABC transporter.
+At position 1 to 125, the domain is characterized as tr-type G.
+At position 10 to 147, the domain is characterized as Response regulatory.
+At position 108 to 316, the domain is characterized as ATP-grasp.
+At position 33 to 58, the domain is characterized as LRRNT.
+At position 20 to 32, the domain is characterized as Sushi 1; incomplete.
+At position 34 to 91, the domain is characterized as Sushi 2.
+At position 92 to 154, the domain is characterized as Sushi 3.
+At position 155 to 214, the domain is characterized as Sushi 4.
+At position 13 to 66, the domain is characterized as LIM zinc-binding 1.
+At position 70 to 122, the domain is characterized as LIM zinc-binding 2.
+At position 791 to 1006, the domain is characterized as Rho-GAP.
+At position 15 to 275, the domain is characterized as Pyruvate carboxyltransferase.
+At position 90 to 286, the domain is characterized as SIS 1.
+At position 320 to 499, the domain is characterized as SIS 2.
+At position 278 to 352, the domain is characterized as PUA.
+At position 41 to 154, the domain is characterized as TBDR plug.
+At position 159 to 611, the domain is characterized as TBDR beta-barrel.
+At position 27 to 75, the domain is characterized as TSP type-1 0.
+At position 76 to 133, the domain is characterized as TSP type-1 1.
+At position 135 to 190, the domain is characterized as TSP type-1 2.
+At position 192 to 254, the domain is characterized as TSP type-1 3.
+At position 256 to 312, the domain is characterized as TSP type-1 4.
+At position 314 to 376, the domain is characterized as TSP type-1 5.
+At position 380 to 463, the domain is characterized as TSP type-1 6.
+At position 36 to 180, the domain is characterized as RUN.
+At position 656 to 779, the domain is characterized as PX.
+At position 25 to 53, the domain is characterized as LRRNT.
+At position 299 to 352, the domain is characterized as LRRCT.
+At position 406 to 443, the domain is characterized as EGF-like.
+At position 463 to 559, the domain is characterized as Fibronectin type-III.
+At position 4 to 154, the domain is characterized as UBC core.
+At position 160 to 200, the domain is characterized as UBA.
+At position 746 to 823, the domain is characterized as BRCT.
+At position 49 to 356, the domain is characterized as ABC transmembrane type-1 1.
+At position 391 to 627, the domain is characterized as ABC transporter 1.
+At position 709 to 1000, the domain is characterized as ABC transmembrane type-1 2.
+At position 1035 to 1272, the domain is characterized as ABC transporter 2.
+At position 108 to 180, the domain is characterized as PRC barrel.
+At position 111 to 363, the domain is characterized as RMT2.
+At position 135 to 199, the domain is characterized as S1 motif.
+At position 301 to 367, the domain is characterized as KH.
+At position 431 to 603, the domain is characterized as tr-type G.
+At position 69 to 438, the domain is characterized as AB hydrolase-1.
+At position 4 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 10 to 211, the domain is characterized as tr-type G.
+At position 250 to 355, the domain is characterized as Fibronectin type-III 1.
+At position 359 to 449, the domain is characterized as Fibronectin type-III 2.
+At position 453 to 545, the domain is characterized as Fibronectin type-III 3.
+At position 549 to 642, the domain is characterized as Fibronectin type-III 4.
+At position 645 to 742, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 264, the domain is characterized as PTS EIIC type-1; first part.
+At position 451 to 602, the domain is characterized as PTS EIIC type-1; second part.
+At position 631 to 713, the domain is characterized as PTS EIIB type-1.
+At position 762 to 875, the domain is characterized as PTS EIIA type-1.
+At position 122 to 179, the domain is characterized as BTB 1.
+At position 274 to 360, the domain is characterized as BTB 2.
+At position 1 to 110, the domain is characterized as SSB.
+At position 112 to 603, the domain is characterized as Peptidase S8.
+At position 386 to 460, the domain is characterized as PA.
+At position 626 to 728, the domain is characterized as Fibronectin type-III 1.
+At position 744 to 838, the domain is characterized as Fibronectin type-III 2.
+At position 843 to 937, the domain is characterized as Fibronectin type-III 3.
+At position 1013 to 1288, the domain is characterized as Protein kinase.
+At position 69 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 944 to 976, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 978 to 1007, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 167 to 232, the domain is characterized as HTH luxR-type.
+At position 28 to 199, the domain is characterized as BPL/LPL catalytic.
+At position 176 to 320, the domain is characterized as YDG.
+At position 4 to 595, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 623 to 929, the domain is characterized as UvrD-like helicase C-terminal.
+At position 156 to 242, the domain is characterized as Ig-like C2-type.
+At position 281 to 420, the domain is characterized as SIS 1.
+At position 327 to 539, the domain is characterized as ATP-grasp.
+At position 4 to 158, the domain is characterized as Thioredoxin.
+At position 1 to 274, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 267 to 565, the domain is characterized as UvrD-like helicase C-terminal.
+At position 13 to 252, the domain is characterized as ABC transporter.
+At position 112 to 210, the domain is characterized as HTH araC/xylS-type.
+At position 30 to 135, the domain is characterized as EamA 1.
+At position 159 to 278, the domain is characterized as EamA 2.
+At position 116 to 325, the domain is characterized as Pentraxin (PTX).
+At position 572 to 648, the domain is characterized as GPS.
+At position 155 to 297, the domain is characterized as N-acetyltransferase.
+At position 585 to 614, the domain is characterized as IQ.
+At position 15 to 101, the domain is characterized as GIY-YIG.
+At position 4 to 200, the domain is characterized as Peptidase M12B.
+At position 3 to 161, the domain is characterized as Obg.
+At position 162 to 333, the domain is characterized as OBG-type G.
+At position 359 to 440, the domain is characterized as OCT.
+At position 1 to 75, the domain is characterized as Sm.
+At position 19 to 77, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 108 to 416, the domain is characterized as IF rod.
+At position 271 to 374, the domain is characterized as CobW C-terminal.
+At position 9 to 68, the domain is characterized as 4Fe-4S.
+At position 34 to 97, the domain is characterized as S5 DRBM.
+At position 1 to 127, the domain is characterized as C2 1.
+At position 134 to 263, the domain is characterized as C2 2.
+At position 306 to 526, the domain is characterized as VWFA.
+At position 1 to 110, the domain is characterized as STAS.
+At position 30 to 565, the domain is characterized as PLA2c.
+At position 86 to 232, the domain is characterized as UBC core.
+At position 44 to 116, the domain is characterized as Bromo 1.
+At position 500 to 582, the domain is characterized as NET.
+At position 192 to 228, the domain is characterized as DFDF.
+At position 283 to 487, the domain is characterized as YjeF N-terminal.
+At position 129 to 335, the domain is characterized as ATP-grasp.
+At position 91 to 274, the domain is characterized as Helicase ATP-binding.
+At position 288 to 463, the domain is characterized as Helicase C-terminal.
+At position 153 to 274, the domain is characterized as C2 1.
+At position 287 to 420, the domain is characterized as C2 2.
+At position 585 to 636, the domain is characterized as GRIP.
+At position 4 to 172, the domain is characterized as MurNAc-LAA.
+At position 180 to 254, the domain is characterized as SPOR.
+At position 2 to 254, the domain is characterized as ABC transporter.
+At position 67 to 130, the domain is characterized as S5 DRBM.
+At position 69 to 215, the domain is characterized as Thioredoxin.
+At position 293 to 525, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 264, the domain is characterized as Alpha-carbonic anhydrase.
+At position 241 to 497, the domain is characterized as CN hydrolase.
+At position 5 to 139, the domain is characterized as ADF-H.
+At position 105 to 468, the domain is characterized as GS catalytic.
+At position 66 to 145, the domain is characterized as RRM 1.
+At position 153 to 233, the domain is characterized as RRM 2.
+At position 306 to 384, the domain is characterized as RRM 3.
+At position 106 to 341, the domain is characterized as Radical SAM core.
+At position 98 to 198, the domain is characterized as FAD-binding FR-type.
+At position 20 to 90, the domain is characterized as S4 RNA-binding.
+At position 2 to 58, the domain is characterized as IBB.
+At position 1120 to 1180, the domain is characterized as v-SNARE coiled-coil homology.
+At position 9 to 126, the domain is characterized as Response regulatory.
+At position 161 to 354, the domain is characterized as CheB-type methylesterase.
+At position 312 to 389, the domain is characterized as Toprim.
+At position 2 to 451, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 478 to 768, the domain is characterized as UvrD-like helicase C-terminal.
+At position 703 to 1073, the domain is characterized as DZF.
+At position 667 to 763, the domain is characterized as BRCT 1.
+At position 915 to 1025, the domain is characterized as BRCT 2.
+At position 9 to 293, the domain is characterized as tr-type G.
+At position 94 to 261, the domain is characterized as Helicase ATP-binding.
+At position 468 to 641, the domain is characterized as Helicase C-terminal.
+At position 100 to 189, the domain is characterized as PDZ.
+At position 20 to 63, the domain is characterized as SMB.
+At position 5 to 476, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 515 to 808, the domain is characterized as UvrD-like helicase C-terminal.
+At position 74 to 146, the domain is characterized as PA.
+At position 125 to 300, the domain is characterized as Helicase ATP-binding.
+At position 328 to 475, the domain is characterized as Helicase C-terminal.
+At position 45 to 169, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 243 to 349, the domain is characterized as Rhodanese.
+At position 87 to 169, the domain is characterized as PDZ 1.
+At position 211 to 293, the domain is characterized as PDZ 2.
+At position 452 to 536, the domain is characterized as PDZ 3.
+At position 33 to 189, the domain is characterized as Thioredoxin.
+At position 178 to 238, the domain is characterized as HTH myb-type.
+At position 240 to 306, the domain is characterized as BIG2.
+At position 11 to 76, the domain is characterized as SAM.
+At position 84 to 178, the domain is characterized as CRIC.
+At position 215 to 297, the domain is characterized as PDZ.
+At position 302 to 515, the domain is characterized as DUF1170.
+At position 570 to 669, the domain is characterized as PH.
+At position 42 to 154, the domain is characterized as tRNA-binding.
+At position 412 to 488, the domain is characterized as B5.
+At position 726 to 819, the domain is characterized as FDX-ACB.
+At position 106 to 291, the domain is characterized as Tyr recombinase.
+At position 22 to 296, the domain is characterized as Septin-type G.
+At position 10 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 391, the domain is characterized as GMPS ATP-PPase.
+At position 375 to 423, the domain is characterized as Collagen-like 1.
+At position 573 to 633, the domain is characterized as Collagen-like 2.
+At position 667 to 721, the domain is characterized as Collagen-like 3.
+At position 788 to 840, the domain is characterized as Collagen-like 4.
+At position 888 to 938, the domain is characterized as Collagen-like 5.
+At position 1018 to 1075, the domain is characterized as Collagen-like 6.
+At position 1472 to 1524, the domain is characterized as Collagen-like 7.
+At position 1528 to 1576, the domain is characterized as Collagen-like 8.
+At position 8 to 57, the domain is characterized as Myosin N-terminal SH3-like.
+At position 62 to 732, the domain is characterized as Myosin motor.
+At position 758 to 787, the domain is characterized as IQ 1.
+At position 783 to 812, the domain is characterized as IQ 2.
+At position 806 to 835, the domain is characterized as IQ 3.
+At position 831 to 860, the domain is characterized as IQ 4.
+At position 854 to 883, the domain is characterized as IQ 5.
+At position 1159 to 1470, the domain is characterized as Dilute.
+At position 127 to 302, the domain is characterized as Helicase ATP-binding.
+At position 335 to 488, the domain is characterized as Helicase C-terminal.
+At position 134 to 164, the domain is characterized as KOW.
+At position 43 to 83, the domain is characterized as EGF-like.
+At position 10 to 103, the domain is characterized as Toprim.
+At position 95 to 166, the domain is characterized as SUI1.
+At position 274 to 481, the domain is characterized as Histidine kinase.
+At position 1 to 122, the domain is characterized as C-type lectin.
+At position 29 to 166, the domain is characterized as PfpI endopeptidase.
+At position 75 to 170, the domain is characterized as CTCK.
+At position 327 to 435, the domain is characterized as EH.
+At position 7 to 190, the domain is characterized as Lon N-terminal.
+At position 589 to 769, the domain is characterized as Lon proteolytic.
+At position 56 to 217, the domain is characterized as TLDc.
+At position 4 to 68, the domain is characterized as TRAM.
+At position 51 to 94, the domain is characterized as LysM.
+At position 158 to 279, the domain is characterized as Peptidase C51.
+At position 1 to 72, the domain is characterized as Helicase C-terminal.
+At position 124 to 170, the domain is characterized as F-box.
+At position 153 to 188, the domain is characterized as EF-hand 1.
+At position 207 to 224, the domain is characterized as EF-hand 2.
+At position 230 to 265, the domain is characterized as EF-hand 3.
+At position 267 to 298, the domain is characterized as EF-hand 4.
+At position 46 to 355, the domain is characterized as AB hydrolase-1.
+At position 19 to 206, the domain is characterized as MHYT.
+At position 254 to 317, the domain is characterized as PAS.
+At position 545 to 795, the domain is characterized as EAL.
+At position 94 to 128, the domain is characterized as EF-hand 1; atypical.
+At position 137 to 170, the domain is characterized as EF-hand 2.
+At position 203 to 231, the domain is characterized as EF-hand 4.
+At position 232 to 266, the domain is characterized as EF-hand 5.
+At position 2 to 195, the domain is characterized as VWFA.
+At position 1041 to 1103, the domain is characterized as MIF4G.
+At position 106 to 417, the domain is characterized as Peptidase A1.
+At position 110 to 266, the domain is characterized as Exonuclease.
+At position 42 to 118, the domain is characterized as GIY-YIG.
+At position 278 to 329, the domain is characterized as HAMP.
+At position 361 to 485, the domain is characterized as Guanylate cyclase.
+At position 217 to 362, the domain is characterized as TrmE-type G.
+At position 97 to 138, the domain is characterized as Collagen-like.
+At position 139 to 259, the domain is characterized as C1q.
+At position 22 to 120, the domain is characterized as Ig-like.
+At position 152 to 335, the domain is characterized as CRAL-TRIO.
+At position 16 to 141, the domain is characterized as N-acetyltransferase 1.
+At position 152 to 320, the domain is characterized as N-acetyltransferase 2.
+At position 38 to 324, the domain is characterized as Protein kinase.
+At position 482 to 670, the domain is characterized as Rho-GAP.
+At position 744 to 803, the domain is characterized as SH3.
+At position 175 to 250, the domain is characterized as SPOR.
+At position 5 to 258, the domain is characterized as tr-type G.
+At position 3 to 108, the domain is characterized as Thioredoxin.
+At position 5 to 135, the domain is characterized as ADF-H.
+At position 9 to 188, the domain is characterized as Guanylate kinase-like.
+At position 7 to 121, the domain is characterized as HIT.
+At position 10 to 193, the domain is characterized as Ku.
+At position 79 to 195, the domain is characterized as Toprim.
+At position 87 to 148, the domain is characterized as S4 RNA-binding.
+At position 56 to 219, the domain is characterized as BUB1 N-terminal.
+At position 756 to 1040, the domain is characterized as Protein kinase.
+At position 202 to 530, the domain is characterized as Protein kinase.
+At position 41 to 151, the domain is characterized as Plastocyanin-like 1.
+At position 162 to 360, the domain is characterized as Plastocyanin-like 2.
+At position 439 to 595, the domain is characterized as Plastocyanin-like 3.
+At position 425 to 585, the domain is characterized as OTU.
+At position 226 to 261, the domain is characterized as EF-hand 1.
+At position 270 to 305, the domain is characterized as EF-hand 2.
+At position 390 to 549, the domain is characterized as Ferric oxidoreductase.
+At position 587 to 711, the domain is characterized as FAD-binding FR-type.
+At position 276 to 351, the domain is characterized as PUA.
+At position 281 to 532, the domain is characterized as Clu.
+At position 42 to 105, the domain is characterized as S5 DRBM.
+At position 572 to 647, the domain is characterized as PilZ.
+At position 4 to 71, the domain is characterized as S4 RNA-binding.
+At position 124 to 453, the domain is characterized as PI3K/PI4K catalytic.
+At position 183 to 303, the domain is characterized as Ferric oxidoreductase.
+At position 332 to 437, the domain is characterized as FAD-binding FR-type.
+At position 27 to 190, the domain is characterized as EngA-type G 1.
+At position 374 to 456, the domain is characterized as KH-like.
+At position 56 to 118, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 21 to 61, the domain is characterized as Chitin-binding type-1.
+At position 12 to 136, the domain is characterized as MH1.
+At position 274 to 468, the domain is characterized as MH2.
+At position 48 to 140, the domain is characterized as G.
+At position 247 to 387, the domain is characterized as Flavodoxin-like.
+At position 65 to 173, the domain is characterized as PRD 1.
+At position 573 to 650, the domain is characterized as Carrier.
+At position 289 to 363, the domain is characterized as U-box.
+At position 95 to 160, the domain is characterized as S4 RNA-binding.
+At position 429 to 517, the domain is characterized as Ig-like C2-type 5.
+At position 827 to 922, the domain is characterized as Fibronectin type-III 3.
+At position 32 to 272, the domain is characterized as GP-PDE.
+At position 76 to 133, the domain is characterized as DPH-type MB.
+At position 72 to 321, the domain is characterized as Dynamin-type G.
+At position 2 to 83, the domain is characterized as RRM 1.
+At position 323 to 401, the domain is characterized as RRM 2.
+At position 506 to 578, the domain is characterized as RRM 3.
+At position 619 to 702, the domain is characterized as RRM 4.
+At position 721 to 798, the domain is characterized as RRM 5.
+At position 33 to 846, the domain is characterized as Protein kinase.
+At position 847 to 890, the domain is characterized as AGC-kinase C-terminal.
+At position 82 to 269, the domain is characterized as B30.2/SPRY.
+At position 25 to 59, the domain is characterized as EF-hand 1.
+At position 6 to 84, the domain is characterized as GIY-YIG.
+At position 319 to 469, the domain is characterized as PI-PLC X-box.
+At position 550 to 666, the domain is characterized as PI-PLC Y-box.
+At position 666 to 794, the domain is characterized as C2.
+At position 532 to 722, the domain is characterized as FtsK.
+At position 37 to 260, the domain is characterized as AIG1-type G.
+At position 220 to 355, the domain is characterized as PAS 1.
+At position 373 to 479, the domain is characterized as PAS 2.
+At position 45 to 263, the domain is characterized as Radical SAM core.
+At position 298 to 437, the domain is characterized as SIS 1.
+At position 470 to 615, the domain is characterized as SIS 2.
+At position 198 to 256, the domain is characterized as TRAM.
+At position 38 to 72, the domain is characterized as Tify.
+At position 49 to 160, the domain is characterized as HIT.
+At position 82 to 262, the domain is characterized as ABC transmembrane type-1.
+At position 110 to 309, the domain is characterized as MAGE.
+At position 26 to 127, the domain is characterized as Gnk2-homologous 1.
+At position 140 to 247, the domain is characterized as Gnk2-homologous 2.
+At position 339 to 611, the domain is characterized as Protein kinase.
+At position 16 to 67, the domain is characterized as Rubredoxin-like.
+At position 1 to 166, the domain is characterized as DHFR.
+At position 42 to 296, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 12 to 175, the domain is characterized as PPIase cyclophilin-type.
+At position 130 to 207, the domain is characterized as PRC barrel.
+At position 12 to 128, the domain is characterized as Response regulatory.
+At position 508 to 679, the domain is characterized as N-acetyltransferase.
+At position 27 to 481, the domain is characterized as Hexokinase.
+At position 15 to 108, the domain is characterized as PH.
+At position 28 to 86, the domain is characterized as TIL.
+At position 358 to 406, the domain is characterized as SOCS box.
+At position 1 to 188, the domain is characterized as UmuC.
+At position 55 to 124, the domain is characterized as EamA.
+At position 50 to 729, the domain is characterized as Myosin motor.
+At position 733 to 753, the domain is characterized as IQ 1.
+At position 754 to 779, the domain is characterized as IQ 2.
+At position 787 to 979, the domain is characterized as TH1.
+At position 1074 to 1135, the domain is characterized as SH3.
+At position 154 to 335, the domain is characterized as Helicase ATP-binding.
+At position 346 to 508, the domain is characterized as Helicase C-terminal.
+At position 21 to 285, the domain is characterized as OBG-type G.
+At position 306 to 389, the domain is characterized as TGS.
+At position 13 to 321, the domain is characterized as Calpain catalytic.
+At position 31 to 151, the domain is characterized as MTTase N-terminal.
+At position 413 to 475, the domain is characterized as TRAM.
+At position 484 to 575, the domain is characterized as SH2.
+At position 1 to 138, the domain is characterized as MGS-like.
+At position 28 to 68, the domain is characterized as LDL-receptor class A.
+At position 115 to 241, the domain is characterized as C-type lectin.
+At position 270 to 333, the domain is characterized as VWFC.
+At position 1 to 41, the domain is characterized as F-box.
+At position 163 to 348, the domain is characterized as Rab-GAP TBC.
+At position 25 to 91, the domain is characterized as Chitin-binding type-3 1.
+At position 128 to 194, the domain is characterized as Chitin-binding type-3 2.
+At position 229 to 295, the domain is characterized as Chitin-binding type-3 3.
+At position 337 to 403, the domain is characterized as Chitin-binding type-3 4.
+At position 459 to 529, the domain is characterized as Chitin-binding type-3 5.
+At position 586 to 877, the domain is characterized as GH18.
+At position 174 to 273, the domain is characterized as ELM2.
+At position 278 to 330, the domain is characterized as SANT.
+At position 36 to 356, the domain is characterized as Asparaginase/glutaminase.
+At position 5 to 102, the domain is characterized as ASCH.
+At position 23 to 165, the domain is characterized as MPN.
+At position 28 to 102, the domain is characterized as S1-like.
+At position 125 to 188, the domain is characterized as bZIP.
+At position 21 to 109, the domain is characterized as Ig-like.
+At position 88 to 211, the domain is characterized as RGS.
+At position 780 to 862, the domain is characterized as DIX.
+At position 29 to 143, the domain is characterized as Cadherin 1.
+At position 144 to 308, the domain is characterized as Cadherin 2.
+At position 309 to 415, the domain is characterized as Cadherin 3.
+At position 424 to 535, the domain is characterized as Cadherin 4.
+At position 536 to 639, the domain is characterized as Cadherin 5.
+At position 640 to 742, the domain is characterized as Cadherin 6.
+At position 745 to 862, the domain is characterized as Cadherin 7.
+At position 63 to 129, the domain is characterized as PWWP.
+At position 2 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 252, the domain is characterized as Deacetylase sirtuin-type.
+At position 298 to 337, the domain is characterized as LIM interaction domain (LID).
+At position 35 to 586, the domain is characterized as PLA2c.
+At position 7 to 139, the domain is characterized as ADF-H.
+At position 56 to 86, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 3 to 145, the domain is characterized as Clp R.
+At position 31 to 92, the domain is characterized as Chitin-binding type R&R.
+At position 291 to 543, the domain is characterized as Glutamine amidotransferase type-1.
+At position 36 to 127, the domain is characterized as Fibronectin type-III.
+At position 85 to 180, the domain is characterized as POU-specific atypical.
+At position 235 to 361, the domain is characterized as C2 tensin-type.
+At position 1472 to 1581, the domain is characterized as SH2.
+At position 1607 to 1743, the domain is characterized as PTB.
+At position 756 to 828, the domain is characterized as KHA.
+At position 168 to 340, the domain is characterized as OBG-type G.
+At position 38 to 196, the domain is characterized as Cupin type-1 1.
+At position 231 to 386, the domain is characterized as Cupin type-1 2.
+At position 15 to 294, the domain is characterized as CNH.
+At position 22 to 185, the domain is characterized as FAD-binding PCMH-type.
+At position 284 to 587, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 161 to 353, the domain is characterized as DH.
+At position 409 to 509, the domain is characterized as PH.
+At position 95 to 411, the domain is characterized as Kinesin motor.
+At position 25 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 290 to 536, the domain is characterized as Glutamine amidotransferase type-1.
+At position 19 to 277, the domain is characterized as Protein kinase.
+At position 3 to 69, the domain is characterized as HMA.
+At position 104 to 303, the domain is characterized as ATP-grasp.
+At position 136 to 573, the domain is characterized as Urease.
+At position 140 to 332, the domain is characterized as ABC transmembrane type-1.
+At position 133 to 325, the domain is characterized as ATP-grasp 1.
+At position 665 to 854, the domain is characterized as ATP-grasp 2.
+At position 910 to 1047, the domain is characterized as MGS-like.
+At position 31 to 252, the domain is characterized as Alpha-carbonic anhydrase.
+At position 120 to 172, the domain is characterized as LIM zinc-binding 2.
+At position 222 to 274, the domain is characterized as LIM zinc-binding 3.
+At position 325 to 377, the domain is characterized as LIM zinc-binding 4.
+At position 421 to 473, the domain is characterized as LIM zinc-binding 5.
+At position 58 to 201, the domain is characterized as Ferric oxidoreductase.
+At position 229 to 349, the domain is characterized as FAD-binding FR-type.
+At position 1 to 71, the domain is characterized as HTH merR-type.
+At position 97 to 388, the domain is characterized as FAE.
+At position 83 to 160, the domain is characterized as Lipoyl-binding 1.
+At position 206 to 283, the domain is characterized as Lipoyl-binding 2.
+At position 342 to 379, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 32 to 72, the domain is characterized as CHCH.
+At position 376 to 468, the domain is characterized as BRCT.
+At position 1 to 146, the domain is characterized as Clp R.
+At position 3 to 68, the domain is characterized as S4 RNA-binding.
+At position 36 to 70, the domain is characterized as LDL-receptor class A 1.
+At position 71 to 112, the domain is characterized as LDL-receptor class A 2.
+At position 208 to 243, the domain is characterized as EF-hand 1.
+At position 244 to 279, the domain is characterized as EF-hand 2.
+At position 418 to 519, the domain is characterized as MRH.
+At position 1 to 138, the domain is characterized as YEATS.
+At position 121 to 504, the domain is characterized as Protein kinase.
+At position 217 to 449, the domain is characterized as NR LBD.
+At position 119 to 371, the domain is characterized as Pterin-binding.
+At position 138 to 421, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 299 to 417, the domain is characterized as Nop.
+At position 16 to 145, the domain is characterized as EamA 1.
+At position 167 to 291, the domain is characterized as EamA 2.
+At position 100 to 172, the domain is characterized as PRC barrel.
+At position 17 to 286, the domain is characterized as tr-type G.
+At position 147 to 336, the domain is characterized as CheB-type methylesterase.
+At position 18 to 268, the domain is characterized as Protein kinase.
+At position 409 to 468, the domain is characterized as SH3.
+At position 12 to 110, the domain is characterized as Rieske.
+At position 857 to 938, the domain is characterized as BRCT.
+At position 58 to 172, the domain is characterized as Cadherin.
+At position 470 to 749, the domain is characterized as Protein kinase.
+At position 3 to 44, the domain is characterized as UBA.
+At position 1686 to 2039, the domain is characterized as USP.
+At position 32 to 201, the domain is characterized as MurNAc-LAA.
+At position 1 to 63, the domain is characterized as HMA.
+At position 6 to 406, the domain is characterized as BRO1.
+At position 422 to 854, the domain is characterized as FH2.
+At position 5 to 39, the domain is characterized as WW.
+At position 55 to 166, the domain is characterized as PpiC.
+At position 30 to 289, the domain is characterized as Protein kinase.
+At position 160 to 242, the domain is characterized as SCAN box.
+At position 278 to 358, the domain is characterized as KRAB 2.
+At position 84 to 207, the domain is characterized as Plastocyanin-like 1.
+At position 216 to 373, the domain is characterized as Plastocyanin-like 2.
+At position 431 to 566, the domain is characterized as Plastocyanin-like 3.
+At position 44 to 200, the domain is characterized as TNase-like.
+At position 30 to 151, the domain is characterized as FZ.
+At position 21 to 117, the domain is characterized as Ig-like.
+At position 203 to 415, the domain is characterized as Helicase ATP-binding.
+At position 454 to 623, the domain is characterized as Helicase C-terminal.
+At position 106 to 321, the domain is characterized as Radical SAM core.
+At position 296 to 580, the domain is characterized as ABC transmembrane type-1 1.
+At position 611 to 840, the domain is characterized as ABC transporter 1.
+At position 897 to 1176, the domain is characterized as ABC transmembrane type-1 2.
+At position 1214 to 1453, the domain is characterized as ABC transporter 2.
+At position 1 to 247, the domain is characterized as KaiC 1.
+At position 261 to 518, the domain is characterized as KaiC 2.
+At position 2 to 148, the domain is characterized as UBC core.
+At position 359 to 437, the domain is characterized as OCT.
+At position 48 to 99, the domain is characterized as bHLH.
+At position 149 to 349, the domain is characterized as Peptidase M12A.
+At position 351 to 463, the domain is characterized as CUB 1.
+At position 464 to 576, the domain is characterized as CUB 2.
+At position 576 to 617, the domain is characterized as EGF-like 1; calcium-binding.
+At position 620 to 732, the domain is characterized as CUB 3.
+At position 732 to 772, the domain is characterized as EGF-like 2; calcium-binding.
+At position 776 to 888, the domain is characterized as CUB 4.
+At position 889 to 1005, the domain is characterized as CUB 5.
+At position 235 to 283, the domain is characterized as G-patch.
+At position 310 to 389, the domain is characterized as RRM.
+At position 37 to 107, the domain is characterized as Ig-like C2-type 1.
+At position 114 to 216, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 311, the domain is characterized as Ig-like C2-type 3.
+At position 315 to 403, the domain is characterized as Ig-like C2-type 4.
+At position 409 to 502, the domain is characterized as Ig-like C2-type 5.
+At position 507 to 587, the domain is characterized as Ig-like C2-type 6.
+At position 597 to 686, the domain is characterized as Ig-like C2-type 7.
+At position 691 to 785, the domain is characterized as Ig-like C2-type 8.
+At position 789 to 886, the domain is characterized as Ig-like C2-type 9.
+At position 888 to 985, the domain is characterized as Fibronectin type-III 1.
+At position 990 to 1089, the domain is characterized as Fibronectin type-III 2.
+At position 1094 to 1190, the domain is characterized as Fibronectin type-III 3.
+At position 1194 to 1289, the domain is characterized as Fibronectin type-III 4.
+At position 1279 to 1368, the domain is characterized as Ig-like C2-type 10.
+At position 1384 to 1478, the domain is characterized as Fibronectin type-III 5.
+At position 1479 to 1579, the domain is characterized as Fibronectin type-III 6.
+At position 575 to 633, the domain is characterized as RAP.
+At position 258 to 349, the domain is characterized as PDZ 1.
+At position 355 to 447, the domain is characterized as PDZ 2.
+At position 25 to 79, the domain is characterized as TIL.
+At position 32 to 190, the domain is characterized as Rhodanese.
+At position 208 to 350, the domain is characterized as Tyrosine-protein phosphatase.
+At position 43 to 305, the domain is characterized as ZP.
+At position 52 to 141, the domain is characterized as Ig-like C2-type 1.
+At position 152 to 238, the domain is characterized as Ig-like C2-type 2.
+At position 243 to 336, the domain is characterized as Ig-like C2-type 3.
+At position 341 to 426, the domain is characterized as Ig-like C2-type 4.
+At position 441 to 535, the domain is characterized as Fibronectin type-III 1.
+At position 541 to 631, the domain is characterized as Fibronectin type-III 2.
+At position 636 to 731, the domain is characterized as Fibronectin type-III 3.
+At position 741 to 831, the domain is characterized as Fibronectin type-III 4.
+At position 856 to 952, the domain is characterized as Fibronectin type-III 5.
+At position 957 to 1054, the domain is characterized as Fibronectin type-III 6.
+At position 1 to 89, the domain is characterized as PTS EIIB type-1.
+At position 109 to 473, the domain is characterized as PTS EIIC type-1.
+At position 50 to 371, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 260 to 316, the domain is characterized as GYF.
+At position 11 to 352, the domain is characterized as Kinesin motor.
+At position 1 to 130, the domain is characterized as PX.
+At position 265 to 342, the domain is characterized as MIT.
+At position 20 to 119, the domain is characterized as Ig-like.
+At position 12 to 276, the domain is characterized as Protein kinase.
+At position 343 to 398, the domain is characterized as L27 1.
+At position 402 to 455, the domain is characterized as L27 2.
+At position 490 to 571, the domain is characterized as PDZ.
+At position 612 to 682, the domain is characterized as SH3.
+At position 739 to 911, the domain is characterized as Guanylate kinase-like.
+At position 24 to 255, the domain is characterized as MRH.
+At position 17 to 136, the domain is characterized as NTF2.
+At position 26 to 472, the domain is characterized as GBD/FH3.
+At position 561 to 951, the domain is characterized as FH2.
+At position 986 to 1018, the domain is characterized as DAD.
+At position 518 to 687, the domain is characterized as tr-type G.
+At position 422 to 765, the domain is characterized as Protein kinase.
+At position 688 to 762, the domain is characterized as U-box.
+At position 30 to 318, the domain is characterized as Protein kinase.
+At position 139 to 336, the domain is characterized as Integrase catalytic.
+At position 45 to 134, the domain is characterized as PPIase FKBP-type.
+At position 251 to 420, the domain is characterized as PCI.
+At position 2 to 206, the domain is characterized as RNase H type-2.
+At position 19 to 262, the domain is characterized as tr-type G.
+At position 3 to 103, the domain is characterized as Glutaredoxin.
+At position 196 to 531, the domain is characterized as Asparagine synthetase.
+At position 7 to 53, the domain is characterized as F-box.
+At position 389 to 548, the domain is characterized as PA14.
+At position 78 to 386, the domain is characterized as USP.
+At position 65 to 151, the domain is characterized as PDZ 1.
+At position 160 to 246, the domain is characterized as PDZ 2.
+At position 313 to 393, the domain is characterized as PDZ 3.
+At position 428 to 498, the domain is characterized as SH3.
+At position 534 to 709, the domain is characterized as Guanylate kinase-like.
+At position 51 to 170, the domain is characterized as Response regulatory.
+At position 45 to 167, the domain is characterized as MsrB.
+At position 26 to 122, the domain is characterized as CARD 1.
+At position 126 to 218, the domain is characterized as CARD 2.
+At position 293 to 618, the domain is characterized as NACHT.
+At position 71 to 142, the domain is characterized as PUB.
+At position 564 to 615, the domain is characterized as UBA.
+At position 206 to 292, the domain is characterized as Ig-like C1-type.
+At position 112 to 300, the domain is characterized as ATP-grasp.
+At position 167 to 480, the domain is characterized as IF rod.
+At position 679 to 768, the domain is characterized as BRCT.
+At position 1065 to 1124, the domain is characterized as SH3.
+At position 92 to 266, the domain is characterized as CRAL-TRIO.
+At position 2 to 118, the domain is characterized as VOC.
+At position 142 to 325, the domain is characterized as Brix.
+At position 233 to 574, the domain is characterized as SET.
+At position 125 to 160, the domain is characterized as EF-hand 3.
+At position 160 to 192, the domain is characterized as EF-hand 4.
+At position 470 to 522, the domain is characterized as F-box.
+At position 235 to 454, the domain is characterized as FAD-binding FR-type.
+At position 437 to 495, the domain is characterized as Prospero-type homeo.
+At position 496 to 592, the domain is characterized as Prospero.
+At position 19 to 446, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 942 to 1246, the domain is characterized as PKS/mFAS DH.
+At position 2294 to 2370, the domain is characterized as Carrier.
+At position 73 to 168, the domain is characterized as BRICHOS.
+At position 1145 to 1221, the domain is characterized as Pre-SET.
+At position 1224 to 1356, the domain is characterized as SET.
+At position 1366 to 1382, the domain is characterized as Post-SET.
+At position 25 to 67, the domain is characterized as CHCH.
+At position 21 to 139, the domain is characterized as Response regulatory.
+At position 200 to 382, the domain is characterized as CheB-type methylesterase.
+At position 186 to 438, the domain is characterized as NR LBD.
+At position 198 to 269, the domain is characterized as Death 1.
+At position 270 to 365, the domain is characterized as Death 2.
+At position 457 to 717, the domain is characterized as Protein kinase.
+At position 718 to 768, the domain is characterized as AGC-kinase C-terminal.
+At position 27 to 55, the domain is characterized as LRRNT.
+At position 89 to 143, the domain is characterized as LRRCT.
+At position 30 to 148, the domain is characterized as Rhodanese.
+At position 206 to 349, the domain is characterized as Tyrosine-protein phosphatase.
+At position 183 to 281, the domain is characterized as HTH araC/xylS-type.
+At position 359 to 566, the domain is characterized as MCM.
+At position 4 to 121, the domain is characterized as PINc.
+At position 21 to 84, the domain is characterized as SAM.
+At position 191 to 437, the domain is characterized as Protein kinase.
+At position 426 to 598, the domain is characterized as tr-type G.
+At position 58 to 234, the domain is characterized as FAD-binding PCMH-type.
+At position 28 to 244, the domain is characterized as tr-type G.
+At position 172 to 287, the domain is characterized as C-type lectin.
+At position 15 to 172, the domain is characterized as Tyrosine-protein phosphatase.
+At position 29 to 131, the domain is characterized as AB hydrolase-1.
+At position 607 to 696, the domain is characterized as BRCT.
+At position 174 to 257, the domain is characterized as HTH araC/xylS-type.
+At position 18 to 159, the domain is characterized as SprT-like.
+At position 8 to 258, the domain is characterized as DOG1.
+At position 136 to 341, the domain is characterized as ATP-grasp.
+At position 24 to 345, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 5 to 79, the domain is characterized as J.
+At position 25 to 168, the domain is characterized as F5/8 type C.
+At position 203 to 355, the domain is characterized as Laminin G-like 1.
+At position 389 to 538, the domain is characterized as Laminin G-like 2.
+At position 540 to 577, the domain is characterized as EGF-like 1.
+At position 576 to 795, the domain is characterized as Fibrinogen C-terminal.
+At position 813 to 956, the domain is characterized as Laminin G-like 3.
+At position 957 to 996, the domain is characterized as EGF-like 2.
+At position 1088 to 1250, the domain is characterized as Laminin G-like 4.
+At position 360 to 771, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1258 to 1579, the domain is characterized as PKS/mFAS DH.
+At position 1627 to 1701, the domain is characterized as Carrier.
+At position 48 to 192, the domain is characterized as AB hydrolase-1.
+At position 273 to 506, the domain is characterized as PX.
+At position 596 to 673, the domain is characterized as BRCT.
+At position 378 to 442, the domain is characterized as TRAM.
+At position 2 to 44, the domain is characterized as CHCH.
+At position 113 to 235, the domain is characterized as MPN.
+At position 24 to 102, the domain is characterized as IGFBP N-terminal.
+At position 1 to 83, the domain is characterized as Core-binding (CB).
+At position 104 to 287, the domain is characterized as Tyr recombinase.
+At position 26 to 314, the domain is characterized as tr-type G.
+At position 619 to 786, the domain is characterized as Integrase catalytic.
+At position 11 to 72, the domain is characterized as HMA 1.
+At position 73 to 134, the domain is characterized as HMA 2.
+At position 172 to 236, the domain is characterized as HMA 3.
+At position 255 to 311, the domain is characterized as CBS 1.
+At position 315 to 373, the domain is characterized as CBS 2.
+At position 161 to 336, the domain is characterized as OBG-type G.
+At position 383 to 613, the domain is characterized as Radical SAM core.
+At position 115 to 221, the domain is characterized as HTH APSES-type.
+At position 351 to 458, the domain is characterized as Calponin-homology (CH).
+At position 31 to 556, the domain is characterized as Helicase ATP-binding.
+At position 48 to 103, the domain is characterized as bHLH.
+At position 121 to 157, the domain is characterized as Orange.
+At position 60 to 307, the domain is characterized as Radical SAM core.
+At position 286 to 326, the domain is characterized as UBA.
+At position 644 to 704, the domain is characterized as Tudor.
+At position 1094 to 1161, the domain is characterized as S1 motif.
+At position 1209 to 1306, the domain is characterized as SH2.
+At position 85 to 303, the domain is characterized as Radical SAM core.
+At position 188 to 380, the domain is characterized as Glutamine amidotransferase type-1.
+At position 16 to 87, the domain is characterized as GRAM.
+At position 123 to 157, the domain is characterized as EF-hand 3.
+At position 158 to 193, the domain is characterized as EF-hand 4.
+At position 1047 to 1334, the domain is characterized as CNH.
+At position 39 to 495, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 524 to 810, the domain is characterized as UvrD-like helicase C-terminal.
+At position 218 to 307, the domain is characterized as RCK C-terminal 1.
+At position 314 to 398, the domain is characterized as RCK C-terminal 2.
+At position 20 to 60, the domain is characterized as LRRNT.
+At position 4 to 258, the domain is characterized as Protein kinase.
+At position 33 to 313, the domain is characterized as IF rod.
+At position 3 to 162, the domain is characterized as Obg.
+At position 163 to 333, the domain is characterized as OBG-type G.
+At position 351 to 428, the domain is characterized as OCT.
+At position 12 to 78, the domain is characterized as J.
+At position 588 to 647, the domain is characterized as KH.
+At position 659 to 728, the domain is characterized as S1 motif.
+At position 1237 to 1594, the domain is characterized as Protein kinase.
+At position 98 to 235, the domain is characterized as PX.
+At position 346 to 588, the domain is characterized as PH.
+At position 609 to 729, the domain is characterized as Arf-GAP.
+At position 1 to 152, the domain is characterized as MGS-like.
+At position 7 to 331, the domain is characterized as DhaK.
+At position 367 to 567, the domain is characterized as DhaL.
+At position 68 to 240, the domain is characterized as hSac2.
+At position 263 to 398, the domain is characterized as C2.
+At position 21 to 71, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 89 to 139, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 130 to 248, the domain is characterized as PX.
+At position 8 to 253, the domain is characterized as ABC transporter.
+At position 44 to 158, the domain is characterized as Cytochrome c 1.
+At position 174 to 260, the domain is characterized as Cytochrome c 2.
+At position 72 to 183, the domain is characterized as Plastocyanin-like 1.
+At position 195 to 343, the domain is characterized as Plastocyanin-like 2.
+At position 151 to 236, the domain is characterized as RRM.
+At position 179 to 425, the domain is characterized as Peptidase S1.
+At position 4 to 83, the domain is characterized as KRAB.
+At position 152 to 248, the domain is characterized as PH 1.
+At position 348 to 442, the domain is characterized as PH 2.
+At position 1 to 82, the domain is characterized as Cytochrome b5 heme-binding.
+At position 96 to 408, the domain is characterized as IF rod.
+At position 109 to 189, the domain is characterized as RRM.
+At position 168 to 246, the domain is characterized as RRM 1.
+At position 267 to 345, the domain is characterized as RRM 2.
+At position 22 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 152 to 240, the domain is characterized as Ig-like C2-type 2.
+At position 249 to 349, the domain is characterized as Ig-like C2-type 3.
+At position 467 to 755, the domain is characterized as Protein kinase.
+At position 216 to 266, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 272 to 322, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 144 to 179, the domain is characterized as EF-hand 1.
+At position 180 to 215, the domain is characterized as EF-hand 2.
+At position 216 to 251, the domain is characterized as EF-hand 3.
+At position 3 to 138, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 20 to 468, the domain is characterized as Sema.
+At position 806 to 895, the domain is characterized as IPT/TIG 1.
+At position 898 to 982, the domain is characterized as IPT/TIG 2.
+At position 986 to 1095, the domain is characterized as IPT/TIG 3.
+At position 161 to 308, the domain is characterized as Cupin type-1.
+At position 1 to 50, the domain is characterized as Disintegrin.
+At position 470 to 525, the domain is characterized as Kazal-like.
+At position 468 to 503, the domain is characterized as EF-hand.
+At position 711 to 794, the domain is characterized as BRCT.
+At position 384 to 538, the domain is characterized as Guanylate cyclase.
+At position 1 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 172 to 295, the domain is characterized as MsrB.
+At position 31 to 79, the domain is characterized as Clip.
+At position 385 to 632, the domain is characterized as Peptidase S1.
+At position 432 to 620, the domain is characterized as VWFA.
+At position 35 to 262, the domain is characterized as GB1/RHD3-type G.
+At position 269 to 355, the domain is characterized as IPT/TIG.
+At position 132 to 190, the domain is characterized as SAM.
+At position 36 to 70, the domain is characterized as ShKT.
+At position 37 to 276, the domain is characterized as ABC transporter.
+At position 313 to 642, the domain is characterized as PDEase.
+At position 144 to 350, the domain is characterized as ATP-grasp.
+At position 225 to 315, the domain is characterized as PA.
+At position 24 to 344, the domain is characterized as MACPF.
+At position 369 to 398, the domain is characterized as EGF-like.
+At position 17 to 132, the domain is characterized as MTTase N-terminal.
+At position 153 to 395, the domain is characterized as Radical SAM core.
+At position 397 to 469, the domain is characterized as TRAM.
+At position 200 to 446, the domain is characterized as Ras-GEF.
+At position 3 to 87, the domain is characterized as ACB.
+At position 169 to 264, the domain is characterized as PPIase FKBP-type.
+At position 1 to 91, the domain is characterized as Pyrin.
+At position 143 to 465, the domain is characterized as NACHT.
+At position 145 to 313, the domain is characterized as 3'-5' exonuclease.
+At position 13 to 230, the domain is characterized as Radical SAM core.
+At position 43 to 327, the domain is characterized as Protein kinase.
+At position 86 to 350, the domain is characterized as AB hydrolase-1.
+At position 10 to 434, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 928 to 1226, the domain is characterized as PKS/mFAS DH.
+At position 2465 to 2542, the domain is characterized as Carrier.
+At position 950 to 1116, the domain is characterized as PNPLA.
+At position 570 to 645, the domain is characterized as BRCT.
+At position 68 to 228, the domain is characterized as CP-type G.
+At position 154 to 198, the domain is characterized as SANT.
+At position 471 to 562, the domain is characterized as SWIRM.
+At position 114 to 175, the domain is characterized as CBS 1.
+At position 1 to 246, the domain is characterized as Pterin-binding.
+At position 596 to 813, the domain is characterized as Rap-GAP.
+At position 951 to 1027, the domain is characterized as PDZ.
+At position 75 to 219, the domain is characterized as HD.
+At position 30 to 179, the domain is characterized as UBC core.
+At position 213 to 278, the domain is characterized as HTH luxR-type.
+At position 6 to 102, the domain is characterized as SH2 1.
+At position 112 to 215, the domain is characterized as SH2 2.
+At position 246 to 517, the domain is characterized as Tyrosine-protein phosphatase.
+At position 25 to 66, the domain is characterized as LRRNT.
+At position 5 to 146, the domain is characterized as RNase H type-1.
+At position 459 to 628, the domain is characterized as tr-type G.
+At position 201 to 386, the domain is characterized as GMPS ATP-PPase.
+At position 6 to 219, the domain is characterized as Radical SAM core.
+At position 181 to 215, the domain is characterized as SAP.
+At position 2 to 115, the domain is characterized as PLAT.
+At position 116 to 663, the domain is characterized as Lipoxygenase.
+At position 27 to 383, the domain is characterized as IF rod.
+At position 425 to 542, the domain is characterized as LTD.
+At position 26 to 67, the domain is characterized as LDL-receptor class A 1.
+At position 70 to 106, the domain is characterized as LDL-receptor class A 2.
+At position 109 to 144, the domain is characterized as LDL-receptor class A 3.
+At position 147 to 183, the domain is characterized as LDL-receptor class A 4.
+At position 190 to 226, the domain is characterized as LDL-receptor class A 5.
+At position 230 to 266, the domain is characterized as LDL-receptor class A 6.
+At position 269 to 305, the domain is characterized as LDL-receptor class A 7.
+At position 311 to 350, the domain is characterized as LDL-receptor class A 8.
+At position 354 to 394, the domain is characterized as EGF-like 1; atypical.
+At position 395 to 434, the domain is characterized as EGF-like 2; calcium-binding.
+At position 698 to 737, the domain is characterized as EGF-like 3.
+At position 37 to 113, the domain is characterized as Inhibitor I9.
+At position 125 to 396, the domain is characterized as Peptidase S8.
+At position 131 to 164, the domain is characterized as WW 1.
+At position 431 to 464, the domain is characterized as WW 2.
+At position 530 to 563, the domain is characterized as WW 3.
+At position 661 to 714, the domain is characterized as FF 1.
+At position 727 to 781, the domain is characterized as FF 2.
+At position 793 to 848, the domain is characterized as FF 3.
+At position 898 to 954, the domain is characterized as FF 4.
+At position 956 to 1012, the domain is characterized as FF 5.
+At position 1014 to 1079, the domain is characterized as FF 6.
+At position 115 to 321, the domain is characterized as ATP-grasp.
+At position 1 to 221, the domain is characterized as Peptidase C83.
+At position 9 to 146, the domain is characterized as N-acetyltransferase.
+At position 374 to 647, the domain is characterized as Protein kinase.
+At position 648 to 719, the domain is characterized as AGC-kinase C-terminal.
+At position 967 to 1055, the domain is characterized as PDZ.
+At position 274 to 355, the domain is characterized as RRM.
+At position 534 to 679, the domain is characterized as CID.
+At position 2 to 218, the domain is characterized as ABC transporter.
+At position 72 to 421, the domain is characterized as Kinesin motor.
+At position 267 to 520, the domain is characterized as Protein kinase.
+At position 49 to 103, the domain is characterized as ClpX-type ZB.
+At position 47 to 142, the domain is characterized as PH.
+At position 160 to 278, the domain is characterized as C2.
+At position 348 to 609, the domain is characterized as Protein kinase.
+At position 610 to 681, the domain is characterized as AGC-kinase C-terminal.
+At position 29 to 235, the domain is characterized as YjeF N-terminal.
+At position 249 to 548, the domain is characterized as YjeF C-terminal.
+At position 35 to 461, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 910 to 1198, the domain is characterized as PKS/mFAS DH.
+At position 1706 to 1785, the domain is characterized as Carrier.
+At position 26 to 79, the domain is characterized as bHLH.
+At position 111 to 175, the domain is characterized as PAS 1.
+At position 270 to 340, the domain is characterized as PAS 2.
+At position 346 to 387, the domain is characterized as PAC.
+At position 9 to 155, the domain is characterized as Nudix hydrolase.
+At position 65 to 241, the domain is characterized as Helicase ATP-binding.
+At position 255 to 425, the domain is characterized as Helicase C-terminal.
+At position 16 to 216, the domain is characterized as RNase H type-2.
+At position 276 to 551, the domain is characterized as B30.2/SPRY.
+At position 86 to 176, the domain is characterized as K-box.
+At position 28 to 99, the domain is characterized as Importin N-terminal.
+At position 63 to 118, the domain is characterized as AWS.
+At position 120 to 237, the domain is characterized as SET.
+At position 244 to 260, the domain is characterized as Post-SET.
+At position 475 to 507, the domain is characterized as WW.
+At position 235 to 330, the domain is characterized as HTH arsR-type.
+At position 92 to 214, the domain is characterized as B12-binding.
+At position 116 to 179, the domain is characterized as PAS 1.
+At position 273 to 340, the domain is characterized as PAS 2.
+At position 116 to 195, the domain is characterized as RRM.
+At position 383 to 533, the domain is characterized as NTF2.
+At position 562 to 616, the domain is characterized as TAP-C.
+At position 10 to 87, the domain is characterized as RRM.
+At position 277 to 416, the domain is characterized as SIS 1.
+At position 441 to 582, the domain is characterized as SIS 2.
+At position 4 to 44, the domain is characterized as SpoVT-AbrB.
+At position 213 to 264, the domain is characterized as LRRCT 1.
+At position 333 to 375, the domain is characterized as LRRNT.
+At position 531 to 582, the domain is characterized as LRRCT 2.
+At position 65 to 331, the domain is characterized as GP-PDE.
+At position 216 to 378, the domain is characterized as TrmE-type G.
+At position 79 to 250, the domain is characterized as Helicase ATP-binding.
+At position 262 to 422, the domain is characterized as Helicase C-terminal.
+At position 154 to 247, the domain is characterized as PpiC.
+At position 239 to 411, the domain is characterized as tr-type G.
+At position 218 to 262, the domain is characterized as TSP type-1.
+At position 289 to 452, the domain is characterized as AMOP.
+At position 102 to 131, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 141 to 170, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 203 to 294, the domain is characterized as Ig-like C1-type.
+At position 5 to 150, the domain is characterized as Ferritin-like diiron.
+At position 9 to 315, the domain is characterized as Protein kinase.
+At position 638 to 667, the domain is characterized as IQ.
+At position 29 to 133, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 225, the domain is characterized as Ig-like C2-type 2.
+At position 245 to 330, the domain is characterized as Ig-like C2-type 3.
+At position 339 to 426, the domain is characterized as Ig-like C2-type 4.
+At position 432 to 524, the domain is characterized as Ig-like C2-type 5.
+At position 521 to 610, the domain is characterized as Ig-like C2-type 6.
+At position 614 to 711, the domain is characterized as Fibronectin type-III 1.
+At position 716 to 813, the domain is characterized as Fibronectin type-III 2.
+At position 818 to 915, the domain is characterized as Fibronectin type-III 3.
+At position 916 to 1017, the domain is characterized as Fibronectin type-III 4.
+At position 1021 to 1119, the domain is characterized as Fibronectin type-III 5.
+At position 70 to 295, the domain is characterized as Radical SAM core.
+At position 7 to 25, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 19 to 216, the domain is characterized as ABC transmembrane type-1.
+At position 20 to 223, the domain is characterized as AIG1-type G.
+At position 561 to 625, the domain is characterized as KH.
+At position 712 to 771, the domain is characterized as Tudor.
+At position 6 to 90, the domain is characterized as MtN3/slv 1.
+At position 124 to 206, the domain is characterized as MtN3/slv 2.
+At position 2 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 123 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 307, the domain is characterized as Ig-like C2-type 3.
+At position 317 to 401, the domain is characterized as Ig-like C2-type 4.
+At position 407 to 494, the domain is characterized as Ig-like C2-type 5.
+At position 498 to 593, the domain is characterized as Ig-like C2-type 6.
+At position 805 to 899, the domain is characterized as Fibronectin type-III 3.
+At position 901 to 994, the domain is characterized as Fibronectin type-III 4.
+At position 6 to 243, the domain is characterized as tr-type G.
+At position 23 to 156, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 188 to 301, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 8 to 199, the domain is characterized as Clp R.
+At position 1 to 277, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 449 to 557, the domain is characterized as Peptidase S74.
+At position 15 to 45, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 54 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 78 to 323, the domain is characterized as ABC transporter 1.
+At position 350 to 570, the domain is characterized as ABC transporter 2.
+At position 160 to 228, the domain is characterized as DRBM.
+At position 15 to 61, the domain is characterized as G-patch.
+At position 379 to 564, the domain is characterized as Roc.
+At position 1185 to 1452, the domain is characterized as Protein kinase.
+At position 164 to 243, the domain is characterized as SH3.
+At position 280 to 473, the domain is characterized as Rho-GAP.
+At position 271 to 301, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 321 to 351, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 122 to 408, the domain is characterized as tr-type G.
+At position 2 to 53, the domain is characterized as F-box.
+At position 25 to 234, the domain is characterized as YjeF N-terminal.
+At position 36 to 80, the domain is characterized as EGF-like 1.
+At position 96 to 134, the domain is characterized as EGF-like 2.
+At position 147 to 192, the domain is characterized as EGF-like 3.
+At position 100 to 175, the domain is characterized as VWFC 1.
+At position 197 to 337, the domain is characterized as CHRD 1.
+At position 339 to 471, the domain is characterized as CHRD 2.
+At position 474 to 588, the domain is characterized as CHRD 3.
+At position 592 to 713, the domain is characterized as CHRD 4.
+At position 742 to 804, the domain is characterized as VWFC 2.
+At position 830 to 899, the domain is characterized as VWFC 3.
+At position 939 to 1020, the domain is characterized as VWFC 4.
+At position 124 to 318, the domain is characterized as BPL/LPL catalytic.
+At position 32 to 80, the domain is characterized as F-box.
+At position 89 to 196, the domain is characterized as EamA.
+At position 368 to 428, the domain is characterized as PAP-associated.
+At position 557 to 617, the domain is characterized as KH.
+At position 627 to 691, the domain is characterized as S1 motif.
+At position 16 to 217, the domain is characterized as ABC transmembrane type-1.
+At position 268 to 477, the domain is characterized as B30.2/SPRY.
+At position 26 to 332, the domain is characterized as Peptidase S6.
+At position 1289 to 1541, the domain is characterized as Autotransporter.
+At position 91 to 120, the domain is characterized as Oxidoreductase-like.
+At position 2 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 16 to 240, the domain is characterized as AB hydrolase-1.
+At position 144 to 202, the domain is characterized as TRAM.
+At position 410 to 488, the domain is characterized as POLO box 1.
+At position 510 to 592, the domain is characterized as POLO box 2.
+At position 16 to 445, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 926 to 1234, the domain is characterized as PKS/mFAS DH.
+At position 2517 to 2594, the domain is characterized as Carrier.
+At position 61 to 326, the domain is characterized as Protein kinase.
+At position 79 to 131, the domain is characterized as bHLH.
+At position 143 to 283, the domain is characterized as N-acetyltransferase.
+At position 39 to 143, the domain is characterized as PTS EIIA type-1.
+At position 374 to 430, the domain is characterized as CBS 1.
+At position 435 to 497, the domain is characterized as CBS 2.
+At position 143 to 272, the domain is characterized as PX.
+At position 302 to 522, the domain is characterized as BAR.
+At position 3 to 134, the domain is characterized as Toprim.
+At position 55 to 306, the domain is characterized as Protein kinase.
+At position 348 to 389, the domain is characterized as UBA.
+At position 46 to 112, the domain is characterized as BTB.
+At position 151 to 247, the domain is characterized as BACK.
+At position 4 to 136, the domain is characterized as Galectin.
+At position 17 to 163, the domain is characterized as N-acetyltransferase 1.
+At position 166 to 306, the domain is characterized as N-acetyltransferase 2.
+At position 8 to 169, the domain is characterized as Exonuclease.
+At position 34 to 129, the domain is characterized as EthD.
+At position 489 to 747, the domain is characterized as ATP-grasp.
+At position 5 to 275, the domain is characterized as Tyrosine-protein phosphatase.
+At position 419 to 457, the domain is characterized as PLD phosphodiesterase 2.
+At position 82 to 300, the domain is characterized as Radical SAM core.
+At position 29 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 4 to 186, the domain is characterized as Guanylate kinase-like.
+At position 7 to 85, the domain is characterized as Ubiquitin-like.
+At position 83 to 118, the domain is characterized as EF-hand 2.
+At position 95 to 311, the domain is characterized as PPIase cyclophilin-type.
+At position 143 to 348, the domain is characterized as ATP-grasp.
+At position 142 to 230, the domain is characterized as PPIase FKBP-type.
+At position 625 to 704, the domain is characterized as BRCT.
+At position 87 to 401, the domain is characterized as FERM.
+At position 2287 to 2526, the domain is characterized as I/LWEQ.
+At position 2 to 110, the domain is characterized as Thioredoxin.
+At position 47 to 80, the domain is characterized as EF-hand 1.
+At position 78 to 113, the domain is characterized as EF-hand 2.
+At position 114 to 149, the domain is characterized as EF-hand 3.
+At position 182 to 493, the domain is characterized as DOT1.
+At position 505 to 614, the domain is characterized as CXC.
+At position 616 to 737, the domain is characterized as SET.
+At position 28 to 297, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 32 to 301, the domain is characterized as Dynamin-type G.
+At position 520 to 612, the domain is characterized as GED.
+At position 225 to 580, the domain is characterized as PUM-HD.
+At position 51 to 730, the domain is characterized as Myosin motor.
+At position 734 to 754, the domain is characterized as IQ 1.
+At position 755 to 780, the domain is characterized as IQ 2.
+At position 788 to 976, the domain is characterized as TH1.
+At position 1077 to 1138, the domain is characterized as SH3.
+At position 95 to 180, the domain is characterized as PNT.
+At position 6 to 67, the domain is characterized as SH3.
+At position 421 to 599, the domain is characterized as C2 DOCK-type.
+At position 1228 to 1635, the domain is characterized as DOCKER.
+At position 403 to 484, the domain is characterized as Disintegrin.
+At position 31 to 103, the domain is characterized as Importin N-terminal.
+At position 60 to 287, the domain is characterized as Radical SAM core.
+At position 188 to 347, the domain is characterized as PCI.
+At position 110 to 202, the domain is characterized as ARID.
+At position 301 to 386, the domain is characterized as REKLES.
+At position 59 to 101, the domain is characterized as UBA 1.
+At position 109 to 150, the domain is characterized as UBA 2.
+At position 190 to 232, the domain is characterized as UBA 3.
+At position 295 to 626, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 2 to 170, the domain is characterized as Era-type G.
+At position 131 to 371, the domain is characterized as VWFA.
+At position 188 to 224, the domain is characterized as EF-hand.
+At position 5 to 57, the domain is characterized as LIM zinc-binding 1.
+At position 126 to 178, the domain is characterized as LIM zinc-binding 2.
+At position 117 to 521, the domain is characterized as Glutamine amidotransferase type-2.
+At position 1 to 59, the domain is characterized as HTH lacI-type.
+At position 14 to 104, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 11 to 212, the domain is characterized as HORMA.
+At position 147 to 182, the domain is characterized as EF-hand 4.
+At position 40 to 208, the domain is characterized as Tyrosine-protein phosphatase.
+At position 24 to 78, the domain is characterized as HTH cro/C1-type.
+At position 8 to 295, the domain is characterized as tr-type G.
+At position 1 to 112, the domain is characterized as C2 1.
+At position 123 to 263, the domain is characterized as C2 2.
+At position 330 to 524, the domain is characterized as Ras-GAP.
+At position 576 to 677, the domain is characterized as PH.
+At position 139 to 314, the domain is characterized as Helicase ATP-binding.
+At position 328 to 498, the domain is characterized as Helicase C-terminal.
+At position 59 to 191, the domain is characterized as Nudix hydrolase.
+At position 141 to 275, the domain is characterized as OTU.
+At position 161 to 278, the domain is characterized as C-type lectin.
+At position 60 to 150, the domain is characterized as UPAR/Ly6.
+At position 265 to 342, the domain is characterized as PUA.
+At position 47 to 111, the domain is characterized as Chitin-binding type-2.
+At position 165 to 382, the domain is characterized as SMP-LTD.
+At position 68 to 200, the domain is characterized as PH 1.
+At position 217 to 301, the domain is characterized as PH 2.
+At position 138 to 388, the domain is characterized as Protein kinase.
+At position 215 to 371, the domain is characterized as TrmE-type G.
+At position 486 to 676, the domain is characterized as SEC7.
+At position 48 to 121, the domain is characterized as J.
+At position 1043 to 1297, the domain is characterized as Glutamine amidotransferase type-1.
+At position 278 to 352, the domain is characterized as U-box.
+At position 291 to 367, the domain is characterized as PUA.
+At position 258 to 467, the domain is characterized as Peptidase M12B.
+At position 476 to 558, the domain is characterized as Disintegrin.
+At position 559 to 614, the domain is characterized as TSP type-1 1.
+At position 854 to 910, the domain is characterized as TSP type-1 2.
+At position 911 to 967, the domain is characterized as TSP type-1 3.
+At position 1 to 76, the domain is characterized as Lipoyl-binding.
+At position 128 to 164, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 44 to 156, the domain is characterized as FAD-binding FR-type.
+At position 35 to 207, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 164, the domain is characterized as C-type lectin.
+At position 187 to 321, the domain is characterized as PX.
+At position 4 to 103, the domain is characterized as FAD-binding FR-type.
+At position 196 to 323, the domain is characterized as Nudix hydrolase.
+At position 20 to 139, the domain is characterized as Ig-like.
+At position 62 to 160, the domain is characterized as Rieske.
+At position 451 to 587, the domain is characterized as VWFA.
+At position 255 to 417, the domain is characterized as PCI.
+At position 53 to 169, the domain is characterized as FZ.
+At position 186 to 306, the domain is characterized as NTR.
+At position 207 to 380, the domain is characterized as EngA-type G 2.
+At position 8 to 167, the domain is characterized as YEATS.
+At position 204 to 393, the domain is characterized as CheB-type methylesterase.
+At position 5 to 234, the domain is characterized as Radical SAM core.
+At position 372 to 790, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1282 to 1591, the domain is characterized as PKS/mFAS DH.
+At position 1653 to 1727, the domain is characterized as Carrier.
+At position 13 to 212, the domain is characterized as ABC transmembrane type-1.
+At position 949 to 1162, the domain is characterized as FtsK.
+At position 151 to 232, the domain is characterized as Doublecortin.
+At position 143 to 445, the domain is characterized as ABC transmembrane type-1.
+At position 479 to 713, the domain is characterized as ABC transporter.
+At position 127 to 462, the domain is characterized as PI3K/PI4K catalytic.
+At position 557 to 617, the domain is characterized as SH3.
+At position 1 to 130, the domain is characterized as Guanylate kinase-like.
+At position 18 to 60, the domain is characterized as JmjN.
+At position 149 to 315, the domain is characterized as JmjC.
+At position 185 to 223, the domain is characterized as LRRCT.
+At position 279 to 317, the domain is characterized as LRRCT.
+At position 290 to 496, the domain is characterized as MCM.
+At position 151 to 201, the domain is characterized as DHHC.
+At position 196 to 285, the domain is characterized as TonB C-terminal.
+At position 7 to 93, the domain is characterized as Acylphosphatase-like.
+At position 129 to 223, the domain is characterized as Rhodanese.
+At position 43 to 160, the domain is characterized as MTTase N-terminal.
+At position 190 to 422, the domain is characterized as Radical SAM core.
+At position 425 to 493, the domain is characterized as TRAM.
+At position 619 to 686, the domain is characterized as S1 motif.
+At position 1 to 246, the domain is characterized as Protein kinase.
+At position 1 to 74, the domain is characterized as GST N-terminal.
+At position 80 to 206, the domain is characterized as GST C-terminal.
+At position 55 to 121, the domain is characterized as TGS.
+At position 7 to 275, the domain is characterized as tr-type G.
+At position 14 to 144, the domain is characterized as VHS.
+At position 210 to 269, the domain is characterized as SH3.
+At position 7 to 185, the domain is characterized as uDENN.
+At position 204 to 337, the domain is characterized as cDENN.
+At position 339 to 440, the domain is characterized as dDENN.
+At position 881 to 969, the domain is characterized as GRAM.
+At position 1121 to 1597, the domain is characterized as Myotubularin phosphatase.
+At position 1762 to 1866, the domain is characterized as PH.
+At position 214 to 414, the domain is characterized as Rho-GAP.
+At position 57 to 286, the domain is characterized as Radical SAM core.
+At position 13 to 85, the domain is characterized as Sm.
+At position 27 to 157, the domain is characterized as EamA 1.
+At position 223 to 329, the domain is characterized as EamA 2.
+At position 1 to 90, the domain is characterized as HPr.
+At position 685 to 828, the domain is characterized as PTS EIIA type-2.
+At position 40 to 163, the domain is characterized as PX.
+At position 107 to 201, the domain is characterized as PB1.
+At position 73 to 247, the domain is characterized as FAD-binding PCMH-type.
+At position 101 to 297, the domain is characterized as ATP-grasp.
+At position 1 to 338, the domain is characterized as Protein kinase.
+At position 2093 to 2223, the domain is characterized as MPN.
+At position 5 to 124, the domain is characterized as C2.
+At position 273 to 818, the domain is characterized as PLA2c.
+At position 457 to 579, the domain is characterized as HD.
+At position 700 to 782, the domain is characterized as ACT 1.
+At position 809 to 887, the domain is characterized as ACT 2.
+At position 49 to 400, the domain is characterized as Peptidase A1.
+At position 141 to 382, the domain is characterized as Radical SAM core.
+At position 385 to 454, the domain is characterized as TRAM.
+At position 262 to 442, the domain is characterized as GATase cobBQ-type.
+At position 49 to 275, the domain is characterized as Peptidase S1.
+At position 1 to 246, the domain is characterized as KaiC 1.
+At position 260 to 519, the domain is characterized as KaiC 2.
+At position 21 to 133, the domain is characterized as Thioredoxin 1.
+At position 123 to 342, the domain is characterized as Radical SAM core.
+At position 19 to 124, the domain is characterized as Ig-like V-type.
+At position 351 to 609, the domain is characterized as TRUD.
+At position 86 to 298, the domain is characterized as TLC.
+At position 264 to 355, the domain is characterized as PDZ 1.
+At position 361 to 468, the domain is characterized as PDZ 2.
+At position 617 to 646, the domain is characterized as IQ.
+At position 816 to 892, the domain is characterized as ACT 2.
+At position 243 to 493, the domain is characterized as CN hydrolase.
+At position 297 to 329, the domain is characterized as NAF.
+At position 152 to 197, the domain is characterized as RPE1 insert.
+At position 160 to 211, the domain is characterized as bHLH.
+At position 19 to 250, the domain is characterized as ABC transporter.
+At position 112 to 341, the domain is characterized as Radical SAM core.
+At position 236 to 334, the domain is characterized as HTH araC/xylS-type.
+At position 200 to 395, the domain is characterized as Glutamine amidotransferase type-1.
+At position 65 to 135, the domain is characterized as KH.
+At position 122 to 307, the domain is characterized as Tyr recombinase.
+At position 23 to 37, the domain is characterized as CRIB.
+At position 614 to 805, the domain is characterized as Collectrin-like.
+At position 556 to 728, the domain is characterized as PCI.
+At position 1 to 105, the domain is characterized as C2.
+At position 49 to 274, the domain is characterized as L-type lectin-like.
+At position 39 to 102, the domain is characterized as HMA.
+At position 9 to 270, the domain is characterized as Protein kinase.
+At position 8 to 97, the domain is characterized as ACB.
+At position 21 to 97, the domain is characterized as UPAR/Ly6.
+At position 19 to 112, the domain is characterized as Ig-like V-type.
+At position 126 to 225, the domain is characterized as Ig-like C2-type.
+At position 118 to 171, the domain is characterized as Oxytoxin-type inhibitor cystine knot (ICK).
+At position 124 to 174, the domain is characterized as DHHC.
+At position 5 to 132, the domain is characterized as ADF-H 1.
+At position 173 to 300, the domain is characterized as ADF-H 2.
+At position 22 to 260, the domain is characterized as ABC transporter.
+At position 1 to 189, the domain is characterized as CheB-type methylesterase.
+At position 8 to 256, the domain is characterized as Protein kinase.
+At position 274 to 314, the domain is characterized as UBA.
+At position 288 to 425, the domain is characterized as PH.
+At position 498 to 643, the domain is characterized as Arf-GAP.
+At position 224 to 407, the domain is characterized as MIF4G.
+At position 515 to 648, the domain is characterized as MI.
+At position 36 to 336, the domain is characterized as Protein kinase.
+At position 186 to 238, the domain is characterized as GPS.
+At position 2 to 108, the domain is characterized as Glutaredoxin.
+At position 5 to 352, the domain is characterized as Trm1 methyltransferase.
+At position 10 to 100, the domain is characterized as EH 1.
+At position 42 to 77, the domain is characterized as EF-hand.
+At position 139 to 227, the domain is characterized as EH 2.
+At position 397 to 474, the domain is characterized as REM-1.
+At position 538 to 599, the domain is characterized as SH3.
+At position 162 to 318, the domain is characterized as C1q.
+At position 218 to 280, the domain is characterized as t-SNARE coiled-coil homology.
+At position 7 to 73, the domain is characterized as MIT.
+At position 36 to 223, the domain is characterized as KIND.
+At position 295 to 313, the domain is characterized as WH2 1.
+At position 359 to 376, the domain is characterized as WH2 2.
+At position 242 to 420, the domain is characterized as PCI.
+At position 282 to 334, the domain is characterized as AFP-like.
+At position 17 to 90, the domain is characterized as S4 RNA-binding.
+At position 224 to 392, the domain is characterized as PCI.
+At position 1 to 129, the domain is characterized as C-type lectin.
+At position 34 to 230, the domain is characterized as Peptidase M12B.
+At position 238 to 319, the domain is characterized as Disintegrin.
+At position 14 to 236, the domain is characterized as RNase H type-2.
+At position 20 to 105, the domain is characterized as Ig-like.
+At position 20 to 54, the domain is characterized as WW.
+At position 466 to 640, the domain is characterized as Helicase ATP-binding.
+At position 669 to 813, the domain is characterized as Helicase C-terminal.
+At position 58 to 288, the domain is characterized as Radical SAM core.
+At position 29 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 132 to 214, the domain is characterized as Ig-like C2-type 2.
+At position 219 to 304, the domain is characterized as Ig-like C2-type 3.
+At position 77 to 305, the domain is characterized as Radical SAM core.
+At position 1 to 405, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 52 to 184, the domain is characterized as RUN.
+At position 24 to 171, the domain is characterized as Reelin.
+At position 34 to 87, the domain is characterized as Sushi.
+At position 104 to 346, the domain is characterized as Peptidase S1.
+At position 48 to 164, the domain is characterized as sHSP.
+At position 53 to 145, the domain is characterized as Ig-like C1-type.
+At position 211 to 269, the domain is characterized as bZIP.
+At position 97 to 229, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 573 to 648, the domain is characterized as PUA.
+At position 68 to 238, the domain is characterized as Helicase ATP-binding.
+At position 249 to 410, the domain is characterized as Helicase C-terminal.
+At position 72 to 125, the domain is characterized as bHLH.
+At position 167 to 240, the domain is characterized as PAS 1.
+At position 307 to 377, the domain is characterized as PAS 2.
+At position 381 to 422, the domain is characterized as PAC.
+At position 46 to 178, the domain is characterized as SCP.
+At position 39 to 106, the domain is characterized as HMA.
+At position 579 to 654, the domain is characterized as BRCT.
+At position 36 to 161, the domain is characterized as PLAT.
+At position 164 to 862, the domain is characterized as Lipoxygenase.
+At position 517 to 699, the domain is characterized as Helicase ATP-binding 1.
+At position 734 to 932, the domain is characterized as Helicase C-terminal 1.
+At position 1008 to 1315, the domain is characterized as SEC63 1.
+At position 1365 to 1540, the domain is characterized as Helicase ATP-binding 2.
+At position 1571 to 1780, the domain is characterized as Helicase C-terminal 2.
+At position 1839 to 2150, the domain is characterized as SEC63 2.
+At position 1 to 95, the domain is characterized as CARD 1.
+At position 99 to 191, the domain is characterized as CARD 2.
+At position 266 to 591, the domain is characterized as NACHT.
+At position 29 to 97, the domain is characterized as KH type-2.
+At position 224 to 480, the domain is characterized as ATP-grasp.
+At position 33 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 287 to 383, the domain is characterized as Ig-like C2-type 2.
+At position 391 to 501, the domain is characterized as Ig-like C2-type 3.
+At position 640 to 931, the domain is characterized as Protein kinase.
+At position 68 to 139, the domain is characterized as GRAM.
+At position 205 to 580, the domain is characterized as Myotubularin phosphatase.
+At position 528 to 605, the domain is characterized as Carrier.
+At position 492 to 535, the domain is characterized as CAP-Gly 3.
+At position 592 to 950, the domain is characterized as USP.
+At position 36 to 262, the domain is characterized as Peptidase S1.
+At position 29 to 416, the domain is characterized as Helicase ATP-binding.
+At position 615 to 650, the domain is characterized as UVR.
+At position 153 to 242, the domain is characterized as Ig-like C2-type.
+At position 449 to 548, the domain is characterized as SH2.
+At position 274 to 350, the domain is characterized as B5.
+At position 3 to 67, the domain is characterized as L27.
+At position 149 to 229, the domain is characterized as PDZ 1.
+At position 318 to 403, the domain is characterized as PDZ 2.
+At position 559 to 648, the domain is characterized as PDZ 3.
+At position 728 to 814, the domain is characterized as PDZ 4.
+At position 64 to 297, the domain is characterized as GB1/RHD3-type G.
+At position 10 to 227, the domain is characterized as YjeF N-terminal.
+At position 196 to 254, the domain is characterized as TRAM.
+At position 56 to 158, the domain is characterized as Calponin-homology (CH).
+At position 234 to 304, the domain is characterized as EB1 C-terminal.
+At position 81 to 301, the domain is characterized as Glutamine amidotransferase type-2.
+At position 650 to 763, the domain is characterized as Calponin-homology (CH).
+At position 1976 to 2054, the domain is characterized as BRCT 1.
+At position 2075 to 2166, the domain is characterized as BRCT 2.
+At position 72 to 137, the domain is characterized as ACT 1.
+At position 259 to 320, the domain is characterized as ACT 2.
+At position 19 to 146, the domain is characterized as C2 1.
+At position 155 to 278, the domain is characterized as C2 2.
+At position 322 to 523, the domain is characterized as VWFA.
+At position 276 to 437, the domain is characterized as Helicase C-terminal.
+At position 4 to 233, the domain is characterized as Peptidase M12B.
+At position 16 to 88, the domain is characterized as Sm.
+At position 251 to 308, the domain is characterized as CBS 1.
+At position 315 to 376, the domain is characterized as CBS 2.
+At position 157 to 340, the domain is characterized as CheB-type methylesterase.
+At position 11 to 306, the domain is characterized as Protein kinase.
+At position 26 to 242, the domain is characterized as BAR.
+At position 83 to 254, the domain is characterized as Helicase ATP-binding.
+At position 282 to 426, the domain is characterized as Helicase C-terminal.
+At position 28 to 265, the domain is characterized as SET.
+At position 188 to 251, the domain is characterized as BTB.
+At position 14 to 101, the domain is characterized as Core-binding (CB).
+At position 129 to 304, the domain is characterized as Tyr recombinase.
+At position 179 to 372, the domain is characterized as CheB-type methylesterase.
+At position 373 to 408, the domain is characterized as EF-hand 1.
+At position 412 to 447, the domain is characterized as EF-hand 2.
+At position 40 to 129, the domain is characterized as SUEL-type lectin.
+At position 139 to 398, the domain is characterized as Olfactomedin-like.
+At position 798 to 849, the domain is characterized as GPS.
+At position 236 to 483, the domain is characterized as CN hydrolase.
+At position 69 to 272, the domain is characterized as ABC transmembrane type-1.
+At position 47 to 328, the domain is characterized as Protein kinase.
+At position 455 to 527, the domain is characterized as ACT.
+At position 44 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 8 to 84, the domain is characterized as Cytochrome b5 heme-binding.
+At position 112 to 207, the domain is characterized as TAFH.
+At position 55 to 127, the domain is characterized as J.
+At position 1339 to 1477, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1611 to 1753, the domain is characterized as RNase H Ty1/copia-type.
+At position 73 to 308, the domain is characterized as Radical SAM core.
+At position 115 to 196, the domain is characterized as PDZ 1.
+At position 223 to 301, the domain is characterized as PDZ 2.
+At position 329 to 412, the domain is characterized as PDZ 3.
+At position 467 to 548, the domain is characterized as PDZ 4.
+At position 273 to 433, the domain is characterized as SSD.
+At position 5 to 105, the domain is characterized as Ig-like 1.
+At position 133 to 233, the domain is characterized as Ig-like 2.
+At position 5 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 318 to 414, the domain is characterized as Chromo 1.
+At position 439 to 501, the domain is characterized as Chromo 2.
+At position 540 to 710, the domain is characterized as Helicase ATP-binding.
+At position 840 to 991, the domain is characterized as Helicase C-terminal.
+At position 53 to 88, the domain is characterized as EF-hand.
+At position 1 to 220, the domain is characterized as Protein kinase.
+At position 22 to 192, the domain is characterized as Chitin-binding type-4.
+At position 435 to 484, the domain is characterized as Chitin-binding type-3.
+At position 1 to 68, the domain is characterized as HMA.
+At position 23 to 329, the domain is characterized as Protein kinase.
+At position 405 to 433, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 443 to 472, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 386 to 723, the domain is characterized as Kinesin motor.
+At position 102 to 165, the domain is characterized as S5 DRBM.
+At position 18 to 261, the domain is characterized as Lon N-terminal.
+At position 667 to 851, the domain is characterized as Lon proteolytic.
+At position 16 to 148, the domain is characterized as VHS.
+At position 164 to 183, the domain is characterized as UIM.
+At position 257 to 316, the domain is characterized as SH3.
+At position 24 to 316, the domain is characterized as ABC transmembrane type-1.
+At position 350 to 583, the domain is characterized as ABC transporter.
+At position 4 to 88, the domain is characterized as Carrier.
+At position 60 to 133, the domain is characterized as RRM 1.
+At position 139 to 224, the domain is characterized as RRM 2.
+At position 342 to 404, the domain is characterized as S4 RNA-binding.
+At position 54 to 242, the domain is characterized as BPL/LPL catalytic.
+At position 3 to 58, the domain is characterized as MADS-box.
+At position 68 to 215, the domain is characterized as N-acetyltransferase.
+At position 405 to 1185, the domain is characterized as Myosin motor.
+At position 1188 to 1217, the domain is characterized as IQ.
+At position 36 to 132, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 219, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 311, the domain is characterized as Ig-like C2-type 3.
+At position 57 to 259, the domain is characterized as uDENN.
+At position 278 to 414, the domain is characterized as cDENN.
+At position 416 to 598, the domain is characterized as dDENN.
+At position 787 to 950, the domain is characterized as RUN 1.
+At position 954 to 1062, the domain is characterized as PLAT.
+At position 1134 to 1282, the domain is characterized as RUN 2.
+At position 212 to 481, the domain is characterized as Sigma-54 factor interaction.
+At position 23 to 150, the domain is characterized as ALOG.
+At position 20 to 241, the domain is characterized as Radical SAM core.
+At position 46 to 320, the domain is characterized as Brix.
+At position 169 to 396, the domain is characterized as TRUD.
+At position 3 to 218, the domain is characterized as ABC transporter.
+At position 238 to 503, the domain is characterized as NR LBD.
+At position 40 to 118, the domain is characterized as RRM.
+At position 756 to 897, the domain is characterized as TIR.
+At position 4 to 255, the domain is characterized as Protein kinase.
+At position 20 to 144, the domain is characterized as RNase III.
+At position 13 to 229, the domain is characterized as ABC transporter.
+At position 33 to 113, the domain is characterized as RRM.
+At position 133 to 327, the domain is characterized as ATP-grasp.
+At position 199 to 568, the domain is characterized as GRAS.
+At position 8 to 187, the domain is characterized as Macro.
+At position 255 to 287, the domain is characterized as LisH.
+At position 52 to 217, the domain is characterized as Helicase ATP-binding.
+At position 345 to 507, the domain is characterized as Helicase C-terminal.
+At position 709 to 900, the domain is characterized as Macro.
+At position 3 to 72, the domain is characterized as BTB.
+At position 13 to 82, the domain is characterized as Sm.
+At position 42 to 128, the domain is characterized as RRM.
+At position 84 to 117, the domain is characterized as KOW.
+At position 190 to 402, the domain is characterized as Helicase ATP-binding.
+At position 456 to 628, the domain is characterized as Helicase C-terminal.
+At position 18 to 141, the domain is characterized as EamA 1.
+At position 160 to 285, the domain is characterized as EamA 2.
+At position 117 to 476, the domain is characterized as PTS EIIC type-1.
+At position 550 to 654, the domain is characterized as PTS EIIA type-1.
+At position 9 to 241, the domain is characterized as ABC transporter.
+At position 114 to 194, the domain is characterized as Ig-like C2-type.
+At position 24 to 92, the domain is characterized as BTB.
+At position 81 to 115, the domain is characterized as EF-hand 2; degenerate.
+At position 286 to 363, the domain is characterized as PUA.
+At position 10 to 64, the domain is characterized as L27 1.
+At position 263 to 354, the domain is characterized as PDZ 1.
+At position 360 to 462, the domain is characterized as PDZ 2.
+At position 27 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 216 to 279, the domain is characterized as KH.
+At position 86 to 150, the domain is characterized as J.
+At position 4 to 194, the domain is characterized as Glutamine amidotransferase type-1.
+At position 55 to 91, the domain is characterized as LRRNT.
+At position 264 to 327, the domain is characterized as bZIP.
+At position 154 to 284, the domain is characterized as SCP.
+At position 1 to 224, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 225 to 473, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 992 to 1147, the domain is characterized as ZU5 1.
+At position 1149 to 1296, the domain is characterized as ZU5 2.
+At position 2336 to 2420, the domain is characterized as Death.
+At position 219 to 401, the domain is characterized as GAF.
+At position 616 to 687, the domain is characterized as PAS 1.
+At position 690 to 746, the domain is characterized as PAC.
+At position 750 to 821, the domain is characterized as PAS 2.
+At position 901 to 1121, the domain is characterized as Histidine kinase.
+At position 1 to 249, the domain is characterized as ABC transporter.
+At position 527 to 702, the domain is characterized as N-acetyltransferase.
+At position 217 to 256, the domain is characterized as BESS.
+At position 27 to 221, the domain is characterized as Lon N-terminal.
+At position 608 to 789, the domain is characterized as Lon proteolytic.
+At position 32 to 111, the domain is characterized as RRM 1.
+At position 121 to 198, the domain is characterized as RRM 2.
+At position 209 to 286, the domain is characterized as RRM 3.
+At position 313 to 390, the domain is characterized as RRM 4.
+At position 2 to 185, the domain is characterized as DOC.
+At position 344 to 417, the domain is characterized as HSA.
+At position 640 to 805, the domain is characterized as Helicase ATP-binding.
+At position 1179 to 1332, the domain is characterized as Helicase C-terminal.
+At position 111 to 146, the domain is characterized as EF-hand 3.
+At position 152 to 187, the domain is characterized as EF-hand 4.
+At position 34 to 260, the domain is characterized as GH16.
+At position 168 to 415, the domain is characterized as Fibrinogen C-terminal.
+At position 139 to 192, the domain is characterized as PAS.
+At position 1226 to 1246, the domain is characterized as WH2.
+At position 64 to 212, the domain is characterized as Nudix hydrolase.
+At position 505 to 702, the domain is characterized as B30.2/SPRY.
+At position 94 to 405, the domain is characterized as IF rod.
+At position 5 to 233, the domain is characterized as ABC transporter.
+At position 33 to 182, the domain is characterized as Ricin B-type lectin.
+At position 164 to 211, the domain is characterized as Fibronectin type-II.
+At position 225 to 341, the domain is characterized as C-type lectin 1.
+At position 368 to 486, the domain is characterized as C-type lectin 2.
+At position 493 to 625, the domain is characterized as C-type lectin 3.
+At position 652 to 791, the domain is characterized as C-type lectin 4.
+At position 959 to 1092, the domain is characterized as C-type lectin 5.
+At position 1111 to 1223, the domain is characterized as C-type lectin 6.
+At position 1252 to 1375, the domain is characterized as C-type lectin 7.
+At position 1402 to 1514, the domain is characterized as C-type lectin 8.
+At position 1543 to 1662, the domain is characterized as C-type lectin 9.
+At position 39 to 120, the domain is characterized as KH type-2.
+At position 260 to 453, the domain is characterized as GATase cobBQ-type.
+At position 1 to 217, the domain is characterized as ThyX.
+At position 7 to 110, the domain is characterized as Glutaredoxin.
+At position 41 to 287, the domain is characterized as Protein kinase.
+At position 72 to 189, the domain is characterized as MSP.
+At position 216 to 366, the domain is characterized as TrmE-type G.
+At position 13 to 207, the domain is characterized as ABC transmembrane type-1.
+At position 390 to 451, the domain is characterized as TGS.
+At position 676 to 750, the domain is characterized as ACT.
+At position 54 to 116, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 96 to 176, the domain is characterized as PRC barrel.
+At position 104 to 299, the domain is characterized as Tyr recombinase.
+At position 5 to 92, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 74 to 494, the domain is characterized as USP.
+At position 134 to 347, the domain is characterized as ATP-grasp.
+At position 207 to 493, the domain is characterized as ABC transmembrane type-1 1.
+At position 581 to 808, the domain is characterized as ABC transporter 1.
+At position 897 to 1175, the domain is characterized as ABC transmembrane type-1 2.
+At position 1213 to 1464, the domain is characterized as ABC transporter 2.
+At position 250 to 444, the domain is characterized as GATase cobBQ-type.
+At position 43 to 101, the domain is characterized as Chromo.
+At position 179 to 240, the domain is characterized as Pre-SET.
+At position 243 to 366, the domain is characterized as SET.
+At position 396 to 412, the domain is characterized as Post-SET.
+At position 49 to 309, the domain is characterized as Protein kinase.
+At position 362 to 463, the domain is characterized as Ig-like C2-type 1.
+At position 468 to 561, the domain is characterized as Ig-like C2-type 2.
+At position 576 to 656, the domain is characterized as Ig-like C2-type 3.
+At position 661 to 745, the domain is characterized as Ig-like C2-type 4.
+At position 756 to 843, the domain is characterized as Ig-like C2-type 5.
+At position 848 to 939, the domain is characterized as Ig-like C2-type 6.
+At position 946 to 1048, the domain is characterized as Fibronectin type-III 1.
+At position 1053 to 1151, the domain is characterized as Fibronectin type-III 2.
+At position 1156 to 1254, the domain is characterized as Fibronectin type-III 3.
+At position 1259 to 1357, the domain is characterized as Fibronectin type-III 4.
+At position 241 to 440, the domain is characterized as Peptidase M12B.
+At position 446 to 533, the domain is characterized as Disintegrin.
+At position 677 to 713, the domain is characterized as EGF-like.
+At position 6 to 183, the domain is characterized as Guanylate kinase-like.
+At position 1 to 80, the domain is characterized as Cohesin 1.
+At position 94 to 240, the domain is characterized as Cohesin 2.
+At position 277 to 435, the domain is characterized as CBM3.
+At position 462 to 607, the domain is characterized as Cohesin 3.
+At position 704 to 771, the domain is characterized as Dockerin.
+At position 1 to 71, the domain is characterized as Ig-like.
+At position 846 to 1172, the domain is characterized as DOT1.
+At position 149 to 250, the domain is characterized as BACK.
+At position 1338 to 1478, the domain is characterized as VPS9.
+At position 237 to 338, the domain is characterized as Cadherin 1.
+At position 339 to 449, the domain is characterized as Cadherin 2.
+At position 444 to 554, the domain is characterized as Cadherin 3.
+At position 551 to 674, the domain is characterized as Cadherin 4.
+At position 204 to 399, the domain is characterized as Peptidase M12B.
+At position 625 to 657, the domain is characterized as EGF-like.
+At position 231 to 400, the domain is characterized as tr-type G.
+At position 188 to 440, the domain is characterized as Olfactomedin-like.
+At position 132 to 181, the domain is characterized as bHLH.
+At position 1 to 415, the domain is characterized as Helicase ATP-binding.
+At position 7 to 269, the domain is characterized as Deacetylase sirtuin-type.
+At position 1 to 178, the domain is characterized as Glutamine amidotransferase type-1.
+At position 179 to 377, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 140, the domain is characterized as N-acetyltransferase 1.
+At position 151 to 300, the domain is characterized as N-acetyltransferase 2.
+At position 291 to 537, the domain is characterized as Glutamine amidotransferase type-1.
+At position 367 to 457, the domain is characterized as SCD.
+At position 103 to 150, the domain is characterized as Fibronectin type-II.
+At position 160 to 198, the domain is characterized as EGF-like 1.
+At position 200 to 240, the domain is characterized as Fibronectin type-I.
+At position 241 to 279, the domain is characterized as EGF-like 2.
+At position 286 to 367, the domain is characterized as Kringle.
+At position 408 to 646, the domain is characterized as Peptidase S1.
+At position 8 to 158, the domain is characterized as Nudix hydrolase.
+At position 7 to 79, the domain is characterized as CARD.
+At position 34 to 158, the domain is characterized as RNase III.
+At position 185 to 254, the domain is characterized as DRBM.
+At position 131 to 329, the domain is characterized as Histone-fold.
+At position 5 to 217, the domain is characterized as Radical SAM core.
+At position 31 to 212, the domain is characterized as tr-type G.
+At position 191 to 416, the domain is characterized as Histidine kinase.
+At position 569 to 686, the domain is characterized as Response regulatory.
+At position 172 to 222, the domain is characterized as DHHC.
+At position 629 to 692, the domain is characterized as R3H.
+At position 765 to 808, the domain is characterized as G-patch.
+At position 1108 to 1177, the domain is characterized as S1 motif.
+At position 1226 to 1326, the domain is characterized as SH2.
+At position 373 to 476, the domain is characterized as Chromo 1.
+At position 501 to 583, the domain is characterized as Chromo 2.
+At position 628 to 812, the domain is characterized as Helicase ATP-binding.
+At position 944 to 1107, the domain is characterized as Helicase C-terminal.
+At position 214 to 249, the domain is characterized as UVR.
+At position 226 to 387, the domain is characterized as TrmE-type G.
+At position 228 to 335, the domain is characterized as HD.
+At position 32 to 67, the domain is characterized as EF-hand.
+At position 258 to 347, the domain is characterized as ABM.
+At position 292 to 355, the domain is characterized as bZIP.
+At position 41 to 98, the domain is characterized as Ubiquitin-like; degenerate.
+At position 162 to 459, the domain is characterized as PI3K/PI4K catalytic.
+At position 21 to 109, the domain is characterized as ATP-cone.
+At position 86 to 242, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 339 to 491, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 493 to 558, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 156 to 233, the domain is characterized as RRM 1.
+At position 267 to 343, the domain is characterized as RRM 2.
+At position 11 to 258, the domain is characterized as Lon N-terminal.
+At position 734 to 921, the domain is characterized as Lon proteolytic.
+At position 26 to 308, the domain is characterized as ABC transmembrane type-1.
+At position 340 to 576, the domain is characterized as ABC transporter.
+At position 9 to 355, the domain is characterized as Asparaginase/glutaminase.
+At position 45 to 173, the domain is characterized as MATH.
+At position 219 to 287, the domain is characterized as BTB.
+At position 3 to 199, the domain is characterized as ABC transporter.
+At position 35 to 303, the domain is characterized as Dynamin-type G.
+At position 579 to 703, the domain is characterized as PH.
+At position 737 to 830, the domain is characterized as GED.
+At position 10 to 175, the domain is characterized as Ku.
+At position 24 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 74, the domain is characterized as HMA.
+At position 1 to 256, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 159 to 187, the domain is characterized as WW 1.
+At position 283 to 313, the domain is characterized as WW 2.
+At position 249 to 496, the domain is characterized as ABC transporter 2.
+At position 181 to 259, the domain is characterized as RRM.
+At position 43 to 290, the domain is characterized as Peptidase S1.
+At position 46 to 270, the domain is characterized as Radical SAM core.
+At position 648 to 918, the domain is characterized as Protein kinase.
+At position 87 to 209, the domain is characterized as SCP.
+At position 322 to 601, the domain is characterized as ABC transporter 1.
+At position 621 to 951, the domain is characterized as ABC transporter 2.
+At position 1 to 115, the domain is characterized as Tyrosine-protein phosphatase.
+At position 113 to 310, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 4 to 259, the domain is characterized as Pyruvate carboxyltransferase.
+At position 84 to 220, the domain is characterized as Cupin type-1 1.
+At position 263 to 418, the domain is characterized as Cupin type-1 2.
+At position 6 to 148, the domain is characterized as Clp R.
+At position 146 to 233, the domain is characterized as Rhodanese.
+At position 6 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 71 to 149, the domain is characterized as PA.
+At position 285 to 425, the domain is characterized as SIS 1.
+At position 256 to 634, the domain is characterized as PDEase.
+At position 95 to 165, the domain is characterized as RRM 1.
+At position 188 to 260, the domain is characterized as RRM 2.
+At position 305 to 370, the domain is characterized as RRM 3.
+At position 525 to 713, the domain is characterized as STAS.
+At position 3 to 133, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 8 to 97, the domain is characterized as WWE 1.
+At position 598 to 686, the domain is characterized as BRCT.
+At position 15 to 224, the domain is characterized as YjeF N-terminal.
+At position 20 to 357, the domain is characterized as F5/8 type A 1.
+At position 20 to 200, the domain is characterized as Plastocyanin-like 1.
+At position 209 to 355, the domain is characterized as Plastocyanin-like 2.
+At position 370 to 712, the domain is characterized as F5/8 type A 2.
+At position 370 to 554, the domain is characterized as Plastocyanin-like 3.
+At position 564 to 710, the domain is characterized as Plastocyanin-like 4.
+At position 724 to 1044, the domain is characterized as F5/8 type A 3.
+At position 724 to 894, the domain is characterized as Plastocyanin-like 5.
+At position 902 to 1040, the domain is characterized as Plastocyanin-like 6.
+At position 320 to 405, the domain is characterized as SCD.
+At position 3 to 134, the domain is characterized as CENP-V/GFA.
+At position 140 to 173, the domain is characterized as WW 1.
+At position 181 to 214, the domain is characterized as WW 2.
+At position 389 to 443, the domain is characterized as FF 1.
+At position 456 to 510, the domain is characterized as FF 2.
+At position 523 to 583, the domain is characterized as FF 3.
+At position 603 to 663, the domain is characterized as FF 4.
+At position 668 to 723, the domain is characterized as FF 5.
+At position 738 to 795, the domain is characterized as FF 6.
+At position 7 to 105, the domain is characterized as Ig-like 1.
+At position 1759 to 1847, the domain is characterized as Ig-like 2.
+At position 1874 to 2106, the domain is characterized as Alpha-type protein kinase.
+At position 10 to 136, the domain is characterized as MH1.
+At position 232 to 425, the domain is characterized as MH2.
+At position 157 to 255, the domain is characterized as CRM 1.
+At position 277 to 373, the domain is characterized as CRM 2.
+At position 96 to 394, the domain is characterized as tr-type G.
+At position 297 to 546, the domain is characterized as Glutamine amidotransferase type-1.
+At position 36 to 183, the domain is characterized as N-acetyltransferase.
+At position 478 to 537, the domain is characterized as SH3.
+At position 38 to 152, the domain is characterized as Ig-like V-type.
+At position 259 to 351, the domain is characterized as Link 2.
+At position 20 to 98, the domain is characterized as BTB.
+At position 45 to 126, the domain is characterized as GOLD.
+At position 356 to 422, the domain is characterized as S4 RNA-binding.
+At position 676 to 815, the domain is characterized as C2.
+At position 229 to 422, the domain is characterized as Helicase C-terminal.
+At position 1373 to 1537, the domain is characterized as PNPLA.
+At position 34 to 143, the domain is characterized as sHSP.
+At position 1465 to 1758, the domain is characterized as Autotransporter.
+At position 188 to 370, the domain is characterized as FAD-binding PCMH-type.
+At position 106 to 268, the domain is characterized as NIDO.
+At position 384 to 424, the domain is characterized as EGF-like 1.
+At position 428 to 665, the domain is characterized as Nidogen G2 beta-barrel.
+At position 666 to 707, the domain is characterized as EGF-like 2.
+At position 708 to 749, the domain is characterized as EGF-like 3; calcium-binding.
+At position 756 to 799, the domain is characterized as EGF-like 4.
+At position 800 to 838, the domain is characterized as EGF-like 5; calcium-binding.
+At position 844 to 917, the domain is characterized as Thyroglobulin type-1.
+At position 1206 to 1242, the domain is characterized as EGF-like 6.
+At position 248 to 415, the domain is characterized as W2.
+At position 300 to 505, the domain is characterized as MCM.
+At position 169 to 197, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 198 to 228, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 255 to 301, the domain is characterized as G-patch.
+At position 131 to 406, the domain is characterized as SMP-LTD.
+At position 125 to 203, the domain is characterized as RRM 1.
+At position 211 to 291, the domain is characterized as RRM 2.
+At position 711 to 804, the domain is characterized as BRCT 1.
+At position 878 to 983, the domain is characterized as BRCT 2.
+At position 585 to 655, the domain is characterized as BRCT.
+At position 82 to 163, the domain is characterized as SH2.
+At position 208 to 256, the domain is characterized as SOCS box.
+At position 549 to 612, the domain is characterized as bZIP.
+At position 194 to 517, the domain is characterized as Asparagine synthetase.
+At position 113 to 164, the domain is characterized as bHLH.
+At position 580 to 853, the domain is characterized as Protein kinase.
+At position 15 to 250, the domain is characterized as HD Cas3-type.
+At position 286 to 471, the domain is characterized as Helicase ATP-binding.
+At position 77 to 185, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 1.
+At position 206 to 328, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 2.
+At position 136 to 263, the domain is characterized as Thioredoxin 1.
+At position 274 to 386, the domain is characterized as Thioredoxin 2.
+At position 387 to 508, the domain is characterized as Thioredoxin 3.
+At position 58 to 108, the domain is characterized as Fibrinogen C-terminal.
+At position 611 to 692, the domain is characterized as BRCT.
+At position 125 to 493, the domain is characterized as Protein kinase.
+At position 80 to 413, the domain is characterized as Asparaginase/glutaminase.
+At position 103 to 258, the domain is characterized as NIDO.
+At position 268 to 309, the domain is characterized as EGF-like 1.
+At position 311 to 347, the domain is characterized as EGF-like 2.
+At position 349 to 385, the domain is characterized as EGF-like 3.
+At position 387 to 423, the domain is characterized as EGF-like 4; calcium-binding.
+At position 429 to 465, the domain is characterized as EGF-like 5.
+At position 468 to 500, the domain is characterized as EGF-like 6.
+At position 541 to 577, the domain is characterized as EGF-like 7.
+At position 580 to 616, the domain is characterized as EGF-like 8.
+At position 619 to 655, the domain is characterized as EGF-like 9.
+At position 657 to 693, the domain is characterized as EGF-like 10.
+At position 696 to 753, the domain is characterized as Sushi.
+At position 753 to 789, the domain is characterized as EGF-like 11; calcium-binding.
+At position 791 to 827, the domain is characterized as EGF-like 12; calcium-binding.
+At position 829 to 865, the domain is characterized as EGF-like 13.
+At position 867 to 903, the domain is characterized as EGF-like 14.
+At position 908 to 1006, the domain is characterized as Fibronectin type-III 1.
+At position 1007 to 1105, the domain is characterized as Fibronectin type-III 2.
+At position 1106 to 1200, the domain is characterized as Fibronectin type-III 3.
+At position 1306 to 1342, the domain is characterized as EGF-like 15.
+At position 28 to 295, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 249 to 443, the domain is characterized as GATase cobBQ-type.
+At position 18 to 57, the domain is characterized as LRRNT 1.
+At position 212 to 263, the domain is characterized as LRRCT 1.
+At position 332 to 373, the domain is characterized as LRRNT 2.
+At position 529 to 580, the domain is characterized as LRRCT 2.
+At position 50 to 140, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 693 to 753, the domain is characterized as KH.
+At position 763 to 832, the domain is characterized as S1 motif.
+At position 221 to 464, the domain is characterized as Sigma-54 factor interaction.
+At position 8 to 125, the domain is characterized as PINc.
+At position 21 to 227, the domain is characterized as tr-type G.
+At position 591 to 650, the domain is characterized as KH.
+At position 662 to 734, the domain is characterized as S1 motif.
+At position 37 to 145, the domain is characterized as PH.
+At position 155 to 349, the domain is characterized as Rho-GAP.
+At position 43 to 119, the domain is characterized as Importin N-terminal.
+At position 42 to 160, the domain is characterized as Rhodanese.
+At position 196 to 337, the domain is characterized as Tyrosine-protein phosphatase.
+At position 5 to 190, the domain is characterized as PfpI endopeptidase 1.
+At position 198 to 383, the domain is characterized as PfpI endopeptidase 2.
+At position 110 to 305, the domain is characterized as ATP-grasp.
+At position 208 to 317, the domain is characterized as Guanylate cyclase.
+At position 76 to 123, the domain is characterized as SpoVT-AbrB 2.
+At position 395 to 490, the domain is characterized as SH2.
+At position 250 to 335, the domain is characterized as Ig-like C2-type 1.
+At position 349 to 441, the domain is characterized as Ig-like C2-type 2.
+At position 156 to 189, the domain is characterized as WW 1.
+At position 215 to 248, the domain is characterized as WW 2.
+At position 30 to 199, the domain is characterized as E1.
+At position 395 to 597, the domain is characterized as E2.
+At position 14 to 156, the domain is characterized as SprT-like.
+At position 353 to 588, the domain is characterized as NR LBD.
+At position 3 to 134, the domain is characterized as VWFA.
+At position 9 to 237, the domain is characterized as DHFR.
+At position 97 to 140, the domain is characterized as CUE.
+At position 180 to 338, the domain is characterized as PCI.
+At position 18 to 416, the domain is characterized as Glutamine amidotransferase type-2.
+At position 85 to 176, the domain is characterized as K-box.
+At position 43 to 247, the domain is characterized as Glutamine amidotransferase type-1.
+At position 248 to 457, the domain is characterized as GMPS ATP-PPase.
+At position 204 to 265, the domain is characterized as CBS 1.
+At position 287 to 345, the domain is characterized as CBS 2.
+At position 363 to 423, the domain is characterized as CBS 3.
+At position 435 to 494, the domain is characterized as CBS 4.
+At position 330 to 622, the domain is characterized as Protein kinase.
+At position 471 to 835, the domain is characterized as TTL.
+At position 347 to 454, the domain is characterized as SH2.
+At position 28 to 102, the domain is characterized as Ubiquitin-like.
+At position 173 to 201, the domain is characterized as STI1 1.
+At position 203 to 242, the domain is characterized as STI1 2.
+At position 381 to 428, the domain is characterized as STI1 3.
+At position 432 to 464, the domain is characterized as STI1 4.
+At position 539 to 579, the domain is characterized as UBA.
+At position 18 to 75, the domain is characterized as Sushi 1; atypical; lacks a Cys.
+At position 76 to 133, the domain is characterized as Sushi 2.
+At position 134 to 190, the domain is characterized as Sushi 3.
+At position 34 to 144, the domain is characterized as MTTase N-terminal.
+At position 162 to 399, the domain is characterized as Radical SAM core.
+At position 402 to 468, the domain is characterized as TRAM.
+At position 117 to 155, the domain is characterized as EGF-like 1.
+At position 157 to 200, the domain is characterized as EGF-like 2; calcium-binding.
+At position 201 to 242, the domain is characterized as EGF-like 3; calcium-binding.
+At position 243 to 283, the domain is characterized as EGF-like 4; calcium-binding.
+At position 299 to 475, the domain is characterized as Laminin G-like 1.
+At position 484 to 665, the domain is characterized as Laminin G-like 2.
+At position 60 to 134, the domain is characterized as Cytochrome b5 heme-binding.
+At position 195 to 825, the domain is characterized as USP.
+At position 51 to 315, the domain is characterized as Peptidase S1 1.
+At position 347 to 573, the domain is characterized as Peptidase S1 2.
+At position 608 to 826, the domain is characterized as Peptidase S1 3.
+At position 10 to 86, the domain is characterized as RRM.
+At position 42 to 100, the domain is characterized as Ig-like C2-type 1.
+At position 135 to 202, the domain is characterized as Ig-like C2-type 2.
+At position 238 to 301, the domain is characterized as Ig-like C2-type 3.
+At position 93 to 308, the domain is characterized as Radical SAM core.
+At position 158 to 278, the domain is characterized as OmpA-like.
+At position 104 to 359, the domain is characterized as Radical SAM core.
+At position 210 to 450, the domain is characterized as Peptidase S1.
+At position 93 to 171, the domain is characterized as Glutaredoxin.
+At position 223 to 407, the domain is characterized as PCI.
+At position 458 to 583, the domain is characterized as CBM-cenC.
+At position 33 to 275, the domain is characterized as GB1/RHD3-type G.
+At position 47 to 93, the domain is characterized as EGF-like; atypical.
+At position 13 to 78, the domain is characterized as Myb-like.
+At position 24 to 507, the domain is characterized as Sema.
+At position 509 to 559, the domain is characterized as PSI 1.
+At position 655 to 702, the domain is characterized as PSI 2.
+At position 803 to 856, the domain is characterized as PSI 3.
+At position 858 to 952, the domain is characterized as IPT/TIG 1.
+At position 954 to 1037, the domain is characterized as IPT/TIG 2.
+At position 1040 to 1139, the domain is characterized as IPT/TIG 3.
+At position 1142 to 1230, the domain is characterized as IPT/TIG 4.
+At position 192 to 379, the domain is characterized as Helicase ATP-binding.
+At position 408 to 560, the domain is characterized as Helicase C-terminal.
+At position 347 to 779, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1269 to 1579, the domain is characterized as PKS/mFAS DH.
+At position 1677 to 1753, the domain is characterized as Carrier.
+At position 17 to 208, the domain is characterized as KARI N-terminal Rossmann.
+At position 279 to 515, the domain is characterized as NR LBD.
+At position 84 to 395, the domain is characterized as IF rod.
+At position 161 to 372, the domain is characterized as ATP-grasp.
+At position 21 to 154, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 184 to 223, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 147 to 331, the domain is characterized as Reverse transcriptase.
+At position 752 to 910, the domain is characterized as Integrase catalytic.
+At position 2 to 215, the domain is characterized as ABC transporter.
+At position 285 to 434, the domain is characterized as YDG.
+At position 153 to 343, the domain is characterized as CheB-type methylesterase.
+At position 86 to 303, the domain is characterized as Radical SAM core.
+At position 135 to 372, the domain is characterized as Radical SAM core.
+At position 1 to 100, the domain is characterized as SSB.
+At position 56 to 102, the domain is characterized as TRM112.
+At position 360 to 745, the domain is characterized as Dilute.
+At position 207 to 400, the domain is characterized as GMPS ATP-PPase.
+At position 162 to 240, the domain is characterized as PPIase FKBP-type.
+At position 10 to 39, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 41 to 70, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 329 to 613, the domain is characterized as Reverse transcriptase.
+At position 117 to 171, the domain is characterized as FAF.
+At position 40 to 147, the domain is characterized as tRNA-binding.
+At position 402 to 479, the domain is characterized as B5.
+At position 707 to 799, the domain is characterized as FDX-ACB.
+At position 44 to 118, the domain is characterized as H15.
+At position 165 to 255, the domain is characterized as TonB C-terminal.
+At position 155 to 214, the domain is characterized as CHORD 2.
+At position 225 to 314, the domain is characterized as CS.
+At position 222 to 386, the domain is characterized as TrmE-type G.
+At position 67 to 121, the domain is characterized as HTH myb-type.
+At position 592 to 666, the domain is characterized as RRM.
+At position 712 to 1065, the domain is characterized as PUM-HD.
+At position 283 to 359, the domain is characterized as SPOR.
+At position 45 to 159, the domain is characterized as sHSP.
+At position 112 to 164, the domain is characterized as bHLH.
+At position 10 to 86, the domain is characterized as Ubiquitin-like.
+At position 113 to 304, the domain is characterized as Rab-GAP TBC.
+At position 479 to 538, the domain is characterized as SH3.
+At position 554 to 717, the domain is characterized as RUN.
+At position 34 to 263, the domain is characterized as GB1/RHD3-type G.
+At position 285 to 614, the domain is characterized as NR LBD.
+At position 260 to 462, the domain is characterized as SEC7.
+At position 512 to 625, the domain is characterized as PH.
+At position 110 to 317, the domain is characterized as ATP-grasp.
+At position 57 to 152, the domain is characterized as Fibronectin type-III.
+At position 150 to 242, the domain is characterized as Ig-like C2-type 1.
+At position 282 to 374, the domain is characterized as Ig-like C2-type 2.
+At position 383 to 517, the domain is characterized as Ig-like C2-type 3.
+At position 639 to 925, the domain is characterized as Protein kinase.
+At position 534 to 645, the domain is characterized as SMC hinge.
+At position 459 to 563, the domain is characterized as PH 1.
+At position 727 to 828, the domain is characterized as PH 2.
+At position 871 to 969, the domain is characterized as PH 3.
+At position 1641 to 1704, the domain is characterized as HP.
+At position 55 to 122, the domain is characterized as SAM.
+At position 663 to 868, the domain is characterized as Rho-GAP.
+At position 899 to 1107, the domain is characterized as START.
+At position 987 to 1061, the domain is characterized as U-box.
+At position 141 to 183, the domain is characterized as P-type.
+At position 188 to 466, the domain is characterized as ZP.
+At position 439 to 751, the domain is characterized as DOT1.
+At position 63 to 237, the domain is characterized as TLDc.
+At position 636 to 730, the domain is characterized as Big-1 1.
+At position 740 to 834, the domain is characterized as Big-1 2.
+At position 841 to 932, the domain is characterized as Big-1 3.
+At position 939 to 1036, the domain is characterized as Big-1 4.
+At position 1043 to 1135, the domain is characterized as Big-1 5.
+At position 1142 to 1239, the domain is characterized as Big-1 6.
+At position 1246 to 1338, the domain is characterized as Big-1 7.
+At position 1345 to 1442, the domain is characterized as Big-1 8.
+At position 1449 to 1542, the domain is characterized as Big-1 9.
+At position 1550 to 1652, the domain is characterized as Big-1 10.
+At position 1660 to 1753, the domain is characterized as Big-1 11.
+At position 1760 to 1856, the domain is characterized as Big-1 12.
+At position 1863 to 1960, the domain is characterized as Big-1 13.
+At position 1967 to 2051, the domain is characterized as Big-1 14.
+At position 2067 to 2160, the domain is characterized as Big-1 15.
+At position 2161 to 2254, the domain is characterized as Big-1 16.
+At position 2263 to 2355, the domain is characterized as Big-1 17.
+At position 7 to 690, the domain is characterized as Myosin motor.
+At position 694 to 714, the domain is characterized as IQ 1.
+At position 716 to 736, the domain is characterized as IQ 2.
+At position 806 to 1007, the domain is characterized as TH1.
+At position 21 to 199, the domain is characterized as Guanylate kinase-like.
+At position 1 to 233, the domain is characterized as SMP-LTD.
+At position 277 to 468, the domain is characterized as PNPLA.
+At position 1 to 62, the domain is characterized as HTH myb-type.
+At position 126 to 200, the domain is characterized as H15.
+At position 45 to 171, the domain is characterized as BAH.
+At position 61 to 300, the domain is characterized as Grh/CP2 DB.
+At position 378 to 413, the domain is characterized as EF-hand.
+At position 337 to 458, the domain is characterized as Thioredoxin.
+At position 34 to 115, the domain is characterized as Inhibitor I9.
+At position 163 to 226, the domain is characterized as bZIP.
+At position 55 to 90, the domain is characterized as EF-hand 1.
+At position 91 to 124, the domain is characterized as EF-hand 2.
+At position 122 to 157, the domain is characterized as EF-hand 3.
+At position 909 to 974, the domain is characterized as HP.
+At position 49 to 139, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 27 to 105, the domain is characterized as UPAR/Ly6.
+At position 74 to 615, the domain is characterized as PLA2c.
+At position 252 to 312, the domain is characterized as KH.
+At position 378 to 471, the domain is characterized as HD.
+At position 5 to 170, the domain is characterized as EngA-type G 1.
+At position 10 to 175, the domain is characterized as PPIase cyclophilin-type.
+At position 41 to 334, the domain is characterized as ABC transmembrane type-1 1.
+At position 374 to 618, the domain is characterized as ABC transporter 1.
+At position 691 to 976, the domain is characterized as ABC transmembrane type-1 2.
+At position 1017 to 1255, the domain is characterized as ABC transporter 2.
+At position 776 to 909, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1229 to 1368, the domain is characterized as DOD-type homing endonuclease 2.
+At position 38 to 111, the domain is characterized as U-box.
+At position 300 to 395, the domain is characterized as Rhodanese.
+At position 514 to 566, the domain is characterized as HTH psq-type.
+At position 344 to 477, the domain is characterized as DOD-type homing endonuclease.
+At position 344 to 545, the domain is characterized as Protein kinase.
+At position 31 to 245, the domain is characterized as BPL/LPL catalytic.
+At position 43 to 285, the domain is characterized as ABC transporter.
+At position 85 to 475, the domain is characterized as Protein kinase.
+At position 10 to 132, the domain is characterized as MsrB.
+At position 179 to 264, the domain is characterized as RRM.
+At position 19 to 65, the domain is characterized as F-box.
+At position 5 to 278, the domain is characterized as CN hydrolase.
+At position 1 to 54, the domain is characterized as Rubredoxin-like.
+At position 6 to 119, the domain is characterized as NTF2.
+At position 92 to 216, the domain is characterized as B12-binding.
+At position 109 to 235, the domain is characterized as MPN.
+At position 268 to 528, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 35 to 491, the domain is characterized as Hexokinase.
+At position 1318 to 1458, the domain is characterized as VPS9.
+At position 64 to 343, the domain is characterized as Protein kinase.
+At position 503 to 654, the domain is characterized as DOD-type homing endonuclease.
+At position 55 to 193, the domain is characterized as Nudix hydrolase.
+At position 185 to 308, the domain is characterized as DOD-type homing endonuclease.
+At position 32 to 148, the domain is characterized as MTTase N-terminal.
+At position 173 to 403, the domain is characterized as Radical SAM core.
+At position 128 to 254, the domain is characterized as DHHC.
+At position 259 to 342, the domain is characterized as Toprim.
+At position 178 to 250, the domain is characterized as S1 motif.
+At position 493 to 656, the domain is characterized as Helicase ATP-binding.
+At position 678 to 854, the domain is characterized as Helicase C-terminal.
+At position 197 to 393, the domain is characterized as Peptidase M12B.
+At position 150 to 222, the domain is characterized as Bromo 1.
+At position 337 to 409, the domain is characterized as Bromo 2.
+At position 506 to 590, the domain is characterized as NET.
+At position 18 to 91, the domain is characterized as S4 RNA-binding.
+At position 57 to 109, the domain is characterized as bHLH.
+At position 34 to 98, the domain is characterized as Sushi.
+At position 3 to 193, the domain is characterized as RNase H type-2.
+At position 53 to 87, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 170 to 312, the domain is characterized as VPS9.
+At position 408 to 451, the domain is characterized as CUE.
+At position 204 to 286, the domain is characterized as Ig-like C1-type.
+At position 45 to 185, the domain is characterized as C-type lectin.
+At position 14 to 121, the domain is characterized as Calponin-homology (CH).
+At position 481 to 808, the domain is characterized as Kinesin motor.
+At position 4 to 237, the domain is characterized as PABS.
+At position 441 to 532, the domain is characterized as RRM 1.
+At position 549 to 631, the domain is characterized as RRM 2.
+At position 46 to 222, the domain is characterized as Helicase ATP-binding.
+At position 404 to 556, the domain is characterized as Helicase C-terminal.
+At position 581 to 671, the domain is characterized as Dicer dsRNA-binding fold.
+At position 882 to 1006, the domain is characterized as PAZ.
+At position 1031 to 1200, the domain is characterized as RNase III 1.
+At position 1241 to 1389, the domain is characterized as RNase III 2.
+At position 1412 to 1481, the domain is characterized as DRBM 1.
+At position 1545 to 1629, the domain is characterized as DRBM 2.
+At position 158 to 217, the domain is characterized as SH3 2.
+At position 345 to 702, the domain is characterized as TTL.
+At position 30 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 133 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 39 to 246, the domain is characterized as RHD.
+At position 814 to 889, the domain is characterized as Death.
+At position 160 to 210, the domain is characterized as DHHC.
+At position 118 to 248, the domain is characterized as Galectin.
+At position 39 to 91, the domain is characterized as HTH cro/C1-type.
+At position 2 to 362, the domain is characterized as Glutamine amidotransferase type-2.
+At position 352 to 411, the domain is characterized as LIM zinc-binding 1.
+At position 412 to 471, the domain is characterized as LIM zinc-binding 2.
+At position 472 to 538, the domain is characterized as LIM zinc-binding 3.
+At position 381 to 467, the domain is characterized as PPIase FKBP-type.
+At position 112 to 163, the domain is characterized as bHLH.
+At position 127 to 196, the domain is characterized as BTB.
+At position 115 to 361, the domain is characterized as PPM-type phosphatase.
+At position 346 to 510, the domain is characterized as Integrase catalytic.
+At position 10 to 292, the domain is characterized as tr-type G.
+At position 15 to 82, the domain is characterized as R3H.
+At position 197 to 366, the domain is characterized as Helicase ATP-binding.
+At position 537 to 711, the domain is characterized as Helicase C-terminal.
+At position 27 to 119, the domain is characterized as UPAR/Ly6.
+At position 146 to 346, the domain is characterized as AH.
+At position 29 to 130, the domain is characterized as Ig-like V-type.
+At position 135 to 221, the domain is characterized as Ig-like C2-type 1.
+At position 226 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 129 to 207, the domain is characterized as RRM 1.
+At position 226 to 304, the domain is characterized as RRM 2.
+At position 462 to 549, the domain is characterized as RRM 3; atypical.
+At position 84 to 310, the domain is characterized as ABC transporter.
+At position 174 to 261, the domain is characterized as Olduvai 1.
+At position 326 to 399, the domain is characterized as Olduvai 2.
+At position 400 to 503, the domain is characterized as Olduvai 3.
+At position 40 to 108, the domain is characterized as BTB.
+At position 1 to 136, the domain is characterized as RNase H type-1.
+At position 187 to 245, the domain is characterized as CTLH.
+At position 98 to 177, the domain is characterized as RRM 1.
+At position 223 to 295, the domain is characterized as RRM 2.
+At position 458 to 559, the domain is characterized as RRM 3.
+At position 20 to 60, the domain is characterized as UBA 1.
+At position 120 to 164, the domain is characterized as UBA 2.
+At position 243 to 437, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 224 to 315, the domain is characterized as CobW C-terminal.
+At position 21 to 110, the domain is characterized as PAN.
+At position 63 to 156, the domain is characterized as Kringle 1.
+At position 160 to 238, the domain is characterized as Kringle 2.
+At position 252 to 345, the domain is characterized as Kringle 3.
+At position 353 to 464, the domain is characterized as Kringle 4.
+At position 488 to 713, the domain is characterized as Peptidase S1.
+At position 136 to 466, the domain is characterized as Protein kinase.
+At position 2 to 365, the domain is characterized as Trm1 methyltransferase.
+At position 92 to 249, the domain is characterized as Upf1 CH-rich.
+At position 82 to 159, the domain is characterized as PAS 1.
+At position 379 to 559, the domain is characterized as Plastocyanin-like 3.
+At position 569 to 717, the domain is characterized as Plastocyanin-like 4.
+At position 730 to 902, the domain is characterized as Plastocyanin-like 5.
+At position 910 to 1086, the domain is characterized as Plastocyanin-like 6.
+At position 128 to 156, the domain is characterized as KOW.
+At position 420 to 483, the domain is characterized as bZIP.
+At position 90 to 125, the domain is characterized as EF-hand 1.
+At position 42 to 104, the domain is characterized as Chitin-binding type-2.
+At position 121 to 157, the domain is characterized as LDL-receptor class A.
+At position 41 to 157, the domain is characterized as Plastocyanin-like 1.
+At position 167 to 320, the domain is characterized as Plastocyanin-like 2.
+At position 420 to 553, the domain is characterized as Plastocyanin-like 3.
+At position 193 to 294, the domain is characterized as PH.
+At position 285 to 405, the domain is characterized as C2.
+At position 459 to 651, the domain is characterized as Ras-GAP.
+At position 181 to 248, the domain is characterized as PAS 1.
+At position 321 to 387, the domain is characterized as PAS 2.
+At position 395 to 438, the domain is characterized as PAC.
+At position 23 to 297, the domain is characterized as CNH.
+At position 38 to 120, the domain is characterized as GOLD.
+At position 335 to 661, the domain is characterized as NACHT.
+At position 40 to 152, the domain is characterized as FAD-binding FR-type.
+At position 1 to 147, the domain is characterized as Clp R.
+At position 15 to 244, the domain is characterized as Radical SAM core.
+At position 449 to 559, the domain is characterized as STAS.
+At position 105 to 289, the domain is characterized as BPL/LPL catalytic.
+At position 816 to 897, the domain is characterized as ACT 2.
+At position 72 to 286, the domain is characterized as Radical SAM core.
+At position 335 to 460, the domain is characterized as DBINO.
+At position 579 to 751, the domain is characterized as Helicase ATP-binding.
+At position 1146 to 1302, the domain is characterized as Helicase C-terminal.
+At position 339 to 617, the domain is characterized as Protein kinase.
+At position 65 to 186, the domain is characterized as EamA.
+At position 80 to 141, the domain is characterized as SH3.
+At position 147 to 244, the domain is characterized as SH2.
+At position 266 to 519, the domain is characterized as Protein kinase.
+At position 280 to 345, the domain is characterized as Mop.
+At position 268 to 331, the domain is characterized as FHA.
+At position 86 to 132, the domain is characterized as F-box.
+At position 226 to 452, the domain is characterized as Lon N-terminal.
+At position 451 to 560, the domain is characterized as CULT.
+At position 273 to 400, the domain is characterized as Ricin B-type lectin 1.
+At position 403 to 527, the domain is characterized as Ricin B-type lectin 2.
+At position 1 to 131, the domain is characterized as PH.
+At position 312 to 456, the domain is characterized as PI-PLC X-box.
+At position 532 to 635, the domain is characterized as SH2 1.
+At position 646 to 735, the domain is characterized as SH2 2.
+At position 769 to 829, the domain is characterized as SH3.
+At position 930 to 1044, the domain is characterized as PI-PLC Y-box.
+At position 1038 to 1169, the domain is characterized as C2.
+At position 38 to 161, the domain is characterized as C2.
+At position 88 to 181, the domain is characterized as PH.
+At position 217 to 347, the domain is characterized as TFIIS central.
+At position 23 to 194, the domain is characterized as uDENN C9ORF72-type.
+At position 200 to 343, the domain is characterized as cDENN C9ORF72-type.
+At position 370 to 464, the domain is characterized as dDENN C9ORF72-type.
+At position 422 to 536, the domain is characterized as Toprim.
+At position 28 to 306, the domain is characterized as Deacetylase sirtuin-type.
+At position 208 to 399, the domain is characterized as ATP-grasp.
+At position 476 to 618, the domain is characterized as MGS-like.
+At position 58 to 321, the domain is characterized as Alpha-carbonic anhydrase.
+At position 349 to 448, the domain is characterized as Fibronectin type-III.
+At position 845 to 1116, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1147 to 1407, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 19 to 185, the domain is characterized as NAC.
+At position 3 to 54, the domain is characterized as F-box.
+At position 306 to 383, the domain is characterized as PUA.
+At position 128 to 216, the domain is characterized as Ig-like C1-type.
+At position 69 to 145, the domain is characterized as BTB.
+At position 184 to 284, the domain is characterized as BACK.
+At position 39 to 100, the domain is characterized as LIM zinc-binding 1.
+At position 101 to 160, the domain is characterized as LIM zinc-binding 2.
+At position 161 to 220, the domain is characterized as LIM zinc-binding 3.
+At position 223 to 283, the domain is characterized as LIM zinc-binding 4.
+At position 37 to 54, the domain is characterized as WH2.
+At position 54 to 340, the domain is characterized as Velvet.
+At position 96 to 175, the domain is characterized as PRC barrel.
+At position 365 to 497, the domain is characterized as NlpC/P60.
+At position 13 to 110, the domain is characterized as HTH hxlR-type.
+At position 9 to 136, the domain is characterized as VHS.
+At position 194 to 284, the domain is characterized as GAT.
+At position 76 to 188, the domain is characterized as sHSP.
+At position 60 to 176, the domain is characterized as OmpA-like.
+At position 679 to 934, the domain is characterized as Protein kinase.
+At position 935 to 992, the domain is characterized as AGC-kinase C-terminal.
+At position 223 to 286, the domain is characterized as bZIP.
+At position 185 to 355, the domain is characterized as Helicase ATP-binding.
+At position 365 to 525, the domain is characterized as Helicase C-terminal.
+At position 76 to 148, the domain is characterized as MBD.
+At position 118 to 420, the domain is characterized as Peptidase S8.
+At position 290 to 381, the domain is characterized as PDZ 1.
+At position 418 to 502, the domain is characterized as PDZ 2.
+At position 1 to 75, the domain is characterized as C2 tensin-type.
+At position 91 to 352, the domain is characterized as Protein kinase.
+At position 353 to 423, the domain is characterized as AGC-kinase C-terminal.
+At position 937 to 1073, the domain is characterized as MGS-like.
+At position 594 to 671, the domain is characterized as BRCT.
+At position 174 to 262, the domain is characterized as Ras-associating.
+At position 270 to 317, the domain is characterized as SARAH.
+At position 17 to 254, the domain is characterized as PABS.
+At position 16 to 217, the domain is characterized as RNase H type-2.
+At position 2 to 121, the domain is characterized as TRM112.
+At position 153 to 410, the domain is characterized as PPM-type phosphatase.
+At position 533 to 581, the domain is characterized as GYF.
+At position 1 to 192, the domain is characterized as PTS EIIB type-5.
+At position 21 to 118, the domain is characterized as XRN2-binding (XTBD).
+At position 507 to 653, the domain is characterized as Response regulatory.
+At position 236 to 518, the domain is characterized as ABC transmembrane type-1.
+At position 552 to 786, the domain is characterized as ABC transporter.
+At position 18 to 292, the domain is characterized as YjeF C-terminal.
+At position 12 to 76, the domain is characterized as CSD.
+At position 4 to 478, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 526 to 867, the domain is characterized as UvrD-like helicase C-terminal.
+At position 91 to 125, the domain is characterized as EF-hand 1; atypical.
+At position 134 to 167, the domain is characterized as EF-hand 2.
+At position 164 to 199, the domain is characterized as EF-hand 3.
+At position 200 to 228, the domain is characterized as EF-hand 4.
+At position 229 to 263, the domain is characterized as EF-hand 5.
+At position 4 to 95, the domain is characterized as ATP-cone.
+At position 584 to 707, the domain is characterized as Glycine radical.
+At position 377 to 534, the domain is characterized as SEFIR.
+At position 215 to 389, the domain is characterized as Helicase ATP-binding.
+At position 419 to 569, the domain is characterized as Helicase C-terminal.
+At position 89 to 400, the domain is characterized as IF rod.
+At position 250 to 312, the domain is characterized as Tudor 1.
+At position 340 to 395, the domain is characterized as Tudor 2.
+At position 620 to 691, the domain is characterized as MBD.
+At position 753 to 826, the domain is characterized as Pre-SET.
+At position 829 to 1244, the domain is characterized as SET.
+At position 1253 to 1269, the domain is characterized as Post-SET.
+At position 1 to 103, the domain is characterized as Peptidase M12A.
+At position 106 to 381, the domain is characterized as PPM-type phosphatase.
+At position 1649 to 1727, the domain is characterized as Carrier 1.
+At position 1766 to 1840, the domain is characterized as Carrier 2.
+At position 137 to 415, the domain is characterized as PPM-type phosphatase.
+At position 126 to 202, the domain is characterized as Ig-like C2-type 1.
+At position 203 to 316, the domain is characterized as Ig-like C2-type 2.
+At position 317 to 373, the domain is characterized as Ig-like C2-type 3.
+At position 14 to 359, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 368 to 692, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 503 to 522, the domain is characterized as UIM 1.
+At position 585 to 604, the domain is characterized as UIM 2.
+At position 610 to 626, the domain is characterized as UIM 3.
+At position 43 to 254, the domain is characterized as START.
+At position 74 to 249, the domain is characterized as PA14.
+At position 46 to 87, the domain is characterized as CHCH.
+At position 219 to 515, the domain is characterized as Protein kinase.
+At position 82 to 117, the domain is characterized as EF-hand 1.
+At position 136 to 153, the domain is characterized as EF-hand 2.
+At position 159 to 194, the domain is characterized as EF-hand 3.
+At position 196 to 227, the domain is characterized as EF-hand 4.
+At position 33 to 87, the domain is characterized as MIR 1.
+At position 95 to 150, the domain is characterized as MIR 2.
+At position 151 to 205, the domain is characterized as MIR 3.
+At position 140 to 242, the domain is characterized as BACK.
+At position 162 to 288, the domain is characterized as C2 1.
+At position 637 to 755, the domain is characterized as MHD1.
+At position 869 to 975, the domain is characterized as MHD2.
+At position 990 to 1114, the domain is characterized as C2 2.
+At position 4 to 128, the domain is characterized as RNase III.
+At position 162 to 332, the domain is characterized as Helicase ATP-binding.
+At position 443 to 597, the domain is characterized as Helicase C-terminal.
+At position 50 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 98 to 127, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 111 to 343, the domain is characterized as Sigma-54 factor interaction.
+At position 462 to 567, the domain is characterized as PRD 1.
+At position 572 to 708, the domain is characterized as PTS EIIA type-4.
+At position 835 to 932, the domain is characterized as PRD 2.
+At position 19 to 59, the domain is characterized as Chitin-binding type-1.
+At position 165 to 237, the domain is characterized as SPOR.
+At position 299 to 504, the domain is characterized as MCM.
+At position 32 to 96, the domain is characterized as KH 1.
+At position 143 to 208, the domain is characterized as KH 2.
+At position 236 to 301, the domain is characterized as KH 3.
+At position 64 to 255, the domain is characterized as Reticulon.
+At position 603 to 679, the domain is characterized as BRCT.
+At position 41 to 119, the domain is characterized as Inhibitor I9.
+At position 128 to 611, the domain is characterized as Peptidase S8.
+At position 376 to 461, the domain is characterized as PA.
+At position 81 to 178, the domain is characterized as Toprim.
+At position 341 to 431, the domain is characterized as IPT/TIG.
+At position 99 to 266, the domain is characterized as Helicase ATP-binding.
+At position 511 to 660, the domain is characterized as Helicase C-terminal.
+At position 4 to 122, the domain is characterized as ADF-H.
+At position 5 to 216, the domain is characterized as ABC transporter.
+At position 490 to 808, the domain is characterized as Protein kinase.
+At position 32 to 197, the domain is characterized as E1.
+At position 240 to 440, the domain is characterized as E2.
+At position 443 to 614, the domain is characterized as tr-type G.
+At position 20 to 59, the domain is characterized as Pentapeptide repeat 1.
+At position 60 to 99, the domain is characterized as Pentapeptide repeat 2.
+At position 100 to 139, the domain is characterized as Pentapeptide repeat 3.
+At position 151 to 190, the domain is characterized as Pentapeptide repeat 4.
+At position 191 to 230, the domain is characterized as Pentapeptide repeat 5.
+At position 231 to 270, the domain is characterized as Pentapeptide repeat 6.
+At position 271 to 310, the domain is characterized as Pentapeptide repeat 7.
+At position 152 to 279, the domain is characterized as Fatty acid hydroxylase.
+At position 751 to 846, the domain is characterized as TNT.
+At position 668 to 703, the domain is characterized as Anaphylatoxin-like.
+At position 1493 to 1638, the domain is characterized as NTR.
+At position 20 to 138, the domain is characterized as C2 1.
+At position 149 to 289, the domain is characterized as C2 2.
+At position 356 to 550, the domain is characterized as Ras-GAP.
+At position 604 to 706, the domain is characterized as PH.
+At position 5 to 197, the domain is characterized as DPCK.
+At position 384 to 581, the domain is characterized as Rho-GAP.
+At position 1 to 29, the domain is characterized as SUZ-C.
+At position 65 to 131, the domain is characterized as Sm.
+At position 112 to 216, the domain is characterized as SH2 2.
+At position 247 to 517, the domain is characterized as Tyrosine-protein phosphatase.
+At position 35 to 139, the domain is characterized as Cystatin kininogen-type 1.
+At position 156 to 260, the domain is characterized as Cystatin kininogen-type 2.
+At position 10 to 126, the domain is characterized as Calponin-homology (CH).
+At position 336 to 496, the domain is characterized as N-acetyltransferase.
+At position 166 to 234, the domain is characterized as Histone-fold.
+At position 79 to 283, the domain is characterized as tr-type G.
+At position 47 to 731, the domain is characterized as Myosin motor.
+At position 734 to 757, the domain is characterized as IQ 1.
+At position 758 to 786, the domain is characterized as IQ 2.
+At position 885 to 1059, the domain is characterized as TH1.
+At position 205 to 306, the domain is characterized as Fe2OG dioxygenase.
+At position 69 to 167, the domain is characterized as Plastocyanin-like.
+At position 3 to 58, the domain is characterized as HTH myb-type 1.
+At position 102 to 177, the domain is characterized as PDZ.
+At position 168 to 435, the domain is characterized as Pyruvate carboxyltransferase.
+At position 5 to 124, the domain is characterized as Response regulatory.
+At position 144 to 209, the domain is characterized as HTH luxR-type.
+At position 105 to 172, the domain is characterized as SUI1.
+At position 205 to 234, the domain is characterized as LysM 1.
+At position 254 to 303, the domain is characterized as LysM 2.
+At position 316 to 372, the domain is characterized as Chitin-binding type-1.
+At position 383 to 735, the domain is characterized as GH18.
+At position 138 to 167, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 6 to 89, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 1 to 59, the domain is characterized as B12-binding.
+At position 93 to 173, the domain is characterized as S4 RNA-binding.
+At position 125 to 222, the domain is characterized as Fibronectin type-III.
+At position 81 to 344, the domain is characterized as F-BAR.
+At position 554 to 757, the domain is characterized as Rho-GAP.
+At position 266 to 427, the domain is characterized as BTB 1.
+At position 485 to 552, the domain is characterized as BTB 2.
+At position 35 to 192, the domain is characterized as PPIase cyclophilin-type.
+At position 348 to 451, the domain is characterized as Cadherin 4.
+At position 452 to 561, the domain is characterized as Cadherin 5.
+At position 38 to 206, the domain is characterized as Nudix hydrolase.
+At position 107 to 290, the domain is characterized as Tyr recombinase.
+At position 384 to 508, the domain is characterized as CBM21.
+At position 242 to 468, the domain is characterized as START.
+At position 329 to 579, the domain is characterized as Clu.
+At position 35 to 198, the domain is characterized as PPIase cyclophilin-type.
+At position 463 to 644, the domain is characterized as DDHD.
+At position 518 to 618, the domain is characterized as tRNA-binding.
+At position 35 to 229, the domain is characterized as Cupin type-1 1.
+At position 282 to 431, the domain is characterized as Cupin type-1 2.
+At position 60 to 129, the domain is characterized as S1 motif.
+At position 137 to 195, the domain is characterized as KH.
+At position 134 to 635, the domain is characterized as Biotin carboxylation.
+At position 292 to 484, the domain is characterized as ATP-grasp.
+At position 763 to 837, the domain is characterized as Biotinyl-binding.
+At position 1532 to 1867, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1871 to 2187, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 8 to 135, the domain is characterized as Fatty acid hydroxylase.
+At position 77 to 238, the domain is characterized as CP-type G.
+At position 70 to 172, the domain is characterized as PA.
+At position 283 to 368, the domain is characterized as B5.
+At position 609 to 697, the domain is characterized as FDX-ACB.
+At position 74 to 183, the domain is characterized as TBDR plug.
+At position 189 to 729, the domain is characterized as TBDR beta-barrel.
+At position 3 to 183, the domain is characterized as Guanylate kinase-like.
+At position 134 to 328, the domain is characterized as ATP-grasp 1.
+At position 676 to 863, the domain is characterized as ATP-grasp 2.
+At position 930 to 1037, the domain is characterized as MGS-like.
+At position 57 to 160, the domain is characterized as THUMP.
+At position 133 to 186, the domain is characterized as HTH cro/C1-type.
+At position 3 to 66, the domain is characterized as HMA.
+At position 63 to 141, the domain is characterized as GIY-YIG.
+At position 254 to 289, the domain is characterized as UVR.
+At position 108 to 177, the domain is characterized as PDZ.
+At position 167 to 237, the domain is characterized as RRM.
+At position 52 to 219, the domain is characterized as Phosphatase tensin-type.
+At position 225 to 363, the domain is characterized as C2 tensin-type.
+At position 846 to 910, the domain is characterized as J.
+At position 505 to 607, the domain is characterized as CXC.
+At position 614 to 729, the domain is characterized as SET.
+At position 96 to 171, the domain is characterized as S4 RNA-binding.
+At position 119 to 501, the domain is characterized as Protein kinase.
+At position 625 to 1068, the domain is characterized as Biotin carboxylation.
+At position 744 to 941, the domain is characterized as ATP-grasp.
+At position 1752 to 1830, the domain is characterized as Biotinyl-binding.
+At position 583 to 686, the domain is characterized as tRNA-binding.
+At position 17 to 346, the domain is characterized as tr-type G.
+At position 7 to 72, the domain is characterized as Ubiquitin-like.
+At position 18 to 262, the domain is characterized as tr-type G.
+At position 364 to 630, the domain is characterized as ZP.
+At position 1169 to 1242, the domain is characterized as Carrier 2.
+At position 1237 to 1313, the domain is characterized as Carrier 3.
+At position 58 to 121, the domain is characterized as S5 DRBM.
+At position 40 to 393, the domain is characterized as Protein kinase.
+At position 316 to 410, the domain is characterized as Rieske.
+At position 150 to 325, the domain is characterized as Helicase ATP-binding.
+At position 353 to 500, the domain is characterized as Helicase C-terminal.
+At position 2 to 368, the domain is characterized as Trm1 methyltransferase.
+At position 135 to 419, the domain is characterized as ABC transmembrane type-1 1.
+At position 481 to 703, the domain is characterized as ABC transporter 1.
+At position 775 to 1060, the domain is characterized as ABC transmembrane type-1 2.
+At position 1103 to 1338, the domain is characterized as ABC transporter 2.
+At position 4 to 63, the domain is characterized as AFP-like.
+At position 31 to 97, the domain is characterized as Importin N-terminal.
+At position 24 to 286, the domain is characterized as Protein kinase.
+At position 43 to 105, the domain is characterized as S4 RNA-binding.
+At position 487 to 624, the domain is characterized as SEFIR.
+At position 106 to 192, the domain is characterized as Ig-like C2-type 1.
+At position 203 to 279, the domain is characterized as Ig-like C2-type 2.
+At position 416 to 692, the domain is characterized as Protein kinase.
+At position 2 to 77, the domain is characterized as PTS EIIB type-1.
+At position 1325 to 1593, the domain is characterized as Autotransporter.
+At position 158 to 209, the domain is characterized as F-box.
+At position 275 to 408, the domain is characterized as SHD.
+At position 412 to 715, the domain is characterized as MHD.
+At position 23 to 133, the domain is characterized as Ig-like V-type.
+At position 139 to 225, the domain is characterized as Ig-like C1-type.
+At position 318 to 417, the domain is characterized as HTH araC/xylS-type.
+At position 101 to 250, the domain is characterized as Rab-GAP TBC.
+At position 268 to 282, the domain is characterized as SAP 2.
+At position 59 to 259, the domain is characterized as MAGE.
+At position 9 to 65, the domain is characterized as DPH-type MB.
+At position 734 to 816, the domain is characterized as ACT 1.
+At position 63 to 243, the domain is characterized as Helicase ATP-binding.
+At position 276 to 430, the domain is characterized as Helicase C-terminal.
+At position 73 to 208, the domain is characterized as HD.
+At position 73 to 154, the domain is characterized as PDZ.
+At position 160 to 230, the domain is characterized as SH3.
+At position 283 to 452, the domain is characterized as Guanylate kinase-like.
+At position 19 to 79, the domain is characterized as HTH tetR-type.
+At position 144 to 319, the domain is characterized as Helicase ATP-binding.
+At position 347 to 494, the domain is characterized as Helicase C-terminal.
+At position 19 to 198, the domain is characterized as ABC transmembrane type-1.
+At position 51 to 134, the domain is characterized as MANSC.
+At position 244 to 294, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 312 to 348, the domain is characterized as LDL-receptor class A.
+At position 369 to 419, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 59 to 107, the domain is characterized as SMB.
+At position 15 to 105, the domain is characterized as Rhodanese.
+At position 56 to 132, the domain is characterized as Lipoyl-binding.
+At position 183 to 220, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 36 to 119, the domain is characterized as Inhibitor I9.
+At position 130 to 402, the domain is characterized as Peptidase S8.
+At position 21 to 135, the domain is characterized as I-type lysozyme.
+At position 9 to 206, the domain is characterized as Lon N-terminal.
+At position 617 to 796, the domain is characterized as Lon proteolytic.
+At position 38 to 116, the domain is characterized as NB-ARC.
+At position 687 to 1006, the domain is characterized as Protein kinase.
+At position 84 to 368, the domain is characterized as Protein kinase.
+At position 86 to 254, the domain is characterized as Helicase ATP-binding.
+At position 437 to 612, the domain is characterized as Helicase C-terminal.
+At position 1 to 232, the domain is characterized as Radical SAM core.
+At position 72 to 155, the domain is characterized as Biotinyl-binding.
+At position 448 to 539, the domain is characterized as Ricin B-type lectin.
+At position 91 to 420, the domain is characterized as Asparaginase/glutaminase.
+At position 84 to 427, the domain is characterized as TTL.
+At position 836 to 902, the domain is characterized as BTB.
+At position 110 to 310, the domain is characterized as ATP-grasp.
+At position 563 to 663, the domain is characterized as tRNA-binding.
+At position 142 to 177, the domain is characterized as EF-hand 4.
+At position 186 to 221, the domain is characterized as EF-hand 5.
+At position 7 to 123, the domain is characterized as RabBD.
+At position 406 to 527, the domain is characterized as C2 1.
+At position 563 to 694, the domain is characterized as C2 2.
+At position 89 to 169, the domain is characterized as S4 RNA-binding.
+At position 50 to 88, the domain is characterized as LRRNT.
+At position 313 to 365, the domain is characterized as LRRCT.
+At position 366 to 454, the domain is characterized as Ig-like C2-type.
+At position 34 to 148, the domain is characterized as PLAT.
+At position 89 to 382, the domain is characterized as Protein kinase.
+At position 383 to 455, the domain is characterized as AGC-kinase C-terminal.
+At position 312 to 357, the domain is characterized as PSI.
+At position 290 to 330, the domain is characterized as UBA.
+At position 453 to 501, the domain is characterized as KA1.
+At position 446 to 552, the domain is characterized as HTH APSES-type.
+At position 129 to 294, the domain is characterized as CRAL-TRIO.
+At position 185 to 255, the domain is characterized as EB1 C-terminal.
+At position 6 to 430, the domain is characterized as PTS EIIC type-1.
+At position 441 to 522, the domain is characterized as PTS EIIB type-1.
+At position 563 to 667, the domain is characterized as PTS EIIA type-1.
+At position 201 to 393, the domain is characterized as Rho-GAP.
+At position 36 to 174, the domain is characterized as PRELI/MSF1.
+At position 103 to 337, the domain is characterized as Radical SAM core.
+At position 9 to 131, the domain is characterized as MsrB.
+At position 303 to 333, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 352 to 381, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 39 to 394, the domain is characterized as G-alpha.
+At position 9 to 197, the domain is characterized as RNase H type-2.
+At position 51 to 113, the domain is characterized as Collagen-like.
+At position 113 to 246, the domain is characterized as C1q.
+At position 13 to 234, the domain is characterized as ABC transporter.
+At position 227 to 476, the domain is characterized as CN hydrolase.
+At position 1 to 227, the domain is characterized as ABC transporter.
+At position 1 to 121, the domain is characterized as C-type lectin.
+At position 501 to 658, the domain is characterized as SUN.
+At position 185 to 364, the domain is characterized as MARVEL.
+At position 437 to 548, the domain is characterized as OCEL.
+At position 4 to 51, the domain is characterized as RsgI N-terminal anti-sigma.
+At position 508 to 671, the domain is characterized as CBM3.
+At position 81 to 296, the domain is characterized as RNase H type-2.
+At position 276 to 353, the domain is characterized as PUA.
+At position 28 to 132, the domain is characterized as Cystatin kininogen-type 1.
+At position 151 to 254, the domain is characterized as Cystatin kininogen-type 2.
+At position 273 to 376, the domain is characterized as Cystatin kininogen-type 3.
+At position 644 to 729, the domain is characterized as PSP1 C-terminal.
+At position 9 to 43, the domain is characterized as SAP.
+At position 396 to 478, the domain is characterized as RRM.
+At position 1 to 109, the domain is characterized as MSP.
+At position 7 to 96, the domain is characterized as GST N-terminal.
+At position 102 to 228, the domain is characterized as GST C-terminal.
+At position 222 to 539, the domain is characterized as NACHT.
+At position 125 to 370, the domain is characterized as Radical SAM core.
+At position 193 to 517, the domain is characterized as Asparagine synthetase.
+At position 426 to 481, the domain is characterized as DEK-C.
+At position 23 to 293, the domain is characterized as Alpha-carbonic anhydrase.
+At position 189 to 501, the domain is characterized as PPM-type phosphatase.
+At position 300 to 508, the domain is characterized as AB hydrolase-1.
+At position 353 to 433, the domain is characterized as SAND.
+At position 202 to 501, the domain is characterized as GH10.
+At position 38 to 163, the domain is characterized as EamA 1.
+At position 187 to 314, the domain is characterized as EamA 2.
+At position 303 to 352, the domain is characterized as bHLH.
+At position 28 to 176, the domain is characterized as Tyrosine-protein phosphatase.
+At position 4 to 79, the domain is characterized as TFIIS N-terminal.
+At position 565 to 609, the domain is characterized as F-box.
+At position 22 to 149, the domain is characterized as Plastocyanin-like.
+At position 75 to 463, the domain is characterized as Protein kinase.
+At position 1 to 87, the domain is characterized as Glutaredoxin.
+At position 376 to 427, the domain is characterized as SANT.
+At position 76 to 338, the domain is characterized as Protein kinase.
+At position 341 to 409, the domain is characterized as AGC-kinase C-terminal.
+At position 479 to 556, the domain is characterized as REM-1.
+At position 949 to 1015, the domain is characterized as RhoBD.
+At position 1118 to 1317, the domain is characterized as PH.
+At position 218 to 387, the domain is characterized as tr-type G.
+At position 25 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 132 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 321, the domain is characterized as Ig-like C2-type 3.
+At position 384 to 539, the domain is characterized as TIR.
+At position 37 to 307, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 36, the domain is characterized as H15.
+At position 687 to 864, the domain is characterized as Helicase ATP-binding.
+At position 886 to 1035, the domain is characterized as Helicase C-terminal.
+At position 1272 to 1351, the domain is characterized as HRDC.
+At position 57 to 159, the domain is characterized as Calponin-homology (CH).
+At position 236 to 306, the domain is characterized as EB1 C-terminal.
+At position 9 to 204, the domain is characterized as HD Cas3-type.
+At position 24 to 137, the domain is characterized as Ig-like V-type.
+At position 144 to 233, the domain is characterized as Ig-like C2-type.
+At position 2 to 85, the domain is characterized as RRM 1.
+At position 94 to 173, the domain is characterized as RRM 2.
+At position 86 to 126, the domain is characterized as SMB 1.
+At position 127 to 170, the domain is characterized as SMB 2.
+At position 10 to 97, the domain is characterized as Lipoyl-binding.
+At position 22 to 202, the domain is characterized as ABC transmembrane type-1.
+At position 12 to 152, the domain is characterized as N-acetyltransferase 1.
+At position 160 to 307, the domain is characterized as N-acetyltransferase 2.
+At position 618 to 852, the domain is characterized as ABC transporter.
+At position 124 to 218, the domain is characterized as PA.
+At position 84 to 135, the domain is characterized as bHLH.
+At position 314 to 501, the domain is characterized as DH.
+At position 8 to 75, the domain is characterized as DRBM 1.
+At position 95 to 181, the domain is characterized as DRBM 2.
+At position 207 to 274, the domain is characterized as DRBM 3.
+At position 307 to 375, the domain is characterized as DRBM 4.
+At position 45 to 196, the domain is characterized as PID.
+At position 82 to 136, the domain is characterized as bHLH.
+At position 4 to 182, the domain is characterized as DPCK.
+At position 1 to 134, the domain is characterized as YEATS.
+At position 293 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 24 to 141, the domain is characterized as Thioredoxin 1.
+At position 354 to 482, the domain is characterized as Thioredoxin 2.
+At position 23 to 136, the domain is characterized as Ig-like V-type.
+At position 144 to 234, the domain is characterized as Ig-like C2-type.
+At position 33 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 415 to 560, the domain is characterized as MATH.
+At position 309 to 563, the domain is characterized as MHD.
+At position 15 to 213, the domain is characterized as AMMECR1.
+At position 50 to 140, the domain is characterized as Rhodanese.
+At position 12 to 175, the domain is characterized as Exonuclease.
+At position 48 to 135, the domain is characterized as Cystatin.
+At position 28 to 140, the domain is characterized as Thioredoxin.
+At position 20 to 272, the domain is characterized as Deacetylase sirtuin-type.
+At position 77 to 281, the domain is characterized as tr-type G.
+At position 22 to 236, the domain is characterized as tr-type G.
+At position 74 to 149, the domain is characterized as ACT.
+At position 19 to 165, the domain is characterized as CENP-V/GFA.
+At position 445 to 579, the domain is characterized as SIS 2.
+At position 121 to 414, the domain is characterized as Protein kinase.
+At position 26 to 131, the domain is characterized as Gnk2-homologous.
+At position 32 to 142, the domain is characterized as Plastocyanin-like 1.
+At position 173 to 350, the domain is characterized as Plastocyanin-like 2.
+At position 445 to 563, the domain is characterized as Plastocyanin-like 3.
+At position 603 to 704, the domain is characterized as tRNA-binding.
+At position 96 to 449, the domain is characterized as IF rod.
+At position 499 to 612, the domain is characterized as LTD.
+At position 8 to 168, the domain is characterized as PNPLA.
+At position 5 to 82, the domain is characterized as Core-binding (CB).
+At position 98 to 274, the domain is characterized as Tyr recombinase.
+At position 204 to 286, the domain is characterized as RCK C-terminal 1.
+At position 289 to 374, the domain is characterized as RCK C-terminal 2.
+At position 292 to 538, the domain is characterized as Glutamine amidotransferase type-1.
+At position 68 to 161, the domain is characterized as Rieske.
+At position 2 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 194 to 334, the domain is characterized as Helicase ATP-binding.
+At position 353 to 518, the domain is characterized as Helicase C-terminal.
+At position 108 to 385, the domain is characterized as Radical SAM core.
+At position 59 to 277, the domain is characterized as Ch-type lysozyme.
+At position 23 to 103, the domain is characterized as IGFBP N-terminal.
+At position 189 to 263, the domain is characterized as Thyroglobulin type-1.
+At position 674 to 779, the domain is characterized as PA.
+At position 112 to 186, the domain is characterized as COMM.
+At position 193 to 239, the domain is characterized as F-box.
+At position 32 to 89, the domain is characterized as HTH lysR-type.
+At position 410 to 544, the domain is characterized as YTH.
+At position 65 to 226, the domain is characterized as CP-type G.
+At position 10 to 250, the domain is characterized as ABC transporter 1.
+At position 313 to 541, the domain is characterized as ABC transporter 2.
+At position 108 to 300, the domain is characterized as ATP-grasp.
+At position 59 to 127, the domain is characterized as J.
+At position 160 to 231, the domain is characterized as POTRA.
+At position 500 to 711, the domain is characterized as Helicase ATP-binding.
+At position 979 to 1146, the domain is characterized as Helicase C-terminal.
+At position 3 to 60, the domain is characterized as TGS.
+At position 29 to 173, the domain is characterized as UBC core.
+At position 442 to 498, the domain is characterized as CBS 2.
+At position 167 to 370, the domain is characterized as TRUD.
+At position 16 to 161, the domain is characterized as MRH.
+At position 264 to 498, the domain is characterized as NR LBD.
+At position 237 to 415, the domain is characterized as FAD-binding PCMH-type.
+At position 27 to 363, the domain is characterized as Transferrin-like.
+At position 43 to 122, the domain is characterized as Carrier.
+At position 25 to 380, the domain is characterized as Kinesin motor.
+At position 22 to 114, the domain is characterized as Ig-like V-type.
+At position 145 to 254, the domain is characterized as Ig-like C1-type.
+At position 31 to 99, the domain is characterized as SAM.
+At position 43 to 85, the domain is characterized as CHCH.
+At position 1 to 27, the domain is characterized as Chitin-binding type-1.
+At position 219 to 404, the domain is characterized as Glutamine amidotransferase type-1.
+At position 551 to 743, the domain is characterized as ATP-grasp 1.
+At position 1093 to 1284, the domain is characterized as ATP-grasp 2.
+At position 1355 to 1500, the domain is characterized as MGS-like.
+At position 48 to 77, the domain is characterized as IQ 1.
+At position 71 to 100, the domain is characterized as IQ 2.
+At position 107 to 136, the domain is characterized as IQ 3.
+At position 8 to 92, the domain is characterized as RH1.
+At position 115 to 185, the domain is characterized as RH2.
+At position 25 to 311, the domain is characterized as RHD.
+At position 332 to 379, the domain is characterized as Myb-like.
+At position 599 to 701, the domain is characterized as CBM-cenC.
+At position 464 to 759, the domain is characterized as NACHT.
+At position 21 to 216, the domain is characterized as ABC transmembrane type-1.
+At position 57 to 229, the domain is characterized as FAD-binding PCMH-type.
+At position 25 to 108, the domain is characterized as Sm.
+At position 143 to 405, the domain is characterized as Protein kinase.
+At position 446 to 481, the domain is characterized as EF-hand 1.
+At position 482 to 517, the domain is characterized as EF-hand 2.
+At position 518 to 557, the domain is characterized as EF-hand 3.
+At position 558 to 587, the domain is characterized as EF-hand 4.
+At position 53 to 138, the domain is characterized as GOLD.
+At position 2 to 302, the domain is characterized as SAM-dependent MTase C5-type.
+At position 175 to 315, the domain is characterized as DOD-type homing endonuclease.
+At position 11 to 141, the domain is characterized as HTH marR-type.
+At position 4 to 274, the domain is characterized as Deacetylase sirtuin-type.
+At position 613 to 938, the domain is characterized as USP.
+At position 128 to 356, the domain is characterized as OTU.
+At position 203 to 518, the domain is characterized as Protein kinase.
+At position 383 to 449, the domain is characterized as TRAM.
+At position 1 to 53, the domain is characterized as TRAM.
+At position 39 to 155, the domain is characterized as sHSP.
+At position 163 to 228, the domain is characterized as TRAM.
+At position 12 to 205, the domain is characterized as Lon N-terminal.
+At position 594 to 775, the domain is characterized as Lon proteolytic.
+At position 111 to 431, the domain is characterized as Protein kinase.
+At position 21 to 246, the domain is characterized as Peptidase S1.
+At position 9 to 677, the domain is characterized as Myosin motor.
+At position 715 to 900, the domain is characterized as TH1.
+At position 1090 to 1147, the domain is characterized as SH3.
+At position 255 to 445, the domain is characterized as GATase cobBQ-type.
+At position 55 to 200, the domain is characterized as Fido.
+At position 15 to 236, the domain is characterized as tr-type G.
+At position 526 to 545, the domain is characterized as WH2.
+At position 259 to 407, the domain is characterized as Ferric oxidoreductase.
+At position 106 to 141, the domain is characterized as EF-hand 3.
+At position 1 to 262, the domain is characterized as CheR-type methyltransferase.
+At position 66 to 291, the domain is characterized as Radical SAM core.
+At position 25 to 134, the domain is characterized as EamA.
+At position 489 to 708, the domain is characterized as FtsK.
+At position 407 to 506, the domain is characterized as Zinc-hook.
+At position 17 to 146, the domain is characterized as VHS.
+At position 163 to 182, the domain is characterized as UIM.
+At position 326 to 495, the domain is characterized as tr-type G.
+At position 14 to 87, the domain is characterized as KRAB.
+At position 2 to 233, the domain is characterized as ABC transporter.
+At position 1 to 55, the domain is characterized as Response regulatory.
+At position 104 to 177, the domain is characterized as PRC barrel.
+At position 182 to 516, the domain is characterized as Protein kinase.
+At position 165 to 476, the domain is characterized as IF rod.
+At position 290 to 388, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 395, the domain is characterized as Protein kinase.
+At position 101 to 228, the domain is characterized as Nudix hydrolase.
+At position 24 to 227, the domain is characterized as AIG1-type G.
+At position 223 to 284, the domain is characterized as LIM zinc-binding 1.
+At position 288 to 348, the domain is characterized as LIM zinc-binding 2.
+At position 349 to 417, the domain is characterized as LIM zinc-binding 3.
+At position 74 to 344, the domain is characterized as Radical SAM core.
+At position 171 to 253, the domain is characterized as Doublecortin 1.
+At position 300 to 384, the domain is characterized as Doublecortin 2.
+At position 25 to 436, the domain is characterized as Kinesin motor.
+At position 1 to 345, the domain is characterized as TBDR beta-barrel.
+At position 1, the domain is characterized as TBDR plug.
+At position 23 to 291, the domain is characterized as PPM-type phosphatase.
+At position 381 to 431, the domain is characterized as DHHC.
+At position 1 to 100, the domain is characterized as Thioredoxin.
+At position 379 to 813, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1308 to 1625, the domain is characterized as PKS/mFAS DH.
+At position 1689 to 1763, the domain is characterized as Carrier.
+At position 154 to 256, the domain is characterized as Glutaredoxin 1.
+At position 284 to 386, the domain is characterized as Glutaredoxin 2.
+At position 391 to 488, the domain is characterized as Glutaredoxin 3.
+At position 47 to 340, the domain is characterized as ABC transmembrane type-1.
+At position 372 to 606, the domain is characterized as ABC transporter.
+At position 31 to 60, the domain is characterized as IQ.
+At position 517 to 593, the domain is characterized as Carrier 1.
+At position 1563 to 1643, the domain is characterized as Carrier 2.
+At position 2130 to 2202, the domain is characterized as Carrier 3.
+At position 155 to 245, the domain is characterized as PpiC.
+At position 345 to 378, the domain is characterized as WW 1.
+At position 377 to 410, the domain is characterized as WW 2.
+At position 452 to 485, the domain is characterized as WW 3.
+At position 492 to 525, the domain is characterized as WW 4.
+At position 584 to 918, the domain is characterized as HECT.
+At position 210 to 431, the domain is characterized as Helicase ATP-binding.
+At position 480 to 656, the domain is characterized as Helicase C-terminal.
+At position 6 to 312, the domain is characterized as SAM-dependent MTase C5-type.
+At position 451 to 614, the domain is characterized as Helicase ATP-binding.
+At position 629 to 812, the domain is characterized as Helicase C-terminal.
+At position 112 to 211, the domain is characterized as PPIase FKBP-type.
+At position 10 to 430, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 941 to 1251, the domain is characterized as PKS/mFAS DH.
+At position 2453 to 2530, the domain is characterized as Carrier.
+At position 15 to 264, the domain is characterized as ABC transporter.
+At position 96 to 154, the domain is characterized as CBS 1.
+At position 158 to 218, the domain is characterized as CBS 2.
+At position 1 to 448, the domain is characterized as Biotin carboxylation.
+At position 120 to 319, the domain is characterized as ATP-grasp.
+At position 578 to 653, the domain is characterized as Biotinyl-binding.
+At position 149 to 314, the domain is characterized as 3'-5' exonuclease.
+At position 246 to 441, the domain is characterized as GATase cobBQ-type.
+At position 43 to 76, the domain is characterized as EF-hand 2.
+At position 121 to 289, the domain is characterized as tr-type G.
+At position 4 to 33, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 56 to 303, the domain is characterized as Radical SAM core.
+At position 5 to 225, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 68, the domain is characterized as LIM zinc-binding 1.
+At position 104 to 164, the domain is characterized as LIM zinc-binding 2.
+At position 492 to 641, the domain is characterized as STAS.
+At position 2 to 109, the domain is characterized as MSP.
+At position 509 to 694, the domain is characterized as DUF724.
+At position 27 to 308, the domain is characterized as ABC transmembrane type-1.
+At position 12 to 89, the domain is characterized as Cytochrome b5 heme-binding.
+At position 670 to 883, the domain is characterized as Histidine kinase.
+At position 11 to 108, the domain is characterized as SSB.
+At position 429 to 462, the domain is characterized as WW 2.
+At position 528 to 561, the domain is characterized as WW 3.
+At position 659 to 712, the domain is characterized as FF 1.
+At position 725 to 779, the domain is characterized as FF 2.
+At position 791 to 846, the domain is characterized as FF 3.
+At position 896 to 952, the domain is characterized as FF 4.
+At position 954 to 1010, the domain is characterized as FF 5.
+At position 1012 to 1077, the domain is characterized as FF 6.
+At position 29 to 340, the domain is characterized as GH18.
+At position 123 to 366, the domain is characterized as TLC.
+At position 21 to 55, the domain is characterized as Pacifastin 1.
+At position 59 to 94, the domain is characterized as Pacifastin 2.
+At position 180 to 224, the domain is characterized as EGF-like.
+At position 222 to 478, the domain is characterized as ZP.
+At position 1440 to 1536, the domain is characterized as PH.
+At position 518 to 642, the domain is characterized as STAS.
+At position 23 to 103, the domain is characterized as Lipoyl-binding.
+At position 386 to 498, the domain is characterized as Cadherin 4.
+At position 686 to 876, the domain is characterized as ATP-grasp 2.
+At position 945 to 1082, the domain is characterized as MGS-like.
+At position 75 to 144, the domain is characterized as POTRA.
+At position 24 to 291, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 416 to 559, the domain is characterized as RCK N-terminal.
+At position 42 to 213, the domain is characterized as VWFA.
+At position 532 to 609, the domain is characterized as IPT/TIG 1.
+At position 612 to 686, the domain is characterized as IPT/TIG 2.
+At position 715 to 796, the domain is characterized as IPT/TIG 3.
+At position 410 to 504, the domain is characterized as SH2.
+At position 15 to 238, the domain is characterized as tr-type G.
+At position 259 to 317, the domain is characterized as HAMP 1.
+At position 357 to 409, the domain is characterized as HAMP 2.
+At position 449 to 501, the domain is characterized as HAMP 3.
+At position 541 to 593, the domain is characterized as HAMP 4.
+At position 633 to 685, the domain is characterized as HAMP 5.
+At position 725 to 777, the domain is characterized as HAMP 6.
+At position 819 to 871, the domain is characterized as HAMP 7.
+At position 911 to 963, the domain is characterized as HAMP 8.
+At position 1003 to 1055, the domain is characterized as HAMP 9.
+At position 1095 to 1147, the domain is characterized as HAMP 10.
+At position 1187 to 1239, the domain is characterized as HAMP 11.
+At position 1279 to 1331, the domain is characterized as HAMP 12.
+At position 1353 to 1575, the domain is characterized as Histidine kinase.
+At position 1590 to 1708, the domain is characterized as Response regulatory 1.
+At position 1730 to 1848, the domain is characterized as Response regulatory 2.
+At position 40 to 197, the domain is characterized as SIS.
+At position 3 to 229, the domain is characterized as ABC transporter.
+At position 120 to 322, the domain is characterized as ATP-grasp.
+At position 493 to 552, the domain is characterized as SH3.
+At position 308 to 397, the domain is characterized as VPS37 C-terminal.
+At position 149 to 472, the domain is characterized as NACHT.
+At position 1147 to 1222, the domain is characterized as DEP.
+At position 71 to 192, the domain is characterized as HD.
+At position 1 to 137, the domain is characterized as PX.
+At position 144 to 237, the domain is characterized as PpiC.
+At position 27 to 468, the domain is characterized as GBD/FH3.
+At position 632 to 1023, the domain is characterized as FH2.
+At position 1059 to 1090, the domain is characterized as DAD.
+At position 165 to 292, the domain is characterized as Fatty acid hydroxylase.
+At position 23 to 217, the domain is characterized as RNase H type-2.
+At position 314 to 356, the domain is characterized as UBA.
+At position 850 to 938, the domain is characterized as Toprim.
+At position 5 to 163, the domain is characterized as UBC core.
+At position 426 to 459, the domain is characterized as KASH.
+At position 66 to 179, the domain is characterized as SCP.
+At position 98 to 158, the domain is characterized as S4 RNA-binding.
+At position 114 to 476, the domain is characterized as GBD/FH3.
+At position 561 to 631, the domain is characterized as FH1.
+At position 636 to 1034, the domain is characterized as FH2.
+At position 1057 to 1087, the domain is characterized as DAD.
+At position 41 to 296, the domain is characterized as Protein kinase.
+At position 493 to 575, the domain is characterized as POLO box 1.
+At position 596 to 678, the domain is characterized as POLO box 2.
+At position 197 to 292, the domain is characterized as EthD.
+At position 27 to 77, the domain is characterized as Myosin N-terminal SH3-like.
+At position 81 to 776, the domain is characterized as Myosin motor.
+At position 779 to 808, the domain is characterized as IQ.
+At position 447 to 616, the domain is characterized as tr-type G.
+At position 21 to 167, the domain is characterized as Thioredoxin 1.
+At position 167 to 299, the domain is characterized as Thioredoxin 2.
+At position 503 to 634, the domain is characterized as Thioredoxin 3.
+At position 196 to 383, the domain is characterized as CheB-type methylesterase.
+At position 64 to 142, the domain is characterized as RRM.
+At position 89 to 237, the domain is characterized as Nudix hydrolase.
+At position 197 to 511, the domain is characterized as IF rod.
+At position 151 to 572, the domain is characterized as Myotubularin phosphatase.
+At position 142 to 226, the domain is characterized as RWP-RK.
+At position 11 to 301, the domain is characterized as FERM.
+At position 37 to 116, the domain is characterized as Inhibitor I9.
+At position 127 to 399, the domain is characterized as Peptidase S8.
+At position 44 to 99, the domain is characterized as bHLH.
+At position 131 to 166, the domain is characterized as Orange.
+At position 22 to 220, the domain is characterized as GH16.
+At position 59 to 301, the domain is characterized as Dynamin-type G.
+At position 137 to 340, the domain is characterized as ATP-grasp.
+At position 3 to 161, the domain is characterized as Thioredoxin.
+At position 92 to 154, the domain is characterized as PWWP.
+At position 30 to 309, the domain is characterized as CN hydrolase.
+At position 1 to 67, the domain is characterized as Histone-fold.
+At position 68 to 282, the domain is characterized as TLC.
+At position 302 to 394, the domain is characterized as PH.
+At position 425 to 550, the domain is characterized as Arf-GAP.
+At position 23 to 140, the domain is characterized as PX.
+At position 1604 to 1654, the domain is characterized as GRIP.
+At position 68 to 135, the domain is characterized as BTB.
+At position 170 to 272, the domain is characterized as BACK.
+At position 28 to 53, the domain is characterized as Antistasin-like 1.
+At position 83 to 108, the domain is characterized as Antistasin-like 2.
+At position 20 to 114, the domain is characterized as HTH arsR-type.
+At position 195 to 247, the domain is characterized as HAMP.
+At position 258 to 323, the domain is characterized as PAS.
+At position 327 to 369, the domain is characterized as PAC.
+At position 382 to 595, the domain is characterized as Histidine kinase.
+At position 22 to 300, the domain is characterized as ABC transmembrane type-1.
+At position 331 to 565, the domain is characterized as ABC transporter.
+At position 283 to 452, the domain is characterized as SUN.
+At position 552 to 628, the domain is characterized as Carrier.
+At position 557 to 619, the domain is characterized as KH.
+At position 629 to 699, the domain is characterized as S1 motif.
+At position 35 to 155, the domain is characterized as Thioredoxin 1.
+At position 156 to 281, the domain is characterized as Thioredoxin 2.
+At position 289 to 417, the domain is characterized as Thioredoxin 3.
+At position 10 to 174, the domain is characterized as PPIase cyclophilin-type.
+At position 6 to 50, the domain is characterized as LEM.
+At position 127 to 400, the domain is characterized as Peptidase S8.
+At position 32 to 158, the domain is characterized as PLAT.
+At position 161 to 870, the domain is characterized as Lipoxygenase.
+At position 37 to 219, the domain is characterized as EngB-type G.
+At position 401 to 1144, the domain is characterized as Myosin motor.
+At position 1146 to 1175, the domain is characterized as IQ.
+At position 24 to 70, the domain is characterized as F-box.
+At position 107 to 350, the domain is characterized as Era-type G.
+At position 376 to 457, the domain is characterized as KH type-2.
+At position 59 to 158, the domain is characterized as Cyclin N-terminal.
+At position 508 to 703, the domain is characterized as B30.2/SPRY.
+At position 21 to 161, the domain is characterized as C2.
+At position 362 to 397, the domain is characterized as PLD phosphodiesterase 1.
+At position 702 to 729, the domain is characterized as PLD phosphodiesterase 2.
+At position 12 to 75, the domain is characterized as SAM.
+At position 21 to 299, the domain is characterized as Protein kinase.
+At position 6 to 220, the domain is characterized as ThyX.
+At position 133 to 208, the domain is characterized as PDZ.
+At position 288 to 363, the domain is characterized as B5.
+At position 586 to 681, the domain is characterized as FDX-ACB.
+At position 155 to 329, the domain is characterized as CRAL-TRIO.
+At position 2 to 88, the domain is characterized as HPr.
+At position 4 to 77, the domain is characterized as Myb-like.
+At position 32 to 154, the domain is characterized as Ig-like C2-type.
+At position 248 to 474, the domain is characterized as Grh/CP2 DB.
+At position 185 to 237, the domain is characterized as HAMP.
+At position 245 to 455, the domain is characterized as Histidine kinase.
+At position 422 to 619, the domain is characterized as 3'-5' exonuclease.
+At position 6 to 35, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 124 to 155, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 157 to 186, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 96 to 260, the domain is characterized as TIR.
+At position 280 to 535, the domain is characterized as NB-ARC.
+At position 16 to 127, the domain is characterized as MTTase N-terminal.
+At position 151 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 454, the domain is characterized as TRAM.
+At position 519 to 791, the domain is characterized as Protein kinase.
+At position 497 to 674, the domain is characterized as PIK helical.
+At position 745 to 1027, the domain is characterized as PI3K/PI4K catalytic.
+At position 9 to 214, the domain is characterized as YjeF N-terminal.
+At position 231 to 387, the domain is characterized as JmjC.
+At position 211 to 411, the domain is characterized as PCI.
+At position 792 to 892, the domain is characterized as HECT.
+At position 20 to 116, the domain is characterized as Ig-like C2-type.
+At position 109 to 214, the domain is characterized as Fibronectin type-III 1.
+At position 215 to 313, the domain is characterized as Fibronectin type-III 2.
+At position 33 to 151, the domain is characterized as BTB.
+At position 210 to 279, the domain is characterized as BACK.
+At position 18 to 151, the domain is characterized as Jacalin-type lectin.
+At position 2 to 295, the domain is characterized as FERM.
+At position 75 to 226, the domain is characterized as N-acetyltransferase.
+At position 181 to 399, the domain is characterized as Helicase ATP-binding.
+At position 433 to 593, the domain is characterized as Helicase C-terminal.
+At position 32 to 226, the domain is characterized as Lon N-terminal.
+At position 612 to 791, the domain is characterized as Lon proteolytic.
+At position 22 to 154, the domain is characterized as VHS.
+At position 200 to 288, the domain is characterized as GAT.
+At position 120 to 317, the domain is characterized as ATP-grasp.
+At position 165 to 256, the domain is characterized as CS.
+At position 273 to 385, the domain is characterized as FAD-binding FR-type.
+At position 229 to 423, the domain is characterized as CheB-type methylesterase.
+At position 28 to 98, the domain is characterized as BTB.
+At position 217 to 502, the domain is characterized as NPH3.
+At position 92 to 581, the domain is characterized as Peptidase S8.
+At position 361 to 438, the domain is characterized as PA.
+At position 19 to 97, the domain is characterized as RRM.
+At position 1 to 314, the domain is characterized as Hcy-binding.
+At position 350 to 609, the domain is characterized as Pterin-binding.
+At position 642 to 735, the domain is characterized as B12-binding N-terminal.
+At position 740 to 877, the domain is characterized as B12-binding.
+At position 907 to 1206, the domain is characterized as AdoMet activation.
+At position 209 to 261, the domain is characterized as HAMP.
+At position 280 to 544, the domain is characterized as Methyl-accepting transducer.
+At position 26 to 93, the domain is characterized as J.
+At position 30 to 100, the domain is characterized as PAH 1.
+At position 145 to 230, the domain is characterized as PAH 2.
+At position 283 to 360, the domain is characterized as PAH 3.
+At position 4 to 79, the domain is characterized as Lipoyl-binding.
+At position 135 to 355, the domain is characterized as AB hydrolase-1.
+At position 164 to 251, the domain is characterized as 5'-3' exonuclease.
+At position 41 to 235, the domain is characterized as TLC.
+At position 70 to 133, the domain is characterized as bZIP.
+At position 14 to 96, the domain is characterized as PB1.
+At position 132 to 149, the domain is characterized as Pseudo-CRIB.
+At position 156 to 249, the domain is characterized as PDZ.
+At position 259 to 468, the domain is characterized as Peptidase M12B.
+At position 477 to 559, the domain is characterized as Disintegrin.
+At position 560 to 615, the domain is characterized as TSP type-1 1.
+At position 855 to 911, the domain is characterized as TSP type-1 2.
+At position 912 to 968, the domain is characterized as TSP type-1 3.
+At position 4 to 289, the domain is characterized as Protein kinase.
+At position 458 to 589, the domain is characterized as Ricin B-type lectin.
+At position 520 to 569, the domain is characterized as bHLH.
+At position 136 to 174, the domain is characterized as F-box.
+At position 11 to 149, the domain is characterized as PINc.
+At position 9 to 132, the domain is characterized as Arf-GAP.
+At position 132 to 233, the domain is characterized as PH 1.
+At position 255 to 361, the domain is characterized as PH 2.
+At position 837 to 885, the domain is characterized as GRIP.
+At position 133 to 223, the domain is characterized as TonB C-terminal.
+At position 26 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 114 to 196, the domain is characterized as Ig-like C2-type 2.
+At position 38 to 70, the domain is characterized as LisH.
+At position 129 to 183, the domain is characterized as HTH cro/C1-type.
+At position 122 to 451, the domain is characterized as SAC.
+At position 53 to 104, the domain is characterized as SANT.
+At position 53 to 136, the domain is characterized as PDZ 1.
+At position 150 to 238, the domain is characterized as PDZ 2.
+At position 252 to 336, the domain is characterized as PDZ 3.
+At position 472 to 561, the domain is characterized as PDZ 4.
+At position 573 to 658, the domain is characterized as PDZ 5.
+At position 673 to 755, the domain is characterized as PDZ 6.
+At position 1004 to 1086, the domain is characterized as PDZ 7.
+At position 31 to 65, the domain is characterized as SAP.
+At position 428 to 506, the domain is characterized as RRM.
+At position 2 to 144, the domain is characterized as Clp R.
+At position 425 to 460, the domain is characterized as UVR.
+At position 43 to 158, the domain is characterized as Response regulatory.
+At position 113 to 326, the domain is characterized as Adrift-type SAM-dependent 2'-O-MTase.
+At position 22 to 120, the domain is characterized as Ig-like V-type.
+At position 139 to 237, the domain is characterized as Ig-like C2-type 1.
+At position 241 to 325, the domain is characterized as Ig-like C2-type 2.
+At position 327 to 412, the domain is characterized as Ig-like C2-type 3.
+At position 413 to 508, the domain is characterized as Ig-like C2-type 4.
+At position 5 to 184, the domain is characterized as DHFR.
+At position 50 to 170, the domain is characterized as Calponin-homology (CH).
+At position 210 to 283, the domain is characterized as GAR.
+At position 281 to 395, the domain is characterized as DEUBAD.
+At position 29 to 130, the domain is characterized as Cadherin 1.
+At position 131 to 239, the domain is characterized as Cadherin 2.
+At position 240 to 343, the domain is characterized as Cadherin 3.
+At position 54 to 126, the domain is characterized as RRM.
+At position 421 to 495, the domain is characterized as PAP-associated.
+At position 7 to 91, the domain is characterized as MtN3/slv 1.
+At position 121 to 205, the domain is characterized as MtN3/slv 2.
+At position 29 to 145, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 187 to 334, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 11 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 210 to 402, the domain is characterized as GMPS ATP-PPase.
+At position 438 to 600, the domain is characterized as Helicase C-terminal.
+At position 648 to 683, the domain is characterized as UVR.
+At position 625 to 677, the domain is characterized as bHLH.
+At position 25 to 411, the domain is characterized as Helicase ATP-binding.
+At position 427 to 591, the domain is characterized as Helicase C-terminal.
+At position 616 to 651, the domain is characterized as UVR.
+At position 153 to 232, the domain is characterized as Doublecortin 2.
+At position 180 to 283, the domain is characterized as Fe2OG dioxygenase.
+At position 52 to 157, the domain is characterized as THUMP.
+At position 14 to 106, the domain is characterized as SH2 1.
+At position 167 to 258, the domain is characterized as SH2 2.
+At position 365 to 625, the domain is characterized as Protein kinase.
+At position 4 to 281, the domain is characterized as Pyruvate carboxyltransferase.
+At position 25 to 191, the domain is characterized as FAD-binding PCMH-type.
+At position 252 to 491, the domain is characterized as ABC transporter 2.
+At position 191 to 327, the domain is characterized as RanBD1.
+At position 69 to 99, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 932 to 964, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 965 to 995, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 73 to 260, the domain is characterized as RNase H type-2.
+At position 614 to 697, the domain is characterized as PB1.
+At position 438 to 833, the domain is characterized as FH2.
+At position 1 to 257, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 264 to 504, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 33 to 108, the domain is characterized as GIY-YIG.
+At position 1730 to 2034, the domain is characterized as Protein kinase.
+At position 2130 to 2271, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 198, the domain is characterized as N-acetyltransferase.
+At position 378 to 440, the domain is characterized as TRAM.
+At position 168 to 360, the domain is characterized as CheB-type methylesterase.
+At position 662 to 822, the domain is characterized as UBC core.
+At position 7 to 166, the domain is characterized as PPIase cyclophilin-type.
+At position 21 to 147, the domain is characterized as Thioredoxin 1.
+At position 355 to 486, the domain is characterized as Thioredoxin 2.
+At position 85 to 397, the domain is characterized as IF rod.
+At position 423 to 557, the domain is characterized as YTH.
+At position 36 to 240, the domain is characterized as Cupin type-1 1.
+At position 309 to 458, the domain is characterized as Cupin type-1 2.
+At position 272 to 539, the domain is characterized as ABC transmembrane type-1 1.
+At position 591 to 823, the domain is characterized as ABC transporter 1.
+At position 902 to 1187, the domain is characterized as ABC transmembrane type-1 2.
+At position 1214 to 1485, the domain is characterized as ABC transporter 2.
+At position 133 to 192, the domain is characterized as DDT.
+At position 7 to 196, the domain is characterized as UmuC.
+At position 3 to 222, the domain is characterized as Glutamine amidotransferase type-1.
+At position 572 to 597, the domain is characterized as EF-hand 1.
+At position 652 to 672, the domain is characterized as EF-hand 3.
+At position 7 to 253, the domain is characterized as ABC transporter.
+At position 146 to 452, the domain is characterized as Peptidase S8.
+At position 11 to 146, the domain is characterized as MPN.
+At position 33 to 106, the domain is characterized as CSD.
+At position 32 to 280, the domain is characterized as Era-type G.
+At position 91 to 365, the domain is characterized as PPM-type phosphatase.
+At position 22 to 222, the domain is characterized as ABC transmembrane type-1.
+At position 107 to 138, the domain is characterized as EamA.
+At position 25 to 273, the domain is characterized as ABC transporter.
+At position 125 to 228, the domain is characterized as Fibronectin type-III.
+At position 161 to 298, the domain is characterized as PPIase FKBP-type.
+At position 381 to 710, the domain is characterized as PDEase.
+At position 600 to 774, the domain is characterized as PCI.
+At position 2 to 52, the domain is characterized as Rubredoxin-like.
+At position 306 to 554, the domain is characterized as Glutamine amidotransferase type-1.
+At position 314 to 357, the domain is characterized as LysM.
+At position 21 to 104, the domain is characterized as Doublecortin 1.
+At position 194 to 277, the domain is characterized as Doublecortin 2.
+At position 17 to 238, the domain is characterized as Peptidase S1.
+At position 11 to 230, the domain is characterized as ABC transporter.
+At position 30 to 134, the domain is characterized as Cadherin 1.
+At position 135 to 243, the domain is characterized as Cadherin 2.
+At position 244 to 348, the domain is characterized as Cadherin 3.
+At position 349 to 453, the domain is characterized as Cadherin 4.
+At position 454 to 563, the domain is characterized as Cadherin 5.
+At position 78 to 190, the domain is characterized as SET.
+At position 38 to 89, the domain is characterized as FHA.
+At position 13 to 266, the domain is characterized as ABC transporter.
+At position 168 to 258, the domain is characterized as Cytochrome c 1.
+At position 265 to 346, the domain is characterized as Cytochrome c 2.
+At position 51 to 83, the domain is characterized as LisH.
+At position 25 to 329, the domain is characterized as Transferrin-like 1.
+At position 340 to 670, the domain is characterized as Transferrin-like 2.
+At position 1 to 96, the domain is characterized as Ig-like 1.
+At position 125 to 218, the domain is characterized as Ig-like 2.
+At position 240 to 339, the domain is characterized as Ig-like 3.
+At position 348 to 444, the domain is characterized as Ig-like 4.
+At position 1 to 86, the domain is characterized as HPr.
+At position 547 to 639, the domain is characterized as PB1.
+At position 6 to 390, the domain is characterized as Kinesin motor.
+At position 240 to 362, the domain is characterized as SET.
+At position 80 to 394, the domain is characterized as Peptidase A1.
+At position 1 to 65, the domain is characterized as LCN-type CS-alpha/beta.
+At position 710 to 786, the domain is characterized as Smr.
+At position 132 to 469, the domain is characterized as Peptidase A1.
+At position 21 to 241, the domain is characterized as Peptidase S1.
+At position 66 to 344, the domain is characterized as tr-type G.
+At position 58 to 321, the domain is characterized as AB hydrolase-1.
+At position 228 to 297, the domain is characterized as Plastocyanin-like.
+At position 59 to 143, the domain is characterized as GST N-terminal.
+At position 152 to 301, the domain is characterized as GST C-terminal.
+At position 226 to 323, the domain is characterized as HTH araC/xylS-type.
+At position 60 to 101, the domain is characterized as JmjN.
+At position 125 to 217, the domain is characterized as ARID.
+At position 422 to 588, the domain is characterized as JmjC.
+At position 167 to 507, the domain is characterized as SAC.
+At position 306 to 581, the domain is characterized as NR LBD.
+At position 34 to 154, the domain is characterized as MTTase N-terminal.
+At position 181 to 414, the domain is characterized as Radical SAM core.
+At position 417 to 479, the domain is characterized as TRAM.
+At position 227 to 458, the domain is characterized as Peptidase S1.
+At position 133 to 200, the domain is characterized as COMM.
+At position 13 to 55, the domain is characterized as CHCH.
+At position 259 to 355, the domain is characterized as RAMA.
+At position 13 to 77, the domain is characterized as J.
+At position 593 to 622, the domain is characterized as IQ.
+At position 856 to 1293, the domain is characterized as CBP/p300-type HAT.
+At position 222 to 402, the domain is characterized as Helicase ATP-binding.
+At position 434 to 601, the domain is characterized as Helicase C-terminal.
+At position 45 to 231, the domain is characterized as DCUN1.
+At position 155 to 234, the domain is characterized as Ig-like C2-type.
+At position 5 to 140, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 260 to 295, the domain is characterized as DMA.
+At position 7 to 120, the domain is characterized as VOC 1.
+At position 144 to 264, the domain is characterized as VOC 2.
+At position 163 to 259, the domain is characterized as PB1.
+At position 39 to 156, the domain is characterized as tRNA-binding.
+At position 409 to 488, the domain is characterized as B5.
+At position 139 to 255, the domain is characterized as Gnk2-homologous 2.
+At position 359 to 631, the domain is characterized as Protein kinase.
+At position 101 to 179, the domain is characterized as RRM.
+At position 82 to 270, the domain is characterized as tr-type G.
+At position 354 to 414, the domain is characterized as TRAM.
+At position 45 to 286, the domain is characterized as ABC transporter.
+At position 19 to 216, the domain is characterized as Cytochrome b561.
+At position 23 to 54, the domain is characterized as LRRNT.
+At position 200 to 252, the domain is characterized as LRRCT.
+At position 253 to 339, the domain is characterized as Ig-like.
+At position 361 to 447, the domain is characterized as Fibronectin type-III.
+At position 8 to 228, the domain is characterized as ABC transporter.
+At position 89 to 153, the domain is characterized as BTB.
+At position 139 to 178, the domain is characterized as STI1 1.
+At position 273 to 478, the domain is characterized as GATase cobBQ-type.
+At position 5 to 56, the domain is characterized as LIM zinc-binding.
+At position 35 to 162, the domain is characterized as Response regulatory.
+At position 1533 to 1721, the domain is characterized as PIK helical.
+At position 1811 to 2089, the domain is characterized as PI3K/PI4K catalytic.
+At position 47 to 368, the domain is characterized as AB hydrolase-1.
+At position 25 to 229, the domain is characterized as AIG1-type G.
+At position 1 to 12, the domain is characterized as Peptidase M12B.
+At position 13 to 18, the domain is characterized as Disintegrin.
+At position 146 to 272, the domain is characterized as Fatty acid hydroxylase.
+At position 38 to 146, the domain is characterized as Inhibitor I9.
+At position 148 to 694, the domain is characterized as Peptidase S8.
+At position 418 to 513, the domain is characterized as PA.
+At position 13 to 271, the domain is characterized as Protein kinase.
+At position 16 to 98, the domain is characterized as Doublecortin 1.
+At position 136 to 217, the domain is characterized as Doublecortin 2.
+At position 271 to 314, the domain is characterized as CUE.
+At position 64 to 117, the domain is characterized as TSP type-1 1.
+At position 120 to 157, the domain is characterized as LDL-receptor class A.
+At position 158 to 504, the domain is characterized as MACPF.
+At position 505 to 535, the domain is characterized as EGF-like.
+At position 545 to 591, the domain is characterized as TSP type-1 2.
+At position 137 to 194, the domain is characterized as COS.
+At position 196 to 300, the domain is characterized as Fibronectin type-III.
+At position 300 to 506, the domain is characterized as B30.2/SPRY.
+At position 141 to 211, the domain is characterized as KH.
+At position 320 to 489, the domain is characterized as tr-type G.
+At position 213 to 273, the domain is characterized as SH3.
+At position 60 to 129, the domain is characterized as POTRA.
+At position 24 to 304, the domain is characterized as Dynamin-type G.
+At position 620 to 711, the domain is characterized as GED.
+At position 25 to 219, the domain is characterized as Lon N-terminal.
+At position 603 to 781, the domain is characterized as Lon proteolytic.
+At position 23 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 231, the domain is characterized as Ig-like C2-type 2.
+At position 240 to 348, the domain is characterized as Ig-like C2-type 3.
+At position 176 to 274, the domain is characterized as HTH araC/xylS-type.
+At position 309 to 398, the domain is characterized as BRCT.
+At position 27 to 127, the domain is characterized as Fibronectin type-III 1.
+At position 129 to 229, the domain is characterized as Fibronectin type-III 2.
+At position 65 to 84, the domain is characterized as UIM 1.
+At position 94 to 113, the domain is characterized as UIM 2.
+At position 131 to 191, the domain is characterized as LIM zinc-binding.
+At position 30 to 112, the domain is characterized as WWE.
+At position 385 to 448, the domain is characterized as SAM.
+At position 495 to 700, the domain is characterized as DDHD.
+At position 69 to 185, the domain is characterized as FZ.
+At position 17 to 94, the domain is characterized as RRM.
+At position 618 to 696, the domain is characterized as BRCT.
+At position 156 to 269, the domain is characterized as Fe2OG dioxygenase.
+At position 229 to 288, the domain is characterized as Plastocyanin-like.
+At position 8 to 371, the domain is characterized as Kinesin motor.
+At position 1145 to 1208, the domain is characterized as SAM.
+At position 40 to 156, the domain is characterized as tRNA-binding.
+At position 411 to 486, the domain is characterized as B5.
+At position 159 to 613, the domain is characterized as TBDR beta-barrel.
+At position 24 to 88, the domain is characterized as Sushi 1.
+At position 89 to 148, the domain is characterized as Sushi 2.
+At position 151 to 210, the domain is characterized as Sushi 3.
+At position 211 to 269, the domain is characterized as Sushi 4.
+At position 272 to 329, the domain is characterized as Sushi 5.
+At position 334 to 391, the domain is characterized as Sushi 6.
+At position 394 to 452, the domain is characterized as Sushi 7.
+At position 453 to 516, the domain is characterized as Sushi 8.
+At position 522 to 580, the domain is characterized as Sushi 9.
+At position 581 to 647, the domain is characterized as Sushi 10.
+At position 1121 to 1176, the domain is characterized as TSP type-1 5.
+At position 1182 to 1219, the domain is characterized as PLAC.
+At position 188 to 347, the domain is characterized as JmjC.
+At position 77 to 296, the domain is characterized as Glutamine amidotransferase type-2.
+At position 30 to 47, the domain is characterized as WH2 1.
+At position 87 to 106, the domain is characterized as WH2 2.
+At position 353 to 468, the domain is characterized as C2.
+At position 491 to 594, the domain is characterized as PH.
+At position 886 to 1057, the domain is characterized as MHD1.
+At position 18 to 159, the domain is characterized as Reelin.
+At position 157 to 213, the domain is characterized as CBS 2.
+At position 1027 to 1111, the domain is characterized as PB1.
+At position 38 to 248, the domain is characterized as TLC.
+At position 122 to 299, the domain is characterized as Prephenate dehydratase.
+At position 313 to 404, the domain is characterized as ACT.
+At position 326 to 749, the domain is characterized as FH2.
+At position 93 to 182, the domain is characterized as PAS.
+At position 216 to 433, the domain is characterized as Histidine kinase.
+At position 62 to 97, the domain is characterized as EF-hand 2.
+At position 135 to 170, the domain is characterized as EF-hand 4.
+At position 21 to 217, the domain is characterized as Peptidase M12B.
+At position 139 to 214, the domain is characterized as TFIIS N-terminal.
+At position 222 to 285, the domain is characterized as bZIP.
+At position 3 to 205, the domain is characterized as ABC transporter.
+At position 44 to 140, the domain is characterized as Ig-like V-type 1.
+At position 162 to 260, the domain is characterized as Ig-like V-type 2.
+At position 280 to 380, the domain is characterized as Ig-like V-type 3.
+At position 387 to 471, the domain is characterized as Ig-like C2-type.
+At position 72 to 356, the domain is characterized as Protein kinase.
+At position 138 to 218, the domain is characterized as RRM 2.
+At position 108 to 345, the domain is characterized as Radical SAM core.
+At position 33 to 95, the domain is characterized as t-SNARE coiled-coil homology.
+At position 25 to 96, the domain is characterized as KRAB.
+At position 716 to 819, the domain is characterized as PH.
+At position 50 to 150, the domain is characterized as Glutaredoxin.
+At position 11 to 214, the domain is characterized as AIG1-type G.
+At position 38 to 168, the domain is characterized as Nudix hydrolase.
+At position 224 to 277, the domain is characterized as CVC.
+At position 358 to 635, the domain is characterized as Reverse transcriptase.
+At position 51 to 435, the domain is characterized as Peptidase A1.
+At position 1 to 50, the domain is characterized as WAP.
+At position 189 to 335, the domain is characterized as Fatty acid hydroxylase.
+At position 26 to 123, the domain is characterized as AB hydrolase-1.
+At position 3 to 33, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 584 to 705, the domain is characterized as PH.
+At position 36 to 118, the domain is characterized as Lipoyl-binding.
+At position 116 to 148, the domain is characterized as EF-hand 3.
+At position 42 to 109, the domain is characterized as GRAM.
+At position 181 to 647, the domain is characterized as Myotubularin phosphatase.
+At position 37 to 286, the domain is characterized as ABC transporter.
+At position 390 to 652, the domain is characterized as ABC transmembrane type-2.
+At position 19 to 94, the domain is characterized as ACT.
+At position 54 to 214, the domain is characterized as UBC core.
+At position 25 to 88, the domain is characterized as S5 DRBM.
+At position 7 to 64, the domain is characterized as TIL.
+At position 211 to 274, the domain is characterized as bZIP.
+At position 261 to 455, the domain is characterized as GATase cobBQ-type.
+At position 15 to 66, the domain is characterized as Rubredoxin-like.
+At position 13 to 71, the domain is characterized as TRAM.
+At position 176 to 228, the domain is characterized as KH.
+At position 635 to 755, the domain is characterized as N-terminal Ras-GEF.
+At position 954 to 1186, the domain is characterized as Ras-GEF.
+At position 26 to 166, the domain is characterized as Peptidase C51.
+At position 2 to 159, the domain is characterized as DHFR.
+At position 27 to 73, the domain is characterized as WAP 1; atypical.
+At position 76 to 128, the domain is characterized as WAP 2.
+At position 291 to 593, the domain is characterized as Protein kinase.
+At position 276 to 365, the domain is characterized as CS.
+At position 128 to 161, the domain is characterized as EF-hand 4.
+At position 400 to 429, the domain is characterized as IQ.
+At position 661 to 742, the domain is characterized as CBS 1.
+At position 816 to 863, the domain is characterized as CBS 2.
+At position 156 to 488, the domain is characterized as Protein kinase.
+At position 178 to 347, the domain is characterized as tr-type G.
+At position 12 to 364, the domain is characterized as Kinesin motor.
+At position 108 to 386, the domain is characterized as Protein kinase.
+At position 205 to 428, the domain is characterized as Fibrinogen C-terminal.
+At position 39 to 66, the domain is characterized as EF-hand 1.
+At position 77 to 95, the domain is characterized as EF-hand 2.
+At position 384 to 474, the domain is characterized as IPT/TIG.
+At position 8 to 175, the domain is characterized as Era-type G.
+At position 17 to 232, the domain is characterized as tr-type G.
+At position 593 to 780, the domain is characterized as Reticulon.
+At position 99 to 292, the domain is characterized as ATP-grasp.
+At position 162 to 465, the domain is characterized as Protein kinase.
+At position 466 to 548, the domain is characterized as AGC-kinase C-terminal.
+At position 35 to 484, the domain is characterized as Sema.
+At position 540 to 593, the domain is characterized as TSP type-1 1.
+At position 595 to 651, the domain is characterized as TSP type-1 2.
+At position 653 to 702, the domain is characterized as TSP type-1 3.
+At position 707 to 765, the domain is characterized as TSP type-1 4.
+At position 784 to 839, the domain is characterized as TSP type-1 5.
+At position 841 to 896, the domain is characterized as TSP type-1 6.
+At position 897 to 944, the domain is characterized as TSP type-1 7.
+At position 126 to 175, the domain is characterized as SANT.
+At position 27 to 111, the domain is characterized as IGFBP N-terminal.
+At position 96 to 155, the domain is characterized as Kazal-like.
+At position 364 to 466, the domain is characterized as PDZ.
+At position 36 to 251, the domain is characterized as GB1/RHD3-type G.
+At position 1 to 58, the domain is characterized as KRAB.
+At position 57 to 114, the domain is characterized as Collagen-like.
+At position 121 to 339, the domain is characterized as Fibrinogen C-terminal.
+At position 28 to 77, the domain is characterized as Myosin N-terminal SH3-like.
+At position 81 to 794, the domain is characterized as Myosin motor.
+At position 175 to 273, the domain is characterized as HTH araC/xylS-type.
+At position 47 to 314, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 148 to 685, the domain is characterized as USP.
+At position 687 to 780, the domain is characterized as DUSP 1.
+At position 789 to 891, the domain is characterized as DUSP 2.
+At position 13 to 244, the domain is characterized as AB hydrolase-1.
+At position 107 to 294, the domain is characterized as Tyr recombinase.
+At position 143 to 315, the domain is characterized as Helicase ATP-binding.
+At position 344 to 493, the domain is characterized as Helicase C-terminal.
+At position 38 to 392, the domain is characterized as Peptidase A1.
+At position 536 to 617, the domain is characterized as RWP-RK.
+At position 710 to 793, the domain is characterized as PB1.
+At position 10 to 416, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1 to 61, the domain is characterized as HTH lacI-type.
+At position 18 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 9 to 105, the domain is characterized as ASCH.
+At position 6 to 280, the domain is characterized as tr-type G.
+At position 56 to 108, the domain is characterized as bHLH.
+At position 171 to 259, the domain is characterized as tr-type G.
+At position 27 to 293, the domain is characterized as Protein kinase.
+At position 343 to 1058, the domain is characterized as Myosin motor.
+At position 1060 to 1089, the domain is characterized as IQ 1.
+At position 1087 to 1116, the domain is characterized as IQ 2.
+At position 9 to 179, the domain is characterized as Era-type G.
+At position 3 to 194, the domain is characterized as DPCK.
+At position 738 to 831, the domain is characterized as Fibronectin type-III 4.
+At position 123 to 212, the domain is characterized as Ricin B-type lectin.
+At position 12 to 74, the domain is characterized as SH3.
+At position 265 to 298, the domain is characterized as WW 1.
+At position 358 to 391, the domain is characterized as WW 2.
+At position 463 to 575, the domain is characterized as PH.
+At position 656 to 844, the domain is characterized as Rho-GAP.
+At position 50 to 81, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 89 to 121, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 130 to 166, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 31 to 759, the domain is characterized as GH81.
+At position 195 to 462, the domain is characterized as SF4 helicase; first part.
+At position 582 to 660, the domain is characterized as DOD-type homing endonuclease.
+At position 612 to 874, the domain is characterized as SF4 helicase; second part.
+At position 47 to 149, the domain is characterized as sHSP.
+At position 2 to 235, the domain is characterized as Glutamine amidotransferase type-2.
+At position 404 to 472, the domain is characterized as B5.
+At position 1045 to 1298, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 337, the domain is characterized as Calpain catalytic.
+At position 518 to 552, the domain is characterized as EF-hand 1.
+At position 561 to 589, the domain is characterized as EF-hand 2.
+At position 591 to 626, the domain is characterized as EF-hand 3.
+At position 396 to 430, the domain is characterized as SAP.
+At position 582 to 688, the domain is characterized as tRNA-binding.
+At position 29 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 54 to 249, the domain is characterized as Laminin G-like.
+At position 605 to 665, the domain is characterized as Collagen-like 1.
+At position 666 to 717, the domain is characterized as Collagen-like 2.
+At position 808 to 850, the domain is characterized as Collagen-like 3.
+At position 863 to 912, the domain is characterized as Collagen-like 4.
+At position 11 to 131, the domain is characterized as Calponin-homology (CH).
+At position 166 to 357, the domain is characterized as CheB-type methylesterase.
+At position 31 to 114, the domain is characterized as Kringle.
+At position 116 to 210, the domain is characterized as WSC.
+At position 214 to 321, the domain is characterized as CUB.
+At position 352 to 442, the domain is characterized as BRCT.
+At position 39 to 156, the domain is characterized as DEUBAD.
+At position 1 to 99, the domain is characterized as PPIase FKBP-type.
+At position 5 to 438, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 930 to 1004, the domain is characterized as Carrier.
+At position 27 to 115, the domain is characterized as Ig-like V-type 1.
+At position 117 to 204, the domain is characterized as Ig-like V-type 2.
+At position 208 to 305, the domain is characterized as Ig-like V-type 3.
+At position 307 to 405, the domain is characterized as Ig-like V-type 4.
+At position 406 to 501, the domain is characterized as Ig-like V-type 5.
+At position 29 to 55, the domain is characterized as IQ.
+At position 54 to 143, the domain is characterized as Ig-like 1.
+At position 147 to 236, the domain is characterized as Ig-like 2.
+At position 343 to 394, the domain is characterized as GPS.
+At position 6 to 165, the domain is characterized as DHFR.
+At position 76 to 308, the domain is characterized as Fibrinogen C-terminal.
+At position 76 to 151, the domain is characterized as ACT.
+At position 251 to 446, the domain is characterized as GATase cobBQ-type.
+At position 85 to 206, the domain is characterized as GST C-terminal.
+At position 188 to 244, the domain is characterized as bZIP.
+At position 47 to 291, the domain is characterized as Peptidase S1 1.
+At position 323 to 567, the domain is characterized as Peptidase S1 2.
+At position 584 to 802, the domain is characterized as Peptidase S1 3.
+At position 376 to 468, the domain is characterized as TRAM.
+At position 67 to 340, the domain is characterized as Dynamin-type G.
+At position 574 to 662, the domain is characterized as GED.
+At position 241 to 360, the domain is characterized as SET.
+At position 305 to 338, the domain is characterized as KOW 1.
+At position 519 to 553, the domain is characterized as KOW 2.
+At position 25 to 246, the domain is characterized as Peptidase S1.
+At position 531 to 762, the domain is characterized as ABC transporter.
+At position 235 to 288, the domain is characterized as bHLH.
+At position 3 to 107, the domain is characterized as SSB.
+At position 34 to 134, the domain is characterized as SRCR 1.
+At position 160 to 266, the domain is characterized as SRCR 2.
+At position 274 to 368, the domain is characterized as SRCR 3.
+At position 108 to 294, the domain is characterized as FAD-binding PCMH-type.
+At position 548 to 592, the domain is characterized as F-box.
+At position 2 to 238, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 100, the domain is characterized as HTH arsR-type.
+At position 9 to 66, the domain is characterized as CBS 1.
+At position 72 to 128, the domain is characterized as CBS 2.
+At position 221 to 398, the domain is characterized as PCI.
+At position 22 to 108, the domain is characterized as PDZ 1.
+At position 116 to 290, the domain is characterized as Guanylate kinase-like.
+At position 295 to 328, the domain is characterized as WW 1.
+At position 341 to 374, the domain is characterized as WW 2.
+At position 412 to 494, the domain is characterized as PDZ 2.
+At position 581 to 657, the domain is characterized as PDZ 3.
+At position 728 to 810, the domain is characterized as PDZ 4.
+At position 852 to 939, the domain is characterized as PDZ 5.
+At position 1024 to 1106, the domain is characterized as PDZ 6.
+At position 76 to 393, the domain is characterized as Peptidase A1.
+At position 713 to 893, the domain is characterized as Helicase C-terminal.
+At position 590 to 938, the domain is characterized as Protein kinase.
+At position 39 to 67, the domain is characterized as LRRNT.
+At position 227 to 283, the domain is characterized as LRRCT.
+At position 288 to 378, the domain is characterized as Ig-like C2-type.
+At position 5 to 137, the domain is characterized as UBC core.
+At position 41 to 73, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 83 to 112, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 212 to 311, the domain is characterized as Fe2OG dioxygenase.
+At position 142 to 264, the domain is characterized as OmpA-like.
+At position 1 to 234, the domain is characterized as Protein kinase.
+At position 52 to 186, the domain is characterized as TIR.
+At position 289 to 354, the domain is characterized as Mop.
+At position 2 to 266, the domain is characterized as OBG-type G.
+At position 314 to 390, the domain is characterized as TGS.
+At position 37 to 201, the domain is characterized as Thioredoxin.
+At position 42 to 160, the domain is characterized as CBM6.
+At position 181 to 474, the domain is characterized as GH26.
+At position 24 to 55, the domain is characterized as Pacifastin.
+At position 75 to 386, the domain is characterized as IF rod.
+At position 30 to 104, the domain is characterized as U-box.
+At position 6 to 133, the domain is characterized as ADF-H.
+At position 725 to 785, the domain is characterized as SH3 1.
+At position 800 to 857, the domain is characterized as SH3 2.
+At position 833 to 950, the domain is characterized as SET.
+At position 959 to 975, the domain is characterized as Post-SET.
+At position 16 to 90, the domain is characterized as CBS 1.
+At position 347 to 409, the domain is characterized as CBS 2.
+At position 59 to 222, the domain is characterized as CP-type G.
+At position 1 to 82, the domain is characterized as GIY-YIG.
+At position 225 to 417, the domain is characterized as B30.2/SPRY.
+At position 195 to 257, the domain is characterized as t-SNARE coiled-coil homology.
+At position 98 to 175, the domain is characterized as RRM 2.
+At position 120 to 190, the domain is characterized as BTB.
+At position 235 to 300, the domain is characterized as BACK.
+At position 569 to 730, the domain is characterized as SUN.
+At position 2 to 248, the domain is characterized as ABC transporter.
+At position 113 to 375, the domain is characterized as Helicase ATP-binding.
+At position 407 to 568, the domain is characterized as Helicase C-terminal.
+At position 36 to 138, the domain is characterized as SCP.
+At position 329 to 539, the domain is characterized as Rab-GAP TBC.
+At position 75 to 191, the domain is characterized as RGS.
+At position 9 to 206, the domain is characterized as ThyX.
+At position 12 to 51, the domain is characterized as Tudor-knot.
+At position 191 to 362, the domain is characterized as MRG.
+At position 84 to 206, the domain is characterized as FAD-binding FR-type.
+At position 43 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 10 to 264, the domain is characterized as Protein kinase.
+At position 65 to 282, the domain is characterized as Radical SAM core.
+At position 513 to 620, the domain is characterized as Toprim.
+At position 120 to 320, the domain is characterized as ATP-grasp.
+At position 266 to 341, the domain is characterized as bHLH.
+At position 105 to 255, the domain is characterized as Flavodoxin-like.
+At position 311 to 559, the domain is characterized as FAD-binding FR-type.
+At position 44 to 112, the domain is characterized as POTRA.
+At position 600 to 706, the domain is characterized as tRNA-binding.
+At position 519 to 646, the domain is characterized as Guanylate cyclase.
+At position 565 to 670, the domain is characterized as tRNA-binding.
+At position 29 to 88, the domain is characterized as 4Fe-4S.
+At position 103 to 132, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 133 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 66 to 200, the domain is characterized as TBDR plug.
+At position 208 to 1066, the domain is characterized as TBDR beta-barrel.
+At position 169 to 355, the domain is characterized as CheB-type methylesterase.
+At position 692 to 784, the domain is characterized as FDX-ACB.
+At position 99 to 162, the domain is characterized as bZIP.
+At position 637 to 719, the domain is characterized as BRCT.
+At position 33 to 260, the domain is characterized as Radical SAM core.
+At position 80 to 207, the domain is characterized as ALOG.
+At position 143 to 280, the domain is characterized as N-acetyltransferase.
+At position 60 to 209, the domain is characterized as Cupin type-1.
+At position 13 to 464, the domain is characterized as ABC transporter.
+At position 214 to 481, the domain is characterized as Protein kinase.
+At position 112 to 193, the domain is characterized as REM-1 2.
+At position 201 to 280, the domain is characterized as REM-1 3.
+At position 307 to 470, the domain is characterized as C2.
+At position 615 to 874, the domain is characterized as Protein kinase.
+At position 875 to 942, the domain is characterized as AGC-kinase C-terminal.
+At position 115 to 370, the domain is characterized as Septin-type G.
+At position 167 to 321, the domain is characterized as Thioredoxin.
+At position 621 to 674, the domain is characterized as bHLH.
+At position 338 to 466, the domain is characterized as Ricin B-type lectin 1.
+At position 467 to 593, the domain is characterized as Ricin B-type lectin 2.
+At position 24 to 129, the domain is characterized as Ig-like 1.
+At position 214 to 380, the domain is characterized as UBC core.
+At position 7 to 118, the domain is characterized as DUSP.
+At position 289 to 933, the domain is characterized as USP.
+At position 20 to 61, the domain is characterized as EGF-like 1.
+At position 114 to 150, the domain is characterized as EGF-like 2.
+At position 152 to 190, the domain is characterized as EGF-like 3; calcium-binding.
+At position 201 to 246, the domain is characterized as EGF-like 4.
+At position 250 to 285, the domain is characterized as EGF-like 5.
+At position 287 to 323, the domain is characterized as EGF-like 6.
+At position 323 to 363, the domain is characterized as EGF-like 7.
+At position 365 to 402, the domain is characterized as EGF-like 8; calcium-binding.
+At position 404 to 441, the domain is characterized as EGF-like 9.
+At position 449 to 492, the domain is characterized as EGF-like 10.
+At position 503 to 541, the domain is characterized as EGF-like 11.
+At position 543 to 579, the domain is characterized as EGF-like 12.
+At position 582 to 619, the domain is characterized as EGF-like 13.
+At position 7 to 324, the domain is characterized as Helicase ATP-binding.
+At position 1 to 112, the domain is characterized as ABC transmembrane type-1.
+At position 521 to 596, the domain is characterized as Cytochrome b5 heme-binding.
+At position 644 to 756, the domain is characterized as FAD-binding FR-type.
+At position 10 to 338, the domain is characterized as Protein kinase.
+At position 166 to 204, the domain is characterized as LRRCT.
+At position 119 to 358, the domain is characterized as Radical SAM core.
+At position 55 to 90, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 161 to 403, the domain is characterized as Protein kinase.
+At position 555 to 647, the domain is characterized as tRNA-binding.
+At position 176 to 241, the domain is characterized as HTH luxR-type.
+At position 305 to 413, the domain is characterized as Rhodanese.
+At position 31 to 416, the domain is characterized as Helicase ATP-binding.
+At position 433 to 596, the domain is characterized as Helicase C-terminal.
+At position 36 to 154, the domain is characterized as C-type lectin.
+At position 515 to 770, the domain is characterized as Protein kinase.
+At position 2 to 247, the domain is characterized as ABC transporter.
+At position 38 to 135, the domain is characterized as Ig-like V-type.
+At position 148 to 229, the domain is characterized as Ig-like C2-type.
+At position 3 to 91, the domain is characterized as PE.
+At position 101 to 284, the domain is characterized as Thioredoxin.
+At position 29 to 159, the domain is characterized as PLAT.
+At position 162 to 860, the domain is characterized as Lipoxygenase.
+At position 29 to 406, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 85 to 229, the domain is characterized as Clp R.
+At position 53 to 301, the domain is characterized as Radical SAM core.
+At position 559 to 708, the domain is characterized as uDENN.
+At position 730 to 863, the domain is characterized as cDENN.
+At position 865 to 960, the domain is characterized as dDENN.
+At position 98 to 335, the domain is characterized as Radical SAM core.
+At position 181 to 251, the domain is characterized as S4 RNA-binding.
+At position 164 to 191, the domain is characterized as PLD phosphodiesterase.
+At position 58 to 135, the domain is characterized as Ubiquitin-like.
+At position 512 to 768, the domain is characterized as ATP-grasp.
+At position 534 to 702, the domain is characterized as N-acetyltransferase.
+At position 1 to 150, the domain is characterized as RPW8.
+At position 156 to 283, the domain is characterized as NB-ARC 1.
+At position 341 to 440, the domain is characterized as NB-ARC 2.
+At position 593 to 670, the domain is characterized as BRCT.
+At position 46 to 165, the domain is characterized as SEA.
+At position 186 to 416, the domain is characterized as Peptidase S1.
+At position 262 to 378, the domain is characterized as Response regulatory.
+At position 17 to 209, the domain is characterized as ABC transporter.
+At position 478 to 514, the domain is characterized as CBM1.
+At position 713 to 788, the domain is characterized as Smr.
+At position 161 to 225, the domain is characterized as EamA.
+At position 2 to 145, the domain is characterized as Clp R.
+At position 29 to 118, the domain is characterized as Ig-like C1-type.
+At position 321 to 448, the domain is characterized as Ricin B-type lectin 1.
+At position 451 to 575, the domain is characterized as Ricin B-type lectin 2.
+At position 314 to 356, the domain is characterized as CAP-Gly 1.
+At position 436 to 478, the domain is characterized as CAP-Gly 2.
+At position 175 to 237, the domain is characterized as t-SNARE coiled-coil homology.
+At position 50 to 177, the domain is characterized as LRAT.
+At position 48 to 115, the domain is characterized as KH 1.
+At position 146 to 212, the domain is characterized as KH 2.
+At position 396 to 463, the domain is characterized as KH 3.
+At position 214 to 282, the domain is characterized as BTB.
+At position 631 to 660, the domain is characterized as IQ.
+At position 34 to 129, the domain is characterized as Phytocyanin.
+At position 119 to 441, the domain is characterized as Dynamin-type G.
+At position 28 to 132, the domain is characterized as Cadherin 1.
+At position 133 to 241, the domain is characterized as Cadherin 2.
+At position 242 to 346, the domain is characterized as Cadherin 3.
+At position 347 to 451, the domain is characterized as Cadherin 4.
+At position 569 to 682, the domain is characterized as Cadherin 6.
+At position 19 to 166, the domain is characterized as CENP-V/GFA.
+At position 1 to 31, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 371 to 649, the domain is characterized as Radical SAM core.
+At position 105 to 222, the domain is characterized as Ferric oxidoreductase.
+At position 248 to 372, the domain is characterized as FAD-binding FR-type.
+At position 816 to 895, the domain is characterized as ACT 2.
+At position 32 to 309, the domain is characterized as Protein kinase.
+At position 414 to 502, the domain is characterized as Fibronectin type-III.
+At position 9 to 171, the domain is characterized as EngA-type G 1.
+At position 201 to 372, the domain is characterized as EngA-type G 2.
+At position 105 to 124, the domain is characterized as HhH.
+At position 229 to 328, the domain is characterized as GIY-YIG.
+At position 196 to 337, the domain is characterized as Nudix hydrolase.
+At position 225 to 384, the domain is characterized as TrmE-type G.
+At position 265 to 340, the domain is characterized as PUA.
+At position 20 to 182, the domain is characterized as PPIase cyclophilin-type.
+At position 52 to 163, the domain is characterized as TBDR plug.
+At position 169 to 746, the domain is characterized as TBDR beta-barrel.
+At position 30 to 73, the domain is characterized as CHCH.
+At position 23 to 209, the domain is characterized as EngB-type G.
+At position 253 to 431, the domain is characterized as Helicase ATP-binding.
+At position 442 to 621, the domain is characterized as Helicase C-terminal.
+At position 30 to 64, the domain is characterized as SAP.
+At position 407 to 485, the domain is characterized as RRM.
+At position 39 to 718, the domain is characterized as Myosin motor.
+At position 722 to 742, the domain is characterized as IQ 1.
+At position 743 to 768, the domain is characterized as IQ 2.
+At position 776 to 965, the domain is characterized as TH1.
+At position 1071 to 1129, the domain is characterized as SH3.
+At position 16 to 272, the domain is characterized as Protein kinase.
+At position 26 to 47, the domain is characterized as IQ.
+At position 48 to 78, the domain is characterized as Collagen-like.
+At position 43 to 131, the domain is characterized as DAGKc.
+At position 14 to 120, the domain is characterized as Thioredoxin.
+At position 208 to 814, the domain is characterized as USP.
+At position 16 to 203, the domain is characterized as RNase H type-2.
+At position 7 to 58, the domain is characterized as Rubredoxin-like.
+At position 29 to 243, the domain is characterized as ABC transporter.
+At position 238 to 273, the domain is characterized as GRAM 1.
+At position 289 to 388, the domain is characterized as PH.
+At position 717 to 783, the domain is characterized as GRAM 2.
+At position 35 to 166, the domain is characterized as FAS1.
+At position 25 to 143, the domain is characterized as Rhodanese 1.
+At position 173 to 288, the domain is characterized as Rhodanese 2.
+At position 177 to 206, the domain is characterized as GS.
+At position 207 to 497, the domain is characterized as Protein kinase.
+At position 180 to 279, the domain is characterized as HTH araC/xylS-type.
+At position 374 to 396, the domain is characterized as WH2.
+At position 510 to 550, the domain is characterized as EGF-like 1.
+At position 651 to 695, the domain is characterized as EGF-like 2.
+At position 699 to 751, the domain is characterized as EGF-like 3.
+At position 1065 to 1188, the domain is characterized as Fibronectin type-III.
+At position 725 to 809, the domain is characterized as PB1.
+At position 758 to 1008, the domain is characterized as Protein kinase.
+At position 30 to 151, the domain is characterized as PX.
+At position 178 to 387, the domain is characterized as BAR.
+At position 115 to 173, the domain is characterized as TCP.
+At position 250 to 267, the domain is characterized as R.
+At position 2 to 125, the domain is characterized as PLAT.
+At position 126 to 677, the domain is characterized as Lipoxygenase.
+At position 37 to 260, the domain is characterized as Cache.
+At position 298 to 352, the domain is characterized as HAMP.
+At position 357 to 593, the domain is characterized as Methyl-accepting transducer.
+At position 11 to 131, the domain is characterized as MTTase N-terminal.
+At position 153 to 385, the domain is characterized as Radical SAM core.
+At position 388 to 449, the domain is characterized as TRAM.
+At position 34 to 291, the domain is characterized as Protein kinase.
+At position 11 to 250, the domain is characterized as KaiC 1.
+At position 251 to 485, the domain is characterized as KaiC 2.
+At position 240 to 300, the domain is characterized as SH3.
+At position 40 to 115, the domain is characterized as RRM.
+At position 167 to 190, the domain is characterized as DAZ.
+At position 44 to 164, the domain is characterized as Plastocyanin-like 1.
+At position 175 to 338, the domain is characterized as Plastocyanin-like 2.
+At position 401 to 537, the domain is characterized as Plastocyanin-like 3.
+At position 102 to 302, the domain is characterized as ATP-grasp.
+At position 112 to 260, the domain is characterized as PA14.
+At position 146 to 314, the domain is characterized as JmjC.
+At position 874 to 919, the domain is characterized as F-box.
+At position 9 to 250, the domain is characterized as ATP-grasp.
+At position 14 to 86, the domain is characterized as PAS.
+At position 91 to 143, the domain is characterized as PAC.
+At position 253 to 453, the domain is characterized as GATase cobBQ-type.
+At position 29 to 282, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 124 to 186, the domain is characterized as t-SNARE coiled-coil homology.
+At position 48 to 90, the domain is characterized as CUE.
+At position 255 to 390, the domain is characterized as Fido.
+At position 25 to 152, the domain is characterized as ALOG.
+At position 344 to 599, the domain is characterized as Clu.
+At position 1016 to 1203, the domain is characterized as Laminin G-like 4.
+At position 1114 to 1183, the domain is characterized as S1 motif.
+At position 1231 to 1331, the domain is characterized as SH2.
+At position 285 to 453, the domain is characterized as Helicase ATP-binding.
+At position 472 to 632, the domain is characterized as Helicase C-terminal.
+At position 4 to 38, the domain is characterized as WW.
+At position 64 to 175, the domain is characterized as PpiC.
+At position 85 to 277, the domain is characterized as DCUN1.
+At position 543 to 795, the domain is characterized as STAS.
+At position 36 to 193, the domain is characterized as Upf1 CH-rich.
+At position 321 to 504, the domain is characterized as Helicase ATP-binding.
+At position 532 to 677, the domain is characterized as Helicase C-terminal.
+At position 6 to 166, the domain is characterized as PPIase cyclophilin-type.
+At position 102 to 458, the domain is characterized as USP.
+At position 105 to 278, the domain is characterized as EngB-type G.
+At position 8 to 83, the domain is characterized as Ubiquitin-like.
+At position 124 to 157, the domain is characterized as STI1 1.
+At position 161 to 200, the domain is characterized as STI1 2.
+At position 289 to 327, the domain is characterized as STI1 3.
+At position 351 to 387, the domain is characterized as STI1 4.
+At position 455 to 501, the domain is characterized as UBA.
+At position 1010 to 1297, the domain is characterized as CNH.
+At position 237 to 377, the domain is characterized as MPN.
+At position 51 to 198, the domain is characterized as FPL.
+At position 181 to 340, the domain is characterized as PCI.
+At position 11 to 77, the domain is characterized as KRAB 1.
+At position 333 to 404, the domain is characterized as KRAB 2.
+At position 63 to 336, the domain is characterized as Protein kinase.
+At position 48 to 152, the domain is characterized as AB hydrolase-1.
+At position 211 to 481, the domain is characterized as Protein kinase.
+At position 96 to 141, the domain is characterized as LysM.
+At position 38 to 151, the domain is characterized as Thioredoxin.
+At position 62 to 193, the domain is characterized as BAH.
+At position 2 to 187, the domain is characterized as DOC.
+At position 110 to 391, the domain is characterized as FERM.
+At position 50 to 245, the domain is characterized as Cupin type-1 1.
+At position 52 to 120, the domain is characterized as CSD.
+At position 93 to 160, the domain is characterized as GRAM.
+At position 370 to 541, the domain is characterized as VASt.
+At position 62 to 385, the domain is characterized as ABC transmembrane type-1 1.
+At position 420 to 656, the domain is characterized as ABC transporter 1.
+At position 759 to 1047, the domain is characterized as ABC transmembrane type-1 2.
+At position 1082 to 1320, the domain is characterized as ABC transporter 2.
+At position 5 to 67, the domain is characterized as TGS.
+At position 500 to 641, the domain is characterized as Flavodoxin-like.
+At position 676 to 904, the domain is characterized as FAD-binding FR-type.
+At position 40 to 109, the domain is characterized as Cystatin.
+At position 145 to 351, the domain is characterized as ATP-grasp.
+At position 73 to 158, the domain is characterized as Core-binding (CB).
+At position 179 to 428, the domain is characterized as Tyr recombinase.
+At position 8 to 128, the domain is characterized as MaoC-like.
+At position 21 to 264, the domain is characterized as ABC transporter.
+At position 33 to 86, the domain is characterized as 4Fe-4S Wbl-type.
+At position 1 to 88, the domain is characterized as Pyrin.
+At position 213 to 413, the domain is characterized as HIN-200.
+At position 42 to 200, the domain is characterized as MABP.
+At position 192 to 364, the domain is characterized as uDENN.
+At position 385 to 521, the domain is characterized as cDENN.
+At position 523 to 641, the domain is characterized as dDENN.
+At position 30 to 225, the domain is characterized as Lon N-terminal.
+At position 612 to 793, the domain is characterized as Lon proteolytic.
+At position 39 to 224, the domain is characterized as Reticulon.
+At position 302 to 400, the domain is characterized as Rhodanese.
+At position 26 to 112, the domain is characterized as Ig-like.
+At position 1 to 128, the domain is characterized as C2 1.
+At position 135 to 262, the domain is characterized as C2 2.
+At position 305 to 504, the domain is characterized as VWFA.
+At position 186 to 221, the domain is characterized as EF-hand 1.
+At position 294 to 329, the domain is characterized as EF-hand 2.
+At position 369 to 404, the domain is characterized as EF-hand 3.
+At position 293 to 583, the domain is characterized as Deacetylase sirtuin-type.
+At position 321 to 539, the domain is characterized as Rap-GAP.
+At position 687 to 763, the domain is characterized as PDZ.
+At position 26 to 280, the domain is characterized as Protein kinase.
+At position 336 to 360, the domain is characterized as NAF.
+At position 25 to 144, the domain is characterized as Bulb-type lectin.
+At position 278 to 314, the domain is characterized as EGF-like; atypical.
+At position 333 to 413, the domain is characterized as PAN.
+At position 494 to 779, the domain is characterized as Protein kinase.
+At position 28 to 74, the domain is characterized as F-box.
+At position 250 to 425, the domain is characterized as Helicase ATP-binding.
+At position 436 to 599, the domain is characterized as Helicase C-terminal.
+At position 161 to 320, the domain is characterized as Ferric oxidoreductase.
+At position 321 to 419, the domain is characterized as FAD-binding FR-type.
+At position 54 to 104, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 125 to 175, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 217 to 267, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 36 to 171, the domain is characterized as N-acetyltransferase.
+At position 75 to 134, the domain is characterized as CBS 1.
+At position 140 to 197, the domain is characterized as CBS 2.
+At position 10 to 157, the domain is characterized as HTH marR-type.
+At position 26 to 77, the domain is characterized as HTH myb-type 1.
+At position 78 to 133, the domain is characterized as HTH myb-type 2.
+At position 134 to 184, the domain is characterized as HTH myb-type 3.
+At position 394 to 620, the domain is characterized as PARP catalytic.
+At position 235 to 403, the domain is characterized as Helicase ATP-binding.
+At position 603 to 767, the domain is characterized as Helicase C-terminal.
+At position 1 to 216, the domain is characterized as Peptidase S1.
+At position 79 to 290, the domain is characterized as Protein kinase.
+At position 9 to 97, the domain is characterized as Acylphosphatase-like.
+At position 404 to 472, the domain is characterized as ACT 1.
+At position 478 to 542, the domain is characterized as ACT 2.
+At position 13 to 137, the domain is characterized as FAD-binding FR-type.
+At position 53 to 112, the domain is characterized as J.
+At position 295 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 40 to 100, the domain is characterized as v-SNARE coiled-coil homology.
+At position 162 to 655, the domain is characterized as USP.
+At position 532 to 690, the domain is characterized as STAS.
+At position 590 to 920, the domain is characterized as Protein kinase.
+At position 63 to 173, the domain is characterized as Expansin-like EG45.
+At position 186 to 267, the domain is characterized as Expansin-like CBD.
+At position 2 to 227, the domain is characterized as ABC transporter.
+At position 125 to 160, the domain is characterized as EF-hand 1.
+At position 179 to 196, the domain is characterized as EF-hand 2.
+At position 202 to 237, the domain is characterized as EF-hand 3.
+At position 239 to 271, the domain is characterized as EF-hand 4.
+At position 43 to 102, the domain is characterized as Collagen-like.
+At position 103 to 240, the domain is characterized as C1q.
+At position 122 to 617, the domain is characterized as Lipoxygenase.
+At position 181 to 270, the domain is characterized as EH 1.
+At position 214 to 249, the domain is characterized as EF-hand 1.
+At position 444 to 533, the domain is characterized as EH 2.
+At position 477 to 512, the domain is characterized as EF-hand 2.
+At position 1417 to 1434, the domain is characterized as WH2.
+At position 1905 to 1934, the domain is characterized as IQ.
+At position 3 to 125, the domain is characterized as MATH.
+At position 2 to 58, the domain is characterized as HTH lysR-type.
+At position 188 to 267, the domain is characterized as RRM.
+At position 149 to 362, the domain is characterized as TRUD.
+At position 111 to 253, the domain is characterized as DAGKc.
+At position 361 to 631, the domain is characterized as Clu.
+At position 105 to 184, the domain is characterized as PRC barrel.
+At position 75 to 233, the domain is characterized as CP-type G.
+At position 66 to 229, the domain is characterized as SIS.
+At position 437 to 611, the domain is characterized as tr-type G.
+At position 143 to 194, the domain is characterized as F-box.
+At position 15 to 90, the domain is characterized as GIY-YIG.
+At position 198 to 233, the domain is characterized as UVR.
+At position 11 to 86, the domain is characterized as U-box.
+At position 1 to 92, the domain is characterized as YcgL.
+At position 17 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 647, the domain is characterized as GH81.
+At position 51 to 256, the domain is characterized as Helicase ATP-binding.
+At position 278 to 453, the domain is characterized as Helicase C-terminal.
+At position 580 to 712, the domain is characterized as B12-binding.
+At position 32 to 95, the domain is characterized as S5 DRBM.
+At position 77 to 227, the domain is characterized as N-acetyltransferase.
+At position 6 to 110, the domain is characterized as SSB.
+At position 1 to 112, the domain is characterized as Response regulatory.
+At position 133 to 362, the domain is characterized as Sigma-54 factor interaction.
+At position 1 to 208, the domain is characterized as SMP-LTD.
+At position 89 to 213, the domain is characterized as N-terminal Ras-GEF.
+At position 244 to 516, the domain is characterized as Ras-GEF.
+At position 651 to 738, the domain is characterized as Ras-associating.
+At position 1 to 61, the domain is characterized as F-box.
+At position 358 to 406, the domain is characterized as FBD.
+At position 202 to 294, the domain is characterized as ARID.
+At position 389 to 479, the domain is characterized as REKLES.
+At position 27 to 115, the domain is characterized as Ig-like C1-type.
+At position 141 to 362, the domain is characterized as Ras-GAP.
+At position 1573 to 1712, the domain is characterized as VPS9.
+At position 13 to 249, the domain is characterized as Radical SAM core.
+At position 27 to 347, the domain is characterized as Tyrosine-protein phosphatase.
+At position 62 to 256, the domain is characterized as Peptidase M12A.
+At position 260 to 429, the domain is characterized as MAM.
+At position 430 to 585, the domain is characterized as MATH.
+At position 604 to 644, the domain is characterized as EGF-like.
+At position 116 to 238, the domain is characterized as Fe2OG dioxygenase.
+At position 248 to 288, the domain is characterized as ShKT.
+At position 71 to 247, the domain is characterized as FAD-binding PCMH-type.
+At position 179 to 256, the domain is characterized as POU-specific.
+At position 207 to 257, the domain is characterized as HNH.
+At position 23 to 98, the domain is characterized as UPAR/Ly6.
+At position 9 to 284, the domain is characterized as tr-type G.
+At position 5 to 225, the domain is characterized as Radical SAM core.
+At position 180 to 342, the domain is characterized as PCI.
+At position 130 to 253, the domain is characterized as Nudix hydrolase.
+At position 106 to 227, the domain is characterized as GST C-terminal.
+At position 38 to 103, the domain is characterized as Inhibitor I9.
+At position 111 to 380, the domain is characterized as Peptidase S8.
+At position 527 to 599, the domain is characterized as Sushi 1.
+At position 612 to 708, the domain is characterized as Ig-like C2-type.
+At position 712 to 770, the domain is characterized as Sushi 2.
+At position 771 to 829, the domain is characterized as Sushi 3.
+At position 830 to 892, the domain is characterized as Sushi 4.
+At position 892 to 954, the domain is characterized as Sushi 5.
+At position 40 to 244, the domain is characterized as Lon N-terminal.
+At position 636 to 816, the domain is characterized as Lon proteolytic.
+At position 64 to 252, the domain is characterized as RNase H type-2.
+At position 129 to 207, the domain is characterized as Ig-like C2-type 1.
+At position 208 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 205 to 240, the domain is characterized as EF-hand.
+At position 366 to 523, the domain is characterized as Ferric oxidoreductase.
+At position 562 to 695, the domain is characterized as FAD-binding FR-type.
+At position 274 to 390, the domain is characterized as C-type lectin.
+At position 28 to 171, the domain is characterized as Helicase ATP-binding.
+At position 26 to 97, the domain is characterized as SH3.
+At position 102 to 210, the domain is characterized as sHSP.
+At position 25 to 55, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 67 to 98, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 309 to 362, the domain is characterized as TSP type-1 1.
+At position 364 to 417, the domain is characterized as TSP type-1 2.
+At position 419 to 472, the domain is characterized as TSP type-1 3.
+At position 475 to 528, the domain is characterized as TSP type-1 4.
+At position 871 to 923, the domain is characterized as GPS.
+At position 19 to 244, the domain is characterized as Radical SAM core.
+At position 168 to 265, the domain is characterized as CRM 1.
+At position 350 to 447, the domain is characterized as CRM 2.
+At position 562 to 662, the domain is characterized as CRM 3.
+At position 398 to 475, the domain is characterized as B5.
+At position 104 to 186, the domain is characterized as PDZ.
+At position 1611 to 1640, the domain is characterized as IQ.
+At position 347 to 515, the domain is characterized as tr-type G.
+At position 273 to 348, the domain is characterized as PUA.
+At position 147 to 444, the domain is characterized as NR LBD.
+At position 295 to 374, the domain is characterized as PUA.
+At position 919 to 992, the domain is characterized as S1 motif.
+At position 90 to 170, the domain is characterized as PA.
+At position 506 to 700, the domain is characterized as B30.2/SPRY.
+At position 99 to 112, the domain is characterized as CRIB.
+At position 10 to 136, the domain is characterized as RNase III.
+At position 163 to 231, the domain is characterized as DRBM.
+At position 19 to 78, the domain is characterized as KH.
+At position 4 to 184, the domain is characterized as Flavodoxin-like.
+At position 7 to 189, the domain is characterized as UmuC.
+At position 2 to 161, the domain is characterized as DHFR.
+At position 54 to 229, the domain is characterized as VWFA.
+At position 235 to 275, the domain is characterized as EGF-like 1.
+At position 276 to 316, the domain is characterized as EGF-like 2.
+At position 317 to 357, the domain is characterized as EGF-like 3.
+At position 358 to 398, the domain is characterized as EGF-like 4.
+At position 21 to 335, the domain is characterized as Protein kinase.
+At position 579 to 681, the domain is characterized as tRNA-binding.
+At position 130 to 311, the domain is characterized as Helicase ATP-binding.
+At position 456 to 613, the domain is characterized as Helicase C-terminal.
+At position 648 to 738, the domain is characterized as Dicer dsRNA-binding fold.
+At position 888 to 1016, the domain is characterized as PAZ.
+At position 1054 to 1199, the domain is characterized as RNase III 1.
+At position 1250 to 1402, the domain is characterized as RNase III 2.
+At position 1436 to 1504, the domain is characterized as DRBM.
+At position 124 to 188, the domain is characterized as LIM zinc-binding 1.
+At position 250 to 313, the domain is characterized as LIM zinc-binding 3.
+At position 502 to 578, the domain is characterized as Cytochrome b5 heme-binding.
+At position 602 to 713, the domain is characterized as FAD-binding FR-type.
+At position 346 to 413, the domain is characterized as S4 RNA-binding.
+At position 267 to 426, the domain is characterized as Helicase ATP-binding.
+At position 445 to 610, the domain is characterized as Helicase C-terminal.
+At position 205 to 352, the domain is characterized as YDG.
+At position 432 to 490, the domain is characterized as Pre-SET.
+At position 493 to 637, the domain is characterized as SET.
+At position 170 to 363, the domain is characterized as CheB-type methylesterase.
+At position 161 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 348 to 414, the domain is characterized as S4 RNA-binding.
+At position 529 to 684, the domain is characterized as CBM3 1.
+At position 736 to 887, the domain is characterized as CBM3 2.
+At position 22 to 171, the domain is characterized as NAC.
+At position 358 to 594, the domain is characterized as TLDc.
+At position 230 to 284, the domain is characterized as HAMP.
+At position 289 to 525, the domain is characterized as Methyl-accepting transducer.
+At position 178 to 344, the domain is characterized as FCP1 homology.
+At position 629 to 728, the domain is characterized as BRCT.
+At position 3 to 169, the domain is characterized as EngA-type G 1.
+At position 1 to 71, the domain is characterized as Cytochrome b5 heme-binding.
+At position 59 to 282, the domain is characterized as SET.
+At position 419 to 594, the domain is characterized as Rab-GAP TBC.
+At position 474 to 522, the domain is characterized as GYF.
+At position 73 to 213, the domain is characterized as SCP.
+At position 277 to 470, the domain is characterized as B30.2/SPRY.
+At position 131 to 197, the domain is characterized as Mop 1.
+At position 202 to 268, the domain is characterized as Mop 2.
+At position 14 to 197, the domain is characterized as UmuC.
+At position 35 to 155, the domain is characterized as FZ.
+At position 172 to 295, the domain is characterized as NTR.
+At position 54 to 108, the domain is characterized as EF-hand 2.
+At position 117 to 146, the domain is characterized as EF-hand 3.
+At position 243 to 324, the domain is characterized as Toprim.
+At position 562 to 621, the domain is characterized as KH.
+At position 631 to 699, the domain is characterized as S1 motif.
+At position 432 to 598, the domain is characterized as Helicase C-terminal.
+At position 101 to 411, the domain is characterized as IF rod.
+At position 26 to 163, the domain is characterized as MOSC.
+At position 216 to 440, the domain is characterized as MIF4G.
+At position 616 to 738, the domain is characterized as MI.
+At position 453 to 807, the domain is characterized as HECT.
+At position 208 to 379, the domain is characterized as PX.
+At position 641 to 668, the domain is characterized as PLD phosphodiesterase 1.
+At position 941 to 968, the domain is characterized as PLD phosphodiesterase 2.
+At position 22 to 165, the domain is characterized as N-acetyltransferase.
+At position 277 to 326, the domain is characterized as bHLH.
+At position 547 to 606, the domain is characterized as KH.
+At position 616 to 684, the domain is characterized as S1 motif.
+At position 65 to 120, the domain is characterized as Tudor 1.
+At position 310 to 369, the domain is characterized as Tudor 2.
+At position 536 to 593, the domain is characterized as Tudor 3.
+At position 816 to 875, the domain is characterized as Tudor 4.
+At position 1033 to 1088, the domain is characterized as Tudor 5.
+At position 1352 to 1411, the domain is characterized as Tudor 6.
+At position 1567 to 1626, the domain is characterized as Tudor 7.
+At position 2026 to 2084, the domain is characterized as Tudor 8.
+At position 113 to 173, the domain is characterized as MIR 1.
+At position 174 to 224, the domain is characterized as MIR 2.
+At position 232 to 288, the domain is characterized as MIR 3.
+At position 295 to 372, the domain is characterized as MIR 4.
+At position 378 to 434, the domain is characterized as MIR 5.
+At position 23 to 275, the domain is characterized as Pyruvate carboxyltransferase.
+At position 47 to 94, the domain is characterized as F-box.
+At position 95 to 227, the domain is characterized as RUN.
+At position 25 to 177, the domain is characterized as N-acetyltransferase.
+At position 19 to 129, the domain is characterized as Ig-like V-type.
+At position 141 to 227, the domain is characterized as Ig-like C2-type.
+At position 70 to 165, the domain is characterized as Rieske.
+At position 11 to 193, the domain is characterized as PPIase cyclophilin-type.
+At position 95 to 152, the domain is characterized as CBS 1.
+At position 153 to 211, the domain is characterized as CBS 2.
+At position 2 to 194, the domain is characterized as Glutamine amidotransferase type-1.
+At position 621 to 736, the domain is characterized as SMC hinge.
+At position 330 to 536, the domain is characterized as MCM.
+At position 937 to 1076, the domain is characterized as MGS-like.
+At position 221 to 379, the domain is characterized as TrmE-type G.
+At position 586 to 823, the domain is characterized as ABC transporter.
+At position 275 to 453, the domain is characterized as GATase cobBQ-type.
+At position 126 to 230, the domain is characterized as Thioredoxin.
+At position 20 to 132, the domain is characterized as Thioredoxin.
+At position 24 to 147, the domain is characterized as EamA 1.
+At position 188 to 334, the domain is characterized as MOSC.
+At position 43 to 148, the domain is characterized as EH.
+At position 86 to 270, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 156, the domain is characterized as N-acetyltransferase 1.
+At position 153 to 297, the domain is characterized as N-acetyltransferase 2.
+At position 624 to 726, the domain is characterized as Fibronectin type-III 1.
+At position 757 to 842, the domain is characterized as Fibronectin type-III 2.
+At position 853 to 947, the domain is characterized as Fibronectin type-III 3.
+At position 1023 to 1298, the domain is characterized as Protein kinase.
+At position 980 to 1250, the domain is characterized as Autotransporter.
+At position 91 to 163, the domain is characterized as Bromo 1.
+At position 364 to 436, the domain is characterized as Bromo 2.
+At position 632 to 714, the domain is characterized as NET.
+At position 68 to 103, the domain is characterized as Tify.
+At position 383 to 437, the domain is characterized as MIR 1.
+At position 466 to 522, the domain is characterized as MIR 2.
+At position 537 to 595, the domain is characterized as MIR 3.
+At position 336 to 397, the domain is characterized as LIM zinc-binding 1.
+At position 401 to 461, the domain is characterized as LIM zinc-binding 2.
+At position 462 to 530, the domain is characterized as LIM zinc-binding 3.
+At position 278 to 314, the domain is characterized as EGF-like.
+At position 333 to 415, the domain is characterized as PAN.
+At position 496 to 781, the domain is characterized as Protein kinase.
+At position 2 to 122, the domain is characterized as MTTase N-terminal.
+At position 143 to 378, the domain is characterized as Radical SAM core.
+At position 106 to 505, the domain is characterized as Glutamine amidotransferase type-2.
+At position 49 to 215, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 42, the domain is characterized as Chitin-binding type-1 1.
+At position 43 to 85, the domain is characterized as Chitin-binding type-1 2.
+At position 86 to 128, the domain is characterized as Chitin-binding type-1 3.
+At position 129 to 171, the domain is characterized as Chitin-binding type-1 4.
+At position 154 to 303, the domain is characterized as N-acetyltransferase 2.
+At position 276 to 352, the domain is characterized as B5.
+At position 48 to 220, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 318 to 833, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 842 to 908, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 85 to 183, the domain is characterized as HTH araC/xylS-type.
+At position 105 to 183, the domain is characterized as RRM.
+At position 104 to 209, the domain is characterized as CBM21.
+At position 22 to 121, the domain is characterized as UPAR/Ly6.
+At position 29 to 147, the domain is characterized as EamA.
+At position 217 to 383, the domain is characterized as PCI.
+At position 24 to 104, the domain is characterized as Thioredoxin.
+At position 118 to 290, the domain is characterized as PITH.
+At position 29 to 63, the domain is characterized as Chitin-binding type-1.
+At position 155 to 331, the domain is characterized as Helicase ATP-binding.
+At position 345 to 515, the domain is characterized as Helicase C-terminal.
+At position 29 to 153, the domain is characterized as Thioredoxin.
+At position 488 to 746, the domain is characterized as ATP-grasp.
+At position 160 to 350, the domain is characterized as CheB-type methylesterase.
+At position 61 to 231, the domain is characterized as Helicase ATP-binding.
+At position 99 to 179, the domain is characterized as S4 RNA-binding.
+At position 125 to 199, the domain is characterized as TFIIS N-terminal.
+At position 34 to 74, the domain is characterized as CHCH.
+At position 6 to 48, the domain is characterized as SpoVT-AbrB 1.
+At position 36 to 285, the domain is characterized as ABC transporter.
+At position 389 to 651, the domain is characterized as ABC transmembrane type-2.
+At position 77 to 127, the domain is characterized as DHHC.
+At position 29 to 120, the domain is characterized as HIG1.
+At position 34 to 64, the domain is characterized as LRRNT.
+At position 145 to 197, the domain is characterized as LRRCT.
+At position 228 to 333, the domain is characterized as HD.
+At position 33 to 135, the domain is characterized as Glutaredoxin.
+At position 978 to 1054, the domain is characterized as Carrier 1.
+At position 2071 to 2147, the domain is characterized as Carrier 2.
+At position 32 to 117, the domain is characterized as ACB.
+At position 507 to 582, the domain is characterized as Carrier.
+At position 32 to 152, the domain is characterized as PX.
+At position 558 to 637, the domain is characterized as Carrier.
+At position 223 to 676, the domain is characterized as TROVE.
+At position 1162 to 1490, the domain is characterized as NACHT.
+At position 55 to 126, the domain is characterized as POTRA.
+At position 188 to 365, the domain is characterized as VWFA.
+At position 71 to 287, the domain is characterized as Radical SAM core.
+At position 110 to 179, the domain is characterized as SH3.
+At position 16 to 105, the domain is characterized as Acylphosphatase-like.
+At position 615 to 776, the domain is characterized as Helicase ATP-binding.
+At position 798 to 951, the domain is characterized as Helicase C-terminal.
+At position 84 to 265, the domain is characterized as Brix.
+At position 4 to 80, the domain is characterized as GIY-YIG.
+At position 26 to 191, the domain is characterized as PID.
+At position 9 to 128, the domain is characterized as C-type lectin.
+At position 61 to 388, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 395 to 721, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 5 to 102, the domain is characterized as Fibronectin type-III 1.
+At position 109 to 211, the domain is characterized as Fibronectin type-III 2.
+At position 1016 to 1091, the domain is characterized as Carrier 1.
+At position 2059 to 2133, the domain is characterized as Carrier 2.
+At position 113 to 148, the domain is characterized as EF-hand 1.
+At position 149 to 179, the domain is characterized as EF-hand 2.
+At position 180 to 215, the domain is characterized as EF-hand 3.
+At position 216 to 252, the domain is characterized as EF-hand 4.
+At position 253 to 282, the domain is characterized as EF-hand 5.
+At position 23 to 486, the domain is characterized as PPM-type phosphatase.
+At position 199 to 218, the domain is characterized as WH2.
+At position 31 to 205, the domain is characterized as BPL/LPL catalytic.
+At position 38 to 184, the domain is characterized as SIS.
+At position 211 to 267, the domain is characterized as CBS 1.
+At position 276 to 329, the domain is characterized as CBS 2.
+At position 4 to 273, the domain is characterized as CN hydrolase.
+At position 75 to 150, the domain is characterized as ACT.
+At position 54 to 172, the domain is characterized as Thioredoxin.
+At position 415 to 524, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 6 to 37, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 45 to 341, the domain is characterized as Calpain catalytic.
+At position 621 to 656, the domain is characterized as EF-hand.
+At position 1 to 150, the domain is characterized as IF rod.
+At position 49 to 199, the domain is characterized as Nudix hydrolase.
+At position 45 to 160, the domain is characterized as sHSP.
+At position 35 to 266, the domain is characterized as Peptidase S1.
+At position 611 to 769, the domain is characterized as MOSC.
+At position 527 to 628, the domain is characterized as tRNA-binding.
+At position 31 to 291, the domain is characterized as Protein kinase.
+At position 627 to 694, the domain is characterized as S1 motif.
+At position 483 to 540, the domain is characterized as HTH myb-type.
+At position 101 to 288, the domain is characterized as RNase H type-2.
+At position 69 to 220, the domain is characterized as N-acetyltransferase.
+At position 119 to 200, the domain is characterized as S1 motif 1.
+At position 338 to 410, the domain is characterized as S1 motif 2.
+At position 510 to 580, the domain is characterized as S1 motif 3.
+At position 607 to 676, the domain is characterized as S1 motif 4.
+At position 690 to 769, the domain is characterized as S1 motif 5.
+At position 794 to 863, the domain is characterized as S1 motif 6.
+At position 895 to 971, the domain is characterized as S1 motif 7.
+At position 1003 to 1083, the domain is characterized as S1 motif 8.
+At position 1088 to 1159, the domain is characterized as S1 motif 9.
+At position 1177 to 1245, the domain is characterized as S1 motif 10.
+At position 1265 to 1336, the domain is characterized as S1 motif 11.
+At position 64 to 222, the domain is characterized as Thioredoxin.
+At position 354 to 584, the domain is characterized as CBM11.
+At position 524 to 584, the domain is characterized as Dockerin.
+At position 4 to 374, the domain is characterized as Trm1 methyltransferase.
+At position 94 to 156, the domain is characterized as S4 RNA-binding.
+At position 110 to 360, the domain is characterized as Protein kinase.
+At position 126 to 177, the domain is characterized as DHHC.
+At position 368 to 619, the domain is characterized as Protein kinase.
+At position 353 to 449, the domain is characterized as Rhodanese.
+At position 57 to 307, the domain is characterized as Peptidase S6.
+At position 1098 to 1364, the domain is characterized as Autotransporter.
+At position 39 to 296, the domain is characterized as Alpha-carbonic anhydrase.
+At position 199 to 243, the domain is characterized as CHCH.
+At position 163 to 252, the domain is characterized as PPIase FKBP-type.
+At position 2 to 29, the domain is characterized as EGF-like.
+At position 4 to 115, the domain is characterized as PH.
+At position 145 to 249, the domain is characterized as IRS-type PTB.
+At position 157 to 304, the domain is characterized as C2 Aida-type.
+At position 212 to 290, the domain is characterized as RRM.
+At position 3 to 483, the domain is characterized as Hexokinase.
+At position 72 to 114, the domain is characterized as CUE.
+At position 229 to 347, the domain is characterized as HD.
+At position 122 to 448, the domain is characterized as G-alpha.
+At position 163 to 213, the domain is characterized as DHHC.
+At position 870 to 1155, the domain is characterized as Protein kinase.
+At position 17 to 118, the domain is characterized as Calponin-homology (CH).
+At position 472 to 800, the domain is characterized as Kinesin motor.
+At position 157 to 208, the domain is characterized as HAMP.
+At position 230 to 445, the domain is characterized as Histidine kinase.
+At position 24 to 331, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 34 to 223, the domain is characterized as RNase H type-2.
+At position 48 to 192, the domain is characterized as SCP.
+At position 81 to 783, the domain is characterized as USP.
+At position 9 to 202, the domain is characterized as Lon N-terminal.
+At position 636 to 835, the domain is characterized as Lon proteolytic.
+At position 31 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 219, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 316, the domain is characterized as Ig-like C2-type 3.
+At position 321 to 423, the domain is characterized as Ig-like C2-type 4.
+At position 428 to 525, the domain is characterized as Ig-like C2-type 5.
+At position 532 to 626, the domain is characterized as Fibronectin type-III 1.
+At position 644 to 745, the domain is characterized as Fibronectin type-III 2.
+At position 21 to 275, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 145 to 180, the domain is characterized as EF-hand 3.
+At position 607 to 664, the domain is characterized as RAP.
+At position 98 to 133, the domain is characterized as EF-hand 1.
+At position 134 to 169, the domain is characterized as EF-hand 2.
+At position 394 to 429, the domain is characterized as EF-hand 3.
+At position 24 to 60, the domain is characterized as EGF-like 1.
+At position 74 to 117, the domain is characterized as EGF-like 2.
+At position 119 to 155, the domain is characterized as EGF-like 3.
+At position 158 to 314, the domain is characterized as F5/8 type C 1.
+At position 319 to 476, the domain is characterized as F5/8 type C 2.
+At position 56 to 128, the domain is characterized as Bromo 1.
+At position 277 to 349, the domain is characterized as Bromo 2.
+At position 516 to 601, the domain is characterized as NET.
+At position 75 to 440, the domain is characterized as GBD/FH3.
+At position 586 to 747, the domain is characterized as FH1.
+At position 752 to 1154, the domain is characterized as FH2.
+At position 1177 to 1205, the domain is characterized as DAD.
+At position 104 to 355, the domain is characterized as Protein kinase.
+At position 22 to 110, the domain is characterized as DM10.
+At position 79 to 391, the domain is characterized as Peptidase A1.
+At position 21 to 240, the domain is characterized as Peptidase S1.
+At position 6 to 90, the domain is characterized as YcgL.
+At position 123 to 404, the domain is characterized as ABC transmembrane type-1 1.
+At position 478 to 702, the domain is characterized as ABC transporter 1.
+At position 792 to 1089, the domain is characterized as ABC transmembrane type-1 2.
+At position 1127 to 1361, the domain is characterized as ABC transporter 2.
+At position 22 to 197, the domain is characterized as DH.
+At position 227 to 331, the domain is characterized as PH.
+At position 7 to 179, the domain is characterized as Clp R.
+At position 34 to 101, the domain is characterized as BTB.
+At position 128 to 160, the domain is characterized as Gla.
+At position 128 to 210, the domain is characterized as S1 motif 1.
+At position 226 to 291, the domain is characterized as S1 motif 2.
+At position 314 to 384, the domain is characterized as S1 motif 3.
+At position 400 to 473, the domain is characterized as S1 motif 4.
+At position 490 to 557, the domain is characterized as S1 motif 5.
+At position 577 to 646, the domain is characterized as S1 motif 6.
+At position 661 to 733, the domain is characterized as S1 motif 7.
+At position 753 to 822, the domain is characterized as S1 motif 8.
+At position 866 to 930, the domain is characterized as S1 motif 9.
+At position 958 to 1031, the domain is characterized as S1 motif 10.
+At position 1054 to 1129, the domain is characterized as S1 motif 11.
+At position 1153 to 1224, the domain is characterized as S1 motif 12.
+At position 1260 to 1334, the domain is characterized as S1 motif 13.
+At position 1369 to 1438, the domain is characterized as S1 motif 14.
+At position 1459 to 1529, the domain is characterized as S1 motif 15.
+At position 266 to 510, the domain is characterized as ABC transporter 1.
+At position 587 to 802, the domain is characterized as ABC transporter 2.
+At position 110 to 396, the domain is characterized as ABC transmembrane type-1 1.
+At position 428 to 652, the domain is characterized as ABC transporter 1.
+At position 720 to 1010, the domain is characterized as ABC transmembrane type-1 2.
+At position 1047 to 1281, the domain is characterized as ABC transporter 2.
+At position 163 to 357, the domain is characterized as CheB-type methylesterase.
+At position 218 to 426, the domain is characterized as Histidine kinase.
+At position 526 to 632, the domain is characterized as Ricin B-type lectin.
+At position 102 to 416, the domain is characterized as Protein kinase.
+At position 60 to 140, the domain is characterized as UPAR/Ly6.
+At position 47 to 158, the domain is characterized as THUMP.
+At position 81 to 103, the domain is characterized as IQ.
+At position 546 to 581, the domain is characterized as EF-hand 1.
+At position 629 to 664, the domain is characterized as EF-hand 2.
+At position 669 to 704, the domain is characterized as EF-hand 3.
+At position 112 to 220, the domain is characterized as RRM 1.
+At position 228 to 312, the domain is characterized as RRM 2.
+At position 51 to 129, the domain is characterized as RRM 1.
+At position 137 to 217, the domain is characterized as RRM 2.
+At position 302 to 380, the domain is characterized as RRM 3.
+At position 118 to 306, the domain is characterized as ATP-grasp.
+At position 601 to 814, the domain is characterized as FtsK.
+At position 32 to 75, the domain is characterized as P-type.
+At position 50 to 354, the domain is characterized as Asparaginase/glutaminase.
+At position 221 to 291, the domain is characterized as KRAB.
+At position 1 to 91, the domain is characterized as BRCT.
+At position 185 to 239, the domain is characterized as Myb-like.
+At position 173 to 575, the domain is characterized as SAC.
+At position 76 to 160, the domain is characterized as LITAF.
+At position 2 to 113, the domain is characterized as Toprim.
+At position 115 to 272, the domain is characterized as Upf1 CH-rich.
+At position 30 to 188, the domain is characterized as Helicase ATP-binding.
+At position 641 to 676, the domain is characterized as UVR.
+At position 1 to 83, the domain is characterized as YcgL.
+At position 1 to 108, the domain is characterized as C2.
+At position 220 to 282, the domain is characterized as CBS 1.
+At position 284 to 344, the domain is characterized as CBS 2.
+At position 60 to 164, the domain is characterized as THUMP.
+At position 184 to 234, the domain is characterized as DHHC.
+At position 222 to 286, the domain is characterized as PWWP 1.
+At position 880 to 942, the domain is characterized as PWWP 2.
+At position 1011 to 1061, the domain is characterized as AWS.
+At position 1063 to 1180, the domain is characterized as SET.
+At position 1187 to 1203, the domain is characterized as Post-SET.
+At position 1 to 492, the domain is characterized as SMP-LTD.
+At position 1 to 101, the domain is characterized as HPt.
+At position 330 to 541, the domain is characterized as Histidine kinase.
+At position 543 to 668, the domain is characterized as CheW-like.
+At position 11 to 256, the domain is characterized as Lon N-terminal.
+At position 693 to 878, the domain is characterized as Lon proteolytic.
+At position 111 to 184, the domain is characterized as PRC barrel.
+At position 5 to 181, the domain is characterized as UmuC.
+At position 60 to 267, the domain is characterized as ABC transmembrane type-1.
+At position 195 to 248, the domain is characterized as KBD.
+At position 303 to 411, the domain is characterized as SPR.
+At position 59 to 143, the domain is characterized as KH-like.
+At position 617 to 769, the domain is characterized as RNase NYN.
+At position 22 to 117, the domain is characterized as Ig-like.
+At position 1 to 133, the domain is characterized as CID.
+At position 219 to 297, the domain is characterized as RRM 2.
+At position 160 to 324, the domain is characterized as GOLD.
+At position 610 to 689, the domain is characterized as BRCT.
+At position 5 to 133, the domain is characterized as Galectin.
+At position 1 to 280, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 276 to 584, the domain is characterized as UvrD-like helicase C-terminal.
+At position 145 to 520, the domain is characterized as PI3K/PI4K catalytic.
+At position 4 to 187, the domain is characterized as YrdC-like.
+At position 234 to 375, the domain is characterized as Helicase ATP-binding.
+At position 399 to 549, the domain is characterized as Helicase C-terminal.
+At position 641 to 817, the domain is characterized as PCI.
+At position 233 to 308, the domain is characterized as PUA.
+At position 28 to 222, the domain is characterized as RNase H type-2.
+At position 255 to 412, the domain is characterized as GAF 1.
+At position 444 to 625, the domain is characterized as GAF 2.
+At position 655 to 978, the domain is characterized as PDEase.
+At position 41 to 254, the domain is characterized as Radical SAM core.
+At position 62 to 198, the domain is characterized as Nudix hydrolase.
+At position 120 to 318, the domain is characterized as ATP-grasp.
+At position 54 to 101, the domain is characterized as F-box.
+At position 162 to 251, the domain is characterized as 5'-3' exonuclease.
+At position 120 to 541, the domain is characterized as Myotubularin phosphatase.
+At position 28 to 123, the domain is characterized as CTCK.
+At position 240 to 480, the domain is characterized as CN hydrolase.
+At position 177 to 205, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 4 to 240, the domain is characterized as PABS.
+At position 35 to 98, the domain is characterized as bZIP.
+At position 1 to 223, the domain is characterized as FAD-binding PCMH-type.
+At position 119 to 312, the domain is characterized as ATP-grasp.
+At position 412 to 497, the domain is characterized as PDZ 1.
+At position 534 to 619, the domain is characterized as PDZ 2.
+At position 35 to 271, the domain is characterized as ABC transporter 1.
+At position 281 to 520, the domain is characterized as ABC transporter 2.
+At position 98 to 166, the domain is characterized as S4 RNA-binding.
+At position 8 to 88, the domain is characterized as ACT.
+At position 9 to 68, the domain is characterized as TRAM.
+At position 252 to 378, the domain is characterized as Thioredoxin.
+At position 302 to 471, the domain is characterized as tr-type G.
+At position 43 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 31 to 88, the domain is characterized as bHLH.
+At position 107 to 136, the domain is characterized as Orange.
+At position 44 to 356, the domain is characterized as PPM-type phosphatase.
+At position 199 to 402, the domain is characterized as ABC transmembrane type-1.
+At position 120 to 299, the domain is characterized as FAD-binding PCMH-type.
+At position 96 to 343, the domain is characterized as PPM-type phosphatase.
+At position 7 to 162, the domain is characterized as N-acetyltransferase.
+At position 46 to 205, the domain is characterized as E1.
+At position 308 to 366, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 375 to 566, the domain is characterized as E2.
+At position 25 to 104, the domain is characterized as GIY-YIG.
+At position 264 to 383, the domain is characterized as YkuD.
+At position 75 to 226, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 46 to 134, the domain is characterized as Cyclin N-terminal.
+At position 117 to 185, the domain is characterized as COMM.
+At position 237 to 257, the domain is characterized as BRCT 1.
+At position 586 to 664, the domain is characterized as BRCT 2.
+At position 11 to 95, the domain is characterized as Sm.
+At position 85 to 246, the domain is characterized as CP-type G.
+At position 248 to 500, the domain is characterized as Velvet.
+At position 25 to 308, the domain is characterized as Protein kinase.
+At position 1727 to 1756, the domain is characterized as IQ.
+At position 3 to 351, the domain is characterized as Kinesin motor.
+At position 500 to 566, the domain is characterized as FHA.
+At position 1538 to 1636, the domain is characterized as PH.
+At position 28 to 243, the domain is characterized as Brix.
+At position 54 to 154, the domain is characterized as Glutaredoxin.
+At position 139 to 482, the domain is characterized as Protein kinase.
+At position 601 to 679, the domain is characterized as Carrier.
+At position 6 to 115, the domain is characterized as Thioredoxin.
+At position 119 to 409, the domain is characterized as ABC transmembrane type-1.
+At position 443 to 679, the domain is characterized as ABC transporter.
+At position 5 to 65, the domain is characterized as LIM zinc-binding.
+At position 119 to 445, the domain is characterized as SAC.
+At position 48 to 273, the domain is characterized as Peptidase S1.
+At position 3 to 151, the domain is characterized as UBC core.
+At position 236 to 464, the domain is characterized as tr-type G.
+At position 48 to 112, the domain is characterized as BTB.
+At position 12 to 82, the domain is characterized as PAS 1.
+At position 212 to 264, the domain is characterized as PAC 1.
+At position 265 to 335, the domain is characterized as PAS 2.
+At position 338 to 390, the domain is characterized as PAC 2.
+At position 428 to 561, the domain is characterized as GGDEF.
+At position 570 to 820, the domain is characterized as EAL.
+At position 325 to 434, the domain is characterized as ERCC4.
+At position 34 to 236, the domain is characterized as Rab-GAP TBC.
+At position 343 to 516, the domain is characterized as TLDc.
+At position 558 to 875, the domain is characterized as Protein kinase.
+At position 872 to 1002, the domain is characterized as Guanylate cyclase.
+At position 44 to 92, the domain is characterized as EGF-like 1.
+At position 94 to 133, the domain is characterized as EGF-like 2.
+At position 309 to 348, the domain is characterized as EGF-like 3.
+At position 349 to 390, the domain is characterized as EGF-like 4.
+At position 392 to 428, the domain is characterized as EGF-like 5.
+At position 430 to 466, the domain is characterized as EGF-like 6.
+At position 468 to 503, the domain is characterized as EGF-like 7.
+At position 505 to 541, the domain is characterized as EGF-like 8; calcium-binding.
+At position 543 to 579, the domain is characterized as EGF-like 9.
+At position 546 to 568, the domain is characterized as Follistatin-like.
+At position 581 to 617, the domain is characterized as EGF-like 10; calcium-binding.
+At position 4 to 166, the domain is characterized as N-acetyltransferase.
+At position 315 to 367, the domain is characterized as bHLH.
+At position 81 to 135, the domain is characterized as Kazal-like.
+At position 250 to 338, the domain is characterized as Ig-like 1.
+At position 63 to 213, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 43 to 309, the domain is characterized as PPM-type phosphatase.
+At position 1 to 75, the domain is characterized as Disintegrin.
+At position 9 to 222, the domain is characterized as ABC transporter.
+At position 39 to 379, the domain is characterized as G-alpha.
+At position 75 to 177, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 33 to 93, the domain is characterized as v-SNARE coiled-coil homology.
+At position 124 to 252, the domain is characterized as Fatty acid hydroxylase.
+At position 6 to 118, the domain is characterized as HotDog ACOT-type 1.
+At position 180 to 295, the domain is characterized as HotDog ACOT-type 2.
+At position 327 to 536, the domain is characterized as START.
+At position 149 to 183, the domain is characterized as SAP.
+At position 322 to 378, the domain is characterized as DEK-C.
+At position 31 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 5 to 109, the domain is characterized as Glutaredoxin.
+At position 632 to 773, the domain is characterized as Tyrosine-protein phosphatase.
+At position 43 to 368, the domain is characterized as Kinesin motor.
+At position 127 to 219, the domain is characterized as WSC 1.
+At position 230 to 324, the domain is characterized as WSC 2.
+At position 132 to 293, the domain is characterized as Exonuclease.
+At position 1 to 58, the domain is characterized as POTRA.
+At position 578 to 745, the domain is characterized as tr-type G.
+At position 768 to 849, the domain is characterized as PKD.
+At position 479 to 651, the domain is characterized as tr-type G.
+At position 51 to 194, the domain is characterized as PI-PLC X-box.
+At position 22 to 325, the domain is characterized as F-BAR.
+At position 489 to 679, the domain is characterized as Rho-GAP.
+At position 728 to 787, the domain is characterized as SH3.
+At position 4 to 66, the domain is characterized as TRAM.
+At position 339 to 402, the domain is characterized as SH3.
+At position 216 to 302, the domain is characterized as Core-binding (CB).
+At position 326 to 513, the domain is characterized as Tyr recombinase.
+At position 16 to 207, the domain is characterized as RNase H type-2.
+At position 2 to 139, the domain is characterized as ADF-H 1.
+At position 175 to 313, the domain is characterized as ADF-H 2.
+At position 38 to 169, the domain is characterized as Nudix hydrolase.
+At position 69 to 171, the domain is characterized as MRH.
+At position 176 to 279, the domain is characterized as DMAP1-binding.
+At position 65 to 252, the domain is characterized as ABC transmembrane type-1.
+At position 193 to 233, the domain is characterized as UBA.
+At position 555 to 615, the domain is characterized as Tudor.
+At position 415 to 596, the domain is characterized as RHD.
+At position 889 to 1033, the domain is characterized as TIR.
+At position 545 to 604, the domain is characterized as KH.
+At position 614 to 684, the domain is characterized as S1 motif.
+At position 40 to 317, the domain is characterized as tr-type G.
+At position 160 to 225, the domain is characterized as PPIase FKBP-type.
+At position 135 to 266, the domain is characterized as Fatty acid hydroxylase.
+At position 29 to 92, the domain is characterized as bZIP.
+At position 202 to 359, the domain is characterized as Cupin type-1.
+At position 49 to 110, the domain is characterized as Sushi 1.
+At position 111 to 172, the domain is characterized as Sushi 2.
+At position 173 to 236, the domain is characterized as Sushi 3.
+At position 297 to 362, the domain is characterized as Sushi 5.
+At position 363 to 424, the domain is characterized as Sushi 6.
+At position 425 to 482, the domain is characterized as Sushi 7.
+At position 483 to 540, the domain is characterized as Sushi 8.
+At position 130 to 308, the domain is characterized as CNNM transmembrane.
+At position 318 to 379, the domain is characterized as CBS 1.
+At position 386 to 452, the domain is characterized as CBS 2.
+At position 480 to 551, the domain is characterized as FHA.
+At position 1 to 71, the domain is characterized as Disintegrin.
+At position 12 to 70, the domain is characterized as HTH tetR-type.
+At position 165 to 268, the domain is characterized as BACK.
+At position 34 to 96, the domain is characterized as BTB.
+At position 184 to 291, the domain is characterized as Ig-like.
+At position 282 to 488, the domain is characterized as B30.2/SPRY.
+At position 21 to 109, the domain is characterized as EH 1.
+At position 53 to 88, the domain is characterized as EF-hand 1.
+At position 221 to 310, the domain is characterized as EH 2.
+At position 254 to 289, the domain is characterized as EF-hand 2.
+At position 738 to 799, the domain is characterized as SH3 1.
+At position 906 to 964, the domain is characterized as SH3 2.
+At position 995 to 1053, the domain is characterized as SH3 3.
+At position 1067 to 1131, the domain is characterized as SH3 4.
+At position 1148 to 1207, the domain is characterized as SH3 5.
+At position 1230 to 1416, the domain is characterized as DH.
+At position 1455 to 1564, the domain is characterized as PH.
+At position 1572 to 1688, the domain is characterized as C2.
+At position 562 to 888, the domain is characterized as Protein kinase.
+At position 959 to 1089, the domain is characterized as Guanylate cyclase.
+At position 209 to 432, the domain is characterized as NR LBD.
+At position 58 to 199, the domain is characterized as DAGKc.
+At position 104 to 300, the domain is characterized as ATP-grasp.
+At position 1 to 61, the domain is characterized as 4Fe-4S.
+At position 14 to 183, the domain is characterized as N-acetyltransferase.
+At position 40 to 314, the domain is characterized as Protein kinase.
+At position 399 to 566, the domain is characterized as Phosphatase tensin-type.
+At position 572 to 710, the domain is characterized as C2 tensin-type.
+At position 1247 to 1311, the domain is characterized as J.
+At position 28 to 98, the domain is characterized as PAS.
+At position 102 to 155, the domain is characterized as PAC.
+At position 187 to 318, the domain is characterized as GGDEF.
+At position 32 to 116, the domain is characterized as MANSC.
+At position 32 to 151, the domain is characterized as FZ.
+At position 65 to 168, the domain is characterized as PH.
+At position 178 to 213, the domain is characterized as EF-hand 1.
+At position 214 to 249, the domain is characterized as EF-hand 2.
+At position 246 to 281, the domain is characterized as EF-hand 3.
+At position 333 to 478, the domain is characterized as PI-PLC X-box.
+At position 524 to 640, the domain is characterized as PI-PLC Y-box.
+At position 636 to 765, the domain is characterized as C2.
+At position 1 to 105, the domain is characterized as VPS28 N-terminal.
+At position 109 to 205, the domain is characterized as VPS28 C-terminal.
+At position 36 to 217, the domain is characterized as SSD.
+At position 44 to 186, the domain is characterized as SIS.
+At position 53 to 307, the domain is characterized as TSP type-1 1.
+At position 676 to 737, the domain is characterized as TSP type-1 2.
+At position 739 to 792, the domain is characterized as TSP type-1 3.
+At position 793 to 851, the domain is characterized as TSP type-1 4.
+At position 852 to 911, the domain is characterized as TSP type-1 5.
+At position 912 to 968, the domain is characterized as TSP type-1 6.
+At position 971 to 1008, the domain is characterized as PLAC.
+At position 27 to 123, the domain is characterized as Ig-like.
+At position 126 to 221, the domain is characterized as Fibronectin type-III 1.
+At position 226 to 319, the domain is characterized as Fibronectin type-III 2.
+At position 320 to 415, the domain is characterized as Fibronectin type-III 3.
+At position 423 to 519, the domain is characterized as Fibronectin type-III 4.
+At position 521 to 620, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 77, the domain is characterized as BMV.
+At position 14 to 188, the domain is characterized as C2 PI3K-type.
+At position 293 to 526, the domain is characterized as PIK helical.
+At position 593 to 859, the domain is characterized as PI3K/PI4K catalytic.
+At position 276 to 362, the domain is characterized as PPIase FKBP-type.
+At position 633 to 1009, the domain is characterized as TTL.
+At position 1 to 85, the domain is characterized as STAS.
+At position 7 to 243, the domain is characterized as ABC transporter 1.
+At position 254 to 496, the domain is characterized as ABC transporter 2.
+At position 3 to 48, the domain is characterized as F-box.
+At position 249 to 500, the domain is characterized as Protein kinase.
+At position 34 to 152, the domain is characterized as C-type lectin.
+At position 910 to 980, the domain is characterized as Bromo.
+At position 20 to 96, the domain is characterized as Saposin B-type.
+At position 18 to 150, the domain is characterized as ENTH.
+At position 15 to 144, the domain is characterized as RNase III.
+At position 169 to 238, the domain is characterized as DRBM.
+At position 219 to 406, the domain is characterized as Glutamine amidotransferase type-1.
+At position 53 to 201, the domain is characterized as Tyrosine-protein phosphatase.
+At position 186 to 299, the domain is characterized as PH.
+At position 409 to 507, the domain is characterized as SH2.
+At position 119 to 219, the domain is characterized as HD.
+At position 473 to 508, the domain is characterized as EF-hand 1.
+At position 510 to 542, the domain is characterized as EF-hand 2.
+At position 336 to 396, the domain is characterized as MIR 1.
+At position 408 to 467, the domain is characterized as MIR 2.
+At position 474 to 529, the domain is characterized as MIR 3.
+At position 220 to 381, the domain is characterized as TrmE-type G.
+At position 3 to 156, the domain is characterized as Thioredoxin.
+At position 357 to 618, the domain is characterized as Pterin-binding.
+At position 651 to 745, the domain is characterized as B12-binding N-terminal.
+At position 747 to 882, the domain is characterized as B12-binding.
+At position 898 to 1226, the domain is characterized as AdoMet activation.
+At position 252 to 420, the domain is characterized as TLDc.
+At position 30 to 121, the domain is characterized as Ig-like.
+At position 58 to 155, the domain is characterized as PH.
+At position 78 to 148, the domain is characterized as HTH iclR-type.
+At position 396 to 466, the domain is characterized as ACT.
+At position 228 to 291, the domain is characterized as bZIP.
+At position 28 to 142, the domain is characterized as Response regulatory.
+At position 158 to 223, the domain is characterized as HTH luxR-type.
+At position 411 to 459, the domain is characterized as G-patch.
+At position 574 to 663, the domain is characterized as BRCT.
+At position 4 to 73, the domain is characterized as DRBM 1.
+At position 171 to 244, the domain is characterized as DRBM 2.
+At position 391 to 563, the domain is characterized as Helicase ATP-binding.
+At position 645 to 818, the domain is characterized as Helicase C-terminal.
+At position 116 to 206, the domain is characterized as RRM.
+At position 698 to 802, the domain is characterized as Bromo.
+At position 363 to 592, the domain is characterized as START.
+At position 150 to 341, the domain is characterized as Histidine kinase.
+At position 26 to 145, the domain is characterized as Peptidase C39.
+At position 176 to 458, the domain is characterized as ABC transmembrane type-1.
+At position 492 to 698, the domain is characterized as ABC transporter.
+At position 136 to 258, the domain is characterized as MPN.
+At position 23 to 129, the domain is characterized as CMP/dCMP-type deaminase.
+At position 78 to 132, the domain is characterized as HAMP 1.
+At position 192 to 247, the domain is characterized as HAMP 2.
+At position 266 to 502, the domain is characterized as Methyl-accepting transducer.
+At position 68 to 330, the domain is characterized as Protein kinase.
+At position 13 to 132, the domain is characterized as C-type lectin.
+At position 428 to 462, the domain is characterized as PLD phosphodiesterase 1.
+At position 585 to 615, the domain is characterized as PLD phosphodiesterase 2.
+At position 24 to 179, the domain is characterized as N-acetyltransferase.
+At position 64 to 139, the domain is characterized as Carrier.
+At position 6 to 256, the domain is characterized as Pyruvate carboxyltransferase.
+At position 24 to 195, the domain is characterized as Helicase ATP-binding.
+At position 428 to 581, the domain is characterized as Helicase C-terminal.
+At position 98 to 336, the domain is characterized as Radical SAM core.
+At position 17 to 193, the domain is characterized as PI-PLC X-box.
+At position 33 to 255, the domain is characterized as Peptidase S1.
+At position 67 to 147, the domain is characterized as PA.
+At position 14 to 176, the domain is characterized as PPIase cyclophilin-type.
+At position 284 to 347, the domain is characterized as bZIP.
+At position 89 to 256, the domain is characterized as Helicase ATP-binding.
+At position 432 to 649, the domain is characterized as Helicase C-terminal.
+At position 20 to 145, the domain is characterized as RNase III.
+At position 461 to 670, the domain is characterized as FtsK.
+At position 289 to 484, the domain is characterized as B30.2/SPRY.
+At position 14 to 56, the domain is characterized as JmjN.
+At position 142 to 308, the domain is characterized as JmjC.
+At position 897 to 954, the domain is characterized as Tudor 1.
+At position 955 to 1011, the domain is characterized as Tudor 2.
+At position 56 to 193, the domain is characterized as Nudix hydrolase.
+At position 45 to 253, the domain is characterized as BPL/LPL catalytic.
+At position 679 to 1002, the domain is characterized as HECT.
+At position 11 to 121, the domain is characterized as PX.
+At position 248 to 600, the domain is characterized as Peptidase S53.
+At position 4 to 70, the domain is characterized as PQ-loop 1.
+At position 154 to 208, the domain is characterized as PQ-loop 2.
+At position 654 to 717, the domain is characterized as bZIP.
+At position 38 to 774, the domain is characterized as PFL.
+At position 782 to 902, the domain is characterized as Glycine radical.
+At position 38 to 186, the domain is characterized as Thioredoxin.
+At position 108 to 192, the domain is characterized as MEIS N-terminal.
+At position 29 to 378, the domain is characterized as GH18.
+At position 404 to 462, the domain is characterized as Chitin-binding type-2.
+At position 53 to 117, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 282 to 407, the domain is characterized as DBINO.
+At position 532 to 703, the domain is characterized as Helicase ATP-binding.
+At position 1108 to 1263, the domain is characterized as Helicase C-terminal.
+At position 20 to 278, the domain is characterized as Alpha-carbonic anhydrase.
+At position 79 to 159, the domain is characterized as ACT.
+At position 297 to 331, the domain is characterized as STI1 1.
+At position 373 to 412, the domain is characterized as STI1 2.
+At position 121 to 307, the domain is characterized as PH.
+At position 328 to 448, the domain is characterized as Arf-GAP.
+At position 84 to 284, the domain is characterized as Laminin G-like.
+At position 41 to 341, the domain is characterized as Protein kinase.
+At position 41 to 251, the domain is characterized as ThyX.
+At position 60 to 378, the domain is characterized as Protein kinase.
+At position 1 to 98, the domain is characterized as SSB.
+At position 54 to 379, the domain is characterized as G-alpha.
+At position 3 to 221, the domain is characterized as Radical SAM core.
+At position 47 to 150, the domain is characterized as THUMP.
+At position 158 to 343, the domain is characterized as Rab-GAP TBC.
+At position 33 to 97, the domain is characterized as NAC-A/B.
+At position 1222 to 1367, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1755 to 1911, the domain is characterized as DOD-type homing endonuclease 2.
+At position 17 to 106, the domain is characterized as PDZ 1.
+At position 249 to 332, the domain is characterized as PDZ 2.
+At position 364 to 448, the domain is characterized as PDZ 3.
+At position 489 to 577, the domain is characterized as PDZ 4.
+At position 584 to 664, the domain is characterized as PDZ 5.
+At position 43 to 150, the domain is characterized as Cytochrome c.
+At position 100 to 411, the domain is characterized as IF rod.
+At position 29 to 87, the domain is characterized as BTB.
+At position 8 to 121, the domain is characterized as MTTase N-terminal.
+At position 131 to 358, the domain is characterized as Radical SAM core.
+At position 41 to 222, the domain is characterized as Helicase ATP-binding.
+At position 388 to 561, the domain is characterized as Helicase C-terminal.
+At position 534 to 626, the domain is characterized as Dicer dsRNA-binding fold.
+At position 798 to 913, the domain is characterized as PAZ.
+At position 940 to 1095, the domain is characterized as RNase III 1.
+At position 1132 to 1276, the domain is characterized as RNase III 2.
+At position 1302 to 1367, the domain is characterized as DRBM.
+At position 694 to 786, the domain is characterized as FDX-ACB.
+At position 19 to 207, the domain is characterized as Albumin 1.
+At position 208 to 398, the domain is characterized as Albumin 2.
+At position 399 to 597, the domain is characterized as Albumin 3.
+At position 46 to 227, the domain is characterized as PCI.
+At position 32 to 267, the domain is characterized as ABC transporter 1.
+At position 267 to 518, the domain is characterized as ABC transporter 2.
+At position 1 to 24, the domain is characterized as LCN-type CS-alpha/beta.
+At position 6 to 240, the domain is characterized as ABC transporter.
+At position 440 to 754, the domain is characterized as Protein kinase.
+At position 114 to 270, the domain is characterized as Thioredoxin.
+At position 2 to 85, the domain is characterized as Core-binding (CB).
+At position 227 to 416, the domain is characterized as FAD-binding PCMH-type.
+At position 208 to 325, the domain is characterized as OmpA-like.
+At position 121 to 402, the domain is characterized as Protein kinase.
+At position 50 to 105, the domain is characterized as HTH myb-type 1.
+At position 106 to 156, the domain is characterized as HTH myb-type 2.
+At position 569 to 649, the domain is characterized as BRCT.
+At position 155 to 383, the domain is characterized as START.
+At position 75 to 443, the domain is characterized as PIPK.
+At position 583 to 720, the domain is characterized as RanBD1.
+At position 79 to 167, the domain is characterized as PB1.
+At position 451 to 558, the domain is characterized as SH2.
+At position 585 to 711, the domain is characterized as PTB.
+At position 24 to 104, the domain is characterized as IGFBP N-terminal.
+At position 182 to 256, the domain is characterized as Thyroglobulin type-1.
+At position 22 to 145, the domain is characterized as Bulb-type lectin.
+At position 283 to 321, the domain is characterized as EGF-like; atypical.
+At position 340 to 423, the domain is characterized as PAN.
+At position 512 to 798, the domain is characterized as Protein kinase.
+At position 201 to 381, the domain is characterized as EngA-type G 2.
+At position 382 to 468, the domain is characterized as KH-like.
+At position 189 to 366, the domain is characterized as tr-type G.
+At position 136 to 165, the domain is characterized as IQ.
+At position 167 to 408, the domain is characterized as Protein kinase.
+At position 9 to 283, the domain is characterized as tr-type G.
+At position 145 to 282, the domain is characterized as Fatty acid hydroxylase.
+At position 233 to 303, the domain is characterized as SUZ.
+At position 8 to 291, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 102 to 137, the domain is characterized as EGF-like.
+At position 140 to 197, the domain is characterized as Sushi 1.
+At position 198 to 256, the domain is characterized as Sushi 2.
+At position 258 to 323, the domain is characterized as Sushi 3.
+At position 325 to 421, the domain is characterized as LCCL.
+At position 436 to 568, the domain is characterized as C-type lectin.
+At position 574 to 636, the domain is characterized as Sushi 4.
+At position 689 to 750, the domain is characterized as Sushi 5.
+At position 763 to 1019, the domain is characterized as Peptidase S1.
+At position 38 to 271, the domain is characterized as ABC transporter.
+At position 73 to 208, the domain is characterized as MPN.
+At position 8 to 155, the domain is characterized as N-acetyltransferase.
+At position 34 to 303, the domain is characterized as GP-PDE.
+At position 17 to 312, the domain is characterized as SET.
+At position 8 to 157, the domain is characterized as Ferritin-like diiron.
+At position 49 to 303, the domain is characterized as Protein kinase.
+At position 304 to 358, the domain is characterized as AGC-kinase C-terminal.
+At position 66 to 126, the domain is characterized as SH3 2.
+At position 145 to 204, the domain is characterized as SH3 3.
+At position 243 to 302, the domain is characterized as SH3 4.
+At position 784 to 967, the domain is characterized as DH.
+At position 1008 to 1217, the domain is characterized as BAR.
+At position 1285 to 1348, the domain is characterized as SH3 5.
+At position 1513 to 1576, the domain is characterized as SH3 6.
+At position 2 to 416, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 70 to 145, the domain is characterized as Rho RNA-BD.
+At position 141 to 178, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 280 to 439, the domain is characterized as Helicase C-terminal.
+At position 387 to 486, the domain is characterized as BRCT.
+At position 29 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 38 to 101, the domain is characterized as S4 RNA-binding.
+At position 488 to 748, the domain is characterized as Protein kinase.
+At position 823 to 953, the domain is characterized as Guanylate cyclase.
+At position 301 to 396, the domain is characterized as CS.
+At position 1 to 78, the domain is characterized as HTH rpiR-type.
+At position 123 to 263, the domain is characterized as SIS.
+At position 77 to 205, the domain is characterized as DOD-type homing endonuclease.
+At position 68 to 231, the domain is characterized as SIS.
+At position 34 to 239, the domain is characterized as N-acetyltransferase.
+At position 107 to 511, the domain is characterized as Glutamine amidotransferase type-2.
+At position 26 to 143, the domain is characterized as Ig-like C2-type 1.
+At position 160 to 284, the domain is characterized as Ig-like C2-type 2.
+At position 301 to 422, the domain is characterized as Ig-like C2-type 3.
+At position 429 to 554, the domain is characterized as Ig-like C2-type 4.
+At position 25 to 138, the domain is characterized as Cystatin fetuin-B-type 1.
+At position 149 to 255, the domain is characterized as Cystatin fetuin-B-type 2.
+At position 1016 to 1078, the domain is characterized as SH3.
+At position 191 to 376, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 154, the domain is characterized as Flavodoxin-like.
+At position 308 to 650, the domain is characterized as PUM-HD.
+At position 30 to 513, the domain is characterized as Sema.
+At position 573 to 659, the domain is characterized as Ig-like C2-type.
+At position 17 to 144, the domain is characterized as EamA 1.
+At position 169 to 292, the domain is characterized as EamA 2.
+At position 84 to 136, the domain is characterized as HAMP 1.
+At position 157 to 210, the domain is characterized as HAMP 2.
+At position 229 to 465, the domain is characterized as Methyl-accepting transducer.
+At position 14 to 357, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 366 to 690, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 62 to 92, the domain is characterized as EF-hand 2.
+At position 36 to 141, the domain is characterized as Gnk2-homologous.
+At position 229 to 367, the domain is characterized as TrmE-type G.
+At position 18 to 206, the domain is characterized as RNase H type-2.
+At position 140 to 198, the domain is characterized as TCP.
+At position 2 to 242, the domain is characterized as CN hydrolase.
+At position 49 to 223, the domain is characterized as EngB-type G.
+At position 10 to 177, the domain is characterized as MH1.
+At position 275 to 468, the domain is characterized as MH2.
+At position 855 to 1043, the domain is characterized as Rho-GAP.
+At position 960 to 996, the domain is characterized as EGF-like 1.
+At position 998 to 1034, the domain is characterized as EGF-like 2; calcium-binding.
+At position 1036 to 1165, the domain is characterized as C-type lectin.
+At position 1165 to 1225, the domain is characterized as Sushi.
+At position 120 to 609, the domain is characterized as Peptidase S8.
+At position 4 to 480, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 523 to 820, the domain is characterized as UvrD-like helicase C-terminal.
+At position 119 to 152, the domain is characterized as EF-hand 4.
+At position 757 to 786, the domain is characterized as IQ 1.
+At position 799 to 828, the domain is characterized as IQ 2.
+At position 875 to 904, the domain is characterized as IQ 3.
+At position 161 to 271, the domain is characterized as TBDR plug.
+At position 276 to 815, the domain is characterized as TBDR beta-barrel.
+At position 259 to 368, the domain is characterized as SEA.
+At position 14 to 196, the domain is characterized as tr-type G.
+At position 4 to 151, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 13 to 140, the domain is characterized as C-type lectin.
+At position 821 to 901, the domain is characterized as ERCC4.
+At position 14 to 101, the domain is characterized as STAS.
+At position 44 to 171, the domain is characterized as Cyclin N-terminal.
+At position 92 to 377, the domain is characterized as ABC transmembrane type-1 1.
+At position 9 to 216, the domain is characterized as YjeF N-terminal.
+At position 181 to 242, the domain is characterized as CBS 1.
+At position 265 to 323, the domain is characterized as CBS 2.
+At position 350 to 409, the domain is characterized as CBS 3.
+At position 429 to 501, the domain is characterized as CBS 4.
+At position 8 to 237, the domain is characterized as ABC transporter.
+At position 125 to 436, the domain is characterized as Protein kinase.
+At position 40 to 89, the domain is characterized as F-box.
+At position 21 to 84, the domain is characterized as S5 DRBM.
+At position 660 to 739, the domain is characterized as BRCT.
+At position 178 to 252, the domain is characterized as ACT.
+At position 290 to 543, the domain is characterized as Protein kinase.
+At position 602 to 683, the domain is characterized as BRCT.
+At position 51 to 253, the domain is characterized as MARVEL.
+At position 396 to 504, the domain is characterized as OCEL.
+At position 516 to 720, the domain is characterized as ATP-grasp.
+At position 1 to 54, the domain is characterized as F-box.
+At position 345 to 408, the domain is characterized as FBD.
+At position 147 to 257, the domain is characterized as OCEL.
+At position 81 to 132, the domain is characterized as bHLH.
+At position 3 to 132, the domain is characterized as PINc.
+At position 584 to 666, the domain is characterized as BRCT.
+At position 181 to 258, the domain is characterized as KH.
+At position 263 to 328, the domain is characterized as R3H.
+At position 29 to 135, the domain is characterized as Gnk2-homologous 1.
+At position 146 to 453, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 124 to 157, the domain is characterized as WW.
+At position 16 to 145, the domain is characterized as RNase III.
+At position 39 to 140, the domain is characterized as Ig-like V-type.
+At position 358 to 431, the domain is characterized as Death.
+At position 221 to 287, the domain is characterized as J.
+At position 204 to 260, the domain is characterized as HAMP.
+At position 268 to 470, the domain is characterized as Histidine kinase.
+At position 29 to 242, the domain is characterized as PIK helical.
+At position 205 to 534, the domain is characterized as Kinesin motor.
+At position 188 to 312, the domain is characterized as AB hydrolase-1.
+At position 2 to 393, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 953 to 1234, the domain is characterized as PKS/mFAS DH.
+At position 2425 to 2503, the domain is characterized as Carrier.
+At position 9 to 246, the domain is characterized as ATP-grasp.
+At position 36 to 290, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 11 to 96, the domain is characterized as GS beta-grasp.
+At position 104 to 468, the domain is characterized as GS catalytic.
+At position 2 to 114, the domain is characterized as Thioredoxin.
+At position 461 to 774, the domain is characterized as Protein kinase.
+At position 27 to 104, the domain is characterized as Ig-like C2-type.
+At position 108 to 205, the domain is characterized as Fibronectin type-III 1.
+At position 206 to 306, the domain is characterized as Fibronectin type-III 2.
+At position 66 to 249, the domain is characterized as Laminin G-like.
+At position 619 to 680, the domain is characterized as Collagen-like 1.
+At position 681 to 731, the domain is characterized as Collagen-like 2.
+At position 823 to 865, the domain is characterized as Collagen-like 3.
+At position 879 to 927, the domain is characterized as Collagen-like 4.
+At position 39 to 130, the domain is characterized as Ig-like C2-type 1.
+At position 241 to 324, the domain is characterized as Ig-like C2-type 3.
+At position 329 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 419 to 506, the domain is characterized as Ig-like C2-type 5.
+At position 511 to 605, the domain is characterized as Ig-like C2-type 6.
+At position 612 to 710, the domain is characterized as Fibronectin type-III 1.
+At position 715 to 812, the domain is characterized as Fibronectin type-III 2.
+At position 817 to 913, the domain is characterized as Fibronectin type-III 3.
+At position 917 to 1008, the domain is characterized as Fibronectin type-III 4.
+At position 18 to 242, the domain is characterized as Radical SAM core.
+At position 65 to 169, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 251 to 352, the domain is characterized as HD.
+At position 524 to 801, the domain is characterized as Protein kinase.
+At position 415 to 629, the domain is characterized as BURP.
+At position 47 to 523, the domain is characterized as Sema.
+At position 525 to 579, the domain is characterized as PSI.
+At position 604 to 663, the domain is characterized as Ig-like C2-type.
+At position 13 to 197, the domain is characterized as HORMA.
+At position 130 to 332, the domain is characterized as ATP-grasp.
+At position 14 to 16, the domain is characterized as Peptidase M12B.
+At position 76 to 250, the domain is characterized as Helicase ATP-binding.
+At position 272 to 435, the domain is characterized as Helicase C-terminal.
+At position 36 to 234, the domain is characterized as Lon N-terminal.
+At position 646 to 828, the domain is characterized as Lon proteolytic.
+At position 225 to 509, the domain is characterized as NR LBD.
+At position 174 to 314, the domain is characterized as PPC.
+At position 55 to 152, the domain is characterized as sHSP.
+At position 44 to 108, the domain is characterized as CSD.
+At position 150 to 357, the domain is characterized as ATP-grasp.
+At position 284 to 502, the domain is characterized as TLDc.
+At position 182 to 259, the domain is characterized as TFIIS N-terminal.
+At position 208 to 389, the domain is characterized as PCI.
+At position 138 to 452, the domain is characterized as NB-ARC.
+At position 644 to 819, the domain is characterized as MOSC.
+At position 6 to 155, the domain is characterized as Ferritin-like diiron.
+At position 489 to 749, the domain is characterized as Protein kinase.
+At position 824 to 954, the domain is characterized as Guanylate cyclase.
+At position 173 to 223, the domain is characterized as DHHC.
+At position 22 to 53, the domain is characterized as CBM1.
+At position 74 to 379, the domain is characterized as GH10.
+At position 8 to 122, the domain is characterized as MTTase N-terminal.
+At position 146 to 376, the domain is characterized as Radical SAM core.
+At position 379 to 444, the domain is characterized as TRAM.
+At position 122 to 157, the domain is characterized as Orange.
+At position 363 to 668, the domain is characterized as Protein kinase.
+At position 307 to 487, the domain is characterized as Helicase ATP-binding.
+At position 498 to 668, the domain is characterized as Helicase C-terminal.
+At position 249 to 339, the domain is characterized as PDZ 1.
+At position 419 to 503, the domain is characterized as PDZ 2.
+At position 92 to 161, the domain is characterized as SH3.
+At position 80 to 256, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 170, the domain is characterized as Miro 1.
+At position 306 to 341, the domain is characterized as EF-hand 2.
+At position 422 to 588, the domain is characterized as Miro 2.
+At position 142 to 522, the domain is characterized as PDEase.
+At position 71 to 122, the domain is characterized as F-box.
+At position 109 to 293, the domain is characterized as Tyr recombinase.
+At position 2 to 77, the domain is characterized as Lipoyl-binding 1.
+At position 121 to 196, the domain is characterized as Lipoyl-binding 2.
+At position 243 to 280, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 33 to 248, the domain is characterized as tr-type G.
+At position 18 to 128, the domain is characterized as RWD.
+At position 22 to 301, the domain is characterized as Dynamin-type G.
+At position 599 to 690, the domain is characterized as GED.
+At position 87 to 141, the domain is characterized as HTH cro/C1-type.
+At position 3 to 170, the domain is characterized as EngA-type G 1.
+At position 183 to 356, the domain is characterized as EngA-type G 2.
+At position 357 to 441, the domain is characterized as KH-like.
+At position 298 to 345, the domain is characterized as F-box.
+At position 285 to 447, the domain is characterized as SUN.
+At position 53 to 154, the domain is characterized as SRCR 1.
+At position 183 to 292, the domain is characterized as SRCR 2.
+At position 316 to 417, the domain is characterized as SRCR 3.
+At position 427 to 536, the domain is characterized as SRCR 4.
+At position 150 to 304, the domain is characterized as TRUD.
+At position 8 to 108, the domain is characterized as BMC circularly permuted.
+At position 1312 to 1452, the domain is characterized as VPS9.
+At position 14 to 131, the domain is characterized as Response regulatory.
+At position 169 to 360, the domain is characterized as CheB-type methylesterase.
+At position 155 to 366, the domain is characterized as HD-GYP.
+At position 39 to 247, the domain is characterized as tr-type G.
+At position 59 to 269, the domain is characterized as YjeF N-terminal.
+At position 654 to 714, the domain is characterized as HTH myb-type.
+At position 609 to 697, the domain is characterized as BRCT.
+At position 291 to 544, the domain is characterized as Glutamine amidotransferase type-1.
+At position 322 to 419, the domain is characterized as ERCC4.
+At position 46 to 137, the domain is characterized as ABM.
+At position 24 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 539 to 595, the domain is characterized as HTH myb-type 1.
+At position 596 to 646, the domain is characterized as Myb-like.
+At position 647 to 702, the domain is characterized as HTH myb-type 2.
+At position 703 to 754, the domain is characterized as HTH myb-type 3.
+At position 19 to 138, the domain is characterized as I-type lysozyme.
+At position 1 to 122, the domain is characterized as ATP-grasp.
+At position 6 to 90, the domain is characterized as BMC.
+At position 357 to 617, the domain is characterized as Protein kinase.
+At position 176 to 259, the domain is characterized as PPIase FKBP-type.
+At position 165 to 285, the domain is characterized as THUMP.
+At position 7 to 98, the domain is characterized as ATP-cone.
+At position 173 to 246, the domain is characterized as Ubiquitin-like.
+At position 57 to 127, the domain is characterized as POTRA.
+At position 49 to 333, the domain is characterized as Reverse transcriptase.
+At position 264 to 347, the domain is characterized as IPT/TIG.
+At position 83 to 257, the domain is characterized as FAD-binding PCMH-type.
+At position 29 to 127, the domain is characterized as Cadherin 1.
+At position 128 to 243, the domain is characterized as Cadherin 2.
+At position 244 to 339, the domain is characterized as Cadherin 3.
+At position 340 to 448, the domain is characterized as Cadherin 4.
+At position 449 to 565, the domain is characterized as Cadherin 5.
+At position 566 to 666, the domain is characterized as Cadherin 6.
+At position 667 to 776, the domain is characterized as Cadherin 7.
+At position 43 to 103, the domain is characterized as MADS-box.
+At position 129 to 219, the domain is characterized as K-box.
+At position 155 to 552, the domain is characterized as TTL.
+At position 90 to 158, the domain is characterized as S4 RNA-binding.
+At position 64 to 314, the domain is characterized as ABC transporter.
+At position 53 to 274, the domain is characterized as Bin3-type SAM.
+At position 21 to 130, the domain is characterized as sHSP.
+At position 1 to 123, the domain is characterized as PX.
+At position 150 to 469, the domain is characterized as NACHT.
+At position 248 to 349, the domain is characterized as Fe2OG dioxygenase.
+At position 3 to 202, the domain is characterized as DPCK.
+At position 171 to 250, the domain is characterized as Toprim.
+At position 203 to 288, the domain is characterized as KH.
+At position 458 to 600, the domain is characterized as PA14.
+At position 131 to 326, the domain is characterized as ATP-grasp 1.
+At position 680 to 871, the domain is characterized as ATP-grasp 2.
+At position 952 to 1089, the domain is characterized as MGS-like.
+At position 115 to 282, the domain is characterized as TNase-like.
+At position 73 to 353, the domain is characterized as Protein kinase.
+At position 70 to 354, the domain is characterized as Protein kinase.
+At position 78 to 378, the domain is characterized as AB hydrolase-1.
+At position 23 to 123, the domain is characterized as RRM 1.
+At position 824 to 890, the domain is characterized as SAM 1.
+At position 898 to 963, the domain is characterized as SAM 2.
+At position 1071 to 1223, the domain is characterized as PID.
+At position 419 to 507, the domain is characterized as PI3K-RBD.
+At position 680 to 839, the domain is characterized as C2 PI3K-type.
+At position 859 to 1035, the domain is characterized as PIK helical.
+At position 1103 to 1381, the domain is characterized as PI3K/PI4K catalytic.
+At position 1420 to 1536, the domain is characterized as PX.
+At position 1554 to 1677, the domain is characterized as C2.
+At position 138 to 206, the domain is characterized as DRBM.
+At position 291 to 617, the domain is characterized as A to I editase.
+At position 2 to 242, the domain is characterized as PPM-type phosphatase.
+At position 555 to 676, the domain is characterized as SET.
+At position 97 to 335, the domain is characterized as Radical SAM core.
+At position 102 to 390, the domain is characterized as tr-type G.
+At position 1 to 98, the domain is characterized as C2 1.
+At position 251 to 372, the domain is characterized as C2 2.
+At position 415 to 546, the domain is characterized as C2 3.
+At position 959 to 1084, the domain is characterized as C2 4.
+At position 1131 to 1257, the domain is characterized as C2 5.
+At position 1460 to 1589, the domain is characterized as C2 6.
+At position 1710 to 1861, the domain is characterized as C2 7.
+At position 211 to 403, the domain is characterized as Helicase ATP-binding.
+At position 414 to 575, the domain is characterized as Helicase C-terminal.
+At position 171 to 330, the domain is characterized as CRAL-TRIO.
+At position 1524 to 1606, the domain is characterized as J.
+At position 63 to 139, the domain is characterized as BTB.
+At position 179 to 253, the domain is characterized as SPOR.
+At position 2 to 280, the domain is characterized as DegV.
+At position 1 to 148, the domain is characterized as Ferritin-like diiron.
+At position 73 to 95, the domain is characterized as Follistatin-like.
+At position 91 to 153, the domain is characterized as Kazal-like.
+At position 263 to 273, the domain is characterized as EF-hand.
+At position 74 to 398, the domain is characterized as Protein kinase.
+At position 482 to 606, the domain is characterized as PH.
+At position 31 to 73, the domain is characterized as EGF-like.
+At position 121 to 316, the domain is characterized as ATP-grasp.
+At position 475 to 698, the domain is characterized as Histidine kinase.
+At position 720 to 831, the domain is characterized as Response regulatory.
+At position 67 to 194, the domain is characterized as ALOG.
+At position 1 to 122, the domain is characterized as MsrB.
+At position 33 to 104, the domain is characterized as Ig-like.
+At position 280 to 413, the domain is characterized as Sox C-terminal.
+At position 399 to 543, the domain is characterized as JmjC.
+At position 51 to 119, the domain is characterized as POTRA.
+At position 59 to 132, the domain is characterized as SCAN box.
+At position 31 to 306, the domain is characterized as CN hydrolase.
+At position 131 to 305, the domain is characterized as Thioredoxin.
+At position 496 to 645, the domain is characterized as SEFIR.
+At position 1 to 86, the domain is characterized as HIG1.
+At position 63 to 155, the domain is characterized as BRICHOS.
+At position 30 to 180, the domain is characterized as Cohesin.
+At position 216 to 280, the domain is characterized as SLH 1.
+At position 281 to 344, the domain is characterized as SLH 2.
+At position 345 to 408, the domain is characterized as SLH 3.
+At position 409 to 429, the domain is characterized as SLH 4; truncated.
+At position 537 to 577, the domain is characterized as CUE.
+At position 148 to 180, the domain is characterized as EGF-like 1.
+At position 286 to 338, the domain is characterized as TB 1.
+At position 406 to 458, the domain is characterized as TB 2.
+At position 588 to 629, the domain is characterized as EGF-like 3.
+At position 630 to 671, the domain is characterized as EGF-like 4; calcium-binding.
+At position 672 to 713, the domain is characterized as EGF-like 5; calcium-binding.
+At position 714 to 751, the domain is characterized as EGF-like 6; calcium-binding.
+At position 753 to 794, the domain is characterized as EGF-like 7; calcium-binding.
+At position 795 to 836, the domain is characterized as EGF-like 8; calcium-binding.
+At position 877 to 919, the domain is characterized as EGF-like 9; calcium-binding.
+At position 920 to 961, the domain is characterized as EGF-like 10; calcium-binding.
+At position 962 to 1002, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1091 to 1132, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1223 to 1277, the domain is characterized as TB 3.
+At position 1295 to 1337, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1338 to 1379, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1391 to 1444, the domain is characterized as TB 4.
+At position 1575 to 1615, the domain is characterized as EGF-like 15.
+At position 1616 to 1660, the domain is characterized as EGF-like 16.
+At position 40 to 143, the domain is characterized as THUMP.
+At position 18 to 114, the domain is characterized as CFEM.
+At position 37 to 313, the domain is characterized as Pyruvate carboxyltransferase.
+At position 103 to 411, the domain is characterized as IF rod.
+At position 555 to 615, the domain is characterized as KH.
+At position 11 to 218, the domain is characterized as YjeF N-terminal.
+At position 587 to 688, the domain is characterized as tRNA-binding.
+At position 242 to 287, the domain is characterized as bZIP.
+At position 264 to 439, the domain is characterized as Helicase ATP-binding.
+At position 468 to 628, the domain is characterized as Helicase C-terminal.
+At position 238 to 339, the domain is characterized as HD.
+At position 24 to 96, the domain is characterized as Importin N-terminal.
+At position 53 to 211, the domain is characterized as FAD-binding PCMH-type.
+At position 1788 to 1889, the domain is characterized as WGR.
+At position 1910 to 2045, the domain is characterized as PARP alpha-helical.
+At position 2047 to 2276, the domain is characterized as PARP catalytic.
+At position 477 to 591, the domain is characterized as Toprim.
+At position 23 to 101, the domain is characterized as Sm.
+At position 226 to 289, the domain is characterized as bZIP.
+At position 668 to 728, the domain is characterized as SH3.
+At position 105 to 261, the domain is characterized as Exonuclease.
+At position 40 to 265, the domain is characterized as Peptidase S1.
+At position 52 to 318, the domain is characterized as GB1/RHD3-type G.
+At position 16 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 140 to 169, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 77 to 247, the domain is characterized as Helicase ATP-binding.
+At position 257 to 417, the domain is characterized as Helicase C-terminal.
+At position 31 to 574, the domain is characterized as PLA2c.
+At position 40 to 243, the domain is characterized as Alpha-type protein kinase.
+At position 27 to 182, the domain is characterized as C-CAP/cofactor C-like.
+At position 280 to 421, the domain is characterized as SIS 1.
+At position 454 to 596, the domain is characterized as SIS 2.
+At position 29 to 194, the domain is characterized as Reelin.
+At position 195 to 388, the domain is characterized as Spondin.
+At position 442 to 495, the domain is characterized as TSP type-1 1.
+At position 501 to 555, the domain is characterized as TSP type-1 2.
+At position 558 to 611, the domain is characterized as TSP type-1 3.
+At position 614 to 666, the domain is characterized as TSP type-1 4.
+At position 668 to 721, the domain is characterized as TSP type-1 5.
+At position 754 to 806, the domain is characterized as TSP type-1 6.
+At position 354 to 559, the domain is characterized as Histidine kinase.
+At position 302 to 536, the domain is characterized as ABC transporter 2.
+At position 1 to 134, the domain is characterized as Thioredoxin.
+At position 21 to 242, the domain is characterized as Peptidase S1.
+At position 406 to 465, the domain is characterized as LIM zinc-binding 1.
+At position 466 to 526, the domain is characterized as LIM zinc-binding 2.
+At position 527 to 595, the domain is characterized as LIM zinc-binding 3.
+At position 122 to 155, the domain is characterized as EF-hand 3.
+At position 150 to 225, the domain is characterized as Ubiquitin-like.
+At position 198 to 513, the domain is characterized as IF rod.
+At position 10 to 225, the domain is characterized as YjeF N-terminal.
+At position 283 to 524, the domain is characterized as MHD.
+At position 64 to 322, the domain is characterized as Protein kinase.
+At position 401 to 436, the domain is characterized as EF-hand 2.
+At position 437 to 472, the domain is characterized as EF-hand 3.
+At position 473 to 508, the domain is characterized as EF-hand 4.
+At position 64 to 191, the domain is characterized as AB hydrolase-1.
+At position 23 to 131, the domain is characterized as Bulb-type lectin.
+At position 18 to 306, the domain is characterized as RHD.
+At position 7 to 225, the domain is characterized as ABC transporter.
+At position 123 to 360, the domain is characterized as Histidine kinase.
+At position 36 to 153, the domain is characterized as MTTase N-terminal.
+At position 176 to 415, the domain is characterized as Radical SAM core.
+At position 416 to 479, the domain is characterized as TRAM.
+At position 313 to 531, the domain is characterized as ABC transporter 2.
+At position 93 to 223, the domain is characterized as GST C-terminal.
+At position 46 to 162, the domain is characterized as SEA.
+At position 186 to 417, the domain is characterized as Peptidase S1.
+At position 405 to 603, the domain is characterized as DUF724.
+At position 50 to 178, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 23 to 274, the domain is characterized as Protein kinase.
+At position 131 to 231, the domain is characterized as Fibronectin type-III.
+At position 152 to 425, the domain is characterized as ABC transporter 1.
+At position 504 to 716, the domain is characterized as ABC transmembrane type-2 1.
+At position 855 to 1107, the domain is characterized as ABC transporter 2.
+At position 1180 to 1394, the domain is characterized as ABC transmembrane type-2 2.
+At position 31 to 153, the domain is characterized as C-type lectin.
+At position 139 to 240, the domain is characterized as HTH LytTR-type.
+At position 35 to 129, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 132 to 273, the domain is characterized as FAD-binding FR-type.
+At position 182 to 471, the domain is characterized as ABC transmembrane type-1.
+At position 504 to 741, the domain is characterized as ABC transporter.
+At position 427 to 589, the domain is characterized as PA14.
+At position 260 to 341, the domain is characterized as Toprim.
+At position 23 to 86, the domain is characterized as PAS.
+At position 494 to 642, the domain is characterized as DOD-type homing endonuclease.
+At position 270 to 521, the domain is characterized as Protein kinase.
+At position 41 to 219, the domain is characterized as FAD-binding PCMH-type.
+At position 396 to 625, the domain is characterized as NR LBD.
+At position 159 to 305, the domain is characterized as TRUD.
+At position 13 to 99, the domain is characterized as MtN3/slv 1.
+At position 135 to 219, the domain is characterized as MtN3/slv 2.
+At position 211 to 271, the domain is characterized as KH.
+At position 337 to 430, the domain is characterized as HD.
+At position 1 to 211, the domain is characterized as tr-type G.
+At position 3 to 133, the domain is characterized as PH.
+At position 214 to 274, the domain is characterized as SH3.
+At position 281 to 377, the domain is characterized as SH2.
+At position 402 to 655, the domain is characterized as Protein kinase.
+At position 58 to 171, the domain is characterized as Cadherin 1.
+At position 172 to 281, the domain is characterized as Cadherin 2.
+At position 282 to 387, the domain is characterized as Cadherin 3.
+At position 394 to 498, the domain is characterized as Cadherin 4.
+At position 499 to 602, the domain is characterized as Cadherin 5.
+At position 603 to 705, the domain is characterized as Cadherin 6.
+At position 709 to 827, the domain is characterized as Cadherin 7.
+At position 11 to 312, the domain is characterized as Protein kinase.
+At position 3 to 371, the domain is characterized as BRO1.
+At position 191 to 230, the domain is characterized as LRRCT.
+At position 961 to 1241, the domain is characterized as Protein kinase.
+At position 382 to 498, the domain is characterized as PI-PLC Y-box.
+At position 498 to 622, the domain is characterized as C2.
+At position 247 to 484, the domain is characterized as Helicase C-terminal.
+At position 3 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 103 to 203, the domain is characterized as FAD-binding FR-type.
+At position 52 to 123, the domain is characterized as SLH.
+At position 1066 to 1254, the domain is characterized as DH.
+At position 280 to 479, the domain is characterized as ABC transmembrane type-1.
+At position 47 to 155, the domain is characterized as Rieske.
+At position 35 to 210, the domain is characterized as BPL/LPL catalytic.
+At position 602 to 635, the domain is characterized as WW 1.
+At position 745 to 777, the domain is characterized as WW 2.
+At position 914 to 1247, the domain is characterized as HECT.
+At position 291 to 332, the domain is characterized as UBA.
+At position 23 to 258, the domain is characterized as Bin3-type SAM.
+At position 535 to 729, the domain is characterized as STAS.
+At position 14 to 316, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 317 to 654, the domain is characterized as UvrD-like helicase C-terminal.
+At position 80 to 142, the domain is characterized as CBS 1.
+At position 145 to 202, the domain is characterized as CBS 2.
+At position 444 to 577, the domain is characterized as Ricin B-type lectin.
+At position 5 to 78, the domain is characterized as Carrier 1.
+At position 1055 to 1131, the domain is characterized as Carrier 2.
+At position 6 to 117, the domain is characterized as CMP/dCMP-type deaminase.
+At position 422 to 540, the domain is characterized as Plastocyanin-like 3.
+At position 344 to 446, the domain is characterized as PDZ.
+At position 36 to 72, the domain is characterized as EF-hand.
+At position 157 to 302, the domain is characterized as PI-PLC X-box.
+At position 377 to 493, the domain is characterized as PI-PLC Y-box.
+At position 493 to 619, the domain is characterized as C2.
+At position 519 to 695, the domain is characterized as Helicase ATP-binding.
+At position 843 to 1002, the domain is characterized as Helicase C-terminal.
+At position 121 to 258, the domain is characterized as BAH.
+At position 555 to 606, the domain is characterized as SANT.
+At position 48 to 755, the domain is characterized as Myosin motor.
+At position 780 to 809, the domain is characterized as IQ 2.
+At position 19 to 206, the domain is characterized as RNase H type-2.
+At position 273 to 389, the domain is characterized as Ferric oxidoreductase.
+At position 411 to 590, the domain is characterized as FAD-binding FR-type.
+At position 116 to 351, the domain is characterized as PABS.
+At position 18 to 110, the domain is characterized as CARD.
+At position 667 to 755, the domain is characterized as PDZ.
+At position 973 to 1140, the domain is characterized as Guanylate kinase-like.
+At position 92 to 154, the domain is characterized as S4 RNA-binding.
+At position 3 to 78, the domain is characterized as Lipoyl-binding.
+At position 11 to 97, the domain is characterized as MtN3/slv 1.
+At position 34 to 273, the domain is characterized as ABC transporter.
+At position 71 to 262, the domain is characterized as HD.
+At position 2 to 68, the domain is characterized as Mop.
+At position 22 to 216, the domain is characterized as Lon N-terminal.
+At position 604 to 785, the domain is characterized as Lon proteolytic.
+At position 12 to 126, the domain is characterized as MTTase N-terminal.
+At position 383 to 443, the domain is characterized as TRAM.
+At position 26 to 131, the domain is characterized as AB hydrolase-1.
+At position 1 to 191, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 210, the domain is characterized as CNNM transmembrane.
+At position 229 to 290, the domain is characterized as CBS 1.
+At position 295 to 355, the domain is characterized as CBS 2.
+At position 21 to 124, the domain is characterized as Gnk2-homologous 1.
+At position 130 to 235, the domain is characterized as Gnk2-homologous 2.
+At position 312 to 585, the domain is characterized as Protein kinase.
+At position 130 to 214, the domain is characterized as PDZ.
+At position 67 to 117, the domain is characterized as bHLH.
+At position 2 to 334, the domain is characterized as SPX.
+At position 591 to 782, the domain is characterized as EXS.
+At position 4 to 162, the domain is characterized as N-acetyltransferase.
+At position 121 to 205, the domain is characterized as LITAF.
+At position 138 to 194, the domain is characterized as CBS 1.
+At position 201 to 258, the domain is characterized as CBS 2.
+At position 17 to 151, the domain is characterized as MPN.
+At position 30 to 90, the domain is characterized as HTH tetR-type.
+At position 140 to 739, the domain is characterized as PLA2c.
+At position 359 to 408, the domain is characterized as bHLH.
+At position 82 to 166, the domain is characterized as S1 motif.
+At position 163 to 337, the domain is characterized as Helicase ATP-binding.
+At position 489 to 643, the domain is characterized as Helicase C-terminal.
+At position 18 to 249, the domain is characterized as Radical SAM core.
+At position 44 to 161, the domain is characterized as MTTase N-terminal.
+At position 191 to 423, the domain is characterized as Radical SAM core.
+At position 426 to 494, the domain is characterized as TRAM.
+At position 198 to 511, the domain is characterized as Protein kinase.
+At position 575 to 610, the domain is characterized as EF-hand 1.
+At position 618 to 640, the domain is characterized as EF-hand 2.
+At position 670 to 703, the domain is characterized as EF-hand 3.
+At position 200 to 309, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 39 to 313, the domain is characterized as Pyruvate carboxyltransferase.
+At position 165 to 235, the domain is characterized as Bromo.
+At position 277 to 327, the domain is characterized as PWWP.
+At position 6 to 244, the domain is characterized as ABC transporter 1.
+At position 31 to 105, the domain is characterized as POTRA 1.
+At position 106 to 182, the domain is characterized as POTRA 2.
+At position 185 to 273, the domain is characterized as POTRA 3.
+At position 276 to 354, the domain is characterized as POTRA 4.
+At position 357 to 430, the domain is characterized as POTRA 5.
+At position 275 to 403, the domain is characterized as Runt.
+At position 210 to 265, the domain is characterized as LRRCT 1.
+At position 394 to 449, the domain is characterized as LRRCT 2.
+At position 185 to 257, the domain is characterized as FHA.
+At position 15 to 265, the domain is characterized as Pyruvate carboxyltransferase.
+At position 5 to 273, the domain is characterized as Peptidase S8.
+At position 115 to 274, the domain is characterized as MyTH4.
+At position 279 to 593, the domain is characterized as FERM.
+At position 888 to 1209, the domain is characterized as Kinesin motor.
+At position 432 to 543, the domain is characterized as RWD.
+At position 280 to 357, the domain is characterized as PUA.
+At position 523 to 617, the domain is characterized as Fibronectin type-III.
+At position 3 to 157, the domain is characterized as PPIase cyclophilin-type.
+At position 13 to 49, the domain is characterized as EF-hand 1.
+At position 55 to 90, the domain is characterized as EF-hand 2.
+At position 92 to 206, the domain is characterized as sHSP.
+At position 4 to 74, the domain is characterized as RRM 1.
+At position 108 to 181, the domain is characterized as RRM 2.
+At position 850 to 1060, the domain is characterized as Helicase ATP-binding.
+At position 1206 to 1359, the domain is characterized as Helicase C-terminal.
+At position 3 to 55, the domain is characterized as HTH merR-type.
+At position 30 to 268, the domain is characterized as GB1/RHD3-type G.
+At position 526 to 617, the domain is characterized as CARD.
+At position 336 to 615, the domain is characterized as Protein kinase.
+At position 280 to 354, the domain is characterized as POU-specific.
+At position 930 to 1062, the domain is characterized as MGS-like.
+At position 38 to 95, the domain is characterized as bHLH.
+At position 114 to 143, the domain is characterized as Orange.
+At position 446 to 554, the domain is characterized as Peptidase S74.
+At position 46 to 72, the domain is characterized as LysM 1; degenerate.
+At position 102 to 148, the domain is characterized as LysM 2.
+At position 167 to 210, the domain is characterized as LysM 3.
+At position 322 to 595, the domain is characterized as Protein kinase.
+At position 41 to 300, the domain is characterized as PPM-type phosphatase.
+At position 570 to 651, the domain is characterized as BRCT.
+At position 13 to 228, the domain is characterized as ABC transporter.
+At position 940 to 1024, the domain is characterized as PB1.
+At position 16 to 273, the domain is characterized as Protein kinase.
+At position 535 to 846, the domain is characterized as CNH.
+At position 9 to 46, the domain is characterized as UBA-like.
+At position 56 to 244, the domain is characterized as DCUN1.
+At position 628 to 708, the domain is characterized as S1 motif.
+At position 3 to 189, the domain is characterized as YrdC-like.
+At position 336 to 422, the domain is characterized as SANTA.
+At position 741 to 796, the domain is characterized as SANT.
+At position 19 to 71, the domain is characterized as bHLH.
+At position 140 to 349, the domain is characterized as ATP-grasp.
+At position 12 to 193, the domain is characterized as UmuC.
+At position 1 to 178, the domain is characterized as Albumin 2.
+At position 179 to 377, the domain is characterized as Albumin 3.
+At position 104 to 244, the domain is characterized as GST C-terminal.
+At position 745 to 1005, the domain is characterized as Tyrosine-protein phosphatase.
+At position 162 to 259, the domain is characterized as 5'-3' exonuclease.
+At position 21 to 99, the domain is characterized as RRM 1.
+At position 112 to 188, the domain is characterized as RRM 2.
+At position 202 to 279, the domain is characterized as RRM 3.
+At position 304 to 381, the domain is characterized as RRM 4.
+At position 93 to 164, the domain is characterized as PRC barrel.
+At position 241 to 420, the domain is characterized as SSD.
+At position 178 to 424, the domain is characterized as ABC transporter 1.
+At position 492 to 707, the domain is characterized as ABC transporter 2.
+At position 5 to 240, the domain is characterized as PABS.
+At position 412 to 570, the domain is characterized as SSD.
+At position 167 to 233, the domain is characterized as KH.
+At position 11 to 150, the domain is characterized as uDENN.
+At position 163 to 332, the domain is characterized as cDENN.
+At position 334 to 437, the domain is characterized as dDENN.
+At position 95 to 222, the domain is characterized as VIT.
+At position 342 to 521, the domain is characterized as VWFA.
+At position 51 to 149, the domain is characterized as Mis18.
+At position 1 to 91, the domain is characterized as Glutaredoxin.
+At position 25 to 65, the domain is characterized as LDL-receptor class A 1.
+At position 66 to 106, the domain is characterized as LDL-receptor class A 2.
+At position 107 to 145, the domain is characterized as LDL-receptor class A 3.
+At position 146 to 185, the domain is characterized as LDL-receptor class A 4.
+At position 193 to 231, the domain is characterized as LDL-receptor class A 5.
+At position 232 to 270, the domain is characterized as LDL-receptor class A 6.
+At position 272 to 311, the domain is characterized as LDL-receptor class A 7.
+At position 312 to 351, the domain is characterized as EGF-like 1.
+At position 352 to 391, the domain is characterized as EGF-like 2; calcium-binding.
+At position 661 to 710, the domain is characterized as EGF-like 3.
+At position 1 to 346, the domain is characterized as Rtt109-type HAT.
+At position 605 to 675, the domain is characterized as Bromo.
+At position 1075 to 1158, the domain is characterized as PWWP.
+At position 3 to 230, the domain is characterized as ABC transporter.
+At position 39 to 322, the domain is characterized as ABC transmembrane type-1.
+At position 355 to 589, the domain is characterized as ABC transporter.
+At position 24 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 218 to 410, the domain is characterized as GMPS ATP-PPase.
+At position 372 to 407, the domain is characterized as EF-hand.
+At position 198 to 393, the domain is characterized as Peptidase M12B.
+At position 401 to 487, the domain is characterized as Disintegrin.
+At position 72 to 285, the domain is characterized as HD.
+At position 1858 to 1887, the domain is characterized as IQ.
+At position 14 to 150, the domain is characterized as uDENN.
+At position 165 to 304, the domain is characterized as cDENN.
+At position 306 to 412, the domain is characterized as dDENN.
+At position 787 to 871, the domain is characterized as GRAM.
+At position 996 to 1447, the domain is characterized as Myotubularin phosphatase.
+At position 1643 to 1743, the domain is characterized as PH.
+At position 501 to 643, the domain is characterized as HD.
+At position 460 to 571, the domain is characterized as EH.
+At position 61 to 111, the domain is characterized as Collagen-like.
+At position 122 to 255, the domain is characterized as C1q.
+At position 23 to 89, the domain is characterized as SH3b.
+At position 14 to 175, the domain is characterized as TIR.
+At position 211 to 472, the domain is characterized as NB-ARC.
+At position 6 to 96, the domain is characterized as Ig-like 1.
+At position 118 to 212, the domain is characterized as Ig-like 2.
+At position 221 to 323, the domain is characterized as Ig-like 3.
+At position 177 to 360, the domain is characterized as Brix.
+At position 196 to 239, the domain is characterized as LysM 2.
+At position 312 to 355, the domain is characterized as LysM 3.
+At position 406 to 524, the domain is characterized as NlpC/P60.
+At position 233 to 320, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 132 to 337, the domain is characterized as ATP-grasp.
+At position 525 to 635, the domain is characterized as OCEL.
+At position 63 to 102, the domain is characterized as Pentapeptide repeat 1.
+At position 103 to 142, the domain is characterized as Pentapeptide repeat 2.
+At position 143 to 182, the domain is characterized as Pentapeptide repeat 3.
+At position 218 to 454, the domain is characterized as Methyl-accepting transducer.
+At position 84 to 124, the domain is characterized as UBA.
+At position 54 to 100, the domain is characterized as F-box.
+At position 102 to 180, the domain is characterized as RRM 1.
+At position 188 to 268, the domain is characterized as RRM 2.
+At position 249 to 318, the domain is characterized as HTH OST-type 2.
+At position 352 to 421, the domain is characterized as HTH OST-type 3.
+At position 528 to 585, the domain is characterized as Tudor 1.
+At position 718 to 775, the domain is characterized as Tudor 2.
+At position 63 to 120, the domain is characterized as Chitin-binding type-2 1.
+At position 228 to 285, the domain is characterized as Chitin-binding type-2 2.
+At position 43 to 114, the domain is characterized as KRAB.
+At position 12 to 113, the domain is characterized as LOB.
+At position 37 to 237, the domain is characterized as Cupin type-1 1.
+At position 290 to 439, the domain is characterized as Cupin type-1 2.
+At position 243 to 302, the domain is characterized as LIM zinc-binding.
+At position 26 to 103, the domain is characterized as Ubiquitin-like.
+At position 30 to 144, the domain is characterized as Ig-like V-type.
+At position 6 to 311, the domain is characterized as SET.
+At position 300 to 525, the domain is characterized as PE-PPE.
+At position 48 to 186, the domain is characterized as 6-Cys 1.
+At position 302 to 433, the domain is characterized as 6-Cys 2.
+At position 413 to 488, the domain is characterized as ACT 1.
+At position 494 to 571, the domain is characterized as ACT 2.
+At position 49 to 315, the domain is characterized as PPM-type phosphatase.
+At position 34 to 423, the domain is characterized as GBD/FH3.
+At position 597 to 623, the domain is characterized as FH1.
+At position 631 to 1031, the domain is characterized as FH2.
+At position 1037 to 1073, the domain is characterized as DAD.
+At position 31 to 208, the domain is characterized as FAD-binding PCMH-type.
+At position 106 to 318, the domain is characterized as ATP-grasp.
+At position 309 to 367, the domain is characterized as SH3.
+At position 281 to 333, the domain is characterized as bHLH.
+At position 232 to 305, the domain is characterized as RRM.
+At position 126 to 230, the domain is characterized as Ig-like C1-type.
+At position 384 to 443, the domain is characterized as SH3.
+At position 306 to 348, the domain is characterized as CCT.
+At position 621 to 707, the domain is characterized as BRCT.
+At position 106 to 228, the domain is characterized as GST C-terminal.
+At position 7 to 190, the domain is characterized as tr-type G.
+At position 41 to 120, the domain is characterized as H15.
+At position 73 to 137, the domain is characterized as BTB.
+At position 172 to 273, the domain is characterized as BACK.
+At position 11 to 65, the domain is characterized as ClpX-type ZB.
+At position 1 to 123, the domain is characterized as MGS-like.
+At position 7 to 56, the domain is characterized as F-box.
+At position 6 to 195, the domain is characterized as RNase H type-2.
+At position 30 to 133, the domain is characterized as Thioredoxin.
+At position 845 to 973, the domain is characterized as RGS 1.
+At position 1014 to 1138, the domain is characterized as RGS 2.
+At position 803 to 890, the domain is characterized as HPt.
+At position 10 to 177, the domain is characterized as PCI.
+At position 227 to 685, the domain is characterized as TROVE.
+At position 1171 to 1578, the domain is characterized as NACHT.
+At position 20 to 58, the domain is characterized as EGF-like 1.
+At position 59 to 99, the domain is characterized as EGF-like 2.
+At position 102 to 139, the domain is characterized as EGF-like 3.
+At position 140 to 176, the domain is characterized as EGF-like 4.
+At position 178 to 216, the domain is characterized as EGF-like 5; calcium-binding.
+At position 218 to 255, the domain is characterized as EGF-like 6.
+At position 257 to 293, the domain is characterized as EGF-like 7; calcium-binding.
+At position 295 to 333, the domain is characterized as EGF-like 8; calcium-binding.
+At position 335 to 371, the domain is characterized as EGF-like 9; calcium-binding.
+At position 372 to 410, the domain is characterized as EGF-like 10.
+At position 412 to 450, the domain is characterized as EGF-like 11; calcium-binding.
+At position 452 to 488, the domain is characterized as EGF-like 12; calcium-binding.
+At position 490 to 526, the domain is characterized as EGF-like 13; calcium-binding.
+At position 528 to 564, the domain is characterized as EGF-like 14; calcium-binding.
+At position 566 to 601, the domain is characterized as EGF-like 15; calcium-binding.
+At position 603 to 639, the domain is characterized as EGF-like 16; calcium-binding.
+At position 641 to 676, the domain is characterized as EGF-like 17; calcium-binding.
+At position 678 to 714, the domain is characterized as EGF-like 18; calcium-binding.
+At position 716 to 751, the domain is characterized as EGF-like 19; calcium-binding.
+At position 753 to 789, the domain is characterized as EGF-like 20; calcium-binding.
+At position 791 to 827, the domain is characterized as EGF-like 21; calcium-binding.
+At position 829 to 867, the domain is characterized as EGF-like 22.
+At position 869 to 905, the domain is characterized as EGF-like 23; calcium-binding.
+At position 907 to 943, the domain is characterized as EGF-like 24.
+At position 945 to 981, the domain is characterized as EGF-like 25; calcium-binding.
+At position 983 to 1019, the domain is characterized as EGF-like 26.
+At position 1021 to 1057, the domain is characterized as EGF-like 27; calcium-binding.
+At position 1059 to 1095, the domain is characterized as EGF-like 28.
+At position 1097 to 1143, the domain is characterized as EGF-like 29.
+At position 1145 to 1181, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1183 to 1219, the domain is characterized as EGF-like 31; calcium-binding.
+At position 1221 to 1265, the domain is characterized as EGF-like 32; calcium-binding.
+At position 1267 to 1305, the domain is characterized as EGF-like 33.
+At position 1307 to 1346, the domain is characterized as EGF-like 34.
+At position 1348 to 1384, the domain is characterized as EGF-like 35.
+At position 1387 to 1426, the domain is characterized as EGF-like 36.
+At position 395 to 529, the domain is characterized as C-CAP/cofactor C-like.
+At position 18 to 154, the domain is characterized as GAF.
+At position 204 to 337, the domain is characterized as GGDEF.
+At position 22 to 132, the domain is characterized as Ig-like V-type.
+At position 5 to 233, the domain is characterized as Radical SAM core.
+At position 9 to 75, the domain is characterized as PQ-loop 1.
+At position 151 to 213, the domain is characterized as PQ-loop 2.
+At position 41 to 72, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 6 to 199, the domain is characterized as MHYT.
+At position 293 to 425, the domain is characterized as GGDEF.
+At position 434 to 685, the domain is characterized as EAL.
+At position 361 to 530, the domain is characterized as tr-type G.
+At position 329 to 586, the domain is characterized as Clu.
+At position 140 to 206, the domain is characterized as HTH crp-type.
+At position 514 to 673, the domain is characterized as Helicase C-terminal.
+At position 6 to 161, the domain is characterized as PPIase cyclophilin-type.
+At position 241 to 319, the domain is characterized as RRM.
+At position 15 to 120, the domain is characterized as Calponin-homology (CH) 1.
+At position 242 to 343, the domain is characterized as HTH araC/xylS-type.
+At position 67 to 247, the domain is characterized as tr-type G.
+At position 92 to 171, the domain is characterized as PUA.
+At position 40 to 156, the domain is characterized as DOMON.
+At position 9 to 208, the domain is characterized as YjeF N-terminal.
+At position 214 to 496, the domain is characterized as YjeF C-terminal.
+At position 1073 to 1331, the domain is characterized as Protein kinase.
+At position 69 to 189, the domain is characterized as sHSP.
+At position 27 to 76, the domain is characterized as PSI.
+At position 136 to 378, the domain is characterized as VWFA.
+At position 5 to 65, the domain is characterized as CSD.
+At position 122 to 192, the domain is characterized as KH.
+At position 1 to 208, the domain is characterized as ThyX.
+At position 130 to 262, the domain is characterized as PINc.
+At position 43 to 98, the domain is characterized as bHLH.
+At position 116 to 153, the domain is characterized as Orange.
+At position 1199 to 1444, the domain is characterized as ABC transporter 2.
+At position 750 to 978, the domain is characterized as MIF4G.
+At position 1215 to 1337, the domain is characterized as MI.
+At position 1410 to 1579, the domain is characterized as W2.
+At position 220 to 294, the domain is characterized as KRAB.
+At position 79 to 149, the domain is characterized as RST.
+At position 404 to 754, the domain is characterized as FERM.
+At position 19 to 351, the domain is characterized as PTS EIIC type-2.
+At position 425 to 519, the domain is characterized as PTS EIIB type-2.
+At position 298 to 460, the domain is characterized as PCI.
+At position 56 to 176, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 194 to 299, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 1 to 53, the domain is characterized as bHLH.
+At position 77 to 147, the domain is characterized as PAS 1.
+At position 218 to 288, the domain is characterized as PAS 2.
+At position 292 to 335, the domain is characterized as PAC.
+At position 336 to 766, the domain is characterized as Single-minded C-terminal.
+At position 1 to 82, the domain is characterized as DhaL.
+At position 465 to 635, the domain is characterized as tr-type G.
+At position 206 to 636, the domain is characterized as Myotubularin phosphatase.
+At position 53 to 180, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 50 to 354, the domain is characterized as ABC transmembrane type-1 1.
+At position 389 to 625, the domain is characterized as ABC transporter 1.
+At position 708 to 997, the domain is characterized as ABC transmembrane type-1 2.
+At position 1032 to 1270, the domain is characterized as ABC transporter 2.
+At position 5 to 90, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 90 to 129, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 227 to 283, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 20 to 66, the domain is characterized as Gla.
+At position 140 to 175, the domain is characterized as EF-hand 2.
+At position 175 to 207, the domain is characterized as EF-hand 3.
+At position 17 to 204, the domain is characterized as B30.2/SPRY.
+At position 14 to 63, the domain is characterized as F-box.
+At position 76 to 356, the domain is characterized as Protein kinase.
+At position 95 to 146, the domain is characterized as bHLH.
+At position 632 to 952, the domain is characterized as Kinesin motor.
+At position 187 to 383, the domain is characterized as Rho-GAP.
+At position 88 to 358, the domain is characterized as AB hydrolase-1.
+At position 28 to 76, the domain is characterized as TSP type-1 0.
+At position 77 to 134, the domain is characterized as TSP type-1 1.
+At position 136 to 191, the domain is characterized as TSP type-1 2.
+At position 193 to 255, the domain is characterized as TSP type-1 3.
+At position 257 to 313, the domain is characterized as TSP type-1 4.
+At position 315 to 377, the domain is characterized as TSP type-1 5.
+At position 379 to 462, the domain is characterized as TSP type-1 6.
+At position 158 to 272, the domain is characterized as SCP.
+At position 148 to 367, the domain is characterized as Radical SAM core.
+At position 177 to 405, the domain is characterized as Sigma-54 factor interaction.
+At position 34 to 315, the domain is characterized as ABC transmembrane type-1.
+At position 100 to 332, the domain is characterized as AB hydrolase-1.
+At position 27 to 131, the domain is characterized as Plastocyanin-like.
+At position 33 to 110, the domain is characterized as RRM.
+At position 160 to 184, the domain is characterized as DAZ.
+At position 1 to 107, the domain is characterized as Glutaredoxin.
+At position 249 to 442, the domain is characterized as GATase cobBQ-type.
+At position 20 to 166, the domain is characterized as CENP-V/GFA.
+At position 3 to 64, the domain is characterized as HMA 1.
+At position 99 to 162, the domain is characterized as HMA 2.
+At position 24 to 85, the domain is characterized as LCN-type CS-alpha/beta.
+At position 5 to 283, the domain is characterized as CN hydrolase.
+At position 111 to 146, the domain is characterized as EF-hand 1.
+At position 156 to 191, the domain is characterized as EF-hand 2.
+At position 368 to 501, the domain is characterized as DAGKc.
+At position 579 to 631, the domain is characterized as Tudor-knot.
+At position 257 to 315, the domain is characterized as CBS 1.
+At position 322 to 379, the domain is characterized as CBS 2.
+At position 25 to 389, the domain is characterized as ABC transporter.
+At position 231 to 352, the domain is characterized as OTU.
+At position 492 to 552, the domain is characterized as Tudor.
+At position 334 to 414, the domain is characterized as PDZ.
+At position 564 to 646, the domain is characterized as S1 motif.
+At position 284 to 343, the domain is characterized as SH3.
+At position 40 to 108, the domain is characterized as KH type-2.
+At position 44 to 113, the domain is characterized as EamA.
+At position 15 to 81, the domain is characterized as SAM.
+At position 4 to 376, the domain is characterized as Trm1 methyltransferase.
+At position 317 to 599, the domain is characterized as ABC transporter 1.
+At position 619 to 947, the domain is characterized as ABC transporter 2.
+At position 290 to 515, the domain is characterized as tr-type G.
+At position 1 to 185, the domain is characterized as tr-type G.
+At position 8 to 83, the domain is characterized as GIY-YIG.
+At position 416 to 588, the domain is characterized as tr-type G.
+At position 386 to 512, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 79 to 564, the domain is characterized as Protein kinase.
+At position 15 to 181, the domain is characterized as Reelin.
+At position 213 to 328, the domain is characterized as DOMON.
+At position 332 to 532, the domain is characterized as Cytochrome b561.
+At position 141 to 245, the domain is characterized as HTH LytTR-type.
+At position 29 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 681 to 872, the domain is characterized as ATP-grasp 2.
+At position 954 to 1106, the domain is characterized as MGS-like.
+At position 171 to 255, the domain is characterized as PPIase FKBP-type.
+At position 175 to 303, the domain is characterized as GGDEF.
+At position 177 to 395, the domain is characterized as Lon N-terminal.
+At position 856 to 1044, the domain is characterized as Lon proteolytic.
+At position 538 to 625, the domain is characterized as RRM.
+At position 141 to 231, the domain is characterized as TNT.
+At position 742 to 841, the domain is characterized as GAE.
+At position 96 to 153, the domain is characterized as CBS 1.
+At position 154 to 212, the domain is characterized as CBS 2.
+At position 393 to 422, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 432 to 461, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 99 to 194, the domain is characterized as Plastocyanin-like 1.
+At position 259 to 360, the domain is characterized as Plastocyanin-like 2.
+At position 43 to 154, the domain is characterized as GST N-terminal.
+At position 189 to 335, the domain is characterized as GST C-terminal.
+At position 60 to 273, the domain is characterized as ATLF-like.
+At position 4 to 120, the domain is characterized as TIR.
+At position 371 to 421, the domain is characterized as DHHC.
+At position 59 to 173, the domain is characterized as OmpA-like.
+At position 1 to 180, the domain is characterized as KARI N-terminal Rossmann.
+At position 181 to 326, the domain is characterized as KARI C-terminal knotted.
+At position 179 to 224, the domain is characterized as EGF-like.
+At position 818 to 1091, the domain is characterized as Protein kinase 2.
+At position 24 to 243, the domain is characterized as ABC transporter.
+At position 750 to 824, the domain is characterized as RRM.
+At position 117 to 229, the domain is characterized as DUF1279.
+At position 166 to 349, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 209, the domain is characterized as VWFA.
+At position 214 to 305, the domain is characterized as Fibronectin type-III 1.
+At position 307 to 403, the domain is characterized as Fibronectin type-III 2.
+At position 27 to 118, the domain is characterized as Fibronectin type-III 1.
+At position 177 to 352, the domain is characterized as VWFA.
+At position 377 to 466, the domain is characterized as Fibronectin type-III 2.
+At position 467 to 556, the domain is characterized as Fibronectin type-III 3.
+At position 557 to 644, the domain is characterized as Fibronectin type-III 4.
+At position 646 to 735, the domain is characterized as Fibronectin type-III 5.
+At position 740 to 831, the domain is characterized as Fibronectin type-III 6.
+At position 840 to 1035, the domain is characterized as Laminin G-like.
+At position 1069 to 1122, the domain is characterized as Collagen-like 1.
+At position 1125 to 1174, the domain is characterized as Collagen-like 2.
+At position 1165 to 1221, the domain is characterized as Collagen-like 3.
+At position 36 to 277, the domain is characterized as ABC transporter.
+At position 30 to 164, the domain is characterized as MPN.
+At position 179 to 401, the domain is characterized as Fibrinogen C-terminal.
+At position 50 to 152, the domain is characterized as LOB.
+At position 237 to 314, the domain is characterized as Sm.
+At position 21 to 277, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 292 to 540, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 15 to 149, the domain is characterized as ADF-H.
+At position 174 to 321, the domain is characterized as Cupin type-1.
+At position 193 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 306 to 361, the domain is characterized as HAMP.
+At position 385 to 633, the domain is characterized as PPM-type phosphatase.
+At position 339 to 399, the domain is characterized as S4 RNA-binding.
+At position 1 to 114, the domain is characterized as CUB.
+At position 217 to 410, the domain is characterized as Letm1 RBD.
+At position 217 to 422, the domain is characterized as SMP-LTD.
+At position 413 to 534, the domain is characterized as C2 1.
+At position 559 to 668, the domain is characterized as C2 2.
+At position 685 to 803, the domain is characterized as C2 3.
+At position 1019 to 1137, the domain is characterized as C2 4.
+At position 101 to 710, the domain is characterized as USP.
+At position 46 to 124, the domain is characterized as RRM.
+At position 2129 to 2199, the domain is characterized as Bromo.
+At position 1 to 170, the domain is characterized as Phosphatase tensin-type.
+At position 175 to 301, the domain is characterized as C2 tensin-type.
+At position 1167 to 1277, the domain is characterized as SH2.
+At position 1305 to 1439, the domain is characterized as PTB.
+At position 14 to 46, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 69 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 11 to 160, the domain is characterized as F5/8 type C 1.
+At position 168 to 220, the domain is characterized as TSP type-1 1.
+At position 224 to 279, the domain is characterized as TSP type-1 2.
+At position 281 to 336, the domain is characterized as TSP type-1 3.
+At position 338 to 393, the domain is characterized as TSP type-1 4.
+At position 403 to 458, the domain is characterized as TSP type-1 5.
+At position 460 to 515, the domain is characterized as TSP type-1 6.
+At position 517 to 572, the domain is characterized as TSP type-1 7.
+At position 595 to 769, the domain is characterized as VWFA 1.
+At position 778 to 958, the domain is characterized as VWFA 2.
+At position 966 to 1141, the domain is characterized as VWFA 3.
+At position 1144 to 1198, the domain is characterized as TSP type-1 8.
+At position 1192 to 1336, the domain is characterized as F5/8 type C 2.
+At position 52 to 163, the domain is characterized as PpiC.
+At position 26 to 267, the domain is characterized as Peptidase S1.
+At position 428 to 670, the domain is characterized as EAL.
+At position 370 to 611, the domain is characterized as TLDc.
+At position 1 to 74, the domain is characterized as REM-1.
+At position 281 to 387, the domain is characterized as PH.
+At position 347 to 407, the domain is characterized as S4 RNA-binding.
+At position 35 to 62, the domain is characterized as IQ.
+At position 59 to 150, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 243, the domain is characterized as Ig-like C2-type 2.
+At position 181 to 336, the domain is characterized as UBC core.
+At position 86 to 369, the domain is characterized as Protein kinase.
+At position 8 to 63, the domain is characterized as bHLH.
+At position 196 to 369, the domain is characterized as EngA-type G 2.
+At position 370 to 454, the domain is characterized as KH-like.
+At position 112 to 215, the domain is characterized as Fibronectin type-III 2.
+At position 82 to 185, the domain is characterized as C-type lectin.
+At position 57 to 142, the domain is characterized as Ig-like C2-type 1.
+At position 154 to 240, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 343, the domain is characterized as Ig-like C2-type 3.
+At position 348 to 432, the domain is characterized as Ig-like C2-type 4.
+At position 438 to 519, the domain is characterized as Ig-like C2-type 5.
+At position 527 to 622, the domain is characterized as Ig-like C2-type 6.
+At position 629 to 727, the domain is characterized as Fibronectin type-III 1.
+At position 732 to 829, the domain is characterized as Fibronectin type-III 2.
+At position 834 to 928, the domain is characterized as Fibronectin type-III 3.
+At position 933 to 1023, the domain is characterized as Fibronectin type-III 4.
+At position 39 to 166, the domain is characterized as SCP.
+At position 202 to 234, the domain is characterized as ShKT.
+At position 124 to 374, the domain is characterized as NR LBD.
+At position 34 to 103, the domain is characterized as Chitin-binding type R&R.
+At position 55 to 269, the domain is characterized as Radical SAM core.
+At position 103 to 173, the domain is characterized as PAS.
+At position 3 to 92, the domain is characterized as ACB.
+At position 2 to 47, the domain is characterized as Plastocyanin-like.
+At position 623 to 709, the domain is characterized as BRCT.
+At position 253 to 495, the domain is characterized as ABC transporter 2.
+At position 23 to 165, the domain is characterized as C2.
+At position 96 to 208, the domain is characterized as DUF1279.
+At position 39 to 133, the domain is characterized as Ras-associating 1.
+At position 246 to 348, the domain is characterized as Ras-associating 2.
+At position 426 to 492, the domain is characterized as FHA.
+At position 653 to 908, the domain is characterized as Dilute.
+At position 1007 to 1093, the domain is characterized as PDZ.
+At position 23 to 202, the domain is characterized as EngB-type G.
+At position 1177 to 1247, the domain is characterized as Bromo 1.
+At position 1330 to 1400, the domain is characterized as Bromo 2.
+At position 264 to 314, the domain is characterized as bHLH.
+At position 281 to 378, the domain is characterized as Fe2OG dioxygenase.
+At position 473 to 586, the domain is characterized as Fibronectin type-III 1.
+At position 590 to 680, the domain is characterized as Fibronectin type-III 2.
+At position 712 to 804, the domain is characterized as Fibronectin type-III 3.
+At position 813 to 912, the domain is characterized as Fibronectin type-III 4.
+At position 994 to 1283, the domain is characterized as Protein kinase.
+At position 127 to 512, the domain is characterized as FH2.
+At position 12 to 141, the domain is characterized as tr-type G.
+At position 205 to 240, the domain is characterized as UVR.
+At position 169 to 274, the domain is characterized as PRD 1.
+At position 282 to 390, the domain is characterized as PRD 2.
+At position 10 to 126, the domain is characterized as Response regulatory.
+At position 9 to 87, the domain is characterized as Chitin-binding type R&R.
+At position 206 to 438, the domain is characterized as Fibrinogen C-terminal.
+At position 369 to 398, the domain is characterized as IQ.
+At position 2 to 72, the domain is characterized as ACT.
+At position 78 to 114, the domain is characterized as PAS.
+At position 206 to 428, the domain is characterized as Sigma-54 factor interaction.
+At position 4 to 88, the domain is characterized as BMC.
+At position 109 to 165, the domain is characterized as EutK-Ctail.
+At position 160 to 259, the domain is characterized as SWIRM.
+At position 32 to 139, the domain is characterized as C-type lectin.
+At position 28 to 96, the domain is characterized as BTB.
+At position 103 to 170, the domain is characterized as S4 RNA-binding.
+At position 102 to 229, the domain is characterized as Laminin G-like.
+At position 506 to 561, the domain is characterized as Collagen-like 1.
+At position 577 to 636, the domain is characterized as Collagen-like 2.
+At position 679 to 738, the domain is characterized as Collagen-like 3.
+At position 742 to 801, the domain is characterized as Collagen-like 4.
+At position 802 to 861, the domain is characterized as Collagen-like 5.
+At position 886 to 945, the domain is characterized as Collagen-like 6.
+At position 946 to 1005, the domain is characterized as Collagen-like 7.
+At position 1006 to 1065, the domain is characterized as Collagen-like 8.
+At position 1072 to 1131, the domain is characterized as Collagen-like 9.
+At position 1135 to 1189, the domain is characterized as Collagen-like 10.
+At position 1191 to 1215, the domain is characterized as Collagen-like 11.
+At position 1220 to 1279, the domain is characterized as Collagen-like 12.
+At position 1316 to 1375, the domain is characterized as Collagen-like 13.
+At position 1376 to 1435, the domain is characterized as Collagen-like 14.
+At position 1439 to 1498, the domain is characterized as Collagen-like 15.
+At position 1534 to 1733, the domain is characterized as Fibrillar collagen NC1.
+At position 106 to 158, the domain is characterized as S4 RNA-binding.
+At position 4 to 174, the domain is characterized as EngA-type G 1.
+At position 183 to 358, the domain is characterized as EngA-type G 2.
+At position 359 to 444, the domain is characterized as KH-like.
+At position 35 to 70, the domain is characterized as EF-hand 1.
+At position 108 to 143, the domain is characterized as EF-hand 3.
+At position 62 to 108, the domain is characterized as F-box.
+At position 279 to 364, the domain is characterized as PDZ 1.
+At position 878 to 950, the domain is characterized as PDZ 2.
+At position 69 to 217, the domain is characterized as Cupin type-1.
+At position 278 to 356, the domain is characterized as UBX.
+At position 1015 to 1288, the domain is characterized as Autotransporter.
+At position 1 to 96, the domain is characterized as Glutaredoxin.
+At position 119 to 261, the domain is characterized as WIF.
+At position 279 to 311, the domain is characterized as EGF-like 1.
+At position 315 to 342, the domain is characterized as EGF-like 2.
+At position 343 to 375, the domain is characterized as EGF-like 3.
+At position 376 to 407, the domain is characterized as EGF-like 4.
+At position 412 to 441, the domain is characterized as EGF-like 5.
+At position 20 to 272, the domain is characterized as Protein kinase.
+At position 293 to 333, the domain is characterized as UBA.
+At position 463 to 511, the domain is characterized as KA1.
+At position 651 to 720, the domain is characterized as S1 motif.
+At position 166 to 276, the domain is characterized as TBDR plug.
+At position 281 to 819, the domain is characterized as TBDR beta-barrel.
+At position 5 to 139, the domain is characterized as RNase III.
+At position 54 to 324, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 7 to 88, the domain is characterized as J.
+At position 399 to 477, the domain is characterized as UBX.
+At position 149 to 414, the domain is characterized as Protein kinase.
+At position 853 to 880, the domain is characterized as PLD phosphodiesterase 2.
+At position 16 to 140, the domain is characterized as MH1.
+At position 273 to 467, the domain is characterized as MH2.
+At position 150 to 328, the domain is characterized as VWFA.
+At position 72 to 122, the domain is characterized as Myosin N-terminal SH3-like.
+At position 126 to 827, the domain is characterized as Myosin motor.
+At position 830 to 859, the domain is characterized as IQ.
+At position 71 to 225, the domain is characterized as UBC core.
+At position 324 to 485, the domain is characterized as Helicase ATP-binding.
+At position 539 to 699, the domain is characterized as Helicase C-terminal.
+At position 8 to 81, the domain is characterized as Sm.
+At position 32 to 144, the domain is characterized as Ig-like V-type.
+At position 148 to 237, the domain is characterized as Ig-like C2-type 1.
+At position 248 to 331, the domain is characterized as Ig-like C2-type 2.
+At position 89 to 131, the domain is characterized as Agouti.
+At position 135 to 292, the domain is characterized as Integrase catalytic.
+At position 217 to 383, the domain is characterized as JmjC.
+At position 155 to 206, the domain is characterized as bHLH.
+At position 37 to 102, the domain is characterized as J.
+At position 20 to 102, the domain is characterized as Lipoyl-binding.
+At position 35 to 179, the domain is characterized as C-type lectin.
+At position 26 to 124, the domain is characterized as Fibronectin type-III 1.
+At position 127 to 224, the domain is characterized as Fibronectin type-III 2.
+At position 137 to 293, the domain is characterized as PID.
+At position 561 to 747, the domain is characterized as Rab-GAP TBC.
+At position 5 to 192, the domain is characterized as AMMECR1.
+At position 8 to 213, the domain is characterized as ABC transporter.
+At position 30 to 291, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 32 to 150, the domain is characterized as C-type lectin.
+At position 1082 to 1157, the domain is characterized as DEP.
+At position 304 to 509, the domain is characterized as MCM.
+At position 25 to 108, the domain is characterized as PB1.
+At position 254 to 522, the domain is characterized as Protein kinase.
+At position 523 to 594, the domain is characterized as AGC-kinase C-terminal.
+At position 353 to 405, the domain is characterized as bHLH.
+At position 45 to 148, the domain is characterized as Cadherin 1.
+At position 149 to 255, the domain is characterized as Cadherin 2.
+At position 256 to 370, the domain is characterized as Cadherin 3.
+At position 371 to 475, the domain is characterized as Cadherin 4.
+At position 476 to 592, the domain is characterized as Cadherin 5.
+At position 2 to 89, the domain is characterized as FAD-binding FR-type.
+At position 2 to 171, the domain is characterized as N-acetyltransferase.
+At position 150 to 353, the domain is characterized as ATP-grasp.
+At position 109 to 317, the domain is characterized as ATP-grasp.
+At position 7 to 128, the domain is characterized as MsrB.
+At position 148 to 242, the domain is characterized as GS beta-grasp.
+At position 249 to 574, the domain is characterized as GS catalytic.
+At position 206 to 592, the domain is characterized as Peptidase S53.
+At position 98 to 127, the domain is characterized as KOW.
+At position 654 to 816, the domain is characterized as SSD.
+At position 297 to 374, the domain is characterized as B5.
+At position 142 to 407, the domain is characterized as Rap-GAP.
+At position 125 to 366, the domain is characterized as Protein kinase.
+At position 59 to 273, the domain is characterized as MurNAc-LAA.
+At position 125 to 369, the domain is characterized as NR LBD.
+At position 16 to 179, the domain is characterized as Helicase ATP-binding.
+At position 203 to 374, the domain is characterized as Helicase C-terminal.
+At position 5 to 262, the domain is characterized as Glutamine amidotransferase type-1.
+At position 199 to 512, the domain is characterized as IF rod.
+At position 346 to 440, the domain is characterized as BRCT.
+At position 117 to 218, the domain is characterized as Fe2OG dioxygenase.
+At position 2 to 251, the domain is characterized as GP-PDE.
+At position 106 to 364, the domain is characterized as Protein kinase.
+At position 407 to 442, the domain is characterized as EF-hand 1.
+At position 443 to 478, the domain is characterized as EF-hand 2.
+At position 479 to 512, the domain is characterized as EF-hand 3.
+At position 513 to 548, the domain is characterized as EF-hand 4.
+At position 636 to 936, the domain is characterized as Autotransporter.
+At position 2 to 184, the domain is characterized as Guanylate kinase-like.
+At position 92 to 188, the domain is characterized as Rieske.
+At position 37 to 178, the domain is characterized as GAF.
+At position 211 to 439, the domain is characterized as Sigma-54 factor interaction.
+At position 157 to 207, the domain is characterized as DHHC.
+At position 35 to 148, the domain is characterized as sHSP.
+At position 172 to 375, the domain is characterized as SMP-LTD.
+At position 366 to 487, the domain is characterized as C2 1.
+At position 512 to 636, the domain is characterized as C2 2.
+At position 640 to 757, the domain is characterized as C2 3.
+At position 976 to 1094, the domain is characterized as C2 4.
+At position 37 to 146, the domain is characterized as Ig-like V-type.
+At position 156 to 243, the domain is characterized as Ig-like C2-type.
+At position 38 to 87, the domain is characterized as FHA-like.
+At position 182 to 287, the domain is characterized as HIT.
+At position 23 to 71, the domain is characterized as F-box.
+At position 416 to 466, the domain is characterized as FBD.
+At position 42 to 105, the domain is characterized as bZIP.
+At position 217 to 399, the domain is characterized as GAF.
+At position 622 to 692, the domain is characterized as PAS 1.
+At position 906 to 1123, the domain is characterized as Histidine kinase.
+At position 5 to 241, the domain is characterized as ABC transporter.
+At position 226 to 437, the domain is characterized as Peptidase M12B.
+At position 447 to 522, the domain is characterized as Disintegrin.
+At position 523 to 578, the domain is characterized as TSP type-1 1.
+At position 804 to 863, the domain is characterized as TSP type-1 2.
+At position 864 to 923, the domain is characterized as TSP type-1 3.
+At position 925 to 978, the domain is characterized as TSP type-1 4.
+At position 1366 to 1414, the domain is characterized as TSP type-1 5.
+At position 1417 to 1477, the domain is characterized as TSP type-1 6.
+At position 1479 to 1522, the domain is characterized as TSP type-1 7.
+At position 1524 to 1584, the domain is characterized as TSP type-1 8.
+At position 1587 to 1627, the domain is characterized as PLAC.
+At position 169 to 427, the domain is characterized as uDENN.
+At position 449 to 586, the domain is characterized as cDENN.
+At position 588 to 919, the domain is characterized as dDENN.
+At position 367 to 439, the domain is characterized as Rho RNA-BD.
+At position 5 to 219, the domain is characterized as tr-type G.
+At position 12 to 162, the domain is characterized as UBC core.
+At position 343 to 397, the domain is characterized as L27 1.
+At position 402 to 461, the domain is characterized as L27 2.
+At position 495 to 576, the domain is characterized as PDZ.
+At position 582 to 651, the domain is characterized as SH3.
+At position 711 to 883, the domain is characterized as Guanylate kinase-like.
+At position 1 to 67, the domain is characterized as Phytocyanin.
+At position 67 to 205, the domain is characterized as C1q.
+At position 583 to 686, the domain is characterized as SH2.
+At position 284 to 438, the domain is characterized as PPIase cyclophilin-type.
+At position 174 to 243, the domain is characterized as HTH OST-type.
+At position 45 to 307, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 19, the domain is characterized as HPr.
+At position 9 to 140, the domain is characterized as DAGKc.
+At position 23 to 159, the domain is characterized as ENTH.
+At position 2 to 124, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 46 to 166, the domain is characterized as sHSP.
+At position 330 to 500, the domain is characterized as tr-type G.
+At position 53 to 222, the domain is characterized as Helicase ATP-binding.
+At position 233 to 394, the domain is characterized as Helicase C-terminal.
+At position 1 to 161, the domain is characterized as Obg.
+At position 162 to 335, the domain is characterized as OBG-type G.
+At position 208 to 361, the domain is characterized as OTU.
+At position 197 to 232, the domain is characterized as EF-hand 2.
+At position 321 to 356, the domain is characterized as EF-hand 3.
+At position 444 to 462, the domain is characterized as EF-hand 4.
+At position 528 to 563, the domain is characterized as EF-hand 5.
+At position 674 to 690, the domain is characterized as EF-hand 6.
+At position 763 to 798, the domain is characterized as EF-hand 7.
+At position 905 to 940, the domain is characterized as EF-hand 8.
+At position 1086 to 1121, the domain is characterized as EF-hand 9.
+At position 1193 to 1228, the domain is characterized as EF-hand 10.
+At position 1229 to 1264, the domain is characterized as EF-hand 11.
+At position 1348 to 1373, the domain is characterized as EF-hand 12.
+At position 1374 to 1409, the domain is characterized as EF-hand 13.
+At position 1454 to 1484, the domain is characterized as EF-hand 14.
+At position 1485 to 1516, the domain is characterized as EF-hand 15.
+At position 1 to 330, the domain is characterized as SAM-dependent MTase C5-type.
+At position 221 to 273, the domain is characterized as HAMP.
+At position 278 to 514, the domain is characterized as Methyl-accepting transducer.
+At position 58 to 141, the domain is characterized as PDZ 1.
+At position 156 to 244, the domain is characterized as PDZ 2.
+At position 258 to 342, the domain is characterized as PDZ 3.
+At position 468 to 555, the domain is characterized as PDZ 4.
+At position 569 to 652, the domain is characterized as PDZ 5.
+At position 667 to 749, the domain is characterized as PDZ 6.
+At position 974 to 1056, the domain is characterized as PDZ 7.
+At position 251 to 497, the domain is characterized as ABC transporter 2.
+At position 15 to 211, the domain is characterized as RNase H type-2.
+At position 112 to 220, the domain is characterized as sHSP.
+At position 152 to 435, the domain is characterized as ABC transmembrane type-1.
+At position 468 to 702, the domain is characterized as ABC transporter.
+At position 64 to 281, the domain is characterized as Radical SAM core.
+At position 19 to 101, the domain is characterized as KRAB.
+At position 238 to 347, the domain is characterized as Guanylate cyclase.
+At position 24 to 351, the domain is characterized as Transferrin-like 1.
+At position 363 to 692, the domain is characterized as Transferrin-like 2.
+At position 99 to 356, the domain is characterized as Protein kinase.
+At position 357 to 432, the domain is characterized as AGC-kinase C-terminal.
+At position 36 to 260, the domain is characterized as Radical SAM core.
+At position 116 to 439, the domain is characterized as YcaO.
+At position 122 to 346, the domain is characterized as Radical SAM core.
+At position 22 to 193, the domain is characterized as Laminin G-like.
+At position 316 to 354, the domain is characterized as EGF-like 1; calcium-binding.
+At position 370 to 410, the domain is characterized as EGF-like 2; calcium-binding.
+At position 414 to 456, the domain is characterized as EGF-like 3.
+At position 727 to 941, the domain is characterized as TSP C-terminal.
+At position 7 to 83, the domain is characterized as RRM 1.
+At position 106 to 184, the domain is characterized as RRM 2.
+At position 214 to 286, the domain is characterized as RRM 3.
+At position 50 to 118, the domain is characterized as POTRA.
+At position 32 to 306, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1 to 230, the domain is characterized as Reverse transcriptase.
+At position 12 to 44, the domain is characterized as LisH.
+At position 94 to 165, the domain is characterized as GRAM.
+At position 230 to 605, the domain is characterized as Myotubularin phosphatase.
+At position 33 to 212, the domain is characterized as SIS.
+At position 77 to 117, the domain is characterized as F-box.
+At position 46 to 229, the domain is characterized as PID.
+At position 374 to 465, the domain is characterized as SH2.
+At position 110 to 202, the domain is characterized as Fibronectin type-III 1.
+At position 203 to 294, the domain is characterized as Fibronectin type-III 2.
+At position 571 to 671, the domain is characterized as Fibronectin type-III 3.
+At position 952 to 1047, the domain is characterized as Fibronectin type-III 4.
+At position 1051 to 1158, the domain is characterized as Fibronectin type-III 5.
+At position 1459 to 1569, the domain is characterized as Fibronectin type-III 6.
+At position 1570 to 1669, the domain is characterized as Fibronectin type-III 7.
+At position 1671 to 1766, the domain is characterized as Fibronectin type-III 8.
+At position 1767 to 1868, the domain is characterized as Fibronectin type-III 9.
+At position 1961 to 2240, the domain is characterized as Protein kinase.
+At position 133 to 218, the domain is characterized as RRM 1.
+At position 264 to 349, the domain is characterized as RRM 2.
+At position 100 to 236, the domain is characterized as PLAT.
+At position 242 to 941, the domain is characterized as Lipoxygenase.
+At position 5 to 128, the domain is characterized as Glycine radical.
+At position 27 to 152, the domain is characterized as NTR.
+At position 23 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 100 to 199, the domain is characterized as Ig-like C2-type 2.
+At position 206 to 301, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 399 to 504, the domain is characterized as Ig-like C2-type 5.
+At position 580 to 922, the domain is characterized as Protein kinase.
+At position 379 to 414, the domain is characterized as EF-hand 1.
+At position 451 to 486, the domain is characterized as EF-hand 2.
+At position 316 to 463, the domain is characterized as Cupin type-1 2.
+At position 8 to 177, the domain is characterized as Thioredoxin.
+At position 143 to 270, the domain is characterized as Fatty acid hydroxylase.
+At position 380 to 775, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1221 to 1530, the domain is characterized as PKS/mFAS DH.
+At position 1574 to 1651, the domain is characterized as Carrier 1.
+At position 1685 to 1761, the domain is characterized as Carrier 2.
+At position 444 to 566, the domain is characterized as HD.
+At position 683 to 762, the domain is characterized as ACT 1.
+At position 791 to 859, the domain is characterized as ACT 2.
+At position 346 to 411, the domain is characterized as S4 RNA-binding.
+At position 659 to 783, the domain is characterized as C2 2.
+At position 1093 to 1236, the domain is characterized as MHD1.
+At position 1345 to 1512, the domain is characterized as MHD2.
+At position 1526 to 1653, the domain is characterized as C2 3.
+At position 22 to 75, the domain is characterized as WAP.
+At position 114 to 163, the domain is characterized as Kazal-like.
+At position 193 to 286, the domain is characterized as Ig-like C2-type.
+At position 314 to 363, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 371 to 421, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 421 to 550, the domain is characterized as NTR.
+At position 9 to 123, the domain is characterized as MSS4.
+At position 386 to 555, the domain is characterized as tr-type G.
+At position 87 to 147, the domain is characterized as Chromo.
+At position 21 to 53, the domain is characterized as LRRNT.
+At position 300 to 352, the domain is characterized as LRRCT.
+At position 211 to 345, the domain is characterized as PADR1 zinc-binding.
+At position 369 to 460, the domain is characterized as BRCT.
+At position 525 to 621, the domain is characterized as WGR.
+At position 645 to 762, the domain is characterized as PARP alpha-helical.
+At position 771 to 997, the domain is characterized as PARP catalytic.
+At position 21 to 71, the domain is characterized as F-box.
+At position 78 to 421, the domain is characterized as USP.
+At position 7 to 263, the domain is characterized as ABC transporter.
+At position 114 to 237, the domain is characterized as MRH.
+At position 181 to 263, the domain is characterized as Cyclin N-terminal.
+At position 40 to 203, the domain is characterized as Helicase ATP-binding.
+At position 236 to 442, the domain is characterized as Helicase C-terminal.
+At position 271 to 334, the domain is characterized as bZIP.
+At position 18 to 232, the domain is characterized as ABC transporter.
+At position 34 to 202, the domain is characterized as Helicase ATP-binding.
+At position 223 to 371, the domain is characterized as Helicase C-terminal.
+At position 529 to 609, the domain is characterized as HRDC.
+At position 402 to 671, the domain is characterized as Histidine kinase.
+At position 987 to 1120, the domain is characterized as Response regulatory.
+At position 406 to 435, the domain is characterized as IQ.
+At position 17 to 255, the domain is characterized as tr-type G.
+At position 22 to 110, the domain is characterized as EH 1.
+At position 54 to 89, the domain is characterized as EF-hand 1.
+At position 244 to 333, the domain is characterized as EH 2.
+At position 277 to 312, the domain is characterized as EF-hand 2.
+At position 757 to 818, the domain is characterized as SH3 1.
+At position 898 to 956, the domain is characterized as SH3 2.
+At position 981 to 1039, the domain is characterized as SH3 3.
+At position 1053 to 1117, the domain is characterized as SH3 4.
+At position 1127 to 1186, the domain is characterized as SH3 5.
+At position 1209 to 1395, the domain is characterized as DH.
+At position 1434 to 1544, the domain is characterized as PH.
+At position 1552 to 1668, the domain is characterized as C2.
+At position 252 to 380, the domain is characterized as MATH.
+At position 26 to 214, the domain is characterized as Reticulon.
+At position 45 to 230, the domain is characterized as GH16.
+At position 37 to 123, the domain is characterized as Inhibitor I9.
+At position 132 to 423, the domain is characterized as Peptidase S8.
+At position 6 to 138, the domain is characterized as Galectin.
+At position 510 to 617, the domain is characterized as Toprim.
+At position 143 to 381, the domain is characterized as Radical SAM core.
+At position 162 to 302, the domain is characterized as Jacalin-type lectin 2.
+At position 312 to 454, the domain is characterized as Jacalin-type lectin 3.
+At position 219 to 404, the domain is characterized as GAF.
+At position 750 to 834, the domain is characterized as PAS 2.
+At position 31 to 80, the domain is characterized as Myosin N-terminal SH3-like.
+At position 84 to 779, the domain is characterized as Myosin motor.
+At position 281 to 422, the domain is characterized as SIS 1.
+At position 4 to 97, the domain is characterized as FAD-binding FR-type.
+At position 280 to 516, the domain is characterized as Methyl-accepting transducer.
+At position 253 to 430, the domain is characterized as VWFA.
+At position 446 to 556, the domain is characterized as Cache.
+At position 23 to 203, the domain is characterized as EngB-type G.
+At position 25 to 94, the domain is characterized as IGFBP N-terminal.
+At position 226 to 271, the domain is characterized as TSP type-1.
+At position 284 to 358, the domain is characterized as CTCK.
+At position 46 to 180, the domain is characterized as Thioredoxin 1.
+At position 394 to 523, the domain is characterized as Thioredoxin 2.
+At position 691 to 953, the domain is characterized as Protein kinase.
+At position 609 to 687, the domain is characterized as BRCT.
+At position 136 to 276, the domain is characterized as Nudix hydrolase.
+At position 2 to 86, the domain is characterized as GST N-terminal.
+At position 93 to 229, the domain is characterized as GST C-terminal.
+At position 160 to 221, the domain is characterized as KH 1.
+At position 253 to 314, the domain is characterized as KH 2.
+At position 1 to 177, the domain is characterized as Macro.
+At position 4 to 96, the domain is characterized as ATP-cone.
+At position 443 to 582, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1063 to 1194, the domain is characterized as DOD-type homing endonuclease 2.
+At position 27 to 161, the domain is characterized as VOC 1.
+At position 193 to 351, the domain is characterized as VOC 2.
+At position 31 to 148, the domain is characterized as SEA.
+At position 158 to 388, the domain is characterized as Peptidase S1.
+At position 16 to 50, the domain is characterized as EF-hand 1.
+At position 112 to 233, the domain is characterized as Calponin-homology (CH) 1.
+At position 261 to 364, the domain is characterized as Calponin-homology (CH) 2.
+At position 385 to 495, the domain is characterized as Calponin-homology (CH) 3.
+At position 508 to 614, the domain is characterized as Calponin-homology (CH) 4.
+At position 7 to 42, the domain is characterized as EF-hand.
+At position 54 to 97, the domain is characterized as F-box.
+At position 232 to 437, the domain is characterized as PNPLA.
+At position 1 to 80, the domain is characterized as Sm.
+At position 296 to 332, the domain is characterized as DFDF.
+At position 152 to 198, the domain is characterized as G-patch.
+At position 72 to 191, the domain is characterized as RGS.
+At position 624 to 706, the domain is characterized as DIX.
+At position 320 to 419, the domain is characterized as Fibronectin type-III 3.
+At position 423 to 520, the domain is characterized as Fibronectin type-III 4.
+At position 20 to 112, the domain is characterized as Ig-like.
+At position 622 to 717, the domain is characterized as S1 motif.
+At position 96 to 256, the domain is characterized as JmjC.
+At position 130 to 180, the domain is characterized as DHHC.
+At position 95 to 165, the domain is characterized as CSD.
+At position 35 to 120, the domain is characterized as Ig-like V-type.
+At position 132 to 209, the domain is characterized as Ig-like C2-type.
+At position 369 to 491, the domain is characterized as Plastocyanin-like 3.
+At position 349 to 548, the domain is characterized as Protein kinase.
+At position 153 to 328, the domain is characterized as Helicase ATP-binding.
+At position 340 to 503, the domain is characterized as Helicase C-terminal.
+At position 6 to 75, the domain is characterized as HTH HARE-type.
+At position 52 to 177, the domain is characterized as Thioredoxin.
+At position 2 to 243, the domain is characterized as ABC transporter.
+At position 213 to 255, the domain is characterized as CHCH.
+At position 320 to 413, the domain is characterized as BRCT.
+At position 360 to 639, the domain is characterized as ABC transporter 1.
+At position 659 to 988, the domain is characterized as ABC transporter 2.
+At position 47 to 103, the domain is characterized as FHA.
+At position 441 to 476, the domain is characterized as UVR.
+At position 20 to 114, the domain is characterized as Ig-like.
+At position 49 to 288, the domain is characterized as Ras-GEF.
+At position 455 to 567, the domain is characterized as PH.
+At position 28 to 292, the domain is characterized as PPM-type phosphatase.
+At position 608 to 697, the domain is characterized as BRCT.
+At position 37 to 112, the domain is characterized as DEP.
+At position 255 to 316, the domain is characterized as G protein gamma.
+At position 333 to 448, the domain is characterized as RGS.
+At position 32 to 221, the domain is characterized as ABC transmembrane type-1.
+At position 182 to 358, the domain is characterized as EngA-type G 2.
+At position 359 to 439, the domain is characterized as KH-like.
+At position 25 to 157, the domain is characterized as MARVEL 1.
+At position 162 to 315, the domain is characterized as MARVEL 2.
+At position 6 to 186, the domain is characterized as YrdC-like.
+At position 60 to 267, the domain is characterized as TLC.
+At position 334 to 391, the domain is characterized as LIM zinc-binding 1.
+At position 393 to 452, the domain is characterized as LIM zinc-binding 2.
+At position 453 to 510, the domain is characterized as LIM zinc-binding 3.
+At position 511 to 569, the domain is characterized as LIM zinc-binding 4.
+At position 118 to 265, the domain is characterized as Ferric oxidoreductase.
+At position 162 to 257, the domain is characterized as 5'-3' exonuclease.
+At position 5 to 255, the domain is characterized as Pyruvate carboxyltransferase.
+At position 457 to 556, the domain is characterized as Tudor; atypical.
+At position 9 to 52, the domain is characterized as SpoVT-AbrB 1.
+At position 560 to 836, the domain is characterized as Protein kinase.
+At position 894 to 1024, the domain is characterized as Guanylate cyclase.
+At position 46 to 273, the domain is characterized as SET.
+At position 21 to 122, the domain is characterized as Ig-like.
+At position 128 to 383, the domain is characterized as Protein kinase.
+At position 384 to 455, the domain is characterized as AGC-kinase C-terminal.
+At position 415 to 550, the domain is characterized as Ricin B-type lectin.
+At position 262 to 460, the domain is characterized as GATase cobBQ-type.
+At position 50 to 89, the domain is characterized as Pentapeptide repeat 1.
+At position 90 to 129, the domain is characterized as Pentapeptide repeat 2.
+At position 140 to 179, the domain is characterized as Pentapeptide repeat 3.
+At position 185 to 224, the domain is characterized as Pentapeptide repeat 4.
+At position 230 to 269, the domain is characterized as Pentapeptide repeat 5.
+At position 1 to 54, the domain is characterized as TRAM.
+At position 28 to 264, the domain is characterized as ABC transporter.
+At position 215 to 424, the domain is characterized as Helicase ATP-binding.
+At position 460 to 626, the domain is characterized as Helicase C-terminal.
+At position 39 to 274, the domain is characterized as AB hydrolase-1.
+At position 2 to 101, the domain is characterized as ABM.
+At position 56 to 115, the domain is characterized as Collagen-like.
+At position 34 to 252, the domain is characterized as Radical SAM core.
+At position 587 to 664, the domain is characterized as BRCT.
+At position 82 to 183, the domain is characterized as Thioredoxin.
+At position 278 to 492, the domain is characterized as tr-type G.
+At position 107 to 314, the domain is characterized as ATP-grasp.
+At position 165 to 369, the domain is characterized as ATP-grasp.
+At position 4 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 100 to 184, the domain is characterized as PDZ.
+At position 346 to 534, the domain is characterized as Rab-GAP TBC.
+At position 93 to 344, the domain is characterized as NR LBD.
+At position 107 to 187, the domain is characterized as S1 motif.
+At position 1074 to 1234, the domain is characterized as N-terminal Ras-GEF.
+At position 1278 to 1508, the domain is characterized as Ras-GEF.
+At position 123 to 165, the domain is characterized as CHCH.
+At position 326 to 376, the domain is characterized as LIM zinc-binding 1.
+At position 385 to 435, the domain is characterized as LIM zinc-binding 2.
+At position 444 to 494, the domain is characterized as LIM zinc-binding 3.
+At position 503 to 553, the domain is characterized as LIM zinc-binding 4.
+At position 67 to 154, the domain is characterized as ABM.
+At position 11 to 68, the domain is characterized as HTH lysR-type.
+At position 11 to 249, the domain is characterized as ABC transporter.
+At position 32 to 177, the domain is characterized as UBC core.
+At position 4 to 246, the domain is characterized as ABC transporter.
+At position 217 to 402, the domain is characterized as GAF.
+At position 29 to 106, the domain is characterized as EMI.
+At position 105 to 135, the domain is characterized as EGF-like 1.
+At position 143 to 178, the domain is characterized as EGF-like 2.
+At position 186 to 221, the domain is characterized as EGF-like 3.
+At position 229 to 264, the domain is characterized as EGF-like 4.
+At position 277 to 307, the domain is characterized as EGF-like 5.
+At position 315 to 350, the domain is characterized as EGF-like 6.
+At position 404 to 439, the domain is characterized as EGF-like 7.
+At position 447 to 482, the domain is characterized as EGF-like 8.
+At position 490 to 525, the domain is characterized as EGF-like 9.
+At position 576 to 611, the domain is characterized as EGF-like 10.
+At position 664 to 699, the domain is characterized as EGF-like 11.
+At position 712 to 742, the domain is characterized as EGF-like 12.
+At position 750 to 785, the domain is characterized as EGF-like 13.
+At position 798 to 828, the domain is characterized as EGF-like 14.
+At position 790 to 1152, the domain is characterized as TTL.
+At position 95 to 180, the domain is characterized as Fibronectin type-III.
+At position 190 to 514, the domain is characterized as GH18.
+At position 6 to 284, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 16 to 94, the domain is characterized as MIT.
+At position 431 to 615, the domain is characterized as Senescence.
+At position 72 to 222, the domain is characterized as HD.
+At position 159 to 477, the domain is characterized as Protein kinase.
+At position 125 to 273, the domain is characterized as N-acetyltransferase.
+At position 49 to 268, the domain is characterized as Radical SAM core.
+At position 199 to 375, the domain is characterized as CRAL-TRIO.
+At position 8 to 95, the domain is characterized as ATP-cone.
+At position 71 to 93, the domain is characterized as Follistatin-like.
+At position 89 to 151, the domain is characterized as Kazal-like.
+At position 261 to 296, the domain is characterized as EF-hand.
+At position 86 to 211, the domain is characterized as GST C-terminal.
+At position 35 to 419, the domain is characterized as Helicase ATP-binding.
+At position 657 to 692, the domain is characterized as UVR.
+At position 25 to 61, the domain is characterized as EF-hand 1.
+At position 115 to 150, the domain is characterized as EF-hand 3.
+At position 28 to 281, the domain is characterized as Protein kinase.
+At position 24 to 90, the domain is characterized as Importin N-terminal.
+At position 7 to 41, the domain is characterized as WW.
+At position 71 to 182, the domain is characterized as PpiC.
+At position 41 to 429, the domain is characterized as Helicase ATP-binding.
+At position 446 to 612, the domain is characterized as Helicase C-terminal.
+At position 650 to 685, the domain is characterized as UVR.
+At position 1 to 241, the domain is characterized as Pyruvate carboxyltransferase.
+At position 291 to 320, the domain is characterized as IQ 1.
+At position 1280 to 1309, the domain is characterized as IQ 2.
+At position 1340 to 1369, the domain is characterized as IQ 3.
+At position 161 to 357, the domain is characterized as CheB-type methylesterase.
+At position 30 to 141, the domain is characterized as STAS.
+At position 93 to 233, the domain is characterized as GST C-terminal.
+At position 21 to 55, the domain is characterized as Anaphylatoxin-like.
+At position 1 to 72, the domain is characterized as Sm.
+At position 42 to 229, the domain is characterized as RNase H type-2.
+At position 122 to 364, the domain is characterized as Radical SAM core.
+At position 41 to 243, the domain is characterized as TLC.
+At position 45 to 246, the domain is characterized as Helicase ATP-binding.
+At position 278 to 436, the domain is characterized as Helicase C-terminal.
+At position 36 to 92, the domain is characterized as 4Fe-4S Wbl-type.
+At position 86 to 368, the domain is characterized as Protein kinase.
+At position 15 to 93, the domain is characterized as EH.
+At position 50 to 83, the domain is characterized as EF-hand 2.
+At position 194 to 429, the domain is characterized as Dynamin-type G.
+At position 25 to 277, the domain is characterized as Protein kinase.
+At position 391 to 469, the domain is characterized as POLO box 1.
+At position 491 to 572, the domain is characterized as POLO box 2.
+At position 16 to 83, the domain is characterized as Histone-fold.
+At position 78 to 170, the domain is characterized as Toprim.
+At position 966 to 995, the domain is characterized as IQ 2.
+At position 18 to 156, the domain is characterized as N-acetyltransferase 1.
+At position 168 to 314, the domain is characterized as N-acetyltransferase 2.
+At position 141 to 406, the domain is characterized as AB hydrolase-1.
+At position 14 to 146, the domain is characterized as ADF-H.
+At position 46 to 354, the domain is characterized as GH10.
+At position 93 to 146, the domain is characterized as ClpX-type ZB.
+At position 63 to 172, the domain is characterized as PH.
+At position 182 to 217, the domain is characterized as EF-hand 1.
+At position 218 to 253, the domain is characterized as EF-hand 2.
+At position 250 to 285, the domain is characterized as EF-hand 3.
+At position 337 to 482, the domain is characterized as PI-PLC X-box.
+At position 528 to 644, the domain is characterized as PI-PLC Y-box.
+At position 644 to 769, the domain is characterized as C2.
+At position 950 to 1110, the domain is characterized as UBC core.
+At position 1 to 251, the domain is characterized as Chorismate mutase.
+At position 3 to 102, the domain is characterized as Glutaredoxin.
+At position 195 to 270, the domain is characterized as RRM 1.
+At position 293 to 361, the domain is characterized as RRM 2.
+At position 34 to 110, the domain is characterized as Inhibitor I9.
+At position 114 to 584, the domain is characterized as Peptidase S8.
+At position 404 to 484, the domain is characterized as Rhodanese.
+At position 265 to 326, the domain is characterized as t-SNARE coiled-coil homology.
+At position 375 to 414, the domain is characterized as UBA.
+At position 1 to 129, the domain is characterized as PINc.
+At position 388 to 563, the domain is characterized as CRAL-TRIO.
+At position 1765 to 1839, the domain is characterized as Carrier 2.
+At position 619 to 781, the domain is characterized as MOSC.
+At position 34 to 206, the domain is characterized as VWFA 1.
+At position 235 to 413, the domain is characterized as VWFA 2.
+At position 430 to 653, the domain is characterized as VWFA 3.
+At position 634 to 811, the domain is characterized as VWFA 4.
+At position 849 to 1018, the domain is characterized as VWFA 5.
+At position 1030 to 1199, the domain is characterized as VWFA 6.
+At position 1776 to 1957, the domain is characterized as VWFA 7.
+At position 1982 to 2187, the domain is characterized as VWFA 8.
+At position 278 to 382, the domain is characterized as tRNA-binding.
+At position 135 to 246, the domain is characterized as Calponin-homology (CH).
+At position 278 to 454, the domain is characterized as DH.
+At position 478 to 668, the domain is characterized as PH.
+At position 761 to 854, the domain is characterized as PB1.
+At position 22 to 116, the domain is characterized as Ig-like.
+At position 98 to 183, the domain is characterized as PB1.
+At position 155 to 385, the domain is characterized as Radical SAM core.
+At position 388 to 450, the domain is characterized as TRAM.
+At position 97 to 387, the domain is characterized as ABC transmembrane type-1 1.
+At position 422 to 667, the domain is characterized as ABC transporter 1.
+At position 764 to 1051, the domain is characterized as ABC transmembrane type-1 2.
+At position 1086 to 1324, the domain is characterized as ABC transporter 2.
+At position 88 to 191, the domain is characterized as Glutaredoxin.
+At position 187 to 216, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 71 to 355, the domain is characterized as Protein kinase.
+At position 1 to 115, the domain is characterized as C2.
+At position 326 to 359, the domain is characterized as WW 1.
+At position 438 to 471, the domain is characterized as WW 3.
+At position 478 to 511, the domain is characterized as WW 4.
+At position 569 to 903, the domain is characterized as HECT.
+At position 31 to 286, the domain is characterized as Protein kinase.
+At position 328 to 352, the domain is characterized as NAF.
+At position 46 to 140, the domain is characterized as Ig-like C2-type 1.
+At position 149 to 244, the domain is characterized as Fibronectin type-III.
+At position 262 to 346, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 76, the domain is characterized as CS.
+At position 32 to 283, the domain is characterized as Protein kinase.
+At position 6 to 125, the domain is characterized as VOC.
+At position 587 to 824, the domain is characterized as ABC transporter.
+At position 90 to 178, the domain is characterized as K-box.
+At position 308 to 516, the domain is characterized as PCI.
+At position 1074 to 1213, the domain is characterized as Guanylate cyclase 2.
+At position 62 to 217, the domain is characterized as Cupin type-1.
+At position 7 to 82, the domain is characterized as ACT.
+At position 9 to 140, the domain is characterized as TsaA-like.
+At position 58 to 207, the domain is characterized as Cupin type-1.
+At position 8 to 172, the domain is characterized as PPIase cyclophilin-type.
+At position 582 to 661, the domain is characterized as BRCT.
+At position 236 to 311, the domain is characterized as PUA.
+At position 96 to 388, the domain is characterized as ABC transmembrane type-1.
+At position 922 to 1322, the domain is characterized as FH2.
+At position 31 to 64, the domain is characterized as LRRNT.
+At position 170 to 220, the domain is characterized as LRRCT.
+At position 86 to 264, the domain is characterized as FBA.
+At position 110 to 297, the domain is characterized as ATP-grasp.
+At position 19 to 142, the domain is characterized as PX.
+At position 348 to 441, the domain is characterized as BRCT.
+At position 554 to 645, the domain is characterized as GED.
+At position 78 to 130, the domain is characterized as bHLH.
+At position 54 to 151, the domain is characterized as Ig-like.
+At position 153 to 244, the domain is characterized as Ig-like C2-type.
+At position 252 to 306, the domain is characterized as TSP type-1 1.
+At position 308 to 360, the domain is characterized as TSP type-1 2.
+At position 542 to 682, the domain is characterized as ZU5.
+At position 859 to 936, the domain is characterized as Death.
+At position 264 to 338, the domain is characterized as POU-specific.
+At position 57 to 468, the domain is characterized as USP.
+At position 8 to 109, the domain is characterized as PH.
+At position 122 to 236, the domain is characterized as IRS-type PTB.
+At position 58 to 174, the domain is characterized as Rieske.
+At position 793 to 869, the domain is characterized as Carrier.
+At position 42 to 77, the domain is characterized as EF-hand 1.
+At position 119 to 154, the domain is characterized as EF-hand 2.
+At position 91 to 213, the domain is characterized as GST C-terminal.
+At position 11 to 442, the domain is characterized as Helicase ATP-binding.
+At position 6 to 81, the domain is characterized as Carrier.
+At position 177 to 363, the domain is characterized as Glutamine amidotransferase type-1.
+At position 522 to 714, the domain is characterized as ATP-grasp 1.
+At position 1057 to 1248, the domain is characterized as ATP-grasp 2.
+At position 1313 to 1469, the domain is characterized as MGS-like.
+At position 31 to 310, the domain is characterized as tr-type G.
+At position 11 to 164, the domain is characterized as MPN.
+At position 15 to 44, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 1 to 121, the domain is characterized as Nudix hydrolase.
+At position 80 to 178, the domain is characterized as Mis18.
+At position 16 to 111, the domain is characterized as Ig-like.
+At position 172 to 294, the domain is characterized as HotDog ACOT-type 1.
+At position 370 to 487, the domain is characterized as HotDog ACOT-type 2.
+At position 127 to 163, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 17 to 112, the domain is characterized as HPt.
+At position 1 to 95, the domain is characterized as PTS EIIB type-2.
+At position 352 to 410, the domain is characterized as S4 RNA-binding.
+At position 49 to 165, the domain is characterized as DOMON.
+At position 13 to 58, the domain is characterized as SCP.
+At position 84 to 170, the domain is characterized as S4 RNA-binding.
+At position 6 to 108, the domain is characterized as LOB.
+At position 60 to 89, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 115 to 143, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 134 to 197, the domain is characterized as bZIP.
+At position 267 to 325, the domain is characterized as COS.
+At position 258 to 378, the domain is characterized as OmpA-like.
+At position 106 to 413, the domain is characterized as Peptidase A1.
+At position 140 to 369, the domain is characterized as Radical SAM core.
+At position 372 to 436, the domain is characterized as TRAM.
+At position 217 to 543, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 38 to 232, the domain is characterized as AMMECR1.
+At position 614 to 861, the domain is characterized as DDHD.
+At position 17 to 147, the domain is characterized as VHS.
+At position 171 to 299, the domain is characterized as GAT.
+At position 510 to 631, the domain is characterized as GAE.
+At position 26 to 246, the domain is characterized as Peptidase S1.
+At position 76 to 184, the domain is characterized as DUSP.
+At position 309 to 930, the domain is characterized as USP.
+At position 40 to 76, the domain is characterized as LDL-receptor class A 1.
+At position 79 to 117, the domain is characterized as LDL-receptor class A 2.
+At position 120 to 158, the domain is characterized as LDL-receptor class A 3.
+At position 160 to 196, the domain is characterized as LDL-receptor class A 4.
+At position 199 to 238, the domain is characterized as LDL-receptor class A 5.
+At position 250 to 287, the domain is characterized as LDL-receptor class A 6.
+At position 290 to 326, the domain is characterized as LDL-receptor class A 7.
+At position 330 to 369, the domain is characterized as LDL-receptor class A 8.
+At position 364 to 408, the domain is characterized as EGF-like 1.
+At position 409 to 448, the domain is characterized as EGF-like 2; calcium-binding.
+At position 11 to 71, the domain is characterized as v-SNARE coiled-coil homology.
+At position 8 to 141, the domain is characterized as ADF-H.
+At position 37 to 302, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 180 to 232, the domain is characterized as HAMP.
+At position 240 to 440, the domain is characterized as Histidine kinase.
+At position 220 to 247, the domain is characterized as PLD phosphodiesterase 1.
+At position 8 to 421, the domain is characterized as PTS EIIC type-3.
+At position 24 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 94 to 236, the domain is characterized as Clp R.
+At position 511 to 546, the domain is characterized as UVR.
+At position 24 to 280, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 22 to 79, the domain is characterized as TSP type-1 1.
+At position 81 to 134, the domain is characterized as TSP type-1 2.
+At position 139 to 174, the domain is characterized as LDL-receptor class A.
+At position 176 to 522, the domain is characterized as MACPF.
+At position 523 to 553, the domain is characterized as EGF-like.
+At position 565 to 612, the domain is characterized as TSP type-1 3.
+At position 642 to 701, the domain is characterized as Sushi 1.
+At position 702 to 763, the domain is characterized as Sushi 2.
+At position 780 to 839, the domain is characterized as Kazal-like 1.
+At position 876 to 932, the domain is characterized as Kazal-like 2.
+At position 80 to 173, the domain is characterized as K-box.
+At position 813 to 877, the domain is characterized as SAM.
+At position 112 to 288, the domain is characterized as VWFD 1.
+At position 472 to 645, the domain is characterized as VWFD 2.
+At position 736 to 791, the domain is characterized as TIL 1.
+At position 937 to 1114, the domain is characterized as VWFD 3.
+At position 1366 to 1418, the domain is characterized as TIL 2.
+At position 1506 to 1695, the domain is characterized as VWFD 4.
+At position 2233 to 2325, the domain is characterized as CTCK.
+At position 373 to 561, the domain is characterized as DH.
+At position 590 to 689, the domain is characterized as PH 1.
+At position 821 to 921, the domain is characterized as PH 2.
+At position 20 to 135, the domain is characterized as PH.
+At position 641 to 825, the domain is characterized as Lon proteolytic.
+At position 109 to 175, the domain is characterized as S4 RNA-binding.
+At position 49 to 147, the domain is characterized as Plastocyanin-like 1.
+At position 194 to 304, the domain is characterized as Plastocyanin-like 2.
+At position 386 to 498, the domain is characterized as Plastocyanin-like 3.
+At position 69 to 377, the domain is characterized as IF rod.
+At position 130 to 165, the domain is characterized as EF-hand 4.
+At position 33 to 284, the domain is characterized as Tyrosine-protein phosphatase.
+At position 610 to 797, the domain is characterized as SEC7.
+At position 86 to 162, the domain is characterized as Biotinyl-binding.
+At position 61 to 202, the domain is characterized as DAGKc.
+At position 39 to 122, the domain is characterized as Ig-like V-type.
+At position 150 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 240 to 336, the domain is characterized as Ig-like C2-type 2.
+At position 262 to 592, the domain is characterized as Kinesin motor.
+At position 182 to 404, the domain is characterized as Letm1 RBD.
+At position 567 to 681, the domain is characterized as Fe2OG dioxygenase.
+At position 50 to 311, the domain is characterized as Protein kinase.
+At position 520 to 770, the domain is characterized as Protein kinase.
+At position 542 to 603, the domain is characterized as SH3.
+At position 372 to 799, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1288 to 1598, the domain is characterized as PKS/mFAS DH.
+At position 1659 to 1733, the domain is characterized as Carrier.
+At position 58 to 238, the domain is characterized as FAD-binding PCMH-type.
+At position 66 to 250, the domain is characterized as SMP-LTD 1.
+At position 66 to 248, the domain is characterized as SMP-LTD 2.
+At position 242 to 362, the domain is characterized as C2 1.
+At position 246 to 364, the domain is characterized as C2.
+At position 461 to 500, the domain is characterized as C2 3.
+At position 88 to 288, the domain is characterized as Helicase ATP-binding.
+At position 321 to 473, the domain is characterized as Helicase C-terminal.
+At position 119 to 314, the domain is characterized as ATP-grasp.
+At position 63 to 201, the domain is characterized as Flavodoxin-like.
+At position 37 to 135, the domain is characterized as Fibronectin type-III 1.
+At position 136 to 242, the domain is characterized as Fibronectin type-III 2.
+At position 208 to 344, the domain is characterized as KARI C-terminal knotted 1.
+At position 96 to 128, the domain is characterized as LisH.
+At position 129 to 190, the domain is characterized as CTLH.
+At position 339 to 546, the domain is characterized as MCM.
+At position 68 to 147, the domain is characterized as Carrier.
+At position 873 to 1327, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 52 to 228, the domain is characterized as PI-PLC X-box.
+At position 30 to 73, the domain is characterized as SMB 1.
+At position 74 to 118, the domain is characterized as SMB 2.
+At position 255 to 464, the domain is characterized as Peptidase M12B.
+At position 465 to 552, the domain is characterized as Disintegrin.
+At position 553 to 608, the domain is characterized as TSP type-1 1.
+At position 843 to 901, the domain is characterized as TSP type-1 2.
+At position 906 to 962, the domain is characterized as TSP type-1 3.
+At position 962 to 1015, the domain is characterized as TSP type-1 4.
+At position 1017 to 1074, the domain is characterized as TSP type-1 5.
+At position 1075 to 1131, the domain is characterized as TSP type-1 6.
+At position 1148 to 1202, the domain is characterized as TSP type-1 7.
+At position 1203 to 1260, the domain is characterized as TSP type-1 8.
+At position 1300 to 1351, the domain is characterized as TSP type-1 9.
+At position 1354 to 1411, the domain is characterized as TSP type-1 10.
+At position 1412 to 1465, the domain is characterized as TSP type-1 11.
+At position 1468 to 1526, the domain is characterized as TSP type-1 12.
+At position 1527 to 1584, the domain is characterized as TSP type-1 13.
+At position 1585 to 1648, the domain is characterized as TSP type-1 14.
+At position 1650 to 1706, the domain is characterized as TSP type-1 15.
+At position 1707 to 1906, the domain is characterized as GON.
+At position 204 to 286, the domain is characterized as Cyclin N-terminal.
+At position 66 to 123, the domain is characterized as 4Fe-4S Wbl-type.
+At position 33 to 201, the domain is characterized as Tyrosine-protein phosphatase.
+At position 25 to 190, the domain is characterized as TIR.
+At position 206 to 434, the domain is characterized as NB-ARC.
+At position 66 to 293, the domain is characterized as Radical SAM core.
+At position 136 to 257, the domain is characterized as Peptidase C51.
+At position 213 to 397, the domain is characterized as Helicase ATP-binding.
+At position 408 to 568, the domain is characterized as Helicase C-terminal.
+At position 16 to 265, the domain is characterized as Pyruvate carboxyltransferase.
+At position 7 to 101, the domain is characterized as Core-binding (CB).
+At position 231 to 333, the domain is characterized as PpiC 1.
+At position 352 to 450, the domain is characterized as PpiC 2.
+At position 1640 to 2185, the domain is characterized as FAT.
+At position 2296 to 2604, the domain is characterized as PI3K/PI4K catalytic.
+At position 2612 to 2644, the domain is characterized as FATC.
+At position 91 to 272, the domain is characterized as Guanylate kinase-like.
+At position 5 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 90, the domain is characterized as Phosphagen kinase N-terminal.
+At position 152 to 200, the domain is characterized as bHLH.
+At position 64 to 210, the domain is characterized as Cadherin 1.
+At position 211 to 321, the domain is characterized as Cadherin 2.
+At position 322 to 536, the domain is characterized as Cadherin 3.
+At position 537 to 640, the domain is characterized as Cadherin 4.
+At position 641 to 743, the domain is characterized as Cadherin 5.
+At position 747 to 864, the domain is characterized as Cadherin 6.
+At position 83 to 170, the domain is characterized as PA.
+At position 1 to 149, the domain is characterized as RPW8.
+At position 247 to 414, the domain is characterized as NB-ARC.
+At position 274 to 323, the domain is characterized as SOCS box.
+At position 174 to 414, the domain is characterized as NR LBD.
+At position 102 to 186, the domain is characterized as GST N-terminal.
+At position 195 to 344, the domain is characterized as GST C-terminal.
+At position 66 to 108, the domain is characterized as LDL-receptor class A.
+At position 141 to 174, the domain is characterized as WW 1.
+At position 199 to 232, the domain is characterized as WW 2.
+At position 833 to 988, the domain is characterized as JmjC.
+At position 28 to 164, the domain is characterized as Ephrin RBD.
+At position 313 to 720, the domain is characterized as Protein kinase.
+At position 514 to 768, the domain is characterized as ATP-grasp.
+At position 101 to 229, the domain is characterized as Thioredoxin.
+At position 19 to 167, the domain is characterized as Thioredoxin.
+At position 1 to 63, the domain is characterized as Kazal-like 1.
+At position 64 to 128, the domain is characterized as Kazal-like 2.
+At position 131 to 185, the domain is characterized as Kazal-like 3.
+At position 1 to 101, the domain is characterized as Fibronectin type-III.
+At position 1556 to 1629, the domain is characterized as DEP.
+At position 113 to 236, the domain is characterized as PX.
+At position 91 to 244, the domain is characterized as CRAL-TRIO.
+At position 276 to 464, the domain is characterized as Rho-GAP.
+At position 170 to 220, the domain is characterized as bHLH.
+At position 180 to 418, the domain is characterized as Histidine kinase.
+At position 43 to 116, the domain is characterized as H15.
+At position 1 to 56, the domain is characterized as PDZ.
+At position 2 to 218, the domain is characterized as Glutamine amidotransferase type-1.
+At position 687 to 762, the domain is characterized as Smr.
+At position 21 to 311, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 312 to 603, the domain is characterized as UvrD-like helicase C-terminal.
+At position 611 to 828, the domain is characterized as Rap-GAP.
+At position 966 to 1042, the domain is characterized as PDZ.
+At position 35 to 362, the domain is characterized as G-alpha.
+At position 165 to 200, the domain is characterized as EF-hand 5.
+At position 200 to 233, the domain is characterized as EF-hand 6.
+At position 232 to 267, the domain is characterized as EF-hand 7.
+At position 269 to 304, the domain is characterized as EF-hand 8.
+At position 20 to 488, the domain is characterized as Sema.
+At position 840 to 933, the domain is characterized as IPT/TIG 1.
+At position 935 to 1020, the domain is characterized as IPT/TIG 2.
+At position 1023 to 1122, the domain is characterized as IPT/TIG 3.
+At position 1125 to 1211, the domain is characterized as IPT/TIG 4.
+At position 71 to 167, the domain is characterized as Ig-like 1.
+At position 174 to 276, the domain is characterized as Ig-like 2.
+At position 232 to 261, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 67, the domain is characterized as PQ-loop 1.
+At position 162 to 212, the domain is characterized as PQ-loop 2.
+At position 36 to 306, the domain is characterized as Deacetylase sirtuin-type.
+At position 127 to 197, the domain is characterized as BTB.
+At position 255 to 562, the domain is characterized as Protein kinase.
+At position 733 to 832, the domain is characterized as GAE.
+At position 45 to 148, the domain is characterized as THUMP.
+At position 17 to 48, the domain is characterized as LRRNT.
+At position 234 to 280, the domain is characterized as LRRCT.
+At position 281 to 367, the domain is characterized as Ig-like.
+At position 405 to 502, the domain is characterized as Fibronectin type-III.
+At position 1 to 64, the domain is characterized as S4 RNA-binding.
+At position 10 to 57, the domain is characterized as F-box.
+At position 78 to 259, the domain is characterized as FBA.
+At position 37 to 153, the domain is characterized as Plastocyanin-like 1.
+At position 162 to 316, the domain is characterized as Plastocyanin-like 2.
+At position 429 to 571, the domain is characterized as Plastocyanin-like 3.
+At position 135 to 345, the domain is characterized as ATP-grasp.
+At position 200 to 290, the domain is characterized as Death.
+At position 895 to 1007, the domain is characterized as VRR-NUC.
+At position 478 to 653, the domain is characterized as Helicase ATP-binding.
+At position 678 to 823, the domain is characterized as Helicase C-terminal.
+At position 1029 to 1111, the domain is characterized as HRDC.
+At position 34 to 139, the domain is characterized as PH.
+At position 664 to 858, the domain is characterized as Rab-GAP TBC.
+At position 346 to 513, the domain is characterized as tr-type G.
+At position 239 to 420, the domain is characterized as PCI.
+At position 47 to 78, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 133 to 218, the domain is characterized as Ig-like C2-type 1.
+At position 223 to 309, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 57, the domain is characterized as UBA.
+At position 569 to 646, the domain is characterized as UBX.
+At position 115 to 182, the domain is characterized as SUI1.
+At position 17 to 135, the domain is characterized as MARVEL.
+At position 66 to 162, the domain is characterized as Rieske.
+At position 4 to 72, the domain is characterized as Sm.
+At position 40 to 102, the domain is characterized as J.
+At position 223 to 449, the domain is characterized as IRG-type G.
+At position 512 to 852, the domain is characterized as PUM-HD.
+At position 18 to 70, the domain is characterized as F-box.
+At position 254 to 291, the domain is characterized as PKD.
+At position 6 to 239, the domain is characterized as Radical SAM core.
+At position 592 to 717, the domain is characterized as DBINO.
+At position 845 to 1017, the domain is characterized as Helicase ATP-binding.
+At position 1422 to 1582, the domain is characterized as Helicase C-terminal.
+At position 52 to 351, the domain is characterized as PPM-type phosphatase.
+At position 14 to 101, the domain is characterized as ATP-cone.
+At position 507 to 634, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1286 to 1426, the domain is characterized as DOD-type homing endonuclease 2.
+At position 134 to 513, the domain is characterized as Myotubularin phosphatase.
+At position 75 to 190, the domain is characterized as HD.
+At position 81 to 133, the domain is characterized as bHLH.
+At position 123 to 211, the domain is characterized as PPIase FKBP-type.
+At position 7 to 63, the domain is characterized as CSD.
+At position 139 to 303, the domain is characterized as FCP1 homology.
+At position 351 to 443, the domain is characterized as BRCT.
+At position 645 to 720, the domain is characterized as Carrier.
+At position 408 to 663, the domain is characterized as Bin3-type SAM.
+At position 150 to 211, the domain is characterized as OVATE.
+At position 24 to 101, the domain is characterized as RRM.
+At position 250 to 288, the domain is characterized as Myb-like 1.
+At position 289 to 343, the domain is characterized as HTH myb-type 1.
+At position 344 to 395, the domain is characterized as Myb-like 2.
+At position 396 to 451, the domain is characterized as HTH myb-type 2.
+At position 452 to 503, the domain is characterized as HTH myb-type 3.
+At position 237 to 264, the domain is characterized as PLD phosphodiesterase 1.
+At position 413 to 440, the domain is characterized as PLD phosphodiesterase 2.
+At position 15 to 256, the domain is characterized as ABC transporter 1.
+At position 266 to 511, the domain is characterized as ABC transporter 2.
+At position 465 to 579, the domain is characterized as Toprim.
+At position 296 to 540, the domain is characterized as ABC transporter 1.
+At position 617 to 832, the domain is characterized as ABC transporter 2.
+At position 440 to 609, the domain is characterized as tr-type G.
+At position 1 to 164, the domain is characterized as KaiA N-terminal.
+At position 174 to 282, the domain is characterized as KaiA C-terminal.
+At position 40 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 140 to 251, the domain is characterized as Ig-like C2-type 2.
+At position 34 to 159, the domain is characterized as PLAT.
+At position 162 to 853, the domain is characterized as Lipoxygenase.
+At position 139 to 344, the domain is characterized as ATP-grasp.
+At position 23 to 168, the domain is characterized as 6-Cys 1.
+At position 169 to 343, the domain is characterized as 6-Cys 2.
+At position 45 to 103, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 578 to 693, the domain is characterized as BAH.
+At position 727 to 1268, the domain is characterized as SAM-dependent MTase C5-type.
+At position 837 to 902, the domain is characterized as Chromo.
+At position 606 to 935, the domain is characterized as ABC transporter 2.
+At position 4 to 144, the domain is characterized as SprT-like.
+At position 59 to 229, the domain is characterized as Helicase ATP-binding.
+At position 240 to 400, the domain is characterized as Helicase C-terminal.
+At position 120 to 212, the domain is characterized as TNT.
+At position 932 to 1066, the domain is characterized as MGS-like.
+At position 19 to 228, the domain is characterized as tr-type G.
+At position 408 to 777, the domain is characterized as GRAS.
+At position 680 to 914, the domain is characterized as NR LBD.
+At position 10 to 72, the domain is characterized as LCN-type CS-alpha/beta.
+At position 30 to 141, the domain is characterized as Thioredoxin 1.
+At position 355 to 487, the domain is characterized as Thioredoxin 2.
+At position 2 to 139, the domain is characterized as Nudix hydrolase.
+At position 38 to 227, the domain is characterized as BPL/LPL catalytic.
+At position 30 to 154, the domain is characterized as ENTH.
+At position 337 to 491, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 29 to 143, the domain is characterized as Ig-like V-type.
+At position 19 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 136 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 133 to 399, the domain is characterized as Peptidase S8.
+At position 3 to 125, the domain is characterized as RNase III.
+At position 152 to 222, the domain is characterized as DRBM.
+At position 681 to 756, the domain is characterized as Smr.
+At position 5 to 148, the domain is characterized as Jacalin-type lectin 1.
+At position 153 to 294, the domain is characterized as Jacalin-type lectin 2.
+At position 300 to 443, the domain is characterized as Jacalin-type lectin 3.
+At position 13 to 66, the domain is characterized as bHLH.
+At position 85 to 156, the domain is characterized as PAS 1.
+At position 271 to 341, the domain is characterized as PAS 2.
+At position 346 to 389, the domain is characterized as PAC.
+At position 221 to 461, the domain is characterized as CN hydrolase.
+At position 17 to 209, the domain is characterized as Lon N-terminal.
+At position 599 to 780, the domain is characterized as Lon proteolytic.
+At position 16 to 261, the domain is characterized as CN hydrolase.
+At position 470 to 662, the domain is characterized as FtsK.
+At position 15 to 166, the domain is characterized as MPN.
+At position 171 to 255, the domain is characterized as Ras-associating.
+At position 295 to 404, the domain is characterized as PH.
+At position 498 to 594, the domain is characterized as SH2.
+At position 197 to 391, the domain is characterized as CheB-type methylesterase.
+At position 15 to 88, the domain is characterized as KRAB.
+At position 306 to 385, the domain is characterized as RRM.
+At position 23 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 118 to 210, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 328, the domain is characterized as Ig-like C2-type 3.
+At position 383 to 538, the domain is characterized as TIR.
+At position 243 to 434, the domain is characterized as GATase cobBQ-type.
+At position 234 to 392, the domain is characterized as Helicase C-terminal.
+At position 208 to 285, the domain is characterized as KH type-2.
+At position 113 to 274, the domain is characterized as CP-type G.
+At position 218 to 587, the domain is characterized as GH16.
+At position 384 to 449, the domain is characterized as TRAM.
+At position 22 to 128, the domain is characterized as Calponin-homology (CH) 1.
+At position 146 to 249, the domain is characterized as Calponin-homology (CH) 2.
+At position 285 to 426, the domain is characterized as SIS 1.
+At position 1 to 47, the domain is characterized as FAS1.
+At position 5 to 91, the domain is characterized as Disintegrin.
+At position 26 to 210, the domain is characterized as EngB-type G.
+At position 1 to 75, the domain is characterized as Core-binding (CB).
+At position 90 to 238, the domain is characterized as Tyr recombinase.
+At position 93 to 353, the domain is characterized as Protein kinase.
+At position 676 to 867, the domain is characterized as ATP-grasp 2.
+At position 949 to 1099, the domain is characterized as MGS-like.
+At position 15 to 113, the domain is characterized as PTS EIIA type-3.
+At position 7 to 88, the domain is characterized as ZAD.
+At position 56 to 88, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 23 to 359, the domain is characterized as MACPF.
+At position 410 to 422, the domain is characterized as EGF-like.
+At position 30 to 321, the domain is characterized as ABC transmembrane type-1.
+At position 353 to 589, the domain is characterized as ABC transporter.
+At position 13 to 64, the domain is characterized as HTH psq-type.
+At position 78 to 155, the domain is characterized as HTH CENPB-type.
+At position 13 to 138, the domain is characterized as Response regulatory.
+At position 329 to 745, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1190 to 1495, the domain is characterized as PKS/mFAS DH.
+At position 1535 to 1612, the domain is characterized as Carrier.
+At position 2 to 142, the domain is characterized as Jacalin-type lectin 1.
+At position 152 to 295, the domain is characterized as Jacalin-type lectin 2.
+At position 15 to 90, the domain is characterized as RRM.
+At position 323 to 362, the domain is characterized as LIM interaction domain (LID).
+At position 2 to 79, the domain is characterized as RRM 1.
+At position 293 to 368, the domain is characterized as RRM 2.
+At position 584 to 656, the domain is characterized as RRM 4.
+At position 722 to 803, the domain is characterized as RRM 5.
+At position 824 to 904, the domain is characterized as RRM 6.
+At position 22 to 105, the domain is characterized as PDZ.
+At position 144 to 357, the domain is characterized as AH.
+At position 13 to 133, the domain is characterized as MARVEL.
+At position 32 to 106, the domain is characterized as Ubiquitin-like.
+At position 48 to 189, the domain is characterized as SLD.
+At position 96 to 407, the domain is characterized as IF rod.
+At position 23 to 281, the domain is characterized as Protein kinase.
+At position 58 to 393, the domain is characterized as Peptidase A1.
+At position 12 to 246, the domain is characterized as ABC transporter.
+At position 1 to 406, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 838 to 1108, the domain is characterized as PKS/mFAS DH.
+At position 2121 to 2198, the domain is characterized as Carrier.
+At position 33 to 157, the domain is characterized as Ricin B-type lectin.
+At position 30 to 265, the domain is characterized as ABC transporter 1.
+At position 265 to 516, the domain is characterized as ABC transporter 2.
+At position 38 to 318, the domain is characterized as IF rod.
+At position 360 to 563, the domain is characterized as DPCK.
+At position 961 to 1066, the domain is characterized as Calponin-homology (CH).
+At position 414 to 724, the domain is characterized as NACHT.
+At position 241 to 421, the domain is characterized as PBS-linker 1.
+At position 482 to 665, the domain is characterized as PBS-linker 2.
+At position 679 to 856, the domain is characterized as PBS-linker 3.
+At position 6 to 268, the domain is characterized as Pyruvate carboxyltransferase.
+At position 12 to 58, the domain is characterized as F-box.
+At position 360 to 410, the domain is characterized as FBD.
+At position 128 to 252, the domain is characterized as Nudix hydrolase.
+At position 24 to 192, the domain is characterized as Laminin G-like.
+At position 345 to 384, the domain is characterized as EGF-like 1; calcium-binding.
+At position 388 to 430, the domain is characterized as EGF-like 2.
+At position 701 to 915, the domain is characterized as TSP C-terminal.
+At position 418 to 500, the domain is characterized as G5 1.
+At position 546 to 628, the domain is characterized as G5 2.
+At position 674 to 756, the domain is characterized as G5 3.
+At position 802 to 884, the domain is characterized as G5 4.
+At position 930 to 1012, the domain is characterized as G5 5.
+At position 1058 to 1140, the domain is characterized as G5 6.
+At position 1186 to 1268, the domain is characterized as G5 7.
+At position 169 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 37 to 209, the domain is characterized as CP-type G.
+At position 4 to 105, the domain is characterized as STAS.
+At position 52 to 366, the domain is characterized as USP.
+At position 91 to 151, the domain is characterized as bZIP.
+At position 152 to 363, the domain is characterized as DOG1.
+At position 23 to 64, the domain is characterized as Chitin-binding type-1.
+At position 174 to 261, the domain is characterized as 5'-3' exonuclease.
+At position 428 to 589, the domain is characterized as 3'-5' exonuclease.
+At position 63 to 246, the domain is characterized as tr-type G.
+At position 536 to 627, the domain is characterized as PH 1.
+At position 686 to 780, the domain is characterized as PH 2.
+At position 702 to 736, the domain is characterized as Anaphylatoxin-like.
+At position 1595 to 1742, the domain is characterized as NTR.
+At position 1 to 75, the domain is characterized as Glutaredoxin.
+At position 499 to 825, the domain is characterized as Kinesin motor.
+At position 289 to 429, the domain is characterized as SIS 1.
+At position 72 to 172, the domain is characterized as BTB.
+At position 181 to 292, the domain is characterized as Fe2OG dioxygenase.
+At position 99 to 140, the domain is characterized as Collagen-like.
+At position 141 to 281, the domain is characterized as C1q.
+At position 7 to 199, the domain is characterized as Flavodoxin-like.
+At position 20 to 287, the domain is characterized as Protein kinase.
+At position 1037 to 1306, the domain is characterized as Protein kinase.
+At position 21 to 84, the domain is characterized as Sushi 1.
+At position 152 to 212, the domain is characterized as Sushi 3.
+At position 213 to 273, the domain is characterized as Sushi 4.
+At position 274 to 344, the domain is characterized as Sushi 5.
+At position 349 to 408, the domain is characterized as Sushi 6.
+At position 409 to 468, the domain is characterized as Sushi 7.
+At position 469 to 524, the domain is characterized as Sushi 8.
+At position 525 to 595, the domain is characterized as Sushi 9.
+At position 600 to 659, the domain is characterized as Sushi 10.
+At position 660 to 716, the domain is characterized as Sushi 11.
+At position 717 to 781, the domain is characterized as Sushi 12.
+At position 786 to 845, the domain is characterized as Sushi 13.
+At position 849 to 909, the domain is characterized as Sushi 14.
+At position 910 to 970, the domain is characterized as Sushi 15.
+At position 11 to 62, the domain is characterized as SpoVT-AbrB 1.
+At position 69 to 210, the domain is characterized as SCP.
+At position 106 to 340, the domain is characterized as Radical SAM core.
+At position 20 to 70, the domain is characterized as WAP.
+At position 739 to 872, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1191 to 1330, the domain is characterized as DOD-type homing endonuclease 2.
+At position 42 to 239, the domain is characterized as Lon N-terminal.
+At position 634 to 818, the domain is characterized as Lon proteolytic.
+At position 85 to 274, the domain is characterized as B30.2/SPRY.
+At position 264 to 315, the domain is characterized as SOCS box.
+At position 152 to 229, the domain is characterized as RRM.
+At position 123 to 319, the domain is characterized as ATP-grasp.
+At position 103 to 185, the domain is characterized as RRM 1.
+At position 199 to 278, the domain is characterized as RRM 2.
+At position 306 to 378, the domain is characterized as RRM 3.
+At position 17 to 272, the domain is characterized as tr-type G.
+At position 881 to 946, the domain is characterized as HP.
+At position 18 to 208, the domain is characterized as KARI N-terminal Rossmann.
+At position 345 to 486, the domain is characterized as KARI C-terminal knotted 2.
+At position 98 to 152, the domain is characterized as bHLH.
+At position 75 to 390, the domain is characterized as IF rod.
+At position 1 to 60, the domain is characterized as PE.
+At position 5 to 107, the domain is characterized as FAD-binding FR-type.
+At position 233 to 318, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 132 to 165, the domain is characterized as EF-hand 1.
+At position 166 to 201, the domain is characterized as EF-hand 2.
+At position 235 to 270, the domain is characterized as EF-hand 3.
+At position 347 to 382, the domain is characterized as EF-hand 4.
+At position 177 to 256, the domain is characterized as Expansin-like CBD.
+At position 457 to 643, the domain is characterized as PID.
+At position 656 to 742, the domain is characterized as PDZ 1.
+At position 747 to 822, the domain is characterized as PDZ 2.
+At position 131 to 204, the domain is characterized as SPOR.
+At position 33 to 319, the domain is characterized as Protein kinase.
+At position 5 to 274, the domain is characterized as CN hydrolase.
+At position 57 to 217, the domain is characterized as UBC core.
+At position 26 to 218, the domain is characterized as GH16.
+At position 93 to 157, the domain is characterized as CSD.
+At position 216 to 264, the domain is characterized as GRIP.
+At position 616 to 748, the domain is characterized as B12-binding.
+At position 16 to 83, the domain is characterized as S4 RNA-binding.
+At position 35 to 124, the domain is characterized as SUEL-type lectin.
+At position 710 to 757, the domain is characterized as GPS.
+At position 239 to 330, the domain is characterized as Fibronectin type-III.
+At position 32 to 135, the domain is characterized as Cadherin 1.
+At position 353 to 457, the domain is characterized as Cadherin 4.
+At position 458 to 567, the domain is characterized as Cadherin 5.
+At position 572 to 685, the domain is characterized as Cadherin 6.
+At position 339 to 411, the domain is characterized as ACT-like 1.
+At position 434 to 504, the domain is characterized as ACT-like 2.
+At position 1 to 82, the domain is characterized as TFIIS N-terminal.
+At position 182 to 298, the domain is characterized as TFIIS central.
+At position 1078 to 1150, the domain is characterized as BIG2.
+At position 30 to 112, the domain is characterized as SCAN box.
+At position 248 to 410, the domain is characterized as CYTH.
+At position 87 to 208, the domain is characterized as GST C-terminal.
+At position 171 to 372, the domain is characterized as Helicase ATP-binding.
+At position 398 to 620, the domain is characterized as Helicase C-terminal.
+At position 23 to 97, the domain is characterized as UPAR/Ly6.
+At position 35 to 127, the domain is characterized as Ig-like V-type.
+At position 139 to 236, the domain is characterized as Ig-like C2-type.
+At position 1 to 120, the domain is characterized as PAS 1.
+At position 138 to 240, the domain is characterized as PAS 2.
+At position 241 to 304, the domain is characterized as bZIP.
+At position 70 to 331, the domain is characterized as Protein kinase.
+At position 2 to 118, the domain is characterized as Response regulatory.
+At position 22 to 165, the domain is characterized as SprT-like.
+At position 169 to 424, the domain is characterized as NR LBD.
+At position 104 to 181, the domain is characterized as RRM.
+At position 7 to 57, the domain is characterized as SpoVT-AbrB 1.
+At position 86 to 129, the domain is characterized as SpoVT-AbrB 2.
+At position 10 to 159, the domain is characterized as Ferritin-like diiron.
+At position 1 to 127, the domain is characterized as Tyrosine-protein phosphatase.
+At position 12 to 149, the domain is characterized as MPN.
+At position 112 to 432, the domain is characterized as GH18.
+At position 21 to 119, the domain is characterized as Ig-like V-type.
+At position 124 to 219, the domain is characterized as Ig-like C2-type 1.
+At position 224 to 307, the domain is characterized as Ig-like C2-type 2.
+At position 35 to 208, the domain is characterized as Helicase ATP-binding.
+At position 219 to 379, the domain is characterized as Helicase C-terminal.
+At position 30 to 351, the domain is characterized as USP.
+At position 307 to 481, the domain is characterized as Helicase ATP-binding.
+At position 466 to 684, the domain is characterized as Helicase C-terminal.
+At position 564 to 617, the domain is characterized as bHLH.
+At position 55 to 284, the domain is characterized as GB1/RHD3-type G.
+At position 230 to 273, the domain is characterized as CUE.
+At position 157 to 464, the domain is characterized as ABC transmembrane type-1 1.
+At position 499 to 744, the domain is characterized as ABC transporter 1.
+At position 838 to 1125, the domain is characterized as ABC transmembrane type-1 2.
+At position 1162 to 1402, the domain is characterized as ABC transporter 2.
+At position 2 to 67, the domain is characterized as KH 1.
+At position 120 to 185, the domain is characterized as KH 2.
+At position 244 to 324, the domain is characterized as KH 3.
+At position 30 to 185, the domain is characterized as F5/8 type C.
+At position 563 to 849, the domain is characterized as Protein kinase.
+At position 190 to 384, the domain is characterized as CheB-type methylesterase.
+At position 45 to 191, the domain is characterized as MABP.
+At position 252 to 301, the domain is characterized as UMA.
+At position 11 to 90, the domain is characterized as Chromo.
+At position 196 to 500, the domain is characterized as MRG.
+At position 275 to 385, the domain is characterized as OCEL.
+At position 4 to 122, the domain is characterized as VOC.
+At position 155 to 256, the domain is characterized as Fe2OG dioxygenase.
+At position 15 to 98, the domain is characterized as RRM.
+At position 610 to 802, the domain is characterized as PH.
+At position 822 to 943, the domain is characterized as Arf-GAP.
+At position 482 to 607, the domain is characterized as DBINO.
+At position 724 to 896, the domain is characterized as Helicase ATP-binding.
+At position 1309 to 1473, the domain is characterized as Helicase C-terminal.
+At position 19 to 450, the domain is characterized as USP.
+At position 36 to 213, the domain is characterized as VWFA.
+At position 218 to 324, the domain is characterized as Fibronectin type-III 1.
+At position 331 to 423, the domain is characterized as Fibronectin type-III 2.
+At position 16 to 204, the domain is characterized as RNase H type-2.
+At position 188 to 336, the domain is characterized as MOSC.
+At position 16 to 251, the domain is characterized as ABC transporter 1.
+At position 251 to 507, the domain is characterized as ABC transporter 2.
+At position 8 to 153, the domain is characterized as Flavodoxin-like.
+At position 221 to 467, the domain is characterized as FAD-binding FR-type.
+At position 181 to 235, the domain is characterized as SANT.
+At position 72 to 162, the domain is characterized as DRBM 1.
+At position 191 to 258, the domain is characterized as DRBM 2.
+At position 293 to 361, the domain is characterized as DRBM 3.
+At position 80 to 157, the domain is characterized as PAS 1.
+At position 228 to 298, the domain is characterized as PAS 2.
+At position 302 to 345, the domain is characterized as PAC.
+At position 151 to 214, the domain is characterized as bZIP.
+At position 98 to 168, the domain is characterized as S4 RNA-binding.
+At position 105 to 288, the domain is characterized as ATP-grasp.
+At position 1 to 45, the domain is characterized as TRAM.
+At position 911 to 1044, the domain is characterized as MGS-like.
+At position 467 to 526, the domain is characterized as Collagen-like 1.
+At position 107 to 280, the domain is characterized as Tyr recombinase.
+At position 242 to 316, the domain is characterized as POU-specific.
+At position 19 to 144, the domain is characterized as MTTase N-terminal.
+At position 167 to 397, the domain is characterized as Radical SAM core.
+At position 400 to 470, the domain is characterized as TRAM.
+At position 145 to 362, the domain is characterized as MIF4G.
+At position 3 to 186, the domain is characterized as YrdC-like.
+At position 1 to 101, the domain is characterized as FAD-binding FR-type.
+At position 54 to 126, the domain is characterized as PAS.
+At position 220 to 268, the domain is characterized as F-box.
+At position 1 to 105, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 251 to 460, the domain is characterized as Ku.
+At position 27 to 206, the domain is characterized as FAD-binding PCMH-type.
+At position 209 to 258, the domain is characterized as bHLH.
+At position 48 to 264, the domain is characterized as Radical SAM core.
+At position 33 to 194, the domain is characterized as N-acetyltransferase.
+At position 408 to 567, the domain is characterized as Exonuclease.
+At position 112 to 230, the domain is characterized as PilZ.
+At position 26 to 117, the domain is characterized as Fibronectin type-III.
+At position 5 to 435, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 938 to 1246, the domain is characterized as PKS/mFAS DH.
+At position 2374 to 2451, the domain is characterized as Carrier.
+At position 120 to 440, the domain is characterized as PPM-type phosphatase.
+At position 380 to 457, the domain is characterized as BAG.
+At position 67 to 341, the domain is characterized as Dynamin-type G.
+At position 575 to 663, the domain is characterized as GED.
+At position 198 to 250, the domain is characterized as KH.
+At position 7 to 76, the domain is characterized as HTH merR-type.
+At position 3 to 211, the domain is characterized as ABC transporter.
+At position 158 to 193, the domain is characterized as QLQ.
+At position 223 to 267, the domain is characterized as WRC.
+At position 227 to 271, the domain is characterized as bZIP.
+At position 292 to 506, the domain is characterized as DOG1.
+At position 29 to 85, the domain is characterized as WHEP-TRS.
+At position 36 to 149, the domain is characterized as Thioredoxin.
+At position 161 to 228, the domain is characterized as BTB.
+At position 78 to 303, the domain is characterized as Radical SAM core.
+At position 23 to 414, the domain is characterized as Helicase ATP-binding.
+At position 128 to 380, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 133 to 232, the domain is characterized as Fibronectin type-III.
+At position 155 to 258, the domain is characterized as BACK.
+At position 131 to 245, the domain is characterized as PX; atypical.
+At position 259 to 321, the domain is characterized as SH3.
+At position 372 to 567, the domain is characterized as Rho-GAP.
+At position 1 to 3, the domain is characterized as Peptidase M12B.
+At position 11 to 96, the domain is characterized as Disintegrin.
+At position 459 to 846, the domain is characterized as USP.
+At position 894 to 1067, the domain is characterized as Exonuclease.
+At position 8 to 141, the domain is characterized as B12-binding.
+At position 181 to 395, the domain is characterized as Radical SAM core.
+At position 156 to 229, the domain is characterized as HTH crp-type.
+At position 5 to 232, the domain is characterized as Radical SAM core.
+At position 12 to 277, the domain is characterized as Peptidase S8.
+At position 13 to 344, the domain is characterized as PTS EIIC type-2.
+At position 371 to 461, the domain is characterized as PTS EIIB type-2.
+At position 170 to 341, the domain is characterized as OBG-type G.
+At position 98 to 210, the domain is characterized as C-type lectin.
+At position 148 to 254, the domain is characterized as Cadherin 1.
+At position 255 to 369, the domain is characterized as Cadherin 2.
+At position 370 to 484, the domain is characterized as Cadherin 3.
+At position 485 to 590, the domain is characterized as Cadherin 4.
+At position 591 to 702, the domain is characterized as Cadherin 5.
+At position 39 to 171, the domain is characterized as SCP.
+At position 54 to 108, the domain is characterized as HTH myb-type.
+At position 21 to 97, the domain is characterized as Importin N-terminal.
+At position 22 to 74, the domain is characterized as HTH myb-type 1.
+At position 75 to 129, the domain is characterized as HTH myb-type 2.
+At position 28 to 160, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 37 to 184, the domain is characterized as Tyrosine-protein phosphatase.
+At position 91 to 122, the domain is characterized as KOW.
+At position 20 to 93, the domain is characterized as PAS.
+At position 161 to 390, the domain is characterized as Histidine kinase.
+At position 411 to 527, the domain is characterized as Response regulatory.
+At position 339 to 441, the domain is characterized as CBM2.
+At position 163 to 240, the domain is characterized as RRM.
+At position 53 to 275, the domain is characterized as Bin3-type SAM.
+At position 175 to 251, the domain is characterized as RRM 1.
+At position 258 to 331, the domain is characterized as RRM 2.
+At position 340 to 429, the domain is characterized as RRM 3.
+At position 420 to 489, the domain is characterized as RRM 4.
+At position 26 to 152, the domain is characterized as EamA 1.
+At position 195 to 323, the domain is characterized as EamA 2.
+At position 42 to 72, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 73 to 102, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 137 to 169, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 88 to 154, the domain is characterized as S4 RNA-binding.
+At position 127 to 409, the domain is characterized as tr-type G.
+At position 528 to 737, the domain is characterized as Lon N-terminal.
+At position 306 to 398, the domain is characterized as ARID.
+At position 572 to 624, the domain is characterized as Tudor-knot.
+At position 601 to 681, the domain is characterized as BRCT.
+At position 3 to 47, the domain is characterized as LysM 1.
+At position 52 to 96, the domain is characterized as LysM 2.
+At position 104 to 430, the domain is characterized as GH18.
+At position 303 to 582, the domain is characterized as Protein kinase.
+At position 121 to 159, the domain is characterized as F-box.
+At position 22 to 98, the domain is characterized as Ubiquitin-like.
+At position 16 to 91, the domain is characterized as RRM 1.
+At position 121 to 195, the domain is characterized as RRM 2.
+At position 1 to 96, the domain is characterized as Peptidase S1 1.
+At position 103 to 213, the domain is characterized as CUB.
+At position 228 to 389, the domain is characterized as Peptidase S1 2.
+At position 447 to 583, the domain is characterized as SEFIR.
+At position 88 to 419, the domain is characterized as Asparaginase/glutaminase.
+At position 62 to 184, the domain is characterized as SCP.
+At position 2 to 158, the domain is characterized as Thioredoxin.
+At position 1 to 244, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 123 to 258, the domain is characterized as FAD-binding PCMH-type.
+At position 70 to 148, the domain is characterized as GST N-terminal.
+At position 126 to 272, the domain is characterized as GST C-terminal.
+At position 147 to 231, the domain is characterized as GST N-terminal.
+At position 240 to 389, the domain is characterized as GST C-terminal.
+At position 21 to 256, the domain is characterized as ABC transporter 1.
+At position 267 to 512, the domain is characterized as ABC transporter 2.
+At position 160 to 476, the domain is characterized as Protein kinase.
+At position 143 to 430, the domain is characterized as NR LBD.
+At position 126 to 224, the domain is characterized as Fibronectin type-III 1.
+At position 226 to 317, the domain is characterized as Fibronectin type-III 2.
+At position 318 to 415, the domain is characterized as Fibronectin type-III 3.
+At position 669 to 868, the domain is characterized as DDHD.
+At position 50 to 119, the domain is characterized as BTB.
+At position 154 to 255, the domain is characterized as BACK.
+At position 117 to 264, the domain is characterized as Ferric oxidoreductase.
+At position 287 to 323, the domain is characterized as DFDF.
+At position 187 to 341, the domain is characterized as Cupin type-1 1.
+At position 386 to 556, the domain is characterized as Cupin type-1 2.
+At position 364 to 450, the domain is characterized as KH-like.
+At position 3 to 80, the domain is characterized as Carrier.
+At position 659 to 738, the domain is characterized as BRCT.
+At position 637 to 727, the domain is characterized as BRCT.
+At position 29 to 278, the domain is characterized as Zn-dependent PLC.
+At position 284 to 398, the domain is characterized as PLAT.
+At position 595 to 812, the domain is characterized as Rap-GAP.
+At position 950 to 1026, the domain is characterized as PDZ.
+At position 88 to 420, the domain is characterized as Protein kinase.
+At position 7 to 282, the domain is characterized as tr-type G.
+At position 70 to 112, the domain is characterized as CHCH.
+At position 166 to 215, the domain is characterized as bHLH.
+At position 2 to 315, the domain is characterized as SAM-dependent MTase C5-type.
+At position 57 to 286, the domain is characterized as GB1/RHD3-type G.
+At position 14 to 84, the domain is characterized as KRAB.
+At position 551 to 644, the domain is characterized as BRCT 1.
+At position 658 to 768, the domain is characterized as BRCT 2.
+At position 13 to 24, the domain is characterized as C-type lectin.
+At position 30 to 168, the domain is characterized as TsaA-like.
+At position 5 to 227, the domain is characterized as ABC transporter.
+At position 21 to 175, the domain is characterized as Toprim.
+At position 195 to 239, the domain is characterized as TSP type-1.
+At position 28 to 107, the domain is characterized as IGFBP N-terminal.
+At position 160 to 234, the domain is characterized as Thyroglobulin type-1.
+At position 245 to 414, the domain is characterized as DOD-type homing endonuclease.
+At position 11 to 155, the domain is characterized as VOC.
+At position 293 to 455, the domain is characterized as Helicase ATP-binding.
+At position 510 to 676, the domain is characterized as Helicase C-terminal.
+At position 48 to 132, the domain is characterized as J.
+At position 269 to 487, the domain is characterized as ABC transporter 2.
+At position 14 to 409, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 925 to 1239, the domain is characterized as PKS/mFAS DH.
+At position 2441 to 2518, the domain is characterized as Carrier.
+At position 28 to 160, the domain is characterized as Nudix hydrolase.
+At position 243 to 276, the domain is characterized as WW 1.
+At position 295 to 328, the domain is characterized as WW 2.
+At position 455 to 509, the domain is characterized as FF 1.
+At position 519 to 577, the domain is characterized as FF 2.
+At position 590 to 643, the domain is characterized as FF 3.
+At position 691 to 748, the domain is characterized as FF 4.
+At position 750 to 815, the domain is characterized as FF 5.
+At position 178 to 211, the domain is characterized as KOW.
+At position 158 to 258, the domain is characterized as HTH araC/xylS-type.
+At position 9 to 143, the domain is characterized as B12-binding.
+At position 190 to 417, the domain is characterized as Radical SAM core.
+At position 143 to 212, the domain is characterized as S1 motif 1.
+At position 263 to 331, the domain is characterized as S1 motif 2.
+At position 305 to 369, the domain is characterized as Mop.
+At position 179 to 240, the domain is characterized as KH 1.
+At position 273 to 334, the domain is characterized as KH 2.
+At position 385 to 447, the domain is characterized as SAM.
+At position 31 to 219, the domain is characterized as B30.2/SPRY.
+At position 244 to 276, the domain is characterized as LisH.
+At position 295 to 353, the domain is characterized as CTLH.
+At position 282 to 395, the domain is characterized as HTH APSES-type.
+At position 36 to 190, the domain is characterized as RUN.
+At position 562 to 1026, the domain is characterized as Rab-GAP TBC.
+At position 125 to 156, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 158 to 187, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 23 to 223, the domain is characterized as GH16.
+At position 302 to 355, the domain is characterized as Collagen-like 2.
+At position 48 to 118, the domain is characterized as Chitin-binding type R&R.
+At position 197 to 342, the domain is characterized as JmjC.
+At position 113 to 371, the domain is characterized as Protein kinase.
+At position 414 to 449, the domain is characterized as EF-hand 1.
+At position 450 to 485, the domain is characterized as EF-hand 2.
+At position 486 to 521, the domain is characterized as EF-hand 3.
+At position 522 to 555, the domain is characterized as EF-hand 4.
+At position 58 to 263, the domain is characterized as TNase-like.
+At position 49 to 318, the domain is characterized as Protein kinase 1.
+At position 319 to 387, the domain is characterized as AGC-kinase C-terminal.
+At position 426 to 687, the domain is characterized as Protein kinase 2.
+At position 1 to 61, the domain is characterized as Sushi 2.
+At position 64 to 121, the domain is characterized as Sushi 3.
+At position 707 to 800, the domain is characterized as FDX-ACB.
+At position 232 to 452, the domain is characterized as Peptidase M12B.
+At position 453 to 542, the domain is characterized as Disintegrin.
+At position 543 to 598, the domain is characterized as TSP type-1 1.
+At position 800 to 860, the domain is characterized as TSP type-1 2.
+At position 861 to 922, the domain is characterized as TSP type-1 3.
+At position 925 to 968, the domain is characterized as TSP type-1 4.
+At position 972 to 1029, the domain is characterized as TSP type-1 5.
+At position 1045 to 1084, the domain is characterized as PLAC.
+At position 2 to 152, the domain is characterized as Macro.
+At position 25 to 230, the domain is characterized as Velvet.
+At position 156 to 472, the domain is characterized as Protein kinase.
+At position 119 to 254, the domain is characterized as BFN.
+At position 285 to 320, the domain is characterized as UVR.
+At position 95 to 216, the domain is characterized as OmpA-like.
+At position 1 to 117, the domain is characterized as MTTase N-terminal.
+At position 371 to 442, the domain is characterized as TRAM.
+At position 1 to 71, the domain is characterized as Sm.
+At position 79 to 173, the domain is characterized as AD.
+At position 338 to 399, the domain is characterized as S4 RNA-binding.
+At position 590 to 692, the domain is characterized as tRNA-binding.
+At position 120 to 444, the domain is characterized as SAC.
+At position 889 to 968, the domain is characterized as RRM.
+At position 595 to 678, the domain is characterized as BRCT.
+At position 345 to 412, the domain is characterized as S4 RNA-binding.
+At position 146 to 234, the domain is characterized as Rieske.
+At position 26 to 105, the domain is characterized as GS beta-grasp.
+At position 112 to 358, the domain is characterized as GS catalytic.
+At position 13 to 283, the domain is characterized as F-BAR.
+At position 385 to 444, the domain is characterized as SH3.
+At position 343 to 441, the domain is characterized as Rhodanese.
+At position 97 to 282, the domain is characterized as ABC transmembrane type-1.
+At position 124 to 291, the domain is characterized as Helicase ATP-binding.
+At position 337 to 524, the domain is characterized as Helicase C-terminal.
+At position 936 to 999, the domain is characterized as Tudor.
+At position 11 to 71, the domain is characterized as HTH tetR-type.
+At position 114 to 419, the domain is characterized as Protein kinase.
+At position 32 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 133 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 219 to 307, the domain is characterized as Ig-like C2-type 3.
+At position 76 to 107, the domain is characterized as EF-hand 2.
+At position 51 to 278, the domain is characterized as ABC transporter.
+At position 270 to 341, the domain is characterized as PUA.
+At position 661 to 792, the domain is characterized as SEC7.
+At position 428 to 624, the domain is characterized as FtsK.
+At position 12 to 87, the domain is characterized as RRM.
+At position 2 to 126, the domain is characterized as Toprim.
+At position 15 to 61, the domain is characterized as EGF-like; atypical.
+At position 23 to 105, the domain is characterized as GIY-YIG.
+At position 224 to 528, the domain is characterized as Helicase ATP-binding.
+At position 578 to 723, the domain is characterized as Helicase C-terminal.
+At position 11 to 313, the domain is characterized as YjeF C-terminal.
+At position 586 to 668, the domain is characterized as Carrier.
+At position 562 to 593, the domain is characterized as Chromo.
+At position 846 to 878, the domain is characterized as LisH.
+At position 4 to 227, the domain is characterized as Radical SAM core.
+At position 1903 to 1932, the domain is characterized as IQ.
+At position 1086 to 1195, the domain is characterized as PH.
+At position 4 to 82, the domain is characterized as MIT.
+At position 271 to 349, the domain is characterized as PUA.
+At position 12 to 65, the domain is characterized as bHLH.
+At position 80 to 150, the domain is characterized as PAS 1.
+At position 225 to 295, the domain is characterized as PAS 2.
+At position 175 to 423, the domain is characterized as MHD.
+At position 245 to 382, the domain is characterized as YTH.
+At position 442 to 557, the domain is characterized as STAS.
+At position 94 to 152, the domain is characterized as S4 RNA-binding.
+At position 14 to 67, the domain is characterized as Tudor-knot.
+At position 131 to 304, the domain is characterized as MRG.
+At position 72 to 148, the domain is characterized as S1-like.
+At position 46 to 115, the domain is characterized as BON 1.
+At position 124 to 191, the domain is characterized as BON 2.
+At position 264 to 449, the domain is characterized as Glutamine amidotransferase type-1.
+At position 598 to 790, the domain is characterized as ATP-grasp 1.
+At position 1133 to 1324, the domain is characterized as ATP-grasp 2.
+At position 1390 to 1552, the domain is characterized as MGS-like.
+At position 662 to 741, the domain is characterized as BRCT.
+At position 115 to 403, the domain is characterized as ABC transmembrane type-1 1.
+At position 438 to 683, the domain is characterized as ABC transporter 1.
+At position 774 to 1063, the domain is characterized as ABC transmembrane type-1 2.
+At position 1098 to 1336, the domain is characterized as ABC transporter 2.
+At position 107 to 192, the domain is characterized as ELM2.
+At position 193 to 244, the domain is characterized as SANT 1.
+At position 481 to 532, the domain is characterized as SANT 2.
+At position 332 to 387, the domain is characterized as MIR 1.
+At position 401 to 457, the domain is characterized as MIR 2.
+At position 465 to 523, the domain is characterized as MIR 3.
+At position 4 to 228, the domain is characterized as SET.
+At position 476 to 586, the domain is characterized as POU-specific.
+At position 1510 to 1588, the domain is characterized as BRCT 1.
+At position 1609 to 1700, the domain is characterized as BRCT 2.
+At position 85 to 185, the domain is characterized as PH.
+At position 194 to 283, the domain is characterized as Ras-associating.
+At position 9 to 247, the domain is characterized as ABC transporter.
+At position 18 to 139, the domain is characterized as MsrB.
+At position 45 to 202, the domain is characterized as C2.
+At position 230 to 485, the domain is characterized as Protein kinase.
+At position 486 to 557, the domain is characterized as AGC-kinase C-terminal.
+At position 38 to 89, the domain is characterized as LysM.
+At position 299 to 347, the domain is characterized as LRRCT.
+At position 32 to 251, the domain is characterized as Fibrinogen C-terminal.
+At position 589 to 667, the domain is characterized as BRCT.
+At position 41 to 145, the domain is characterized as FAD-binding FR-type.
+At position 146 to 374, the domain is characterized as Radical SAM core.
+At position 377 to 438, the domain is characterized as TRAM.
+At position 36 to 105, the domain is characterized as DRBM.
+At position 167 to 492, the domain is characterized as A to I editase.
+At position 62 to 172, the domain is characterized as MsrB.
+At position 125 to 206, the domain is characterized as Ig-like C2-type 2.
+At position 213 to 306, the domain is characterized as Fibronectin type-III 1.
+At position 311 to 401, the domain is characterized as Fibronectin type-III 2.
+At position 503 to 774, the domain is characterized as Protein kinase.
+At position 16 to 147, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 178 to 293, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 38 to 93, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 8 to 326, the domain is characterized as Kinesin motor.
+At position 57 to 225, the domain is characterized as Helicase ATP-binding.
+At position 248 to 447, the domain is characterized as Helicase C-terminal.
+At position 26 to 91, the domain is characterized as Chitin-binding type R&R.
+At position 14 to 60, the domain is characterized as Agenet-like 1.
+At position 73 to 125, the domain is characterized as Agenet-like 2.
+At position 228 to 276, the domain is characterized as KH 1.
+At position 291 to 340, the domain is characterized as KH 2.
+At position 137 to 201, the domain is characterized as S1 motif.
+At position 243 to 291, the domain is characterized as KH 1.
+At position 331 to 378, the domain is characterized as KH 2.
+At position 62 to 159, the domain is characterized as Ig-like.
+At position 161 to 256, the domain is characterized as Ig-like C2-type.
+At position 260 to 314, the domain is characterized as TSP type-1 1.
+At position 316 to 368, the domain is characterized as TSP type-1 2.
+At position 530 to 664, the domain is characterized as ZU5.
+At position 850 to 929, the domain is characterized as Death.
+At position 753 to 819, the domain is characterized as HP.
+At position 3 to 150, the domain is characterized as Toprim.
+At position 117 to 191, the domain is characterized as BTB.
+At position 484 to 559, the domain is characterized as Cytochrome b5 heme-binding.
+At position 602 to 719, the domain is characterized as FAD-binding FR-type.
+At position 341 to 412, the domain is characterized as Ubiquitin-like.
+At position 212 to 373, the domain is characterized as CP-type G.
+At position 28 to 122, the domain is characterized as Ig-like V-type 1.
+At position 134 to 228, the domain is characterized as Ig-like V-type 2.
+At position 129 to 307, the domain is characterized as CP-type G.
+At position 18 to 85, the domain is characterized as COMM.
+At position 287 to 316, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 339 to 367, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1034 to 1310, the domain is characterized as Protein kinase.
+At position 54 to 174, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 192 to 297, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 348 to 477, the domain is characterized as Thioredoxin 2.
+At position 17 to 122, the domain is characterized as Calponin-homology (CH).
+At position 32 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 2 to 77, the domain is characterized as Cytochrome b5 heme-binding.
+At position 138 to 212, the domain is characterized as POU-specific.
+At position 39 to 118, the domain is characterized as KH type-2.
+At position 35 to 108, the domain is characterized as Inhibitor I9.
+At position 112 to 613, the domain is characterized as Peptidase S8.
+At position 381 to 465, the domain is characterized as PA.
+At position 39 to 126, the domain is characterized as Death.
+At position 125 to 201, the domain is characterized as Ig-like C2-type 1.
+At position 212 to 305, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 90, the domain is characterized as B12-binding N-terminal.
+At position 93 to 216, the domain is characterized as B12-binding.
+At position 13 to 93, the domain is characterized as NAB.
+At position 92 to 138, the domain is characterized as F-box.
+At position 121 to 154, the domain is characterized as WW 1.
+At position 162 to 195, the domain is characterized as WW 2.
+At position 318 to 455, the domain is characterized as C-CAP/cofactor C-like.
+At position 44 to 107, the domain is characterized as bZIP.
+At position 111 to 327, the domain is characterized as DOG1.
+At position 57 to 126, the domain is characterized as POTRA.
+At position 1 to 151, the domain is characterized as CID.
+At position 406 to 478, the domain is characterized as RRM.
+At position 8 to 57, the domain is characterized as F-box.
+At position 29 to 137, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 174 to 321, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 251 to 469, the domain is characterized as Fibrinogen C-terminal.
+At position 345 to 395, the domain is characterized as FBD.
+At position 453 to 822, the domain is characterized as USP.
+At position 871 to 1049, the domain is characterized as Exonuclease.
+At position 147 to 197, the domain is characterized as DHHC.
+At position 5 to 282, the domain is characterized as DegV.
+At position 524 to 546, the domain is characterized as Protein kinase.
+At position 324 to 660, the domain is characterized as TTL.
+At position 124 to 300, the domain is characterized as Helicase ATP-binding.
+At position 314 to 484, the domain is characterized as Helicase C-terminal.
+At position 588 to 678, the domain is characterized as Cadherin 6.
+At position 120 to 148, the domain is characterized as IQ 1.
+At position 149 to 171, the domain is characterized as IQ 2.
+At position 70 to 262, the domain is characterized as ABC transmembrane type-1.
+At position 856 to 899, the domain is characterized as Myb-like.
+At position 100 to 211, the domain is characterized as Ferric oxidoreductase.
+At position 240 to 368, the domain is characterized as FAD-binding FR-type.
+At position 124 to 386, the domain is characterized as Protein kinase.
+At position 428 to 464, the domain is characterized as EF-hand 1.
+At position 465 to 500, the domain is characterized as EF-hand 2.
+At position 501 to 540, the domain is characterized as EF-hand 3.
+At position 543 to 572, the domain is characterized as EF-hand 4.
+At position 168 to 265, the domain is characterized as HTH araC/xylS-type.
+At position 34 to 247, the domain is characterized as GH16.
+At position 31 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 66 to 95, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 53 to 85, the domain is characterized as LisH.
+At position 30 to 209, the domain is characterized as VWFA 1.
+At position 268 to 445, the domain is characterized as VWFA 2.
+At position 474 to 644, the domain is characterized as VWFA 3.
+At position 660 to 829, the domain is characterized as VWFA 4.
+At position 846 to 1023, the domain is characterized as VWFA 5.
+At position 1037 to 1214, the domain is characterized as VWFA 6.
+At position 1226 to 1413, the domain is characterized as VWFA 7.
+At position 1426 to 1478, the domain is characterized as Collagen-like 1.
+At position 1474 to 1524, the domain is characterized as Collagen-like 2.
+At position 1557 to 1614, the domain is characterized as Collagen-like 3.
+At position 1632 to 1689, the domain is characterized as Collagen-like 4.
+At position 1706 to 1762, the domain is characterized as Collagen-like 5.
+At position 1790 to 1970, the domain is characterized as VWFA 8.
+At position 1996 to 2186, the domain is characterized as VWFA 9.
+At position 2321 to 2516, the domain is characterized as VWFA 10.
+At position 337 to 506, the domain is characterized as tr-type G.
+At position 1 to 140, the domain is characterized as uDENN.
+At position 165 to 299, the domain is characterized as cDENN.
+At position 301 to 357, the domain is characterized as dDENN.
+At position 39 to 202, the domain is characterized as FAD-binding PCMH-type.
+At position 27 to 151, the domain is characterized as MsrB.
+At position 477 to 595, the domain is characterized as Ricin B-type lectin.
+At position 8 to 153, the domain is characterized as Nudix hydrolase.
+At position 635 to 781, the domain is characterized as MOSC.
+At position 300 to 533, the domain is characterized as ABC transporter 2.
+At position 727 to 808, the domain is characterized as PKD 1.
+At position 816 to 905, the domain is characterized as PKD 2.
+At position 1 to 98, the domain is characterized as Ig-like.
+At position 3 to 411, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1 to 92, the domain is characterized as Pyrin.
+At position 580 to 775, the domain is characterized as B30.2/SPRY.
+At position 41 to 233, the domain is characterized as Helicase ATP-binding.
+At position 260 to 431, the domain is characterized as Helicase C-terminal.
+At position 132 to 570, the domain is characterized as Urease.
+At position 91 to 213, the domain is characterized as MsrB.
+At position 6 to 176, the domain is characterized as Brix.
+At position 5 to 282, the domain is characterized as Deacetylase sirtuin-type.
+At position 3 to 227, the domain is characterized as VWFA.
+At position 6 to 95, the domain is characterized as PPIase FKBP-type.
+At position 98 to 497, the domain is characterized as Glutamine amidotransferase type-2.
+At position 9 to 102, the domain is characterized as HIG1.
+At position 51 to 100, the domain is characterized as WAP.
+At position 29 to 127, the domain is characterized as Ig-like V-type.
+At position 61 to 117, the domain is characterized as bZIP.
+At position 26 to 129, the domain is characterized as PINc.
+At position 364 to 592, the domain is characterized as TLDc.
+At position 169 to 266, the domain is characterized as Rhodanese.
+At position 6 to 43, the domain is characterized as UBA-like.
+At position 54 to 250, the domain is characterized as DCUN1.
+At position 23 to 198, the domain is characterized as Laminin G-like.
+At position 312 to 349, the domain is characterized as EGF-like 1; calcium-binding.
+At position 365 to 408, the domain is characterized as EGF-like 2; calcium-binding.
+At position 409 to 451, the domain is characterized as EGF-like 3.
+At position 720 to 934, the domain is characterized as TSP C-terminal.
+At position 127 to 312, the domain is characterized as ATP-grasp.
+At position 39 to 137, the domain is characterized as Rieske.
+At position 266 to 333, the domain is characterized as BTB 1.
+At position 500 to 567, the domain is characterized as BTB 2.
+At position 7 to 91, the domain is characterized as GST N-terminal.
+At position 93 to 209, the domain is characterized as GST C-terminal.
+At position 644 to 875, the domain is characterized as NR LBD.
+At position 1 to 43, the domain is characterized as KRAB.
+At position 55 to 241, the domain is characterized as tr-type G.
+At position 26 to 487, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 515 to 799, the domain is characterized as UvrD-like helicase C-terminal.
+At position 222 to 288, the domain is characterized as SH3.
+At position 31 to 306, the domain is characterized as Pyruvate carboxyltransferase.
+At position 275 to 330, the domain is characterized as PAP-associated.
+At position 114 to 357, the domain is characterized as Radical SAM core.
+At position 26 to 55, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 56 to 86, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 52 to 159, the domain is characterized as Expansin-like EG45.
+At position 172 to 253, the domain is characterized as Expansin-like CBD.
+At position 339 to 455, the domain is characterized as PAZ.
+At position 620 to 912, the domain is characterized as Piwi.
+At position 60 to 135, the domain is characterized as BTB.
+At position 1 to 207, the domain is characterized as ABC transporter.
+At position 115 to 256, the domain is characterized as PA14.
+At position 340 to 768, the domain is characterized as FH2.
+At position 130 to 199, the domain is characterized as COMM.
+At position 242 to 270, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 269 to 299, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 94, the domain is characterized as WGR.
+At position 148 to 285, the domain is characterized as PARP alpha-helical.
+At position 309 to 535, the domain is characterized as PARP catalytic.
+At position 241 to 505, the domain is characterized as Protein kinase.
+At position 83 to 258, the domain is characterized as VWFA.
+At position 264 to 305, the domain is characterized as EGF-like 1.
+At position 306 to 347, the domain is characterized as EGF-like 2.
+At position 348 to 389, the domain is characterized as EGF-like 3.
+At position 390 to 431, the domain is characterized as EGF-like 4.
+At position 191 to 268, the domain is characterized as UBX.
+At position 38 to 136, the domain is characterized as CBM2.
+At position 163 to 289, the domain is characterized as CBM6.
+At position 67 to 134, the domain is characterized as BTB.
+At position 169 to 270, the domain is characterized as BACK.
+At position 349 to 603, the domain is characterized as Protein kinase.
+At position 604 to 675, the domain is characterized as AGC-kinase C-terminal.
+At position 46 to 90, the domain is characterized as Fibronectin type-II 1.
+At position 91 to 139, the domain is characterized as Fibronectin type-II 2.
+At position 146 to 192, the domain is characterized as Fibronectin type-II 3.
+At position 199 to 245, the domain is characterized as Fibronectin type-II 4.
+At position 179 to 240, the domain is characterized as DRBM 1.
+At position 527 to 601, the domain is characterized as DRBM 2.
+At position 670 to 953, the domain is characterized as A to I editase.
+At position 643 to 677, the domain is characterized as EF-hand 1.
+At position 686 to 719, the domain is characterized as EF-hand 2.
+At position 716 to 751, the domain is characterized as EF-hand 3.
+At position 781 to 815, the domain is characterized as EF-hand 4.
+At position 542 to 847, the domain is characterized as USP.
+At position 218 to 401, the domain is characterized as GAF.
+At position 617 to 687, the domain is characterized as PAS 1.
+At position 901 to 1120, the domain is characterized as Histidine kinase.
+At position 462 to 637, the domain is characterized as Helicase ATP-binding.
+At position 662 to 807, the domain is characterized as Helicase C-terminal.
+At position 1018 to 1100, the domain is characterized as HRDC.
+At position 33 to 140, the domain is characterized as Plastocyanin-like 1.
+At position 154 to 317, the domain is characterized as Plastocyanin-like 2.
+At position 426 to 543, the domain is characterized as Plastocyanin-like 3.
+At position 261 to 447, the domain is characterized as Glutamine amidotransferase type-1.
+At position 355 to 406, the domain is characterized as Rubredoxin-like.
+At position 416 to 586, the domain is characterized as tr-type G.
+At position 5 to 190, the domain is characterized as VWFA.
+At position 305 to 324, the domain is characterized as UIM 3.
+At position 41 to 132, the domain is characterized as Ubiquitin-like.
+At position 4 to 118, the domain is characterized as Response regulatory.
+At position 154 to 656, the domain is characterized as Peptidase S8.
+At position 4 to 240, the domain is characterized as SET.
+At position 75 to 351, the domain is characterized as Protein kinase.
+At position 108 to 444, the domain is characterized as DZF.
+At position 68 to 328, the domain is characterized as Protein kinase.
+At position 45 to 87, the domain is characterized as CHCH.
+At position 439 to 487, the domain is characterized as RPE1 insert.
+At position 796 to 942, the domain is characterized as VPS9.
+At position 31 to 515, the domain is characterized as Sema.
+At position 88 to 222, the domain is characterized as GST C-terminal.
+At position 272 to 343, the domain is characterized as Collagen-like.
+At position 352 to 452, the domain is characterized as SRCR.
+At position 34 to 116, the domain is characterized as RRM 1.
+At position 119 to 196, the domain is characterized as RRM 2.
+At position 50 to 122, the domain is characterized as Bromo 1.
+At position 325 to 397, the domain is characterized as Bromo 2.
+At position 563 to 645, the domain is characterized as NET.
+At position 45 to 329, the domain is characterized as ABC transmembrane type-1.
+At position 363 to 597, the domain is characterized as ABC transporter.
+At position 85 to 171, the domain is characterized as PPIase FKBP-type.
+At position 67 to 215, the domain is characterized as Cupin type-1.
+At position 555 to 609, the domain is characterized as FHA.
+At position 53 to 81, the domain is characterized as ITAM.
+At position 99 to 189, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 140 to 213, the domain is characterized as RRM 2.
+At position 1 to 224, the domain is characterized as Glutamine amidotransferase type-1.
+At position 25 to 103, the domain is characterized as Importin N-terminal.
+At position 5 to 79, the domain is characterized as DWNN.
+At position 355 to 453, the domain is characterized as GTD-binding.
+At position 28 to 207, the domain is characterized as Laminin G-like 1.
+At position 260 to 459, the domain is characterized as Laminin G-like 2.
+At position 466 to 658, the domain is characterized as Laminin G-like 3.
+At position 662 to 699, the domain is characterized as EGF-like 2.
+At position 704 to 876, the domain is characterized as Laminin G-like 4.
+At position 890 to 1065, the domain is characterized as Laminin G-like 5.
+At position 1068 to 1105, the domain is characterized as EGF-like 3.
+At position 1109 to 1309, the domain is characterized as Laminin G-like 6.
+At position 42 to 198, the domain is characterized as N-acetyltransferase.
+At position 877 to 955, the domain is characterized as IPT/TIG.
+At position 1549 to 1585, the domain is characterized as IQ 1.
+At position 1586 to 1608, the domain is characterized as IQ 2.
+At position 1609 to 1631, the domain is characterized as IQ 3.
+At position 860 to 1156, the domain is characterized as ABC transmembrane type-1 2.
+At position 1212 to 1445, the domain is characterized as ABC transporter 2.
+At position 388 to 637, the domain is characterized as Protein kinase.
+At position 25 to 75, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 20 to 281, the domain is characterized as Protein kinase.
+At position 173 to 481, the domain is characterized as USP.
+At position 4 to 138, the domain is characterized as N-acetyltransferase 1.
+At position 149 to 295, the domain is characterized as N-acetyltransferase 2.
+At position 49 to 118, the domain is characterized as S4 RNA-binding.
+At position 39 to 129, the domain is characterized as GOLD.
+At position 30 to 386, the domain is characterized as IF rod.
+At position 429 to 546, the domain is characterized as LTD.
+At position 49 to 172, the domain is characterized as N-terminal Ras-GEF.
+At position 466 to 501, the domain is characterized as EF-hand 1.
+At position 502 to 528, the domain is characterized as EF-hand 2.
+At position 142 to 446, the domain is characterized as NB-ARC.
+At position 58 to 172, the domain is characterized as RGS.
+At position 187 to 452, the domain is characterized as Protein kinase.
+At position 453 to 518, the domain is characterized as AGC-kinase C-terminal.
+At position 165 to 342, the domain is characterized as OBG-type G.
+At position 357 to 434, the domain is characterized as OCT.
+At position 29 to 118, the domain is characterized as Ig-like V-type.
+At position 5 to 159, the domain is characterized as N-acetyltransferase.
+At position 77 to 250, the domain is characterized as Helicase ATP-binding.
+At position 278 to 423, the domain is characterized as Helicase C-terminal.
+At position 35 to 125, the domain is characterized as GS beta-grasp.
+At position 132 to 380, the domain is characterized as GS catalytic.
+At position 119 to 213, the domain is characterized as Fibronectin type-III.
+At position 135 to 163, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 350 to 468, the domain is characterized as LTD.
+At position 63 to 116, the domain is characterized as bHLH.
+At position 134 to 209, the domain is characterized as PAS 1.
+At position 323 to 393, the domain is characterized as PAS 2.
+At position 398 to 441, the domain is characterized as PAC.
+At position 549 to 608, the domain is characterized as DDT.
+At position 731 to 800, the domain is characterized as HTH HARE-type.
+At position 428 to 597, the domain is characterized as tr-type G.
+At position 19 to 183, the domain is characterized as PPIase cyclophilin-type.
+At position 2 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 59, the domain is characterized as ClpX-type ZB.
+At position 9 to 196, the domain is characterized as Era-type G.
+At position 227 to 303, the domain is characterized as KH type-2.
+At position 29 to 140, the domain is characterized as Ig-like V-type 1.
+At position 142 to 234, the domain is characterized as Ig-like V-type 2.
+At position 236 to 355, the domain is characterized as Ig-like V-type 3.
+At position 355 to 509, the domain is characterized as SEFIR.
+At position 14 to 194, the domain is characterized as Guanylate kinase-like.
+At position 155 to 341, the domain is characterized as Integrase catalytic.
+At position 22 to 80, the domain is characterized as TRAM.
+At position 155 to 327, the domain is characterized as Helicase ATP-binding.
+At position 356 to 502, the domain is characterized as Helicase C-terminal.
+At position 141 to 337, the domain is characterized as Peptidase M12B.
+At position 339 to 421, the domain is characterized as Disintegrin.
+At position 333 to 527, the domain is characterized as Protein kinase.
+At position 288 to 648, the domain is characterized as Protein kinase.
+At position 221 to 284, the domain is characterized as bZIP.
+At position 4 to 405, the domain is characterized as PTS EIIC type-3.
+At position 476 to 577, the domain is characterized as PTS EIIB type-3.
+At position 9 to 98, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 128 to 216, the domain is characterized as RRM.
+At position 1705 to 1822, the domain is characterized as SET.
+At position 1828 to 1844, the domain is characterized as Post-SET.
+At position 30 to 345, the domain is characterized as MACPF.
+At position 519 to 752, the domain is characterized as ABC transporter 1.
+At position 1366 to 1599, the domain is characterized as ABC transporter 2.
+At position 341 to 401, the domain is characterized as S4 RNA-binding.
+At position 9 to 59, the domain is characterized as bHLH.
+At position 82 to 152, the domain is characterized as PAS 1.
+At position 237 to 307, the domain is characterized as PAS 2.
+At position 311 to 354, the domain is characterized as PAC.
+At position 74 to 263, the domain is characterized as Thioredoxin.
+At position 18 to 112, the domain is characterized as CFEM.
+At position 26 to 108, the domain is characterized as PDZ.
+At position 705 to 807, the domain is characterized as ASD1.
+At position 1185 to 1476, the domain is characterized as ASD2.
+At position 28 to 92, the domain is characterized as J.
+At position 117 to 243, the domain is characterized as Thioredoxin.
+At position 33 to 162, the domain is characterized as EamA 1.
+At position 210 to 335, the domain is characterized as EamA 2.
+At position 48 to 152, the domain is characterized as FAD-binding FR-type.
+At position 29 to 245, the domain is characterized as SET.
+At position 10 to 130, the domain is characterized as MaoC-like.
+At position 5 to 74, the domain is characterized as HTH merR-type.
+At position 180 to 299, the domain is characterized as B12-binding.
+At position 186 to 407, the domain is characterized as RMT2.
+At position 1 to 86, the domain is characterized as ACB.
+At position 272 to 375, the domain is characterized as CobW C-terminal.
+At position 94 to 202, the domain is characterized as sHSP.
+At position 281 to 562, the domain is characterized as UvrD-like helicase C-terminal.
+At position 5 to 68, the domain is characterized as SH3.
+At position 23 to 87, the domain is characterized as LCN-type CS-alpha/beta.
+At position 304 to 553, the domain is characterized as Glutamine amidotransferase type-1.
+At position 607 to 721, the domain is characterized as SMC hinge.
+At position 34 to 102, the domain is characterized as BTB.
+At position 26 to 68, the domain is characterized as Chitin-binding type-1.
+At position 5 to 165, the domain is characterized as UBC core.
+At position 2 to 119, the domain is characterized as PINc.
+At position 173 to 238, the domain is characterized as HTH luxR-type.
+At position 663 to 754, the domain is characterized as GED.
+At position 145 to 364, the domain is characterized as Radical SAM core.
+At position 8 to 80, the domain is characterized as Pyrin.
+At position 8 to 311, the domain is characterized as Hcy-binding.
+At position 536 to 674, the domain is characterized as Flavodoxin-like.
+At position 727 to 967, the domain is characterized as FAD-binding FR-type.
+At position 17 to 368, the domain is characterized as tr-type G.
+At position 203 to 564, the domain is characterized as Peptidase A1.
+At position 119 to 165, the domain is characterized as LysM 1.
+At position 186 to 231, the domain is characterized as LysM 2.
+At position 283 to 601, the domain is characterized as Protein kinase.
+At position 37 to 115, the domain is characterized as GIY-YIG.
+At position 225 to 260, the domain is characterized as UVR.
+At position 294 to 527, the domain is characterized as Glutamine amidotransferase type-1.
+At position 279 to 394, the domain is characterized as PX.
+At position 256 to 494, the domain is characterized as ABC transporter 2.
+At position 16 to 164, the domain is characterized as N-acetyltransferase.
+At position 125 to 176, the domain is characterized as UPAR/Ly6.
+At position 1 to 96, the domain is characterized as Chorismate mutase.
+At position 97 to 272, the domain is characterized as Prephenate dehydratase.
+At position 284 to 361, the domain is characterized as ACT.
+At position 114 to 168, the domain is characterized as FAF.
+At position 121 to 230, the domain is characterized as C-type lectin.
+At position 374 to 729, the domain is characterized as Rab-GAP TBC.
+At position 82 to 200, the domain is characterized as Response regulatory.
+At position 712 to 754, the domain is characterized as CCT.
+At position 4 to 233, the domain is characterized as ABC transporter.
+At position 80 to 349, the domain is characterized as Protein kinase.
+At position 20 to 135, the domain is characterized as Ig-like.
+At position 4 to 119, the domain is characterized as PH.
+At position 151 to 259, the domain is characterized as IRS-type PTB.
+At position 6 to 124, the domain is characterized as MTTase N-terminal.
+At position 380 to 443, the domain is characterized as TRAM.
+At position 1 to 21, the domain is characterized as Peptidase S1.
+At position 304 to 412, the domain is characterized as SCP2.
+At position 63 to 130, the domain is characterized as CSD.
+At position 229 to 278, the domain is characterized as SOCS box.
+At position 1053 to 1295, the domain is characterized as Glutamine amidotransferase type-1.
+At position 74 to 182, the domain is characterized as PET.
+At position 184 to 249, the domain is characterized as LIM zinc-binding 1.
+At position 250 to 309, the domain is characterized as LIM zinc-binding 2.
+At position 310 to 373, the domain is characterized as LIM zinc-binding 3.
+At position 159 to 207, the domain is characterized as F-box.
+At position 94 to 158, the domain is characterized as S4 RNA-binding.
+At position 175 to 271, the domain is characterized as PH 1.
+At position 353 to 447, the domain is characterized as PH 2.
+At position 990 to 1221, the domain is characterized as ABC transporter 1.
+At position 2051 to 2286, the domain is characterized as ABC transporter 2.
+At position 5 to 288, the domain is characterized as Protein kinase.
+At position 69 to 106, the domain is characterized as VM.
+At position 45 to 323, the domain is characterized as Reverse transcriptase.
+At position 210 to 307, the domain is characterized as Fibronectin type-III.
+At position 5 to 129, the domain is characterized as PX.
+At position 152 to 211, the domain is characterized as SH3 1.
+At position 221 to 280, the domain is characterized as SH3 2.
+At position 368 to 427, the domain is characterized as SH3 3.
+At position 847 to 908, the domain is characterized as SH3 4.
+At position 169 to 366, the domain is characterized as N-acetyltransferase.
+At position 56 to 168, the domain is characterized as PH.
+At position 173 to 186, the domain is characterized as CRIB.
+At position 498 to 776, the domain is characterized as Protein kinase.
+At position 180 to 258, the domain is characterized as RRM.
+At position 3 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 17 to 135, the domain is characterized as MTTase N-terminal.
+At position 158 to 388, the domain is characterized as Radical SAM core.
+At position 35 to 194, the domain is characterized as N-acetyltransferase.
+At position 311 to 483, the domain is characterized as VWFA.
+At position 601 to 788, the domain is characterized as SEC7.
+At position 649 to 703, the domain is characterized as bHLH.
+At position 159 to 218, the domain is characterized as SH3.
+At position 240 to 420, the domain is characterized as DH.
+At position 442 to 547, the domain is characterized as PH.
+At position 404 to 489, the domain is characterized as Disintegrin.
+At position 305 to 431, the domain is characterized as Ricin B-type lectin 1.
+At position 434 to 559, the domain is characterized as Ricin B-type lectin 2.
+At position 256 to 425, the domain is characterized as PCI.
+At position 1282 to 1520, the domain is characterized as ABC transporter 2.
+At position 2 to 29, the domain is characterized as LCN-type CS-alpha/beta.
+At position 10 to 96, the domain is characterized as Acylphosphatase-like.
+At position 518 to 630, the domain is characterized as SMC hinge.
+At position 86 to 300, the domain is characterized as RNase H type-2.
+At position 167 to 475, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 247 to 395, the domain is characterized as Ferric oxidoreductase.
+At position 84 to 194, the domain is characterized as Ig-like.
+At position 1029 to 1147, the domain is characterized as PH.
+At position 237 to 300, the domain is characterized as KH.
+At position 363 to 456, the domain is characterized as HD.
+At position 6 to 58, the domain is characterized as HTH cro/C1-type.
+At position 6 to 125, the domain is characterized as MTTase N-terminal.
+At position 149 to 385, the domain is characterized as Radical SAM core.
+At position 167 to 190, the domain is characterized as DAZ 1.
+At position 191 to 214, the domain is characterized as DAZ 2.
+At position 215 to 238, the domain is characterized as DAZ 3.
+At position 239 to 262, the domain is characterized as DAZ 4.
+At position 263 to 286, the domain is characterized as DAZ 5.
+At position 287 to 310, the domain is characterized as DAZ 6.
+At position 311 to 334, the domain is characterized as DAZ 7.
+At position 335 to 358, the domain is characterized as DAZ 8.
+At position 359 to 382, the domain is characterized as DAZ 9.
+At position 383 to 406, the domain is characterized as DAZ 10.
+At position 407 to 430, the domain is characterized as DAZ 11.
+At position 431 to 454, the domain is characterized as DAZ 12.
+At position 455 to 478, the domain is characterized as DAZ 13.
+At position 479 to 502, the domain is characterized as DAZ 14.
+At position 503 to 526, the domain is characterized as DAZ 15.
+At position 1 to 74, the domain is characterized as Ubiquitin-like.
+At position 528 to 603, the domain is characterized as Cytochrome b5 heme-binding.
+At position 642 to 754, the domain is characterized as FAD-binding FR-type.
+At position 7 to 55, the domain is characterized as SpoVT-AbrB 1.
+At position 78 to 147, the domain is characterized as Fe2OG dioxygenase.
+At position 72 to 145, the domain is characterized as KRAB.
+At position 55 to 245, the domain is characterized as PIK helical.
+At position 523 to 789, the domain is characterized as PI3K/PI4K catalytic.
+At position 340 to 509, the domain is characterized as tr-type G.
+At position 19 to 107, the domain is characterized as Rhodanese.
+At position 289 to 355, the domain is characterized as Mop.
+At position 7 to 109, the domain is characterized as Glutaredoxin.
+At position 123 to 526, the domain is characterized as GRAS.
+At position 520 to 575, the domain is characterized as LRRCT.
+At position 640 to 781, the domain is characterized as TIR.
+At position 212 to 296, the domain is characterized as RCK C-terminal 1.
+At position 319 to 404, the domain is characterized as RCK C-terminal 2.
+At position 408 to 493, the domain is characterized as RCK C-terminal 3.
+At position 499 to 586, the domain is characterized as RCK C-terminal 4.
+At position 172 to 445, the domain is characterized as ABC transporter 1.
+At position 523 to 736, the domain is characterized as ABC transmembrane type-2 1.
+At position 869 to 1121, the domain is characterized as ABC transporter 2.
+At position 1194 to 1408, the domain is characterized as ABC transmembrane type-2 2.
+At position 263 to 341, the domain is characterized as RRM 1.
+At position 366 to 443, the domain is characterized as RRM 2.
+At position 81 to 277, the domain is characterized as B30.2/SPRY.
+At position 18 to 238, the domain is characterized as tr-type G.
+At position 131 to 161, the domain is characterized as KOW.
+At position 22 to 249, the domain is characterized as Phosphagen kinase C-terminal.
+At position 187 to 445, the domain is characterized as Peptidase M12B.
+At position 446 to 535, the domain is characterized as Disintegrin.
+At position 94 to 267, the domain is characterized as CRAL-TRIO.
+At position 6 to 102, the domain is characterized as ASCH.
+At position 305 to 367, the domain is characterized as AFP-like.
+At position 381 to 440, the domain is characterized as Dockerin.
+At position 2 to 87, the domain is characterized as GST N-terminal.
+At position 88 to 216, the domain is characterized as GST C-terminal.
+At position 281 to 442, the domain is characterized as EF-1-gamma C-terminal.
+At position 315 to 395, the domain is characterized as PB1.
+At position 399 to 458, the domain is characterized as SH3.
+At position 62 to 95, the domain is characterized as EF-hand 1.
+At position 44 to 253, the domain is characterized as BPL/LPL catalytic.
+At position 26 to 73, the domain is characterized as WAP.
+At position 10 to 83, the domain is characterized as RRM.
+At position 54 to 227, the domain is characterized as Helicase ATP-binding.
+At position 238 to 399, the domain is characterized as Helicase C-terminal.
+At position 1 to 246, the domain is characterized as ThyX 1.
+At position 271 to 476, the domain is characterized as ThyX 2.
+At position 143 to 265, the domain is characterized as VOC 2.
+At position 268 to 343, the domain is characterized as B5.
+At position 7 to 29, the domain is characterized as GoLoco 1.
+At position 47 to 69, the domain is characterized as GoLoco 2.
+At position 101 to 264, the domain is characterized as CP-type G.
+At position 133 to 342, the domain is characterized as ATP-grasp.
+At position 37 to 111, the domain is characterized as Ubiquitin-like.
+At position 182 to 210, the domain is characterized as STI1 1.
+At position 212 to 251, the domain is characterized as STI1 2.
+At position 387 to 434, the domain is characterized as STI1 3.
+At position 438 to 470, the domain is characterized as STI1 4.
+At position 546 to 586, the domain is characterized as UBA.
+At position 22 to 88, the domain is characterized as CARD.
+At position 29 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 147 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 246 to 354, the domain is characterized as Ig-like C2-type 3.
+At position 339 to 596, the domain is characterized as Clu.
+At position 249 to 418, the domain is characterized as tr-type G.
+At position 4 to 157, the domain is characterized as Thioredoxin.
+At position 18 to 132, the domain is characterized as HD.
+At position 361 to 594, the domain is characterized as Peptidase S1.
+At position 35 to 117, the domain is characterized as S1 motif.
+At position 157 to 348, the domain is characterized as CheB-type methylesterase.
+At position 193 to 362, the domain is characterized as tr-type G.
+At position 223 to 542, the domain is characterized as NACHT.
+At position 30 to 169, the domain is characterized as MPN.
+At position 43 to 269, the domain is characterized as Radical SAM core.
+At position 222 to 390, the domain is characterized as TrmE-type G.
+At position 27 to 138, the domain is characterized as Ig-like V-type.
+At position 143 to 244, the domain is characterized as Ig-like C1-type.
+At position 570 to 633, the domain is characterized as KH.
+At position 639 to 714, the domain is characterized as S1 motif.
+At position 378 to 493, the domain is characterized as C2.
+At position 519 to 622, the domain is characterized as PH.
+At position 933 to 1113, the domain is characterized as MHD1.
+At position 1 to 259, the domain is characterized as F-BAR.
+At position 460 to 550, the domain is characterized as SH2.
+At position 563 to 816, the domain is characterized as Protein kinase.
+At position 87 to 302, the domain is characterized as ABC transmembrane type-1.
+At position 19 to 227, the domain is characterized as FAD-binding PCMH-type.
+At position 67 to 119, the domain is characterized as bHLH.
+At position 113 to 177, the domain is characterized as KH.
+At position 398 to 427, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 436 to 466, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 133 to 235, the domain is characterized as BACK.
+At position 583 to 660, the domain is characterized as BRCT.
+At position 26 to 324, the domain is characterized as Protein kinase.
+At position 456 to 598, the domain is characterized as Thioredoxin.
+At position 292 to 380, the domain is characterized as Ras-associating.
+At position 995 to 1275, the domain is characterized as PPM-type phosphatase.
+At position 1332 to 1469, the domain is characterized as Guanylate cyclase.
+At position 43 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 101 to 385, the domain is characterized as Protein kinase.
+At position 109 to 345, the domain is characterized as GT92.
+At position 76 to 206, the domain is characterized as N-terminal Ras-GEF.
+At position 246 to 494, the domain is characterized as Ras-GEF.
+At position 47 to 82, the domain is characterized as EF-hand.
+At position 291 to 538, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 276, the domain is characterized as Radical SAM core.
+At position 206 to 295, the domain is characterized as EH 1.
+At position 239 to 274, the domain is characterized as EF-hand 1.
+At position 569 to 657, the domain is characterized as EH 2.
+At position 601 to 636, the domain is characterized as EF-hand 2.
+At position 42 to 110, the domain is characterized as SH3.
+At position 116 to 208, the domain is characterized as SH2.
+At position 234 to 491, the domain is characterized as Protein kinase.
+At position 37 to 94, the domain is characterized as Ig-like.
+At position 149 to 177, the domain is characterized as ITAM.
+At position 179 to 492, the domain is characterized as IF rod.
+At position 70 to 98, the domain is characterized as EGF-like 1.
+At position 142 to 180, the domain is characterized as EGF-like 2; calcium-binding.
+At position 181 to 219, the domain is characterized as EGF-like 3; calcium-binding.
+At position 220 to 262, the domain is characterized as EGF-like 4; calcium-binding.
+At position 384 to 441, the domain is characterized as VWFC 1.
+At position 442 to 502, the domain is characterized as VWFC 2.
+At position 503 to 560, the domain is characterized as VWFC 3.
+At position 566 to 626, the domain is characterized as VWFC 4.
+At position 627 to 685, the domain is characterized as VWFC 5.
+At position 686 to 743, the domain is characterized as VWFC 6.
+At position 616 to 771, the domain is characterized as BAH.
+At position 20 to 97, the domain is characterized as RRM.
+At position 28 to 285, the domain is characterized as Protein kinase.
+At position 258 to 426, the domain is characterized as Senescence.
+At position 38 to 456, the domain is characterized as uDENN FNIP1/2-type.
+At position 464 to 1034, the domain is characterized as cDENN FNIP1/2-type.
+At position 1044 to 1099, the domain is characterized as dDENN FNIP1/2-type.
+At position 6 to 131, the domain is characterized as C2 1.
+At position 138 to 263, the domain is characterized as C2 2.
+At position 57 to 224, the domain is characterized as FCP1 homology.
+At position 390 to 424, the domain is characterized as SAP.
+At position 129 to 211, the domain is characterized as Ig-like 2.
+At position 281 to 496, the domain is characterized as B30.2/SPRY.
+At position 177 to 243, the domain is characterized as R3H.
+At position 20 to 103, the domain is characterized as Apple 1.
+At position 110 to 193, the domain is characterized as Apple 2.
+At position 200 to 283, the domain is characterized as Apple 3.
+At position 291 to 374, the domain is characterized as Apple 4.
+At position 388 to 623, the domain is characterized as Peptidase S1.
+At position 12 to 267, the domain is characterized as Protein kinase.
+At position 298 to 333, the domain is characterized as NAF.
+At position 211 to 491, the domain is characterized as ABC transporter.
+At position 199 to 563, the domain is characterized as Peptidase S53.
+At position 47 to 115, the domain is characterized as POTRA.
+At position 28 to 116, the domain is characterized as Plastocyanin-like.
+At position 176 to 262, the domain is characterized as 5'-3' exonuclease.
+At position 97 to 344, the domain is characterized as Radical SAM core.
+At position 98 to 189, the domain is characterized as Ig-like C2-type 1.
+At position 195 to 281, the domain is characterized as Ig-like C2-type 2.
+At position 299 to 384, the domain is characterized as Ig-like C2-type 3.
+At position 389 to 473, the domain is characterized as Ig-like C2-type 4.
+At position 479 to 568, the domain is characterized as Ig-like C2-type 5.
+At position 570 to 659, the domain is characterized as Ig-like C2-type 6.
+At position 672 to 770, the domain is characterized as Fibronectin type-III 1.
+At position 775 to 872, the domain is characterized as Fibronectin type-III 2.
+At position 877 to 971, the domain is characterized as Fibronectin type-III 3.
+At position 976 to 1066, the domain is characterized as Fibronectin type-III 4.
+At position 380 to 499, the domain is characterized as SPR.
+At position 36 to 53, the domain is characterized as WH2.
+At position 516 to 709, the domain is characterized as SEC7.
+At position 773 to 865, the domain is characterized as PH.
+At position 300 to 555, the domain is characterized as Tyrosine-protein phosphatase.
+At position 48 to 134, the domain is characterized as PINc.
+At position 147 to 483, the domain is characterized as Protein kinase.
+At position 3 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 647 to 840, the domain is characterized as DH.
+At position 869 to 963, the domain is characterized as PH 1.
+At position 1120 to 1218, the domain is characterized as PH 2.
+At position 62 to 226, the domain is characterized as BUB1 N-terminal.
+At position 766 to 1050, the domain is characterized as Protein kinase.
+At position 380 to 642, the domain is characterized as Bin3-type SAM.
+At position 220 to 341, the domain is characterized as C2 1.
+At position 352 to 485, the domain is characterized as C2 2.
+At position 42 to 413, the domain is characterized as Peptidase A1.
+At position 466 to 512, the domain is characterized as G-patch.
+At position 58 to 136, the domain is characterized as KH.
+At position 141 to 207, the domain is characterized as R3H.
+At position 23 to 84, the domain is characterized as Chitin-binding type R&R.
+At position 196 to 260, the domain is characterized as PAS.
+At position 316 to 527, the domain is characterized as Histidine kinase.
+At position 8 to 196, the domain is characterized as tr-type G.
+At position 7 to 147, the domain is characterized as N-acetyltransferase.
+At position 677 to 868, the domain is characterized as ATP-grasp 2.
+At position 951 to 1099, the domain is characterized as MGS-like.
+At position 37 to 158, the domain is characterized as C2 1.
+At position 198 to 321, the domain is characterized as C2 2.
+At position 364 to 492, the domain is characterized as C2 3.
+At position 8 to 245, the domain is characterized as ABC transporter.
+At position 4 to 188, the domain is characterized as YrdC-like.
+At position 17 to 341, the domain is characterized as Kinesin motor.
+At position 10 to 50, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 176 to 476, the domain is characterized as USP.
+At position 28 to 120, the domain is characterized as Ig-like V-type 1.
+At position 125 to 234, the domain is characterized as Ig-like V-type 2.
+At position 245 to 328, the domain is characterized as Ig-like C2-type 1.
+At position 333 to 409, the domain is characterized as Ig-like C2-type 2.
+At position 416 to 501, the domain is characterized as Ig-like C2-type 3.
+At position 352 to 580, the domain is characterized as TLDc.
+At position 331 to 391, the domain is characterized as S4 RNA-binding.
+At position 56 to 137, the domain is characterized as Lipoyl-binding.
+At position 26 to 280, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 90 to 125, the domain is characterized as EF-hand 2.
+At position 23 to 83, the domain is characterized as HTH tetR-type.
+At position 6 to 73, the domain is characterized as J.
+At position 82 to 413, the domain is characterized as Asparaginase/glutaminase.
+At position 114 to 313, the domain is characterized as ATP-grasp.
+At position 80 to 147, the domain is characterized as BTB.
+At position 182 to 284, the domain is characterized as BACK.
+At position 72 to 250, the domain is characterized as Helicase ATP-binding.
+At position 415 to 579, the domain is characterized as Helicase C-terminal.
+At position 609 to 712, the domain is characterized as Dicer dsRNA-binding fold.
+At position 988 to 1127, the domain is characterized as RNase III 1.
+At position 1168 to 1358, the domain is characterized as RNase III 2.
+At position 1388 to 1469, the domain is characterized as DRBM.
+At position 37 to 119, the domain is characterized as U-box.
+At position 312 to 469, the domain is characterized as PPIase cyclophilin-type.
+At position 138 to 166, the domain is characterized as KOW.
+At position 98 to 205, the domain is characterized as PRC barrel.
+At position 101 to 170, the domain is characterized as PRC barrel.
+At position 277 to 475, the domain is characterized as B30.2/SPRY.
+At position 75 to 110, the domain is characterized as EF-hand 3.
+At position 113 to 148, the domain is characterized as EF-hand 4.
+At position 257 to 440, the domain is characterized as MIF4G.
+At position 548 to 664, the domain is characterized as MI.
+At position 33 to 199, the domain is characterized as Helicase ATP-binding.
+At position 232 to 426, the domain is characterized as Helicase C-terminal.
+At position 38 to 224, the domain is characterized as Helicase ATP-binding.
+At position 248 to 404, the domain is characterized as Helicase C-terminal.
+At position 260 to 483, the domain is characterized as GATase cobBQ-type.
+At position 356 to 531, the domain is characterized as N-acetyltransferase.
+At position 99 to 350, the domain is characterized as Protein kinase.
+At position 60 to 377, the domain is characterized as PPM-type phosphatase.
+At position 89 to 300, the domain is characterized as ABC transmembrane type-1.
+At position 13 to 253, the domain is characterized as Radical SAM core.
+At position 445 to 506, the domain is characterized as SH3 3.
+At position 829 to 888, the domain is characterized as SH3 4.
+At position 93 to 170, the domain is characterized as RRM.
+At position 156 to 206, the domain is characterized as DHHC.
+At position 168 to 355, the domain is characterized as Glutamine amidotransferase type-1.
+At position 291 to 408, the domain is characterized as Nop.
+At position 1006 to 1071, the domain is characterized as R3H.
+At position 1 to 106, the domain is characterized as HD.
+At position 513 to 660, the domain is characterized as GGDEF.
+At position 827 to 917, the domain is characterized as PKD.
+At position 15 to 70, the domain is characterized as HTH deoR-type.
+At position 38 to 91, the domain is characterized as TSP type-1 1.
+At position 94 to 132, the domain is characterized as LDL-receptor class A.
+At position 136 to 498, the domain is characterized as MACPF.
+At position 499 to 529, the domain is characterized as EGF-like.
+At position 542 to 586, the domain is characterized as TSP type-1 2.
+At position 61 to 167, the domain is characterized as Expansin-like EG45.
+At position 159 to 353, the domain is characterized as CheB-type methylesterase.
+At position 411 to 647, the domain is characterized as ABC transporter 1.
+At position 673 to 1000, the domain is characterized as ABC transporter 2.
+At position 10 to 173, the domain is characterized as PPIase cyclophilin-type.
+At position 68 to 114, the domain is characterized as F-box.
+At position 160 to 223, the domain is characterized as bZIP.
+At position 75 to 112, the domain is characterized as EF-hand 1.
+At position 163 to 198, the domain is characterized as EF-hand 3.
+At position 200 to 235, the domain is characterized as EF-hand 4.
+At position 241 to 276, the domain is characterized as EF-hand 5.
+At position 277 to 312, the domain is characterized as EF-hand 6.
+At position 143 to 354, the domain is characterized as DOG1.
+At position 33 to 162, the domain is characterized as RNase III.
+At position 188 to 257, the domain is characterized as DRBM.
+At position 17 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 591 to 678, the domain is characterized as Carrier.
+At position 879 to 1024, the domain is characterized as N-acetyltransferase.
+At position 36 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 95 to 220, the domain is characterized as MPN.
+At position 5 to 197, the domain is characterized as Glutamine amidotransferase type-1.
+At position 198 to 390, the domain is characterized as GMPS ATP-PPase.
+At position 44 to 270, the domain is characterized as Radical SAM core.
+At position 156 to 670, the domain is characterized as USP.
+At position 672 to 765, the domain is characterized as DUSP 1.
+At position 773 to 876, the domain is characterized as DUSP 2.
+At position 3 to 47, the domain is characterized as LEM.
+At position 281 to 389, the domain is characterized as CUB 1.
+At position 391 to 450, the domain is characterized as Sushi 1.
+At position 452 to 562, the domain is characterized as CUB 2.
+At position 565 to 626, the domain is characterized as Sushi 2.
+At position 628 to 739, the domain is characterized as CUB 3.
+At position 743 to 802, the domain is characterized as Sushi 3.
+At position 804 to 867, the domain is characterized as Sushi 4.
+At position 871 to 932, the domain is characterized as Sushi 5.
+At position 38 to 385, the domain is characterized as G-alpha.
+At position 1059 to 1138, the domain is characterized as G5 1.
+At position 1150 to 1230, the domain is characterized as G5 2.
+At position 79 to 433, the domain is characterized as Peptidase A1.
+At position 25 to 169, the domain is characterized as FAS1.
+At position 67 to 237, the domain is characterized as Helicase ATP-binding.
+At position 247 to 407, the domain is characterized as Helicase C-terminal.
+At position 4 to 219, the domain is characterized as Radical SAM core.
+At position 1098 to 1171, the domain is characterized as U-box.
+At position 559 to 617, the domain is characterized as RAP.
+At position 82 to 167, the domain is characterized as Core-binding (CB).
+At position 189 to 375, the domain is characterized as Tyr recombinase.
+At position 15 to 89, the domain is characterized as S4 RNA-binding.
+At position 13 to 76, the domain is characterized as SAM.
+At position 462 to 497, the domain is characterized as EF-hand 1.
+At position 506 to 541, the domain is characterized as EF-hand 2.
+At position 622 to 766, the domain is characterized as Ferric oxidoreductase.
+At position 794 to 942, the domain is characterized as FAD-binding FR-type.
+At position 79 to 188, the domain is characterized as Plastocyanin-like.
+At position 63 to 119, the domain is characterized as WHEP-TRS.
+At position 201 to 391, the domain is characterized as ATP-grasp 1.
+At position 734 to 931, the domain is characterized as ATP-grasp 2.
+At position 999 to 1154, the domain is characterized as MGS-like.
+At position 82 to 111, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 151 to 180, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 23 to 131, the domain is characterized as BTB.
+At position 35 to 124, the domain is characterized as CTCK.
+At position 50 to 164, the domain is characterized as Expansin-like EG45.
+At position 174 to 253, the domain is characterized as Expansin-like CBD.
+At position 300 to 405, the domain is characterized as C-type lectin.
+At position 69 to 247, the domain is characterized as FAD-binding PCMH-type.
+At position 1083 to 1251, the domain is characterized as DH.
+At position 1263 to 1370, the domain is characterized as PH.
+At position 63 to 266, the domain is characterized as ABC transmembrane type-1.
+At position 185 to 419, the domain is characterized as NR LBD.
+At position 50 to 299, the domain is characterized as Peptidase S1 1.
+At position 312 to 425, the domain is characterized as CUB 1.
+At position 435 to 547, the domain is characterized as CUB 2.
+At position 590 to 819, the domain is characterized as Peptidase S1 2.
+At position 93 to 342, the domain is characterized as Dynamin-type G.
+At position 33 to 216, the domain is characterized as BPL/LPL catalytic.
+At position 58 to 239, the domain is characterized as BPL/LPL catalytic.
+At position 297 to 321, the domain is characterized as HhH.
+At position 12 to 338, the domain is characterized as SET.
+At position 238 to 298, the domain is characterized as HTH myb-type.
+At position 274 to 465, the domain is characterized as PNPLA.
+At position 15 to 196, the domain is characterized as UmuC.
+At position 245 to 292, the domain is characterized as EGF-like 1.
+At position 293 to 334, the domain is characterized as EGF-like 2; calcium-binding.
+At position 415 to 698, the domain is characterized as Protein kinase.
+At position 28 to 139, the domain is characterized as Ig-like V-type 1.
+At position 151 to 237, the domain is characterized as Ig-like V-type 2.
+At position 316 to 509, the domain is characterized as B30.2/SPRY.
+At position 366 to 465, the domain is characterized as PFU.
+At position 533 to 794, the domain is characterized as PUL.
+At position 14 to 162, the domain is characterized as NAC.
+At position 19 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 129 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 317 to 403, the domain is characterized as Ig-like C2-type 3.
+At position 113 to 177, the domain is characterized as H15.
+At position 104 to 222, the domain is characterized as C-type lectin.
+At position 171 to 197, the domain is characterized as KH.
+At position 66 to 369, the domain is characterized as Protein kinase.
+At position 22 to 76, the domain is characterized as HTH cro/C1-type.
+At position 40 to 82, the domain is characterized as Fibronectin type-I.
+At position 83 to 121, the domain is characterized as EGF-like.
+At position 128 to 209, the domain is characterized as Kringle.
+At position 226 to 476, the domain is characterized as Peptidase S1.
+At position 92 to 131, the domain is characterized as Agouti.
+At position 336 to 511, the domain is characterized as Helicase ATP-binding.
+At position 522 to 684, the domain is characterized as Helicase C-terminal.
+At position 251 to 415, the domain is characterized as UBC core.
+At position 145 to 232, the domain is characterized as Ig-like C2-type 1.
+At position 237 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 323 to 413, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 406, the domain is characterized as Rho RNA-BD.
+At position 443 to 478, the domain is characterized as UVR.
+At position 151 to 283, the domain is characterized as PH.
+At position 32 to 123, the domain is characterized as Fibronectin type-III 1.
+At position 241 to 334, the domain is characterized as Fibronectin type-III 2.
+At position 328 to 489, the domain is characterized as Helicase ATP-binding.
+At position 543 to 703, the domain is characterized as Helicase C-terminal.
+At position 50 to 101, the domain is characterized as F-box; degenerate.
+At position 8 to 246, the domain is characterized as ABC transporter.
+At position 421 to 608, the domain is characterized as DH.
+At position 378 to 606, the domain is characterized as BPL/LPL catalytic.
+At position 382 to 545, the domain is characterized as ELMO.
+At position 8 to 124, the domain is characterized as MTTase N-terminal.
+At position 82 to 145, the domain is characterized as bZIP.
+At position 153 to 363, the domain is characterized as DOG1.
+At position 134 to 283, the domain is characterized as Fatty acid hydroxylase.
+At position 139 to 240, the domain is characterized as BACK.
+At position 35 to 131, the domain is characterized as BRCT.
+At position 660 to 753, the domain is characterized as BRCT 1.
+At position 821 to 913, the domain is characterized as BRCT 2.
+At position 481 to 676, the domain is characterized as VWFA.
+At position 356 to 441, the domain is characterized as Death.
+At position 21 to 83, the domain is characterized as LIM zinc-binding 1.
+At position 85 to 147, the domain is characterized as LIM zinc-binding 2.
+At position 1 to 72, the domain is characterized as FERM.
+At position 46 to 232, the domain is characterized as DCUN1.
+At position 1 to 99, the domain is characterized as VPS28 N-terminal.
+At position 109 to 179, the domain is characterized as PAS.
+At position 265 to 397, the domain is characterized as GGDEF.
+At position 406 to 658, the domain is characterized as EAL.
+At position 350 to 499, the domain is characterized as MATH.
+At position 62 to 310, the domain is characterized as Protein kinase 1.
+At position 311 to 380, the domain is characterized as AGC-kinase C-terminal.
+At position 407 to 664, the domain is characterized as Protein kinase 2.
+At position 269 to 332, the domain is characterized as bZIP.
+At position 339 to 466, the domain is characterized as MRH 2.
+At position 98 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 133 to 329, the domain is characterized as ATP-grasp 1.
+At position 686 to 878, the domain is characterized as ATP-grasp 2.
+At position 945 to 1081, the domain is characterized as MGS-like.
+At position 250 to 472, the domain is characterized as Lon N-terminal.
+At position 74 to 287, the domain is characterized as YjeF N-terminal.
+At position 558 to 587, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 588 to 617, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 10 to 240, the domain is characterized as ABC transporter.
+At position 39 to 258, the domain is characterized as Peptidase S1.
+At position 2 to 74, the domain is characterized as H15.
+At position 9 to 120, the domain is characterized as MSS4.
+At position 171 to 415, the domain is characterized as NR LBD.
+At position 155 to 444, the domain is characterized as Peptidase S8.
+At position 133 to 284, the domain is characterized as Exonuclease.
+At position 851 to 1120, the domain is characterized as Protein kinase.
+At position 32 to 195, the domain is characterized as EngA-type G 1.
+At position 380 to 462, the domain is characterized as KH-like.
+At position 209 to 299, the domain is characterized as Ig-like C1-type.
+At position 1 to 373, the domain is characterized as SAM-dependent MTase C5-type.
+At position 36 to 152, the domain is characterized as Cytochrome c.
+At position 232 to 423, the domain is characterized as Helicase ATP-binding.
+At position 434 to 594, the domain is characterized as Helicase C-terminal.
+At position 231 to 391, the domain is characterized as Helicase C-terminal.
+At position 69 to 296, the domain is characterized as AB hydrolase-1.
+At position 65 to 151, the domain is characterized as PNT.
+At position 1050 to 1112, the domain is characterized as FIP-RBD.
+At position 40 to 104, the domain is characterized as Sushi.
+At position 153 to 480, the domain is characterized as Histidine kinase.
+At position 142 to 480, the domain is characterized as Peptidase A1.
+At position 83 to 351, the domain is characterized as Protein kinase.
+At position 352 to 426, the domain is characterized as AGC-kinase C-terminal.
+At position 1026 to 1154, the domain is characterized as PH.
+At position 1181 to 1479, the domain is characterized as CNH.
+At position 1544 to 1557, the domain is characterized as CRIB.
+At position 1 to 83, the domain is characterized as Sm.
+At position 241 to 277, the domain is characterized as DFDF.
+At position 82 to 176, the domain is characterized as Toprim.
+At position 98 to 176, the domain is characterized as S4 RNA-binding.
+At position 514 to 697, the domain is characterized as Helicase ATP-binding 1.
+At position 731 to 941, the domain is characterized as Helicase C-terminal 1.
+At position 1006 to 1308, the domain is characterized as SEC63 1.
+At position 1360 to 1537, the domain is characterized as Helicase ATP-binding 2.
+At position 1574 to 1779, the domain is characterized as Helicase C-terminal 2.
+At position 1839 to 2157, the domain is characterized as SEC63 2.
+At position 66 to 274, the domain is characterized as HD.
+At position 1 to 200, the domain is characterized as Protein kinase.
+At position 4 to 75, the domain is characterized as HTH deoR-type.
+At position 468 to 566, the domain is characterized as Fe2OG dioxygenase.
+At position 106 to 261, the domain is characterized as CP-type G.
+At position 38 to 180, the domain is characterized as SLD.
+At position 76 to 342, the domain is characterized as PPM-type phosphatase.
+At position 498 to 549, the domain is characterized as ATP-grasp.
+At position 142 to 205, the domain is characterized as 3'-5' exonuclease.
+At position 99 to 329, the domain is characterized as Radical SAM core.
+At position 94 to 227, the domain is characterized as Fatty acid hydroxylase.
+At position 288 to 386, the domain is characterized as HTH araC/xylS-type.
+At position 199 to 269, the domain is characterized as HARP 1.
+At position 286 to 357, the domain is characterized as HARP 2.
+At position 404 to 559, the domain is characterized as Helicase ATP-binding.
+At position 674 to 827, the domain is characterized as Helicase C-terminal.
+At position 291 to 392, the domain is characterized as Fe2OG dioxygenase.
+At position 194 to 274, the domain is characterized as KH type-2.
+At position 316 to 372, the domain is characterized as MIR 1.
+At position 382 to 438, the domain is characterized as MIR 2.
+At position 443 to 499, the domain is characterized as MIR 3.
+At position 299 to 343, the domain is characterized as CHCH.
+At position 1 to 30, the domain is characterized as HNF-p1.
+At position 103 to 199, the domain is characterized as POU-specific atypical.
+At position 178 to 334, the domain is characterized as Nudix hydrolase.
+At position 53 to 135, the domain is characterized as Lipoyl-binding.
+At position 33 to 163, the domain is characterized as C-type lectin.
+At position 136 to 237, the domain is characterized as BACK.
+At position 304 to 356, the domain is characterized as TSP type-1.
+At position 153 to 280, the domain is characterized as NB-ARC 1.
+At position 339 to 438, the domain is characterized as NB-ARC 2.
+At position 477 to 675, the domain is characterized as MAGE.
+At position 86 to 159, the domain is characterized as PRC barrel.
+At position 902 to 976, the domain is characterized as RRM.
+At position 28 to 192, the domain is characterized as Helicase ATP-binding.
+At position 250 to 420, the domain is characterized as Helicase C-terminal.
+At position 117 to 428, the domain is characterized as IF rod.
+At position 17 to 179, the domain is characterized as DHFR.
+At position 226 to 389, the domain is characterized as TrmE-type G.
+At position 595 to 654, the domain is characterized as KH.
+At position 666 to 735, the domain is characterized as S1 motif.
+At position 14 to 305, the domain is characterized as Lon N-terminal.
+At position 773 to 969, the domain is characterized as Lon proteolytic.
+At position 41 to 156, the domain is characterized as Calponin-homology (CH).
+At position 594 to 627, the domain is characterized as WW.
+At position 690 to 719, the domain is characterized as IQ 1.
+At position 720 to 749, the domain is characterized as IQ 2.
+At position 750 to 779, the domain is characterized as IQ 3.
+At position 917 to 1150, the domain is characterized as Ras-GAP.
+At position 517 to 799, the domain is characterized as UvrD-like helicase C-terminal.
+At position 43 to 310, the domain is characterized as Pyruvate carboxyltransferase.
+At position 11 to 133, the domain is characterized as RNase III.
+At position 160 to 230, the domain is characterized as DRBM.
+At position 174 to 380, the domain is characterized as Helicase ATP-binding.
+At position 413 to 611, the domain is characterized as Helicase C-terminal.
+At position 359 to 389, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 399 to 428, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 84, the domain is characterized as Sm.
+At position 124 to 223, the domain is characterized as C-type lectin.
+At position 286 to 421, the domain is characterized as Fido.
+At position 12 to 127, the domain is characterized as MTTase N-terminal.
+At position 148 to 390, the domain is characterized as Radical SAM core.
+At position 392 to 464, the domain is characterized as TRAM.
+At position 710 to 787, the domain is characterized as ACT 1.
+At position 817 to 888, the domain is characterized as ACT 2.
+At position 1 to 175, the domain is characterized as PRELI/MSF1.
+At position 319 to 495, the domain is characterized as CRAL-TRIO.
+At position 521 to 674, the domain is characterized as GOLD.
+At position 1 to 107, the domain is characterized as Tyrosine-protein phosphatase.
+At position 150 to 287, the domain is characterized as OTU.
+At position 1 to 84, the domain is characterized as BMV.
+At position 189 to 446, the domain is characterized as NB-ARC.
+At position 102 to 162, the domain is characterized as LIM zinc-binding 2.
+At position 393 to 669, the domain is characterized as Protein kinase.
+At position 539 to 597, the domain is characterized as CBS 1.
+At position 756 to 809, the domain is characterized as CBS 2.
+At position 60 to 232, the domain is characterized as FAD-binding PCMH-type.
+At position 305 to 499, the domain is characterized as B30.2/SPRY.
+At position 38 to 249, the domain is characterized as Cupin type-1 1.
+At position 357 to 502, the domain is characterized as Cupin type-1 2.
+At position 1 to 31, the domain is characterized as WW 1.
+At position 42 to 72, the domain is characterized as WW 2.
+At position 132 to 188, the domain is characterized as FF 1.
+At position 201 to 257, the domain is characterized as FF 2.
+At position 262 to 332, the domain is characterized as FF 3.
+At position 354 to 413, the domain is characterized as FF 4.
+At position 427 to 488, the domain is characterized as FF 5.
+At position 491 to 552, the domain is characterized as FF 6.
+At position 23 to 311, the domain is characterized as Protein kinase.
+At position 2050 to 2285, the domain is characterized as ABC transporter 2.
+At position 52 to 103, the domain is characterized as HTH psq-type.
+At position 117 to 190, the domain is characterized as HTH CENPB-type.
+At position 238 to 358, the domain is characterized as DDE-1.
+At position 389 to 549, the domain is characterized as PA14.
+At position 1 to 174, the domain is characterized as VWFA.
+At position 210 to 229, the domain is characterized as UIM 1.
+At position 255 to 274, the domain is characterized as UIM 2.
+At position 288 to 307, the domain is characterized as UIM 3.
+At position 194 to 406, the domain is characterized as Helicase ATP-binding.
+At position 455 to 631, the domain is characterized as Helicase C-terminal.
+At position 21 to 79, the domain is characterized as LCN-type CS-alpha/beta.
+At position 1310 to 1864, the domain is characterized as FAT.
+At position 1968 to 2271, the domain is characterized as PI3K/PI4K catalytic.
+At position 2255 to 2287, the domain is characterized as FATC.
+At position 463 to 622, the domain is characterized as C2 DOCK-type.
+At position 1379 to 1828, the domain is characterized as DOCKER.
+At position 80 to 397, the domain is characterized as Peptidase A1.
+At position 2 to 186, the domain is characterized as YrdC-like.
+At position 528 to 603, the domain is characterized as Carrier.
+At position 19 to 100, the domain is characterized as Lipoyl-binding.
+At position 70 to 287, the domain is characterized as Radical SAM core.
+At position 460 to 629, the domain is characterized as tr-type G.
+At position 25 to 395, the domain is characterized as PIPK.
+At position 1 to 105, the domain is characterized as Tyrosine-protein phosphatase.
+At position 20 to 218, the domain is characterized as PNPLA.
+At position 5 to 163, the domain is characterized as Obg.
+At position 164 to 330, the domain is characterized as OBG-type G.
+At position 267 to 542, the domain is characterized as Protein kinase.
+At position 33 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 116 to 198, the domain is characterized as Ig-like C2-type 2.
+At position 35 to 100, the domain is characterized as NAC-A/B.
+At position 7 to 217, the domain is characterized as RNase H type-2.
+At position 6 to 136, the domain is characterized as TsaA-like.
+At position 228 to 288, the domain is characterized as bZIP.
+At position 412 to 502, the domain is characterized as EH.
+At position 21 to 222, the domain is characterized as Collectrin-like.
+At position 9 to 136, the domain is characterized as RNase III.
+At position 17 to 143, the domain is characterized as Nudix hydrolase.
+At position 281 to 650, the domain is characterized as GRAS.
+At position 154 to 240, the domain is characterized as Doublecortin 1.
+At position 309 to 392, the domain is characterized as Doublecortin 2.
+At position 473 to 731, the domain is characterized as Protein kinase.
+At position 87 to 171, the domain is characterized as PDZ 1.
+At position 211 to 295, the domain is characterized as PDZ 2.
+At position 752 to 839, the domain is characterized as PDZ 3.
+At position 29 to 130, the domain is characterized as Gnk2-homologous 1.
+At position 136 to 240, the domain is characterized as Gnk2-homologous 2.
+At position 333 to 620, the domain is characterized as Protein kinase.
+At position 33 to 134, the domain is characterized as Gnk2-homologous 1.
+At position 140 to 252, the domain is characterized as Gnk2-homologous 2.
+At position 58 to 121, the domain is characterized as bZIP.
+At position 141 to 379, the domain is characterized as Radical SAM core.
+At position 382 to 445, the domain is characterized as TRAM.
+At position 88 to 217, the domain is characterized as GST C-terminal.
+At position 60 to 217, the domain is characterized as PID.
+At position 347 to 548, the domain is characterized as Protein kinase.
+At position 116 to 219, the domain is characterized as PH.
+At position 296 to 357, the domain is characterized as SH3.
+At position 127 to 418, the domain is characterized as NR LBD.
+At position 5 to 120, the domain is characterized as VOC 1.
+At position 142 to 270, the domain is characterized as VOC 2.
+At position 185 to 287, the domain is characterized as PB1.
+At position 225 to 480, the domain is characterized as GP-PDE.
+At position 29 to 105, the domain is characterized as PAN.
+At position 110 to 188, the domain is characterized as Kringle 1.
+At position 192 to 269, the domain is characterized as Kringle 2.
+At position 282 to 359, the domain is characterized as Kringle 3.
+At position 384 to 461, the domain is characterized as Kringle 4.
+At position 485 to 564, the domain is characterized as Kringle 5.
+At position 584 to 810, the domain is characterized as Peptidase S1.
+At position 33 to 236, the domain is characterized as Peptidase S1.
+At position 640 to 760, the domain is characterized as P/Homo B.
+At position 328 to 438, the domain is characterized as Fibronectin type-III 1.
+At position 439 to 536, the domain is characterized as Fibronectin type-III 2.
+At position 620 to 881, the domain is characterized as Protein kinase.
+At position 3 to 190, the domain is characterized as KIND.
+At position 565 to 865, the domain is characterized as FERM.
+At position 1084 to 1170, the domain is characterized as PDZ 1.
+At position 1357 to 1442, the domain is characterized as PDZ 2.
+At position 1491 to 1579, the domain is characterized as PDZ 3.
+At position 1764 to 1845, the domain is characterized as PDZ 4.
+At position 1857 to 1942, the domain is characterized as PDZ 5.
+At position 2180 to 2434, the domain is characterized as Tyrosine-protein phosphatase.
+At position 183 to 288, the domain is characterized as Fe2OG dioxygenase.
+At position 228 to 413, the domain is characterized as Glutamine amidotransferase type-1.
+At position 562 to 754, the domain is characterized as ATP-grasp 1.
+At position 1099 to 1290, the domain is characterized as ATP-grasp 2.
+At position 1356 to 1508, the domain is characterized as MGS-like.
+At position 100 to 341, the domain is characterized as Radical SAM core.
+At position 14 to 241, the domain is characterized as Phosphagen kinase C-terminal.
+At position 94 to 293, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 1 to 163, the domain is characterized as HD Cas3-type.
+At position 213 to 404, the domain is characterized as Helicase ATP-binding.
+At position 434 to 592, the domain is characterized as Helicase C-terminal.
+At position 52 to 161, the domain is characterized as sHSP.
+At position 3 to 204, the domain is characterized as ABC transporter.
+At position 1 to 128, the domain is characterized as C-type lysozyme.
+At position 38 to 154, the domain is characterized as Urease.
+At position 75 to 138, the domain is characterized as S5 DRBM.
+At position 65 to 290, the domain is characterized as OBG-type G.
+At position 290 to 366, the domain is characterized as TGS.
+At position 40 to 266, the domain is characterized as GB1/RHD3-type G.
+At position 224 to 324, the domain is characterized as Fe2OG dioxygenase.
+At position 18 to 64, the domain is characterized as CHCH.
+At position 18 to 72, the domain is characterized as MADS-box.
+At position 651 to 823, the domain is characterized as MOSC.
+At position 46 to 126, the domain is characterized as G protein gamma.
+At position 10 to 153, the domain is characterized as HTH marR-type.
+At position 43 to 155, the domain is characterized as HotDog ACOT-type 1.
+At position 216 to 329, the domain is characterized as HotDog ACOT-type 2.
+At position 375 to 585, the domain is characterized as START.
+At position 811 to 876, the domain is characterized as SAM.
+At position 16 to 84, the domain is characterized as HTH gntR-type.
+At position 32 to 67, the domain is characterized as EF-hand 1.
+At position 67 to 98, the domain is characterized as EF-hand 2.
+At position 53 to 484, the domain is characterized as IF rod.
+At position 3 to 65, the domain is characterized as HTH asnC-type.
+At position 78 to 201, the domain is characterized as Plastocyanin-like 1.
+At position 210 to 367, the domain is characterized as Plastocyanin-like 2.
+At position 430 to 566, the domain is characterized as Plastocyanin-like 3.
+At position 189 to 252, the domain is characterized as bZIP.
+At position 256 to 473, the domain is characterized as DOG1.
+At position 32 to 316, the domain is characterized as Protein kinase.
+At position 27 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 54 to 159, the domain is characterized as HD.
+At position 403 to 464, the domain is characterized as TGS.
+At position 669 to 744, the domain is characterized as ACT.
+At position 141 to 223, the domain is characterized as RRM 2.
+At position 236 to 308, the domain is characterized as RRM 3.
+At position 101 to 196, the domain is characterized as Fibronectin type-III 1.
+At position 197 to 285, the domain is characterized as Fibronectin type-III 2.
+At position 557 to 671, the domain is characterized as Fibronectin type-III 3.
+At position 947 to 1042, the domain is characterized as Fibronectin type-III 4.
+At position 1043 to 1150, the domain is characterized as Fibronectin type-III 5.
+At position 1450 to 1556, the domain is characterized as Fibronectin type-III 6.
+At position 1557 to 1656, the domain is characterized as Fibronectin type-III 7.
+At position 1658 to 1751, the domain is characterized as Fibronectin type-III 8.
+At position 1752 to 1854, the domain is characterized as Fibronectin type-III 9.
+At position 1945 to 2222, the domain is characterized as Protein kinase.
+At position 18 to 459, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 485 to 755, the domain is characterized as UvrD-like helicase C-terminal.
+At position 271 to 472, the domain is characterized as MCM.
+At position 1 to 57, the domain is characterized as HTH deoR-type.
+At position 27 to 311, the domain is characterized as Protein kinase.
+At position 156 to 318, the domain is characterized as N-acetyltransferase.
+At position 131 to 351, the domain is characterized as Radical SAM core.
+At position 92 to 392, the domain is characterized as AB hydrolase-1.
+At position 33 to 152, the domain is characterized as EamA.
+At position 78 to 120, the domain is characterized as PAS.
+At position 37 to 312, the domain is characterized as Cupin type-1 1.
+At position 380 to 529, the domain is characterized as Cupin type-1 2.
+At position 281 to 357, the domain is characterized as RRM 1.
+At position 371 to 445, the domain is characterized as RRM 2.
+At position 461 to 535, the domain is characterized as RRM 3.
+At position 553 to 628, the domain is characterized as RRM 4.
+At position 54 to 136, the domain is characterized as SCAN box.
+At position 231 to 306, the domain is characterized as KRAB.
+At position 182 to 278, the domain is characterized as Inhibitor I9.
+At position 289 to 614, the domain is characterized as Peptidase S8.
+At position 139 to 236, the domain is characterized as HTH araC/xylS-type.
+At position 586 to 651, the domain is characterized as J.
+At position 99 to 775, the domain is characterized as Peptidase M13.
+At position 297 to 339, the domain is characterized as UBA.
+At position 94 to 162, the domain is characterized as POTRA.
+At position 27 to 116, the domain is characterized as UPAR/Ly6.
+At position 9 to 235, the domain is characterized as ATP-grasp.
+At position 362 to 428, the domain is characterized as CobW C-terminal.
+At position 2 to 85, the domain is characterized as Sm.
+At position 821 to 850, the domain is characterized as IQ 1.
+At position 844 to 873, the domain is characterized as IQ 2.
+At position 4 to 187, the domain is characterized as PBC.
+At position 30 to 128, the domain is characterized as Plastocyanin-like 1.
+At position 157 to 345, the domain is characterized as Plastocyanin-like 2.
+At position 461 to 584, the domain is characterized as Plastocyanin-like 3.
+At position 162 to 496, the domain is characterized as Peptidase A1.
+At position 44 to 163, the domain is characterized as Rieske.
+At position 12 to 156, the domain is characterized as Nudix hydrolase.
+At position 208 to 336, the domain is characterized as OmpA-like.
+At position 474 to 628, the domain is characterized as Helicase C-terminal.
+At position 20 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 125 to 216, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 305, the domain is characterized as Ig-like C2-type 3.
+At position 313 to 401, the domain is characterized as Ig-like C2-type 4.
+At position 407 to 500, the domain is characterized as Ig-like C2-type 5.
+At position 504 to 592, the domain is characterized as Ig-like C2-type 6.
+At position 596 to 685, the domain is characterized as Ig-like C2-type 7.
+At position 690 to 783, the domain is characterized as Ig-like C2-type 8.
+At position 787 to 883, the domain is characterized as Ig-like C2-type 9.
+At position 885 to 982, the domain is characterized as Fibronectin type-III 1.
+At position 987 to 1086, the domain is characterized as Fibronectin type-III 2.
+At position 1091 to 1187, the domain is characterized as Fibronectin type-III 3.
+At position 1191 to 1285, the domain is characterized as Fibronectin type-III 4.
+At position 1285 to 1377, the domain is characterized as Ig-like C2-type 10.
+At position 1379 to 1473, the domain is characterized as Fibronectin type-III 5.
+At position 1474 to 1575, the domain is characterized as Fibronectin type-III 6.
+At position 8 to 60, the domain is characterized as F-box.
+At position 132 to 170, the domain is characterized as LRRCT.
+At position 39 to 297, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 237 to 499, the domain is characterized as Olfactomedin-like.
+At position 138 to 179, the domain is characterized as STI1 1.
+At position 192 to 231, the domain is characterized as STI1 2.
+At position 357 to 394, the domain is characterized as STI1 3.
+At position 398 to 433, the domain is characterized as STI1 4.
+At position 491 to 535, the domain is characterized as UBA.
+At position 120 to 380, the domain is characterized as Protein kinase.
+At position 396 to 556, the domain is characterized as PA14.
+At position 92 to 407, the domain is characterized as IF rod.
+At position 164 to 261, the domain is characterized as HTH araC/xylS-type.
+At position 346 to 514, the domain is characterized as tr-type G.
+At position 2 to 226, the domain is characterized as Glutamine amidotransferase type-2.
+At position 295 to 434, the domain is characterized as SIS 1.
+At position 467 to 608, the domain is characterized as SIS 2.
+At position 2 to 206, the domain is characterized as ABC transporter.
+At position 40 to 165, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 59 to 198, the domain is characterized as FAS1.
+At position 1 to 379, the domain is characterized as Trm1 methyltransferase.
+At position 225 to 288, the domain is characterized as bZIP.
+At position 8 to 109, the domain is characterized as PPIase FKBP-type.
+At position 745 to 813, the domain is characterized as BTB.
+At position 3 to 22, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 47 to 77, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 78 to 107, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 114 to 147, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 218 to 252, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 305 to 500, the domain is characterized as B30.2/SPRY.
+At position 69 to 289, the domain is characterized as Radical SAM core.
+At position 569 to 598, the domain is characterized as IQ.
+At position 70 to 336, the domain is characterized as AB hydrolase-1.
+At position 30 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 317, the domain is characterized as Plastocyanin-like 2.
+At position 424 to 564, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 60, the domain is characterized as Helicase ATP-binding.
+At position 115 to 316, the domain is characterized as Helicase C-terminal.
+At position 34 to 100, the domain is characterized as KH.
+At position 111 to 384, the domain is characterized as Dynamin-type G.
+At position 616 to 705, the domain is characterized as GED.
+At position 41 to 140, the domain is characterized as PH.
+At position 4 to 90, the domain is characterized as Disintegrin.
+At position 253 to 657, the domain is characterized as USP.
+At position 51 to 119, the domain is characterized as BTB.
+At position 90 to 246, the domain is characterized as HD.
+At position 130 to 359, the domain is characterized as Sigma-54 factor interaction.
+At position 350 to 499, the domain is characterized as CBM3.
+At position 43 to 176, the domain is characterized as TLDc.
+At position 44 to 122, the domain is characterized as RRM.
+At position 141 to 235, the domain is characterized as Rieske.
+At position 220 to 529, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 31 to 99, the domain is characterized as Importin N-terminal.
+At position 58 to 285, the domain is characterized as Radical SAM core.
+At position 18 to 275, the domain is characterized as GH16.
+At position 243 to 335, the domain is characterized as ARID.
+At position 449 to 546, the domain is characterized as REKLES.
+At position 155 to 311, the domain is characterized as N-acetyltransferase.
+At position 5 to 277, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 278 to 593, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 82, the domain is characterized as Ubiquitin-like.
+At position 398 to 438, the domain is characterized as UBA.
+At position 2 to 199, the domain is characterized as DPCK.
+At position 34 to 213, the domain is characterized as VWFA.
+At position 307 to 405, the domain is characterized as Fibronectin type-III 2.
+At position 33 to 274, the domain is characterized as ABC transporter.
+At position 102 to 200, the domain is characterized as PDZ.
+At position 8 to 90, the domain is characterized as PDZ.
+At position 280 to 339, the domain is characterized as LIM zinc-binding 1.
+At position 2018 to 2078, the domain is characterized as LIM zinc-binding 2.
+At position 2079 to 2138, the domain is characterized as LIM zinc-binding 3.
+At position 2139 to 2194, the domain is characterized as LIM zinc-binding 4.
+At position 410 to 617, the domain is characterized as MCM.
+At position 23 to 224, the domain is characterized as Pentraxin (PTX).
+At position 164 to 553, the domain is characterized as NR LBD.
+At position 61 to 146, the domain is characterized as PSP1 C-terminal.
+At position 276 to 296, the domain is characterized as IQ.
+At position 16 to 211, the domain is characterized as tr-type G.
+At position 19 to 90, the domain is characterized as Inhibitor I9.
+At position 115 to 447, the domain is characterized as Peptidase S8.
+At position 174 to 209, the domain is characterized as EF-hand 3.
+At position 460 to 508, the domain is characterized as KA1.
+At position 9 to 126, the domain is characterized as MTTase N-terminal.
+At position 149 to 381, the domain is characterized as Radical SAM core.
+At position 384 to 448, the domain is characterized as TRAM.
+At position 88 to 148, the domain is characterized as S4 RNA-binding.
+At position 143 to 370, the domain is characterized as Radical SAM core.
+At position 373 to 437, the domain is characterized as TRAM.
+At position 11 to 142, the domain is characterized as VHS.
+At position 212 to 272, the domain is characterized as SH3.
+At position 31 to 329, the domain is characterized as GH10.
+At position 109 to 208, the domain is characterized as PPIase FKBP-type.
+At position 1 to 52, the domain is characterized as F-box.
+At position 96 to 269, the domain is characterized as Collagen-like 1.
+At position 277 to 291, the domain is characterized as Collagen-like 2.
+At position 2 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 33 to 144, the domain is characterized as HIT.
+At position 578 to 851, the domain is characterized as Protein kinase.
+At position 9 to 246, the domain is characterized as ABC transporter.
+At position 335 to 434, the domain is characterized as Rhodanese.
+At position 38 to 52, the domain is characterized as EF-hand 2.
+At position 14 to 212, the domain is characterized as N-acetyltransferase.
+At position 229 to 484, the domain is characterized as CN hydrolase.
+At position 77 to 198, the domain is characterized as Barwin.
+At position 116 to 326, the domain is characterized as Alpha-type protein kinase.
+At position 356 to 404, the domain is characterized as SOCS box.
+At position 17 to 233, the domain is characterized as ABC transporter.
+At position 102 to 154, the domain is characterized as bHLH.
+At position 839 to 920, the domain is characterized as BRCT.
+At position 358 to 424, the domain is characterized as S4 RNA-binding.
+At position 163 to 255, the domain is characterized as Enkurin.
+At position 179 to 190, the domain is characterized as IQ.
+At position 8 to 74, the domain is characterized as Chitin-binding type R&R.
+At position 149 to 261, the domain is characterized as PilZ.
+At position 643 to 732, the domain is characterized as BRCT.
+At position 134 to 382, the domain is characterized as Dynamin-type G.
+At position 429 to 519, the domain is characterized as IPT/TIG.
+At position 70 to 103, the domain is characterized as EF-hand 2.
+At position 22 to 130, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 141 to 254, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 218 to 418, the domain is characterized as Helicase ATP-binding.
+At position 451 to 616, the domain is characterized as Helicase C-terminal.
+At position 159 to 268, the domain is characterized as Cadherin 2.
+At position 386 to 499, the domain is characterized as Cadherin 4.
+At position 23 to 131, the domain is characterized as WAC.
+At position 375 to 435, the domain is characterized as DDT.
+At position 45 to 298, the domain is characterized as GH26.
+At position 655 to 900, the domain is characterized as CBM11.
+At position 827 to 900, the domain is characterized as Dockerin.
+At position 6 to 115, the domain is characterized as Fibronectin type-III.
+At position 298 to 492, the domain is characterized as B30.2/SPRY.
+At position 132 to 232, the domain is characterized as Ig-like C2-type 2.
+At position 503 to 837, the domain is characterized as Protein kinase.
+At position 349 to 484, the domain is characterized as PLAT.
+At position 564 to 808, the domain is characterized as Alpha-type protein kinase.
+At position 87 to 143, the domain is characterized as HTH cro/C1-type.
+At position 121 to 197, the domain is characterized as RRM.
+At position 22 to 130, the domain is characterized as PH 1.
+At position 208 to 233, the domain is characterized as IQ.
+At position 244 to 430, the domain is characterized as DH.
+At position 460 to 588, the domain is characterized as PH 2.
+At position 635 to 749, the domain is characterized as N-terminal Ras-GEF.
+At position 1027 to 1259, the domain is characterized as Ras-GEF.
+At position 185 to 280, the domain is characterized as RRM 1.
+At position 287 to 364, the domain is characterized as RRM 2.
+At position 38 to 116, the domain is characterized as RRM 1.
+At position 126 to 203, the domain is characterized as RRM 2.
+At position 219 to 296, the domain is characterized as RRM 3.
+At position 322 to 399, the domain is characterized as RRM 4.
+At position 488 to 567, the domain is characterized as PABC.
+At position 69 to 240, the domain is characterized as Helicase ATP-binding.
+At position 263 to 411, the domain is characterized as Helicase C-terminal.
+At position 70 to 213, the domain is characterized as Cupin type-1.
+At position 2 to 222, the domain is characterized as Glutamine amidotransferase type-1.
+At position 155 to 275, the domain is characterized as TFIIS central.
+At position 212 to 261, the domain is characterized as bHLH.
+At position 7 to 147, the domain is characterized as DAC.
+At position 36 to 278, the domain is characterized as ABC transporter.
+At position 163 to 351, the domain is characterized as Rho-GAP.
+At position 32 to 166, the domain is characterized as MATH.
+At position 202 to 269, the domain is characterized as BTB.
+At position 15 to 104, the domain is characterized as EH 1.
+At position 128 to 216, the domain is characterized as EH 2.
+At position 160 to 195, the domain is characterized as EF-hand 2.
+At position 223 to 258, the domain is characterized as EF-hand 3.
+At position 224 to 314, the domain is characterized as EH 3.
+At position 262 to 292, the domain is characterized as EF-hand 4.
+At position 852 to 871, the domain is characterized as UIM 1.
+At position 878 to 897, the domain is characterized as UIM 2.
+At position 14 to 370, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 26 to 139, the domain is characterized as Plastocyanin-like 1.
+At position 168 to 368, the domain is characterized as Plastocyanin-like 2.
+At position 466 to 585, the domain is characterized as Plastocyanin-like 3.
+At position 306 to 365, the domain is characterized as SH3.
+At position 248 to 333, the domain is characterized as PDZ.
+At position 421 to 495, the domain is characterized as DEP.
+At position 4 to 67, the domain is characterized as HMA.
+At position 63 to 219, the domain is characterized as F5/8 type C.
+At position 139 to 307, the domain is characterized as PPIase cyclophilin-type.
+At position 9 to 162, the domain is characterized as Nudix hydrolase.
+At position 49 to 120, the domain is characterized as KRAB.
+At position 1689 to 2042, the domain is characterized as USP.
+At position 32 to 116, the domain is characterized as Inhibitor I9.
+At position 120 to 644, the domain is characterized as Peptidase S8.
+At position 401 to 489, the domain is characterized as PA.
+At position 112 to 352, the domain is characterized as Radical SAM core.
+At position 226 to 344, the domain is characterized as BAH.
+At position 21 to 79, the domain is characterized as F-box; degenerate.
+At position 202 to 280, the domain is characterized as PDZ.
+At position 126 to 235, the domain is characterized as sHSP.
+At position 174 to 277, the domain is characterized as PpiC 1.
+At position 216 to 270, the domain is characterized as bZIP.
+At position 50 to 335, the domain is characterized as AB hydrolase-1.
+At position 422 to 627, the domain is characterized as Helicase ATP-binding.
+At position 651 to 799, the domain is characterized as Helicase C-terminal.
+At position 13 to 66, the domain is characterized as Tudor-knot.
+At position 138 to 315, the domain is characterized as MRG.
+At position 36 to 214, the domain is characterized as Eph LBD.
+At position 333 to 443, the domain is characterized as Fibronectin type-III 1.
+At position 444 to 538, the domain is characterized as Fibronectin type-III 2.
+At position 651 to 912, the domain is characterized as Protein kinase.
+At position 941 to 1013, the domain is characterized as SAM.
+At position 3 to 104, the domain is characterized as HIT.
+At position 340 to 426, the domain is characterized as RRM.
+At position 557 to 913, the domain is characterized as PUM-HD.
+At position 93 to 210, the domain is characterized as PX.
+At position 289 to 573, the domain is characterized as Protein kinase.
+At position 937 to 1000, the domain is characterized as Tudor.
+At position 27 to 143, the domain is characterized as MTTase N-terminal.
+At position 166 to 402, the domain is characterized as Radical SAM core.
+At position 405 to 476, the domain is characterized as TRAM.
+At position 277 to 341, the domain is characterized as J.
+At position 363 to 510, the domain is characterized as ZP.
+At position 22 to 73, the domain is characterized as Myosin N-terminal SH3-like.
+At position 77 to 755, the domain is characterized as Myosin motor.
+At position 758 to 787, the domain is characterized as IQ.
+At position 703 to 778, the domain is characterized as Smr.
+At position 169 to 383, the domain is characterized as BURP.
+At position 194 to 295, the domain is characterized as Fe2OG dioxygenase.
+At position 2182 to 2311, the domain is characterized as MPN.
+At position 28 to 317, the domain is characterized as ABC transmembrane type-1.
+At position 349 to 583, the domain is characterized as ABC transporter.
+At position 161 to 355, the domain is characterized as CheB-type methylesterase.
+At position 176 to 246, the domain is characterized as KRAB.
+At position 267 to 450, the domain is characterized as ATP-grasp.
+At position 71 to 182, the domain is characterized as sHSP.
+At position 22 to 159, the domain is characterized as SprT-like.
+At position 231 to 355, the domain is characterized as GAF.
+At position 356 to 571, the domain is characterized as Histidine kinase.
+At position 246 to 434, the domain is characterized as TrmE-type G.
+At position 644 to 673, the domain is characterized as IQ.
+At position 7 to 187, the domain is characterized as Josephin.
+At position 243 to 262, the domain is characterized as UIM.
+At position 87 to 247, the domain is characterized as Bms1-type G.
+At position 572 to 872, the domain is characterized as FERM.
+At position 1093 to 1178, the domain is characterized as PDZ 1.
+At position 1368 to 1452, the domain is characterized as PDZ 2.
+At position 1501 to 1588, the domain is characterized as PDZ 3.
+At position 1788 to 1868, the domain is characterized as PDZ 4.
+At position 1882 to 1965, the domain is characterized as PDZ 5.
+At position 2213 to 2467, the domain is characterized as Tyrosine-protein phosphatase.
+At position 7 to 171, the domain is characterized as uDENN.
+At position 190 to 323, the domain is characterized as cDENN.
+At position 325 to 426, the domain is characterized as dDENN.
+At position 869 to 955, the domain is characterized as GRAM.
+At position 1105 to 1613, the domain is characterized as Myotubularin phosphatase.
+At position 1767 to 1871, the domain is characterized as PH.
+At position 36 to 123, the domain is characterized as YebF/Cmi.
+At position 62 to 184, the domain is characterized as TBDR plug.
+At position 189 to 687, the domain is characterized as TBDR beta-barrel.
+At position 48 to 164, the domain is characterized as Ig-like V-type.
+At position 166 to 261, the domain is characterized as Link 1.
+At position 266 to 358, the domain is characterized as Link 2.
+At position 46 to 433, the domain is characterized as Helicase ATP-binding.
+At position 450 to 616, the domain is characterized as Helicase C-terminal.
+At position 647 to 682, the domain is characterized as UVR.
+At position 139 to 265, the domain is characterized as Cyclin N-terminal.
+At position 220 to 347, the domain is characterized as OmpA-like.
+At position 181 to 227, the domain is characterized as F-box.
+At position 96 to 180, the domain is characterized as PDZ.
+At position 26 to 209, the domain is characterized as FAD-binding PCMH-type.
+At position 28 to 179, the domain is characterized as Tyrosine-protein phosphatase.
+At position 23 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 174, the domain is characterized as Ig-like C2-type 2.
+At position 68 to 284, the domain is characterized as Radical SAM core.
+At position 173 to 217, the domain is characterized as DSL.
+At position 218 to 251, the domain is characterized as EGF-like 1.
+At position 252 to 282, the domain is characterized as EGF-like 2.
+At position 284 to 322, the domain is characterized as EGF-like 3.
+At position 324 to 360, the domain is characterized as EGF-like 4.
+At position 362 to 400, the domain is characterized as EGF-like 5.
+At position 402 to 438, the domain is characterized as EGF-like 6.
+At position 440 to 476, the domain is characterized as EGF-like 7.
+At position 480 to 518, the domain is characterized as EGF-like 8.
+At position 570 to 842, the domain is characterized as Protein kinase.
+At position 17 to 211, the domain is characterized as GH11.
+At position 249 to 366, the domain is characterized as CBM6.
+At position 402 to 578, the domain is characterized as NodB homology.
+At position 148 to 383, the domain is characterized as Collagen-like.
+At position 389 to 483, the domain is characterized as SRCR.
+At position 59 to 310, the domain is characterized as Protein kinase.
+At position 324 to 368, the domain is characterized as UBA.
+At position 703 to 752, the domain is characterized as KA1.
+At position 118 to 156, the domain is characterized as LRRCT.
+At position 22 to 245, the domain is characterized as Phosphagen kinase C-terminal.
+At position 260 to 904, the domain is characterized as USP.
+At position 188 to 325, the domain is characterized as C-type lectin.
+At position 3 to 115, the domain is characterized as MTTase N-terminal.
+At position 9 to 91, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 14 to 276, the domain is characterized as Protein kinase.
+At position 18 to 87, the domain is characterized as J.
+At position 417 to 742, the domain is characterized as HECT.
+At position 138 to 259, the domain is characterized as C2.
+At position 320 to 578, the domain is characterized as Protein kinase.
+At position 579 to 649, the domain is characterized as AGC-kinase C-terminal.
+At position 2 to 175, the domain is characterized as Miro 1.
+At position 191 to 226, the domain is characterized as EF-hand 1.
+At position 311 to 346, the domain is characterized as EF-hand 2.
+At position 420 to 616, the domain is characterized as Miro 2.
+At position 64 to 194, the domain is characterized as PTB.
+At position 530 to 589, the domain is characterized as SH3.
+At position 1 to 104, the domain is characterized as BTB.
+At position 98 to 185, the domain is characterized as PDZ 1.
+At position 193 to 280, the domain is characterized as PDZ 2.
+At position 421 to 502, the domain is characterized as PDZ 3.
+At position 412 to 487, the domain is characterized as ACT 1.
+At position 493 to 570, the domain is characterized as ACT 2.
+At position 277 to 357, the domain is characterized as UBX.
+At position 702 to 794, the domain is characterized as FDX-ACB.
+At position 49 to 154, the domain is characterized as HD.
+At position 4 to 221, the domain is characterized as tr-type G.
+At position 100 to 126, the domain is characterized as Tudor-knot.
+At position 211 to 385, the domain is characterized as MRG.
+At position 5 to 164, the domain is characterized as UBC core.
+At position 19 to 149, the domain is characterized as VIT.
+At position 361 to 529, the domain is characterized as VWFA.
+At position 26 to 309, the domain is characterized as UmuC.
+At position 6 to 286, the domain is characterized as CN hydrolase.
+At position 43 to 88, the domain is characterized as Gla.
+At position 212 to 450, the domain is characterized as Peptidase S1.
+At position 137 to 241, the domain is characterized as HTH LytTR-type.
+At position 7 to 353, the domain is characterized as DhaK.
+At position 386 to 582, the domain is characterized as DhaL.
+At position 6 to 214, the domain is characterized as AIG1-type G.
+At position 78 to 209, the domain is characterized as HD.
+At position 718 to 811, the domain is characterized as BRCT 1.
+At position 890 to 1002, the domain is characterized as BRCT 2.
+At position 7 to 171, the domain is characterized as PPIase cyclophilin-type.
+At position 128 to 247, the domain is characterized as PX.
+At position 145 to 187, the domain is characterized as P-type.
+At position 192 to 470, the domain is characterized as ZP.
+At position 426 to 592, the domain is characterized as Helicase ATP-binding.
+At position 766 to 923, the domain is characterized as Helicase C-terminal.
+At position 113 to 205, the domain is characterized as ARID.
+At position 304 to 389, the domain is characterized as REKLES.
+At position 87 to 397, the domain is characterized as Peptidase A1.
+At position 44 to 146, the domain is characterized as Rhodanese.
+At position 101 to 296, the domain is characterized as ATP-grasp.
+At position 698 to 732, the domain is characterized as Anaphylatoxin-like.
+At position 1532 to 1676, the domain is characterized as NTR.
+At position 708 to 979, the domain is characterized as Protein kinase.
+At position 247 to 442, the domain is characterized as GATase cobBQ-type.
+At position 60 to 90, the domain is characterized as HhH 1.
+At position 91 to 120, the domain is characterized as HhH 2.
+At position 60 to 140, the domain is characterized as RRM 1.
+At position 154 to 233, the domain is characterized as RRM 2.
+At position 260 to 332, the domain is characterized as RRM 3.
+At position 102 to 233, the domain is characterized as GST C-terminal.
+At position 24 to 87, the domain is characterized as bZIP.
+At position 23 to 134, the domain is characterized as Ig-like V-type.
+At position 145 to 229, the domain is characterized as Ig-like C2-type.
+At position 49 to 116, the domain is characterized as KH 1.
+At position 171 to 237, the domain is characterized as KH 2.
+At position 421 to 488, the domain is characterized as KH 3.
+At position 392 to 489, the domain is characterized as Zinc-hook.
+At position 21 to 196, the domain is characterized as EngB-type G.
+At position 17 to 61, the domain is characterized as WAP; atypical.
+At position 62 to 120, the domain is characterized as Sushi 1.
+At position 122 to 190, the domain is characterized as Sushi 2.
+At position 191 to 248, the domain is characterized as Sushi 3.
+At position 249 to 306, the domain is characterized as Sushi 4.
+At position 307 to 364, the domain is characterized as Sushi 5.
+At position 365 to 422, the domain is characterized as Sushi 6.
+At position 423 to 483, the domain is characterized as Sushi 7.
+At position 484 to 558, the domain is characterized as Sushi 8.
+At position 231 to 274, the domain is characterized as CUE.
+At position 21 to 134, the domain is characterized as I-type lysozyme.
+At position 17 to 173, the domain is characterized as NHR.
+At position 29 to 208, the domain is characterized as Radical SAM core.
+At position 491 to 690, the domain is characterized as MAGE 1.
+At position 745 to 936, the domain is characterized as MAGE 2.
+At position 65 to 279, the domain is characterized as ABC transmembrane type-1.
+At position 162 to 424, the domain is characterized as FAD-binding FR-type.
+At position 16 to 263, the domain is characterized as Protein kinase.
+At position 30 to 143, the domain is characterized as sHSP.
+At position 389 to 523, the domain is characterized as YTH.
+At position 72 to 132, the domain is characterized as Tudor.
+At position 228 to 322, the domain is characterized as Spaetzle.
+At position 570 to 843, the domain is characterized as Protein kinase.
+At position 123 to 158, the domain is characterized as EF-hand 4.
+At position 191 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 27 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 129 to 258, the domain is characterized as MTTase N-terminal.
+At position 282 to 535, the domain is characterized as Radical SAM core.
+At position 538 to 618, the domain is characterized as TRAM.
+At position 661 to 737, the domain is characterized as Ubiquitin-like.
+At position 1816 to 1886, the domain is characterized as Bromo.
+At position 71 to 379, the domain is characterized as Peptidase A1.
+At position 24 to 198, the domain is characterized as EngB-type G.
+At position 13 to 140, the domain is characterized as CMP/dCMP-type deaminase.
+At position 93 to 308, the domain is characterized as RNase H type-2.
+At position 15 to 306, the domain is characterized as CNH.
+At position 5 to 294, the domain is characterized as RHD.
+At position 159 to 205, the domain is characterized as F-box.
+At position 570 to 662, the domain is characterized as tRNA-binding.
+At position 186 to 354, the domain is characterized as PCI.
+At position 1176 to 1246, the domain is characterized as Bromo 1.
+At position 1333 to 1403, the domain is characterized as Bromo 2.
+At position 41 to 198, the domain is characterized as PPIase cyclophilin-type.
+At position 293 to 442, the domain is characterized as SIS 1.
+At position 476 to 617, the domain is characterized as SIS 2.
+At position 217 to 370, the domain is characterized as GAF 1.
+At position 402 to 558, the domain is characterized as GAF 2.
+At position 588 to 912, the domain is characterized as PDEase.
+At position 1 to 288, the domain is characterized as 5'-3' exonuclease.
+At position 488 to 580, the domain is characterized as Fibronectin type-III.
+At position 9 to 327, the domain is characterized as Kinesin motor.
+At position 796 to 880, the domain is characterized as PB1.
+At position 816 to 899, the domain is characterized as ACT 2.
+At position 347 to 398, the domain is characterized as FBD.
+At position 31 to 66, the domain is characterized as EF-hand.
+At position 130 to 332, the domain is characterized as GST C-terminal.
+At position 9 to 229, the domain is characterized as ABC transporter.
+At position 23 to 282, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 144, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 144 to 474, the domain is characterized as SAC.
+At position 2 to 252, the domain is characterized as Pyruvate carboxyltransferase.
+At position 30 to 76, the domain is characterized as PSI.
+At position 135 to 377, the domain is characterized as VWFA.
+At position 436 to 498, the domain is characterized as EGF-like 1.
+At position 499 to 548, the domain is characterized as EGF-like 2.
+At position 549 to 585, the domain is characterized as EGF-like 3.
+At position 586 to 629, the domain is characterized as EGF-like 4.
+At position 346 to 450, the domain is characterized as Fibronectin type-III.
+At position 30 to 125, the domain is characterized as EthD.
+At position 531 to 603, the domain is characterized as ACT.
+At position 290 to 478, the domain is characterized as Helicase ATP-binding.
+At position 519 to 720, the domain is characterized as Helicase C-terminal.
+At position 777 to 1092, the domain is characterized as SEC63.
+At position 72 to 312, the domain is characterized as ABC transporter.
+At position 2 to 152, the domain is characterized as N-acetyltransferase.
+At position 113 to 320, the domain is characterized as ATP-grasp.
+At position 15 to 84, the domain is characterized as TGS.
+At position 29 to 75, the domain is characterized as KH.
+At position 42 to 203, the domain is characterized as Thioredoxin.
+At position 75 to 416, the domain is characterized as Peptidase A1.
+At position 24 to 220, the domain is characterized as VWFA 1.
+At position 221 to 261, the domain is characterized as EGF-like.
+At position 262 to 450, the domain is characterized as VWFA 2.
+At position 101 to 349, the domain is characterized as Radical SAM core.
+At position 352 to 471, the domain is characterized as BRCT.
+At position 542 to 646, the domain is characterized as PTS EIIA type-1.
+At position 223 to 341, the domain is characterized as BAH.
+At position 28 to 115, the domain is characterized as Fibronectin type-III 1.
+At position 116 to 202, the domain is characterized as Fibronectin type-III 2.
+At position 289 to 373, the domain is characterized as Fibronectin type-III 4.
+At position 374 to 459, the domain is characterized as Fibronectin type-III 5.
+At position 460 to 544, the domain is characterized as Fibronectin type-III 6.
+At position 545 to 632, the domain is characterized as Fibronectin type-III 7.
+At position 631 to 715, the domain is characterized as Fibronectin type-III 8.
+At position 4 to 67, the domain is characterized as SAM.
+At position 394 to 658, the domain is characterized as Protein kinase.
+At position 58 to 358, the domain is characterized as PPM-type phosphatase.
+At position 323 to 416, the domain is characterized as BRCT.
+At position 202 to 235, the domain is characterized as ShKT.
+At position 4 to 63, the domain is characterized as LIM zinc-binding 1.
+At position 64 to 122, the domain is characterized as LIM zinc-binding 2.
+At position 386 to 643, the domain is characterized as Protein kinase.
+At position 91 to 345, the domain is characterized as Protein kinase.
+At position 175 to 240, the domain is characterized as SEP.
+At position 286 to 363, the domain is characterized as UBX.
+At position 137 to 259, the domain is characterized as MPN.
+At position 9 to 128, the domain is characterized as Response regulatory.
+At position 60 to 269, the domain is characterized as MARVEL.
+At position 414 to 522, the domain is characterized as OCEL.
+At position 237 to 327, the domain is characterized as Fibronectin type-III.
+At position 3 to 413, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 36 to 227, the domain is characterized as VWFA.
+At position 147 to 377, the domain is characterized as NR LBD.
+At position 126 to 214, the domain is characterized as Ig-like C1-type.
+At position 4 to 147, the domain is characterized as Flavodoxin-like.
+At position 272 to 534, the domain is characterized as FAD-binding FR-type.
+At position 34 to 131, the domain is characterized as SRCR 1.
+At position 157 to 266, the domain is characterized as SRCR 2.
+At position 274 to 364, the domain is characterized as SRCR 3.
+At position 1 to 56, the domain is characterized as IBB.
+At position 66 to 279, the domain is characterized as START.
+At position 5 to 216, the domain is characterized as AIG1-type G.
+At position 75 to 127, the domain is characterized as bHLH.
+At position 18 to 247, the domain is characterized as BAR.
+At position 320 to 379, the domain is characterized as SH3.
+At position 102 to 340, the domain is characterized as Radical SAM core.
+At position 300 to 378, the domain is characterized as PDZ 1.
+At position 779 to 854, the domain is characterized as PDZ 2.
+At position 88 to 151, the domain is characterized as S4 RNA-binding.
+At position 34 to 130, the domain is characterized as Glutaredoxin.
+At position 2 to 227, the domain is characterized as Glutamine amidotransferase type-1.
+At position 167 to 225, the domain is characterized as MADS-box.
+At position 11 to 200, the domain is characterized as RNase H type-2.
+At position 91 to 276, the domain is characterized as TR mART core.
+At position 1011 to 1081, the domain is characterized as HTH CENPB-type.
+At position 1113 to 1319, the domain is characterized as DDE-1.
+At position 688 to 754, the domain is characterized as SAM 1.
+At position 803 to 867, the domain is characterized as SAM 2.
+At position 891 to 960, the domain is characterized as SAM 3.
+At position 311 to 486, the domain is characterized as tr-type G.
+At position 202 to 274, the domain is characterized as S1 motif.
+At position 518 to 681, the domain is characterized as Helicase ATP-binding.
+At position 699 to 879, the domain is characterized as Helicase C-terminal.
+At position 429 to 554, the domain is characterized as DBINO.
+At position 667 to 839, the domain is characterized as Helicase ATP-binding.
+At position 1244 to 1398, the domain is characterized as Helicase C-terminal.
+At position 624 to 797, the domain is characterized as PCI.
+At position 33 to 71, the domain is characterized as LRRNT.
+At position 18 to 120, the domain is characterized as Ig-like V-type.
+At position 184 to 219, the domain is characterized as UVR.
+At position 14 to 67, the domain is characterized as HTH cro/C1-type.
+At position 1050 to 1303, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1765 to 1904, the domain is characterized as SET.
+At position 1914 to 1930, the domain is characterized as Post-SET.
+At position 216 to 337, the domain is characterized as SET.
+At position 231 to 293, the domain is characterized as t-SNARE coiled-coil homology.
+At position 23 to 253, the domain is characterized as ABC transporter.
+At position 14 to 81, the domain is characterized as PAS.
+At position 147 to 366, the domain is characterized as Histidine kinase.
+At position 36 to 150, the domain is characterized as sHSP.
+At position 458 to 689, the domain is characterized as NR LBD.
+At position 22 to 85, the domain is characterized as LCN-type CS-alpha/beta.
+At position 748 to 804, the domain is characterized as WHEP-TRS 1.
+At position 821 to 877, the domain is characterized as WHEP-TRS 2.
+At position 899 to 955, the domain is characterized as WHEP-TRS 3.
+At position 6 to 207, the domain is characterized as Lon N-terminal.
+At position 592 to 773, the domain is characterized as Lon proteolytic.
+At position 481 to 500, the domain is characterized as UIM 1.
+At position 517 to 536, the domain is characterized as UIM 2.
+At position 547 to 566, the domain is characterized as UIM 3.
+At position 572 to 588, the domain is characterized as UIM 4.
+At position 19 to 164, the domain is characterized as SprT-like.
+At position 3 to 142, the domain is characterized as Toprim.
+At position 39 to 104, the domain is characterized as BTB.
+At position 206 to 494, the domain is characterized as NPH3.
+At position 164 to 339, the domain is characterized as DAGKc.
+At position 158 to 232, the domain is characterized as HTH crp-type.
+At position 23 to 153, the domain is characterized as EamA 1.
+At position 216 to 333, the domain is characterized as EamA 2.
+At position 2 to 187, the domain is characterized as Glutamine amidotransferase type-2.
+At position 291 to 607, the domain is characterized as Asparagine synthetase.
+At position 680 to 709, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 736 to 765, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 25 to 159, the domain is characterized as HTH marR-type.
+At position 1 to 130, the domain is characterized as HTH rrf2-type.
+At position 31 to 254, the domain is characterized as Peptidase S1.
+At position 1 to 20, the domain is characterized as TCTP.
+At position 106 to 169, the domain is characterized as bZIP.
+At position 13 to 127, the domain is characterized as Response regulatory.
+At position 78 to 122, the domain is characterized as EGF-like.
+At position 381 to 444, the domain is characterized as bZIP.
+At position 220 to 373, the domain is characterized as TrmE-type G.
+At position 21 to 117, the domain is characterized as SH2.
+At position 1195 to 1257, the domain is characterized as SAM.
+At position 2 to 102, the domain is characterized as Thioredoxin.
+At position 105 to 282, the domain is characterized as Helicase ATP-binding.
+At position 316 to 466, the domain is characterized as Helicase C-terminal.
+At position 18 to 179, the domain is characterized as Exonuclease.
+At position 1 to 50, the domain is characterized as Kazal-like 1.
+At position 51 to 103, the domain is characterized as Kazal-like 2.
+At position 22 to 302, the domain is characterized as Dynamin-type G.
+At position 644 to 735, the domain is characterized as GED.
+At position 37 to 478, the domain is characterized as uDENN FNIP1/2-type.
+At position 486 to 1091, the domain is characterized as cDENN FNIP1/2-type.
+At position 1101 to 1156, the domain is characterized as dDENN FNIP1/2-type.
+At position 373 to 443, the domain is characterized as TRAM.
+At position 154 to 229, the domain is characterized as RRM 1.
+At position 283 to 359, the domain is characterized as RRM 2.
+At position 401 to 478, the domain is characterized as RRM 3.
+At position 760 to 836, the domain is characterized as RRM 4.
+At position 343 to 365, the domain is characterized as WH2.
+At position 12 to 192, the domain is characterized as UmuC.
+At position 3 to 211, the domain is characterized as AIG1-type G.
+At position 176 to 520, the domain is characterized as USP.
+At position 123 to 410, the domain is characterized as ABC transmembrane type-1.
+At position 453 to 659, the domain is characterized as ABC transporter.
+At position 712 to 979, the domain is characterized as Protein kinase.
+At position 8 to 58, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 62 to 117, the domain is characterized as bHLH.
+At position 128 to 159, the domain is characterized as Orange.
+At position 13 to 193, the domain is characterized as Guanylate kinase-like.
+At position 5 to 42, the domain is characterized as UBA-like.
+At position 49 to 242, the domain is characterized as DCUN1.
+At position 15 to 256, the domain is characterized as ABC transporter.
+At position 3 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 6 to 56, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 68 to 259, the domain is characterized as BURP.
+At position 122 to 685, the domain is characterized as Lipoxygenase.
+At position 6 to 154, the domain is characterized as MGS-like.
+At position 5 to 140, the domain is characterized as SprT-like.
+At position 100 to 330, the domain is characterized as Radical SAM core.
+At position 601 to 707, the domain is characterized as tRNA-binding.
+At position 30 to 147, the domain is characterized as EamA.
+At position 1 to 116, the domain is characterized as CMP/dCMP-type deaminase.
+At position 340 to 394, the domain is characterized as MIR 1.
+At position 409 to 467, the domain is characterized as MIR 2.
+At position 482 to 540, the domain is characterized as MIR 3.
+At position 13 to 85, the domain is characterized as RRM 1.
+At position 39 to 83, the domain is characterized as Fibronectin type-II 1.
+At position 84 to 130, the domain is characterized as Fibronectin type-II 2.
+At position 267 to 344, the domain is characterized as ACT 1.
+At position 345 to 405, the domain is characterized as ACT 2.
+At position 77 to 112, the domain is characterized as EF-hand 3.
+At position 26 to 132, the domain is characterized as CBM21.
+At position 179 to 354, the domain is characterized as Macro.
+At position 1 to 25, the domain is characterized as C-type lectin.
+At position 206 to 492, the domain is characterized as GT23.
+At position 501 to 562, the domain is characterized as SH3.
+At position 134 to 613, the domain is characterized as Peptidase S8.
+At position 35 to 95, the domain is characterized as v-SNARE coiled-coil homology.
+At position 135 to 408, the domain is characterized as ABC transporter 1.
+At position 486 to 699, the domain is characterized as ABC transmembrane type-2 1.
+At position 818 to 1070, the domain is characterized as ABC transporter 2.
+At position 1143 to 1357, the domain is characterized as ABC transmembrane type-2 2.
+At position 78 to 178, the domain is characterized as AB hydrolase-1.
+At position 44 to 170, the domain is characterized as SCP.
+At position 210 to 241, the domain is characterized as ShKT.
+At position 402 to 640, the domain is characterized as PH.
+At position 661 to 781, the domain is characterized as Arf-GAP.
+At position 8 to 98, the domain is characterized as EH 1.
+At position 40 to 75, the domain is characterized as EF-hand.
+At position 135 to 224, the domain is characterized as EH 2.
+At position 7 to 71, the domain is characterized as J.
+At position 271 to 410, the domain is characterized as Cupin type-1 1.
+At position 455 to 625, the domain is characterized as Cupin type-1 2.
+At position 37 to 190, the domain is characterized as Ricin B-type lectin.
+At position 181 to 229, the domain is characterized as Fibronectin type-II.
+At position 243 to 359, the domain is characterized as C-type lectin 1.
+At position 388 to 504, the domain is characterized as C-type lectin 2.
+At position 527 to 643, the domain is characterized as C-type lectin 3.
+At position 677 to 808, the domain is characterized as C-type lectin 4.
+At position 831 to 950, the domain is characterized as C-type lectin 5.
+At position 978 to 1106, the domain is characterized as C-type lectin 6.
+At position 1131 to 1242, the domain is characterized as C-type lectin 7.
+At position 1271 to 1391, the domain is characterized as C-type lectin 8.
+At position 72 to 177, the domain is characterized as FAD-binding FR-type.
+At position 15 to 161, the domain is characterized as MGS-like.
+At position 435 to 513, the domain is characterized as RRM 3.
+At position 2 to 189, the domain is characterized as UmuC.
+At position 34 to 179, the domain is characterized as FAS1.
+At position 14 to 139, the domain is characterized as Response regulatory.
+At position 584 to 644, the domain is characterized as KH.
+At position 665 to 732, the domain is characterized as S1 motif.
+At position 42 to 269, the domain is characterized as Radical SAM core.
+At position 74 to 226, the domain is characterized as Cupin type-1 1.
+At position 268 to 435, the domain is characterized as Cupin type-1 2.
+At position 289 to 374, the domain is characterized as PDZ 1.
+At position 877 to 958, the domain is characterized as PDZ 2.
+At position 127 to 323, the domain is characterized as B30.2/SPRY.
+At position 724 to 962, the domain is characterized as NR LBD.
+At position 1 to 66, the domain is characterized as MENTAL.
+At position 79 to 292, the domain is characterized as START.
+At position 65 to 235, the domain is characterized as FAD-binding PCMH-type.
+At position 122 to 313, the domain is characterized as ATP-grasp.
+At position 396 to 537, the domain is characterized as MGS-like.
+At position 363 to 426, the domain is characterized as bZIP.
+At position 1256 to 1353, the domain is characterized as SH2.
+At position 7 to 147, the domain is characterized as SprT-like.
+At position 405 to 574, the domain is characterized as tr-type G.
+At position 82 to 99, the domain is characterized as EF-hand 2.
+At position 142 to 173, the domain is characterized as EF-hand 4.
+At position 147 to 231, the domain is characterized as Ig-like C2-type.
+At position 59 to 329, the domain is characterized as Protein kinase.
+At position 237 to 312, the domain is characterized as Lipoyl-binding 3.
+At position 372 to 409, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 11 to 82, the domain is characterized as J.
+At position 93 to 148, the domain is characterized as DPH-type MB.
+At position 4 to 97, the domain is characterized as KRAB.
+At position 348 to 526, the domain is characterized as Helicase ATP-binding.
+At position 564 to 713, the domain is characterized as Helicase C-terminal.
+At position 414 to 551, the domain is characterized as YTH.
+At position 291 to 541, the domain is characterized as Histidine kinase.
+At position 543 to 671, the domain is characterized as CheW-like.
+At position 167 to 219, the domain is characterized as HAMP.
+At position 234 to 432, the domain is characterized as Histidine kinase.
+At position 38 to 52, the domain is characterized as CRIB.
+At position 366 to 433, the domain is characterized as TRAM.
+At position 203 to 399, the domain is characterized as ATP-grasp 1.
+At position 761 to 954, the domain is characterized as ATP-grasp 2.
+At position 1021 to 1162, the domain is characterized as MGS-like.
+At position 89 to 141, the domain is characterized as HAMP.
+At position 149 to 356, the domain is characterized as Histidine kinase.
+At position 5 to 111, the domain is characterized as SSB.
+At position 27 to 74, the domain is characterized as WAP 1.
+At position 75 to 121, the domain is characterized as WAP 2.
+At position 730 to 1057, the domain is characterized as HECT.
+At position 32 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 38 to 50, the domain is characterized as EF-hand.
+At position 71 to 258, the domain is characterized as RNase H type-2.
+At position 162 to 337, the domain is characterized as Helicase ATP-binding.
+At position 351 to 521, the domain is characterized as Helicase C-terminal.
+At position 22 to 164, the domain is characterized as SIS.
+At position 81 to 137, the domain is characterized as EF-hand 1; degenerate.
+At position 176 to 211, the domain is characterized as EF-hand 3.
+At position 224 to 259, the domain is characterized as EF-hand 4.
+At position 167 to 194, the domain is characterized as IQ 1.
+At position 195 to 217, the domain is characterized as IQ 2.
+At position 23 to 143, the domain is characterized as MTTase N-terminal.
+At position 170 to 402, the domain is characterized as Radical SAM core.
+At position 405 to 467, the domain is characterized as TRAM.
+At position 29 to 301, the domain is characterized as CN hydrolase.
+At position 11 to 68, the domain is characterized as PWWP.
+At position 17 to 236, the domain is characterized as Glutamine amidotransferase type-1.
+At position 14 to 170, the domain is characterized as NAC.
+At position 50 to 202, the domain is characterized as NAC.
+At position 619 to 698, the domain is characterized as BTB 1.
+At position 758 to 829, the domain is characterized as BTB 2.
+At position 20 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 116 to 205, the domain is characterized as Ig-like C2-type 2.
+At position 212 to 301, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 403, the domain is characterized as Ig-like C2-type 4.
+At position 499 to 598, the domain is characterized as Fibronectin type-III 1.
+At position 600 to 696, the domain is characterized as Fibronectin type-III 2.
+At position 158 to 345, the domain is characterized as B30.2/SPRY.
+At position 14 to 112, the domain is characterized as Rieske.
+At position 40 to 161, the domain is characterized as FZ.
+At position 80 to 247, the domain is characterized as Phosphatase tensin-type.
+At position 253 to 391, the domain is characterized as C2 tensin-type.
+At position 874 to 938, the domain is characterized as J.
+At position 8 to 93, the domain is characterized as IPT/TIG.
+At position 406 to 484, the domain is characterized as RRM.
+At position 30 to 347, the domain is characterized as G-alpha.
+At position 14 to 92, the domain is characterized as GIY-YIG.
+At position 528 to 595, the domain is characterized as KH.
+At position 689 to 747, the domain is characterized as Tudor.
+At position 6 to 61, the domain is characterized as HTH cro/C1-type.
+At position 65 to 103, the domain is characterized as Sin.
+At position 405 to 488, the domain is characterized as RRM 2.
+At position 2 to 147, the domain is characterized as Jacalin-type lectin 1.
+At position 150 to 294, the domain is characterized as Jacalin-type lectin 2.
+At position 297 to 444, the domain is characterized as Jacalin-type lectin 3.
+At position 451 to 597, the domain is characterized as Jacalin-type lectin 4.
+At position 27 to 140, the domain is characterized as Ig-like V-type.
+At position 141 to 234, the domain is characterized as Ig-like C1-type.
+At position 233 to 435, the domain is characterized as Peptidase M12B.
+At position 464 to 546, the domain is characterized as Disintegrin.
+At position 708 to 759, the domain is characterized as TSP type-1 1.
+At position 761 to 802, the domain is characterized as TSP type-1 2.
+At position 804 to 852, the domain is characterized as TSP type-1 3.
+At position 853 to 898, the domain is characterized as TSP type-1 4.
+At position 903 to 952, the domain is characterized as TSP type-1 5.
+At position 955 to 1000, the domain is characterized as TSP type-1 6.
+At position 1035 to 1083, the domain is characterized as TSP type-1 7.
+At position 1087 to 1133, the domain is characterized as TSP type-1 8.
+At position 1148 to 1200, the domain is characterized as TSP type-1 9.
+At position 1203 to 1260, the domain is characterized as TSP type-1 10.
+At position 1265 to 1321, the domain is characterized as TSP type-1 11.
+At position 1324 to 1378, the domain is characterized as TSP type-1 12.
+At position 1382 to 1435, the domain is characterized as TSP type-1 13.
+At position 139 to 371, the domain is characterized as Radical SAM core.
+At position 369 to 436, the domain is characterized as TRAM.
+At position 36 to 276, the domain is characterized as ABC transporter.
+At position 700 to 874, the domain is characterized as DH.
+At position 100 to 295, the domain is characterized as ATP-grasp.
+At position 116 to 153, the domain is characterized as LRRNT.
+At position 19 to 293, the domain is characterized as Peptidase S8.
+At position 379 to 649, the domain is characterized as Clu.
+At position 76 to 386, the domain is characterized as Peptidase A1.
+At position 21 to 63, the domain is characterized as CUE.
+At position 51 to 157, the domain is characterized as Expansin-like EG45.
+At position 170 to 256, the domain is characterized as Expansin-like CBD.
+At position 690 to 880, the domain is characterized as SEC7.
+At position 590 to 658, the domain is characterized as SH3 1.
+At position 669 to 763, the domain is characterized as SH2.
+At position 780 to 840, the domain is characterized as SH3 2.
+At position 26 to 80, the domain is characterized as HTH cro/C1-type.
+At position 1 to 116, the domain is characterized as PTS EIIA type-5.
+At position 2 to 69, the domain is characterized as S4 RNA-binding.
+At position 10 to 245, the domain is characterized as ABC transporter 1.
+At position 255 to 498, the domain is characterized as ABC transporter 2.
+At position 160 to 388, the domain is characterized as START.
+At position 420 to 626, the domain is characterized as MCM.
+At position 51 to 351, the domain is characterized as ABC transmembrane type-1 1.
+At position 387 to 623, the domain is characterized as ABC transporter 1.
+At position 694 to 981, the domain is characterized as ABC transmembrane type-1 2.
+At position 1016 to 1254, the domain is characterized as ABC transporter 2.
+At position 17 to 101, the domain is characterized as PDZ 1.
+At position 109 to 283, the domain is characterized as Guanylate kinase-like.
+At position 301 to 334, the domain is characterized as WW 1.
+At position 347 to 380, the domain is characterized as WW 2.
+At position 425 to 509, the domain is characterized as PDZ 2.
+At position 604 to 682, the domain is characterized as PDZ 3.
+At position 777 to 859, the domain is characterized as PDZ 4.
+At position 919 to 1009, the domain is characterized as PDZ 5.
+At position 1139 to 1221, the domain is characterized as PDZ 6.
+At position 24 to 294, the domain is characterized as tr-type G.
+At position 9 to 286, the domain is characterized as YjeF C-terminal.
+At position 229 to 556, the domain is characterized as FERM.
+At position 357 to 453, the domain is characterized as PH.
+At position 1756 to 1986, the domain is characterized as Alpha-type protein kinase.
+At position 29 to 92, the domain is characterized as S5 DRBM.
+At position 139 to 216, the domain is characterized as RRM 2.
+At position 232 to 309, the domain is characterized as RRM 3.
+At position 335 to 465, the domain is characterized as RRM 4.
+At position 649 to 726, the domain is characterized as PABC.
+At position 482 to 755, the domain is characterized as Protein kinase.
+At position 38 to 96, the domain is characterized as VWFC.
+At position 1228 to 1463, the domain is characterized as Fibrillar collagen NC1.
+At position 189 to 258, the domain is characterized as HMA.
+At position 282 to 570, the domain is characterized as NB-ARC.
+At position 916 to 1200, the domain is characterized as ABC transmembrane type-1 2.
+At position 1237 to 1471, the domain is characterized as ABC transporter 2.
+At position 111 to 199, the domain is characterized as Disintegrin.
+At position 351 to 385, the domain is characterized as EGF-like.
+At position 71 to 146, the domain is characterized as MBD.
+At position 3 to 68, the domain is characterized as CSD.
+At position 18 to 78, the domain is characterized as CBS.
+At position 25 to 466, the domain is characterized as GH18 1.
+At position 485 to 536, the domain is characterized as CNA-B.
+At position 1142 to 1483, the domain is characterized as GH18 2.
+At position 407 to 495, the domain is characterized as B5.
+At position 716 to 809, the domain is characterized as FDX-ACB.
+At position 335 to 374, the domain is characterized as CBM1.
+At position 33 to 150, the domain is characterized as MTTase N-terminal.
+At position 173 to 407, the domain is characterized as Radical SAM core.
+At position 408 to 471, the domain is characterized as TRAM.
+At position 14 to 155, the domain is characterized as MPN.
+At position 30 to 207, the domain is characterized as Helicase ATP-binding.
+At position 236 to 408, the domain is characterized as Helicase C-terminal.
+At position 320 to 426, the domain is characterized as HTH APSES-type.
+At position 113 to 193, the domain is characterized as RRM.
+At position 375 to 529, the domain is characterized as NTF2.
+At position 618 to 672, the domain is characterized as TAP-C.
+At position 29 to 206, the domain is characterized as Laminin G-like 1.
+At position 202 to 242, the domain is characterized as EGF-like 1.
+At position 289 to 486, the domain is characterized as Laminin G-like 2.
+At position 493 to 686, the domain is characterized as Laminin G-like 3.
+At position 690 to 727, the domain is characterized as EGF-like 2.
+At position 732 to 904, the domain is characterized as Laminin G-like 4.
+At position 918 to 1093, the domain is characterized as Laminin G-like 5.
+At position 1096 to 1133, the domain is characterized as EGF-like 3.
+At position 1137 to 1345, the domain is characterized as Laminin G-like 6.
+At position 348 to 445, the domain is characterized as BEN.
+At position 38 to 106, the domain is characterized as R3H.
+At position 203 to 369, the domain is characterized as Helicase ATP-binding.
+At position 612 to 784, the domain is characterized as Helicase C-terminal.
+At position 1288 to 1418, the domain is characterized as YTH.
+At position 6 to 41, the domain is characterized as QLQ.
+At position 80 to 124, the domain is characterized as WRC.
+At position 2 to 99, the domain is characterized as PH.
+At position 37 to 149, the domain is characterized as CUB 1.
+At position 159 to 273, the domain is characterized as CUB 2.
+At position 318 to 437, the domain is characterized as NTR.
+At position 80 to 646, the domain is characterized as Protein kinase.
+At position 209 to 290, the domain is characterized as BCNT-C.
+At position 42 to 226, the domain is characterized as BPL/LPL catalytic.
+At position 591 to 668, the domain is characterized as BRCT.
+At position 58 to 164, the domain is characterized as FAD-binding FR-type.
+At position 299 to 380, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 5 to 89, the domain is characterized as YcgL.
+At position 736 to 767, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 2 to 127, the domain is characterized as Plastocyanin-like 1.
+At position 139 to 281, the domain is characterized as Plastocyanin-like 2.
+At position 348 to 470, the domain is characterized as Plastocyanin-like 3.
+At position 34 to 211, the domain is characterized as FAD-binding PCMH-type.
+At position 108 to 215, the domain is characterized as Cadherin 1.
+At position 216 to 328, the domain is characterized as Cadherin 2.
+At position 329 to 440, the domain is characterized as Cadherin 3.
+At position 441 to 546, the domain is characterized as Cadherin 4.
+At position 547 to 650, the domain is characterized as Cadherin 5.
+At position 229 to 466, the domain is characterized as START.
+At position 390 to 641, the domain is characterized as SF4 helicase.
+At position 12 to 282, the domain is characterized as Protein kinase.
+At position 337 to 350, the domain is characterized as CRIB.
+At position 620 to 871, the domain is characterized as Protein kinase.
+At position 45 to 316, the domain is characterized as Septin-type G.
+At position 172 to 363, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 126, the domain is characterized as VOC.
+At position 40 to 215, the domain is characterized as Helicase ATP-binding.
+At position 239 to 386, the domain is characterized as Helicase C-terminal.
+At position 19 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 930 to 1059, the domain is characterized as MGS-like.
+At position 48 to 302, the domain is characterized as Protein kinase.
+At position 109 to 173, the domain is characterized as CBS 1.
+At position 203 to 262, the domain is characterized as CBS 2.
+At position 277 to 334, the domain is characterized as CBS 3.
+At position 146 to 209, the domain is characterized as S4 RNA-binding.
+At position 283 to 393, the domain is characterized as OCEL.
+At position 8 to 115, the domain is characterized as HTH APSES-type.
+At position 543 to 604, the domain is characterized as SH3.
+At position 27 to 79, the domain is characterized as HTH myb-type 1.
+At position 80 to 134, the domain is characterized as HTH myb-type 2.
+At position 311 to 340, the domain is characterized as IQ.
+At position 646 to 839, the domain is characterized as SEC7.
+At position 852 to 985, the domain is characterized as PH.
+At position 90 to 150, the domain is characterized as K-box; partial.
+At position 109 to 325, the domain is characterized as ABC transmembrane type-1.
+At position 27 to 135, the domain is characterized as Gnk2-homologous 1.
+At position 381 to 498, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 499 to 602, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 660 to 739, the domain is characterized as POLO box.
+At position 60 to 240, the domain is characterized as tr-type G.
+At position 61 to 134, the domain is characterized as RRM 1.
+At position 140 to 225, the domain is characterized as RRM 2.
+At position 426 to 679, the domain is characterized as Protein kinase.
+At position 64 to 223, the domain is characterized as Cupin type-1 1.
+At position 278 to 448, the domain is characterized as Cupin type-1 2.
+At position 62 to 150, the domain is characterized as PPIase FKBP-type 1.
+At position 174 to 262, the domain is characterized as PPIase FKBP-type 2.
+At position 286 to 374, the domain is characterized as PPIase FKBP-type 3.
+At position 399 to 486, the domain is characterized as PPIase FKBP-type 4.
+At position 497 to 532, the domain is characterized as EF-hand 1.
+At position 542 to 577, the domain is characterized as EF-hand 2.
+At position 32 to 97, the domain is characterized as BTB.
+At position 1 to 236, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 242 to 470, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 4 to 107, the domain is characterized as SSB.
+At position 9 to 86, the domain is characterized as BAG 1.
+At position 95 to 167, the domain is characterized as BAG 2.
+At position 182 to 260, the domain is characterized as BAG 3.
+At position 275 to 350, the domain is characterized as BAG 4.
+At position 365 to 442, the domain is characterized as BAG 5.
+At position 36 to 63, the domain is characterized as EF-hand 1.
+At position 67 to 94, the domain is characterized as EF-hand 2.
+At position 4 to 164, the domain is characterized as UBC core.
+At position 193 to 372, the domain is characterized as DH.
+At position 401 to 503, the domain is characterized as PH.
+At position 591 to 659, the domain is characterized as SH3 1.
+At position 670 to 764, the domain is characterized as SH2.
+At position 781 to 841, the domain is characterized as SH3 2.
+At position 228 to 605, the domain is characterized as Peptidase A1.
+At position 60 to 347, the domain is characterized as tr-type G.
+At position 31 to 165, the domain is characterized as FAS1 1.
+At position 249 to 392, the domain is characterized as FAS1 2.
+At position 1 to 156, the domain is characterized as PPIase cyclophilin-type.
+At position 323 to 391, the domain is characterized as SAM.
+At position 47 to 276, the domain is characterized as Radical SAM core.
+At position 22 to 54, the domain is characterized as LRRNT.
+At position 197 to 249, the domain is characterized as LRRCT.
+At position 250 to 342, the domain is characterized as Ig-like.
+At position 364 to 449, the domain is characterized as Fibronectin type-III.
+At position 124 to 370, the domain is characterized as Lon N-terminal.
+At position 759 to 949, the domain is characterized as Lon proteolytic.
+At position 55 to 183, the domain is characterized as VHS.
+At position 228 to 315, the domain is characterized as GAT.
+At position 4 to 216, the domain is characterized as Glutamine amidotransferase type-1.
+At position 249 to 342, the domain is characterized as TonB C-terminal.
+At position 108 to 293, the domain is characterized as ATP-grasp.
+At position 15 to 302, the domain is characterized as Protein kinase.
+At position 1060 to 1123, the domain is characterized as Pre-SET.
+At position 1126 to 1243, the domain is characterized as SET.
+At position 273 to 309, the domain is characterized as LRRNT 2.
+At position 439 to 489, the domain is characterized as LRRCT 2.
+At position 504 to 540, the domain is characterized as LRRNT 3.
+At position 671 to 721, the domain is characterized as LRRCT 3.
+At position 725 to 761, the domain is characterized as LRRNT 4.
+At position 866 to 916, the domain is characterized as LRRCT 4.
+At position 927 to 962, the domain is characterized as EGF-like 1.
+At position 964 to 1003, the domain is characterized as EGF-like 2.
+At position 1005 to 1041, the domain is characterized as EGF-like 3.
+At position 1043 to 1081, the domain is characterized as EGF-like 4.
+At position 1083 to 1119, the domain is characterized as EGF-like 5.
+At position 1127 to 1163, the domain is characterized as EGF-like 6.
+At position 1166 to 1339, the domain is characterized as Laminin G-like.
+At position 1340 to 1374, the domain is characterized as EGF-like 7.
+At position 1377 to 1413, the domain is characterized as EGF-like 8.
+At position 1418 to 1454, the domain is characterized as EGF-like 9.
+At position 1459 to 1534, the domain is characterized as CTCK.
+At position 254 to 369, the domain is characterized as C-type lectin.
+At position 140 to 214, the domain is characterized as RRM 2.
+At position 1 to 116, the domain is characterized as Ig-like.
+At position 483 to 653, the domain is characterized as tr-type G.
+At position 165 to 356, the domain is characterized as CheB-type methylesterase.
+At position 6 to 311, the domain is characterized as Protein kinase.
+At position 7 to 165, the domain is characterized as Thioredoxin.
+At position 304 to 487, the domain is characterized as Helicase ATP-binding.
+At position 515 to 660, the domain is characterized as Helicase C-terminal.
+At position 186 to 359, the domain is characterized as EngA-type G 2.
+At position 166 to 430, the domain is characterized as AB hydrolase-1.
+At position 158 to 243, the domain is characterized as PPIase FKBP-type.
+At position 130 to 222, the domain is characterized as EH 2.
+At position 146 to 164, the domain is characterized as EF-hand 2.
+At position 267 to 330, the domain is characterized as bZIP.
+At position 212 to 310, the domain is characterized as Fibronectin type-III.
+At position 29 to 411, the domain is characterized as Helicase ATP-binding.
+At position 428 to 590, the domain is characterized as Helicase C-terminal.
+At position 609 to 644, the domain is characterized as UVR.
+At position 11 to 138, the domain is characterized as Galectin.
+At position 77 to 120, the domain is characterized as LysM.
+At position 190 to 249, the domain is characterized as GRAM.
+At position 696 to 857, the domain is characterized as TLDc.
+At position 94 to 172, the domain is characterized as S4 RNA-binding.
+At position 382 to 511, the domain is characterized as CBM6.
+At position 488 to 609, the domain is characterized as Cadherin 5.
+At position 417 to 589, the domain is characterized as tr-type G.
+At position 74 to 148, the domain is characterized as PAS 1.
+At position 220 to 290, the domain is characterized as PAS 2.
+At position 295 to 334, the domain is characterized as PAC.
+At position 33 to 117, the domain is characterized as MANSC.
+At position 96 to 167, the domain is characterized as PAS.
+At position 10 to 289, the domain is characterized as tr-type G.
+At position 24 to 291, the domain is characterized as Protein kinase.
+At position 41 to 126, the domain is characterized as Cytochrome b5 heme-binding.
+At position 404 to 475, the domain is characterized as B5.
+At position 110 to 299, the domain is characterized as ABC transmembrane type-1.
+At position 27 to 68, the domain is characterized as WAP 1; atypical.
+At position 117 to 169, the domain is characterized as WAP 2.
+At position 1183 to 1252, the domain is characterized as S1 motif.
+At position 1300 to 1389, the domain is characterized as SH2.
+At position 324 to 586, the domain is characterized as Radical SAM core.
+At position 68 to 201, the domain is characterized as N-terminal Ras-GEF.
+At position 345 to 579, the domain is characterized as Ras-GEF.
+At position 60 to 167, the domain is characterized as THUMP.
+At position 41 to 153, the domain is characterized as TBDR plug.
+At position 158 to 606, the domain is characterized as TBDR beta-barrel.
+At position 324 to 376, the domain is characterized as bHLH.
+At position 165 to 480, the domain is characterized as IF rod.
+At position 133 to 173, the domain is characterized as EGF-like.
+At position 28 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 251, the domain is characterized as CN hydrolase.
+At position 31 to 179, the domain is characterized as VOC 1.
+At position 209 to 369, the domain is characterized as VOC 2.
+At position 134 to 385, the domain is characterized as AB hydrolase-1.
+At position 28 to 217, the domain is characterized as ABC transmembrane type-1.
+At position 70 to 244, the domain is characterized as Helicase ATP-binding.
+At position 257 to 421, the domain is characterized as Helicase C-terminal.
+At position 148 to 471, the domain is characterized as NACHT.
+At position 248 to 323, the domain is characterized as PUA.
+At position 18 to 191, the domain is characterized as CRAL-TRIO.
+At position 206 to 316, the domain is characterized as GOLD.
+At position 135 to 412, the domain is characterized as Peptidase S8.
+At position 60 to 140, the domain is characterized as Cytochrome c 1.
+At position 161 to 239, the domain is characterized as Cytochrome c 2.
+At position 202 to 244, the domain is characterized as PDZ.
+At position 196 to 223, the domain is characterized as PLD phosphodiesterase 1.
+At position 411 to 437, the domain is characterized as PLD phosphodiesterase 2.
+At position 141 to 224, the domain is characterized as SPOR.
+At position 503 to 611, the domain is characterized as Ig-like C2-type 1.
+At position 616 to 704, the domain is characterized as Ig-like C2-type 2.
+At position 716 to 785, the domain is characterized as Ig-like C2-type 3.
+At position 11 to 43, the domain is characterized as LisH.
+At position 666 to 805, the domain is characterized as C2.
+At position 260 to 344, the domain is characterized as RCK C-terminal.
+At position 330 to 392, the domain is characterized as t-SNARE coiled-coil homology.
+At position 47 to 292, the domain is characterized as Peptidase S1.
+At position 83 to 202, the domain is characterized as GST C-terminal.
+At position 205 to 575, the domain is characterized as GRAS.
+At position 3 to 67, the domain is characterized as HMA.
+At position 13 to 76, the domain is characterized as TGS.
+At position 563 to 648, the domain is characterized as S1 motif.
+At position 108 to 274, the domain is characterized as NIDO.
+At position 500 to 540, the domain is characterized as EGF-like 1.
+At position 544 to 774, the domain is characterized as Nidogen G2 beta-barrel.
+At position 775 to 816, the domain is characterized as EGF-like 2.
+At position 817 to 859, the domain is characterized as EGF-like 3; calcium-binding.
+At position 864 to 907, the domain is characterized as EGF-like 4.
+At position 908 to 944, the domain is characterized as EGF-like 5; calcium-binding.
+At position 958 to 1026, the domain is characterized as Thyroglobulin type-1 1.
+At position 1037 to 1105, the domain is characterized as Thyroglobulin type-1 2.
+At position 319 to 355, the domain is characterized as CBM1.
+At position 1 to 78, the domain is characterized as Disintegrin.
+At position 570 to 669, the domain is characterized as tRNA-binding.
+At position 8 to 191, the domain is characterized as UmuC.
+At position 36 to 117, the domain is characterized as Disintegrin.
+At position 101 to 223, the domain is characterized as MPN.
+At position 349 to 422, the domain is characterized as PAS.
+At position 370 to 383, the domain is characterized as CRIB.
+At position 394 to 646, the domain is characterized as Protein kinase.
+At position 43 to 107, the domain is characterized as KH 1.
+At position 156 to 221, the domain is characterized as KH 2.
+At position 258 to 326, the domain is characterized as KH 3.
+At position 9 to 136, the domain is characterized as MsrB.
+At position 52 to 276, the domain is characterized as Radical SAM core.
+At position 168 to 253, the domain is characterized as PPIase FKBP-type.
+At position 266 to 373, the domain is characterized as Rhodanese.
+At position 1 to 125, the domain is characterized as PIK helical.
+At position 679 to 960, the domain is characterized as PI3K/PI4K catalytic.
+At position 203 to 247, the domain is characterized as TSP type-1.
+At position 274 to 437, the domain is characterized as AMOP.
+At position 2 to 375, the domain is characterized as Trm1 methyltransferase.
+At position 666 to 957, the domain is characterized as Piwi.
+At position 95 to 322, the domain is characterized as Radical SAM core.
+At position 41 to 158, the domain is characterized as Ig-like.
+At position 110 to 139, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 201 to 235, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 7 to 124, the domain is characterized as Arf-GAP.
+At position 1225 to 1389, the domain is characterized as PNPLA.
+At position 28 to 77, the domain is characterized as F-box.
+At position 444 to 613, the domain is characterized as tr-type G.
+At position 161 to 395, the domain is characterized as NR LBD.
+At position 20 to 172, the domain is characterized as MARVEL.
+At position 158 to 280, the domain is characterized as MPN.
+At position 187 to 315, the domain is characterized as Runt.
+At position 66 to 194, the domain is characterized as WIF.
+At position 330 to 603, the domain is characterized as Protein kinase.
+At position 18 to 190, the domain is characterized as PITH.
+At position 24 to 138, the domain is characterized as Response regulatory.
+At position 80 to 192, the domain is characterized as SET.
+At position 1407 to 1600, the domain is characterized as Calpain catalytic 1.
+At position 1695 to 1997, the domain is characterized as Calpain catalytic 2.
+At position 345 to 551, the domain is characterized as MCM.
+At position 577 to 654, the domain is characterized as BRCT.
+At position 30 to 44, the domain is characterized as CRIB.
+At position 287 to 436, the domain is characterized as N-acetyltransferase.
+At position 497 to 929, the domain is characterized as FH2.
+At position 46 to 236, the domain is characterized as GH11.
+At position 5 to 164, the domain is characterized as Obg.
+At position 356 to 433, the domain is characterized as OCT.
+At position 373 to 413, the domain is characterized as UBA 1.
+At position 423 to 469, the domain is characterized as UBA 2.
+At position 488 to 528, the domain is characterized as UBA 3.
+At position 173 to 407, the domain is characterized as NR LBD.
+At position 231 to 283, the domain is characterized as bHLH.
+At position 4 to 111, the domain is characterized as HIT.
+At position 90 to 288, the domain is characterized as KARI N-terminal Rossmann.
+At position 289 to 437, the domain is characterized as KARI C-terminal knotted 1.
+At position 438 to 574, the domain is characterized as KARI C-terminal knotted 2.
+At position 57 to 156, the domain is characterized as HD.
+At position 400 to 461, the domain is characterized as TGS.
+At position 662 to 736, the domain is characterized as ACT.
+At position 34 to 191, the domain is characterized as RUN.
+At position 566 to 938, the domain is characterized as Rab-GAP TBC.
+At position 1 to 74, the domain is characterized as Carrier.
+At position 1 to 112, the domain is characterized as C2.
+At position 572 to 900, the domain is characterized as Kinesin motor.
+At position 80 to 271, the domain is characterized as OTU.
+At position 119 to 151, the domain is characterized as EF-hand 3.
+At position 5 to 210, the domain is characterized as ThyX.
+At position 121 to 202, the domain is characterized as RRM 2.
+At position 260 to 338, the domain is characterized as RRM 3.
+At position 170 to 444, the domain is characterized as ABC transporter 1.
+At position 522 to 735, the domain is characterized as ABC transmembrane type-2 1.
+At position 8 to 210, the domain is characterized as AIG1-type G 1.
+At position 245 to 435, the domain is characterized as AIG1-type G 2.
+At position 436 to 644, the domain is characterized as AIG1-type G 3.
+At position 142 to 244, the domain is characterized as Gnk2-homologous 2.
+At position 26 to 153, the domain is characterized as C2.
+At position 183 to 416, the domain is characterized as Radical SAM core.
+At position 482 to 715, the domain is characterized as ABC transporter.
+At position 2 to 109, the domain is characterized as PH.
+At position 1 to 103, the domain is characterized as Thioredoxin.
+At position 10 to 77, the domain is characterized as CARD.
+At position 7 to 110, the domain is characterized as Longin.
+At position 125 to 185, the domain is characterized as v-SNARE coiled-coil homology.
+At position 67 to 166, the domain is characterized as PINc.
+At position 659 to 748, the domain is characterized as BRCT 1.
+At position 809 to 912, the domain is characterized as BRCT 2.
+At position 2 to 67, the domain is characterized as HMA 1.
+At position 80 to 146, the domain is characterized as HMA 2.
+At position 41 to 161, the domain is characterized as Thioredoxin.
+At position 1 to 431, the domain is characterized as PTS EIIC type-1.
+At position 449 to 530, the domain is characterized as PTS EIIB type-1.
+At position 30 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 297 to 595, the domain is characterized as ABC transmembrane type-1 1.
+At position 669 to 909, the domain is characterized as ABC transporter 1.
+At position 991 to 1271, the domain is characterized as ABC transmembrane type-1 2.
+At position 1309 to 1543, the domain is characterized as ABC transporter 2.
+At position 109 to 341, the domain is characterized as Peptidase S1.
+At position 22 to 304, the domain is characterized as ABC transmembrane type-1.
+At position 338 to 571, the domain is characterized as ABC transporter.
+At position 7 to 322, the domain is characterized as Helicase ATP-binding.
+At position 239 to 422, the domain is characterized as Helicase ATP-binding.
+At position 518 to 738, the domain is characterized as Helicase C-terminal.
+At position 26 to 131, the domain is characterized as C-type lectin 1.
+At position 159 to 275, the domain is characterized as C-type lectin 2.
+At position 713 to 797, the domain is characterized as PB1.
+At position 163 to 382, the domain is characterized as ABC transmembrane type-2.
+At position 329 to 596, the domain is characterized as NR LBD.
+At position 664 to 858, the domain is characterized as ATP-grasp 2.
+At position 925 to 1060, the domain is characterized as MGS-like.
+At position 61 to 130, the domain is characterized as H15.
+At position 1021 to 1157, the domain is characterized as RanBD1 1.
+At position 1318 to 1454, the domain is characterized as RanBD1 2.
+At position 1685 to 1735, the domain is characterized as GRIP.
+At position 1 to 147, the domain is characterized as SPX.
+At position 459 to 507, the domain is characterized as KA1.
+At position 223 to 390, the domain is characterized as Hflx-type G.
+At position 54 to 319, the domain is characterized as PPM-type phosphatase.
+At position 68 to 307, the domain is characterized as GB1/RHD3-type G.
+At position 669 to 741, the domain is characterized as S1 motif.
+At position 360 to 476, the domain is characterized as BRCT.
+At position 26 to 170, the domain is characterized as Tyrosine-protein phosphatase.
+At position 114 to 150, the domain is characterized as EGF-like 1.
+At position 180 to 213, the domain is characterized as EGF-like 2.
+At position 139 to 297, the domain is characterized as CRAL-TRIO.
+At position 345 to 428, the domain is characterized as OCT.
+At position 163 to 469, the domain is characterized as NACHT.
+At position 341 to 550, the domain is characterized as START.
+At position 271 to 513, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 10 to 201, the domain is characterized as DPCK.
+At position 201 to 316, the domain is characterized as C-type lectin.
+At position 217 to 381, the domain is characterized as PID.
+At position 394 to 480, the domain is characterized as PDZ 1.
+At position 485 to 560, the domain is characterized as PDZ 2.
+At position 186 to 362, the domain is characterized as Hflx-type G.
+At position 216 to 386, the domain is characterized as PCI.
+At position 109 to 315, the domain is characterized as ATP-grasp.
+At position 92 to 329, the domain is characterized as PABS.
+At position 40 to 123, the domain is characterized as RRM 1.
+At position 132 to 212, the domain is characterized as RRM 2.
+At position 423 to 501, the domain is characterized as RRM 3.
+At position 2 to 123, the domain is characterized as PINc.
+At position 1278 to 1453, the domain is characterized as Helicase ATP-binding.
+At position 1636 to 1790, the domain is characterized as Helicase C-terminal.
+At position 685 to 740, the domain is characterized as DEK-C.
+At position 55 to 232, the domain is characterized as Helicase ATP-binding.
+At position 243 to 475, the domain is characterized as Helicase C-terminal.
+At position 2 to 93, the domain is characterized as HIG1.
+At position 141 to 304, the domain is characterized as PPIase cyclophilin-type.
+At position 233 to 457, the domain is characterized as NR LBD.
+At position 36 to 114, the domain is characterized as Inhibitor I9.
+At position 128 to 377, the domain is characterized as Peptidase S8.
+At position 7 to 129, the domain is characterized as PINc.
+At position 137 to 338, the domain is characterized as ATP-grasp.
+At position 264 to 338, the domain is characterized as ACT 1.
+At position 340 to 407, the domain is characterized as ACT 2.
+At position 86 to 222, the domain is characterized as PLAT.
+At position 225 to 919, the domain is characterized as Lipoxygenase.
+At position 3 to 136, the domain is characterized as B12-binding.
+At position 9 to 92, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 1 to 185, the domain is characterized as PPIase cyclophilin-type.
+At position 262 to 340, the domain is characterized as RRM.
+At position 302 to 372, the domain is characterized as KH.
+At position 289 to 530, the domain is characterized as Glutamine amidotransferase type-1.
+At position 19 to 144, the domain is characterized as RNase III.
+At position 59 to 311, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 21 to 95, the domain is characterized as S1-like.
+At position 72 to 116, the domain is characterized as LEM.
+At position 227 to 460, the domain is characterized as START.
+At position 352 to 430, the domain is characterized as PAN.
+At position 28 to 188, the domain is characterized as MDFI.
+At position 754 to 1025, the domain is characterized as Protein kinase.
+At position 478 to 600, the domain is characterized as C2 2.
+At position 79 to 173, the domain is characterized as Fe2OG dioxygenase.
+At position 549 to 849, the domain is characterized as Histidine kinase.
+At position 934 to 1054, the domain is characterized as Response regulatory.
+At position 41 to 137, the domain is characterized as HPt.
+At position 16 to 72, the domain is characterized as bHLH.
+At position 88 to 119, the domain is characterized as Orange.
+At position 207 to 269, the domain is characterized as t-SNARE coiled-coil homology.
+At position 348 to 426, the domain is characterized as OCT.
+At position 89 to 125, the domain is characterized as LDL-receptor class A 1.
+At position 128 to 167, the domain is characterized as LDL-receptor class A 2.
+At position 183 to 221, the domain is characterized as LDL-receptor class A 3.
+At position 226 to 263, the domain is characterized as LDL-receptor class A 4.
+At position 265 to 305, the domain is characterized as LDL-receptor class A 5.
+At position 306 to 347, the domain is characterized as EGF-like 1.
+At position 348 to 388, the domain is characterized as EGF-like 2; calcium-binding.
+At position 660 to 701, the domain is characterized as EGF-like 3.
+At position 984 to 1026, the domain is characterized as EGF-like 4.
+At position 1024 to 1063, the domain is characterized as LDL-receptor class A 6.
+At position 1073 to 1110, the domain is characterized as LDL-receptor class A 7.
+At position 1117 to 1153, the domain is characterized as LDL-receptor class A 8.
+At position 1157 to 1194, the domain is characterized as LDL-receptor class A 9.
+At position 1197 to 1233, the domain is characterized as LDL-receptor class A 10.
+At position 1242 to 1280, the domain is characterized as LDL-receptor class A 11.
+At position 1282 to 1319, the domain is characterized as LDL-receptor class A 12.
+At position 1339 to 1376, the domain is characterized as LDL-receptor class A 13.
+At position 1375 to 1417, the domain is characterized as EGF-like 5.
+At position 1418 to 1457, the domain is characterized as EGF-like 6; calcium-binding.
+At position 1734 to 1770, the domain is characterized as EGF-like 7.
+At position 85 to 273, the domain is characterized as PXA.
+At position 782 to 905, the domain is characterized as PX.
+At position 262 to 303, the domain is characterized as LRRCT.
+At position 334 to 424, the domain is characterized as Ubiquitin-like.
+At position 237 to 436, the domain is characterized as Peptidase M12B.
+At position 442 to 529, the domain is characterized as Disintegrin.
+At position 673 to 710, the domain is characterized as EGF-like.
+At position 65 to 117, the domain is characterized as bHLH.
+At position 48 to 257, the domain is characterized as Helicase ATP-binding.
+At position 291 to 444, the domain is characterized as Helicase C-terminal.
+At position 433 to 491, the domain is characterized as Prospero-type homeo.
+At position 492 to 591, the domain is characterized as Prospero.
+At position 59 to 196, the domain is characterized as MPN.
+At position 129 to 316, the domain is characterized as ATP-grasp.
+At position 245 to 315, the domain is characterized as LIM zinc-binding.
+At position 6 to 156, the domain is characterized as NAC.
+At position 25 to 129, the domain is characterized as Gnk2-homologous 1.
+At position 135 to 248, the domain is characterized as Gnk2-homologous 2.
+At position 350 to 629, the domain is characterized as Protein kinase.
+At position 200 to 258, the domain is characterized as CTLH.
+At position 26 to 138, the domain is characterized as Ricin B-type lectin.
+At position 70 to 361, the domain is characterized as Reverse transcriptase.
+At position 25 to 257, the domain is characterized as Peptidase S1.
+At position 26 to 239, the domain is characterized as YjeF N-terminal.
+At position 58 to 160, the domain is characterized as THUMP.
+At position 400 to 482, the domain is characterized as Rhodanese.
+At position 43 to 116, the domain is characterized as KH type-2.
+At position 24 to 332, the domain is characterized as Protein kinase.
+At position 35 to 286, the domain is characterized as Protein kinase.
+At position 393 to 471, the domain is characterized as POLO box 1.
+At position 500 to 581, the domain is characterized as POLO box 2.
+At position 29 to 127, the domain is characterized as Plastocyanin-like.
+At position 326 to 449, the domain is characterized as MATH.
+At position 128 to 382, the domain is characterized as AB hydrolase-1.
+At position 32 to 116, the domain is characterized as BMC 1.
+At position 138 to 222, the domain is characterized as BMC 2.
+At position 107 to 224, the domain is characterized as C-type lectin.
+At position 41 to 187, the domain is characterized as VOC 1.
+At position 218 to 376, the domain is characterized as VOC 2.
+At position 120 to 193, the domain is characterized as PAS 1.
+At position 194 to 248, the domain is characterized as PAC 1.
+At position 376 to 449, the domain is characterized as PAS 2.
+At position 450 to 504, the domain is characterized as PAC 2.
+At position 577 to 864, the domain is characterized as Protein kinase.
+At position 382 to 401, the domain is characterized as WH2.
+At position 31 to 87, the domain is characterized as Sushi.
+At position 102 to 344, the domain is characterized as Peptidase S1.
+At position 74 to 198, the domain is characterized as GST C-terminal.
+At position 841 to 897, the domain is characterized as WHEP-TRS.
+At position 40 to 96, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 179, the domain is characterized as Ig-like C2-type 2.
+At position 153 to 357, the domain is characterized as ATP-grasp.
+At position 1 to 188, the domain is characterized as IF rod.
+At position 250 to 419, the domain is characterized as tr-type G.
+At position 380 to 551, the domain is characterized as tr-type G.
+At position 188 to 250, the domain is characterized as BTB.
+At position 13 to 84, the domain is characterized as RRM 1.
+At position 101 to 172, the domain is characterized as RRM 2.
+At position 129 to 249, the domain is characterized as YkuD.
+At position 25 to 84, the domain is characterized as AFP-like.
+At position 561 to 745, the domain is characterized as Helicase ATP-binding 1.
+At position 755 to 990, the domain is characterized as Helicase C-terminal 1.
+At position 1050 to 1356, the domain is characterized as SEC63 1.
+At position 1407 to 1584, the domain is characterized as Helicase ATP-binding 2.
+At position 1657 to 1832, the domain is characterized as Helicase C-terminal 2.
+At position 1892 to 2215, the domain is characterized as SEC63 2.
+At position 41 to 214, the domain is characterized as Helicase ATP-binding.
+At position 225 to 430, the domain is characterized as Helicase C-terminal.
+At position 215 to 364, the domain is characterized as Exonuclease.
+At position 157 to 277, the domain is characterized as PX.
+At position 331 to 586, the domain is characterized as BAR.
+At position 538 to 609, the domain is characterized as MBD.
+At position 839 to 904, the domain is characterized as DDT.
+At position 1794 to 1864, the domain is characterized as Bromo.
+At position 12 to 87, the domain is characterized as S1-like.
+At position 967 to 1026, the domain is characterized as SH3.
+At position 2328 to 2363, the domain is characterized as EF-hand 1.
+At position 2371 to 2406, the domain is characterized as EF-hand 2.
+At position 2409 to 2444, the domain is characterized as EF-hand 3.
+At position 67 to 179, the domain is characterized as C2.
+At position 231 to 295, the domain is characterized as GRAM.
+At position 399 to 572, the domain is characterized as VASt.
+At position 23 to 84, the domain is characterized as KH; atypical.
+At position 248 to 433, the domain is characterized as GATase cobBQ-type.
+At position 22 to 135, the domain is characterized as Ig-like V-type.
+At position 37 to 137, the domain is characterized as Phytocyanin.
+At position 491 to 759, the domain is characterized as Protein kinase.
+At position 762 to 890, the domain is characterized as KEN.
+At position 768 to 935, the domain is characterized as PNPLA.
+At position 8 to 84, the domain is characterized as Carrier 1.
+At position 1145 to 1221, the domain is characterized as Carrier 2.
+At position 2216 to 2294, the domain is characterized as Carrier 3.
+At position 14 to 88, the domain is characterized as PPIase FKBP-type.
+At position 304 to 620, the domain is characterized as Protein kinase.
+At position 6 to 216, the domain is characterized as ABC transporter.
+At position 93 to 152, the domain is characterized as CBS 1.
+At position 75 to 246, the domain is characterized as FAD-binding PCMH-type.
+At position 29 to 187, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 44, the domain is characterized as Thioredoxin 1.
+At position 151 to 208, the domain is characterized as Thioredoxin 2.
+At position 59 to 151, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 394 to 421, the domain is characterized as PLD phosphodiesterase 2.
+At position 1 to 67, the domain is characterized as TGS.
+At position 1 to 436, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 459 to 746, the domain is characterized as UvrD-like helicase C-terminal.
+At position 321 to 374, the domain is characterized as HAMP.
+At position 386 to 458, the domain is characterized as PAS.
+At position 511 to 728, the domain is characterized as Histidine kinase.
+At position 41 to 269, the domain is characterized as Radical SAM core.
+At position 424 to 552, the domain is characterized as Guanylate cyclase.
+At position 28 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 196 to 251, the domain is characterized as bHLH.
+At position 8 to 33, the domain is characterized as Disintegrin.
+At position 33 to 114, the domain is characterized as RRM.
+At position 155 to 180, the domain is characterized as DAZ.
+At position 16 to 80, the domain is characterized as NAC-A/B.
+At position 140 to 178, the domain is characterized as UBA.
+At position 455 to 572, the domain is characterized as Toprim.
+At position 36 to 147, the domain is characterized as TBDR plug.
+At position 158 to 723, the domain is characterized as TBDR beta-barrel.
+At position 14 to 229, the domain is characterized as tr-type G.
+At position 1 to 148, the domain is characterized as UBC core.
+At position 4 to 87, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 24 to 246, the domain is characterized as ABC transporter.
+At position 398 to 442, the domain is characterized as LysM.
+At position 57 to 228, the domain is characterized as Helicase ATP-binding.
+At position 239 to 399, the domain is characterized as Helicase C-terminal.
+At position 145 to 242, the domain is characterized as SWIRM.
+At position 362 to 413, the domain is characterized as SANT.
+At position 13 to 84, the domain is characterized as KRAB.
+At position 391 to 454, the domain is characterized as TRAM.
+At position 2 to 44, the domain is characterized as EGF-like.
+At position 343 to 516, the domain is characterized as tr-type G.
+At position 8 to 140, the domain is characterized as CMP/dCMP-type deaminase.
+At position 21 to 244, the domain is characterized as Peptidase S1.
+At position 18 to 78, the domain is characterized as v-SNARE coiled-coil homology.
+At position 256 to 444, the domain is characterized as GATase cobBQ-type.
+At position 666 to 695, the domain is characterized as IQ.
+At position 294 to 629, the domain is characterized as NACHT.
+At position 45 to 78, the domain is characterized as WW 1.
+At position 92 to 125, the domain is characterized as WW 2.
+At position 685 to 805, the domain is characterized as C2.
+At position 214 to 368, the domain is characterized as TrmE-type G.
+At position 449 to 644, the domain is characterized as PNPLA.
+At position 32 to 369, the domain is characterized as Kinesin motor.
+At position 260 to 433, the domain is characterized as GATase cobBQ-type.
+At position 4 to 237, the domain is characterized as ABC transporter.
+At position 279 to 438, the domain is characterized as Helicase C-terminal.
+At position 405 to 586, the domain is characterized as Helicase ATP-binding.
+At position 621 to 781, the domain is characterized as Helicase C-terminal.
+At position 4 to 197, the domain is characterized as RNase H type-2.
+At position 111 to 278, the domain is characterized as tr-type G.
+At position 70 to 242, the domain is characterized as Laminin G-like.
+At position 440 to 488, the domain is characterized as Collagen-like 1.
+At position 530 to 584, the domain is characterized as Collagen-like 2.
+At position 581 to 639, the domain is characterized as Collagen-like 3.
+At position 607 to 664, the domain is characterized as Collagen-like 4.
+At position 641 to 698, the domain is characterized as Collagen-like 5.
+At position 746 to 804, the domain is characterized as Collagen-like 6.
+At position 1391 to 1449, the domain is characterized as Collagen-like 7.
+At position 1442 to 1492, the domain is characterized as Collagen-like 8.
+At position 1481 to 1539, the domain is characterized as Collagen-like 9.
+At position 1575 to 1803, the domain is characterized as Fibrillar collagen NC1.
+At position 1 to 175, the domain is characterized as Obg.
+At position 176 to 345, the domain is characterized as OBG-type G.
+At position 1 to 102, the domain is characterized as Glutamine amidotransferase type-2.
+At position 13 to 216, the domain is characterized as Cytochrome b561.
+At position 404 to 479, the domain is characterized as B5.
+At position 706 to 808, the domain is characterized as FDX-ACB.
+At position 176 to 213, the domain is characterized as UBA.
+At position 8 to 126, the domain is characterized as MTTase N-terminal.
+At position 148 to 378, the domain is characterized as Radical SAM core.
+At position 381 to 444, the domain is characterized as TRAM.
+At position 10 to 287, the domain is characterized as Deacetylase sirtuin-type.
+At position 195 to 269, the domain is characterized as POU-specific.
+At position 362 to 425, the domain is characterized as FBD.
+At position 1 to 138, the domain is characterized as Thioredoxin.
+At position 41 to 120, the domain is characterized as KRAB.
+At position 593 to 718, the domain is characterized as DBINO.
+At position 847 to 1019, the domain is characterized as Helicase ATP-binding.
+At position 1423 to 1583, the domain is characterized as Helicase C-terminal.
+At position 4 to 248, the domain is characterized as KaiC.
+At position 245 to 384, the domain is characterized as DAGKc.
+At position 181 to 255, the domain is characterized as POU-specific.
+At position 3 to 347, the domain is characterized as SAM-dependent MTase C5-type.
+At position 73 to 411, the domain is characterized as TTL.
+At position 54 to 163, the domain is characterized as Rieske.
+At position 52 to 74, the domain is characterized as Follistatin-like.
+At position 68 to 137, the domain is characterized as Kazal-like.
+At position 224 to 259, the domain is characterized as EF-hand.
+At position 192 to 379, the domain is characterized as Glutamine amidotransferase type-1.
+At position 332 to 422, the domain is characterized as BRCT.
+At position 552 to 612, the domain is characterized as KH.
+At position 55 to 251, the domain is characterized as tr-type G.
+At position 7 to 246, the domain is characterized as ABC transporter.
+At position 11 to 52, the domain is characterized as F-box; degenerate.
+At position 414 to 478, the domain is characterized as Disintegrin.
+At position 204 to 251, the domain is characterized as F-box.
+At position 25 to 192, the domain is characterized as N-acetyltransferase.
+At position 24 to 218, the domain is characterized as RNase H type-2.
+At position 77 to 265, the domain is characterized as Rab-GAP TBC.
+At position 29 to 97, the domain is characterized as BTB.
+At position 207 to 488, the domain is characterized as NPH3.
+At position 243 to 344, the domain is characterized as HTH araC/xylS-type.
+At position 706 to 999, the domain is characterized as Protein kinase.
+At position 26 to 130, the domain is characterized as Calponin-homology (CH) 1.
+At position 139 to 245, the domain is characterized as Calponin-homology (CH) 2.
+At position 741 to 776, the domain is characterized as EF-hand 1.
+At position 780 to 815, the domain is characterized as EF-hand 2.
+At position 84 to 259, the domain is characterized as Helicase ATP-binding.
+At position 287 to 432, the domain is characterized as Helicase C-terminal.
+At position 61 to 232, the domain is characterized as Thioredoxin.
+At position 116 to 335, the domain is characterized as Radical SAM core.
+At position 126 to 156, the domain is characterized as KOW.
+At position 7 to 409, the domain is characterized as PTS EIIC type-3.
+At position 466 to 568, the domain is characterized as PTS EIIB type-3.
+At position 581 to 676, the domain is characterized as tRNA-binding.
+At position 99 to 161, the domain is characterized as S4 RNA-binding.
+At position 419 to 580, the domain is characterized as Helicase C-terminal.
+At position 27 to 141, the domain is characterized as CUB 1.
+At position 147 to 265, the domain is characterized as CUB 2.
+At position 275 to 424, the domain is characterized as F5/8 type C 1.
+At position 431 to 583, the domain is characterized as F5/8 type C 2.
+At position 645 to 811, the domain is characterized as MAM.
+At position 26 to 156, the domain is characterized as Ig-like V-type 1.
+At position 159 to 291, the domain is characterized as Ig-like V-type 2.
+At position 283 to 378, the domain is characterized as LCCL 1.
+At position 384 to 487, the domain is characterized as LCCL 2.
+At position 152 to 206, the domain is characterized as TCP.
+At position 276 to 354, the domain is characterized as PUA.
+At position 339 to 392, the domain is characterized as TSP type-1.
+At position 136 to 218, the domain is characterized as Ig-like C2-type 2.
+At position 222 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 127 to 215, the domain is characterized as EH 2.
+At position 159 to 194, the domain is characterized as EF-hand 2.
+At position 274 to 309, the domain is characterized as EF-hand 3.
+At position 275 to 365, the domain is characterized as EH 3.
+At position 310 to 343, the domain is characterized as EF-hand 4.
+At position 82 to 182, the domain is characterized as Rhodanese.
+At position 30 to 147, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 313, the domain is characterized as Plastocyanin-like 2.
+At position 423 to 560, the domain is characterized as Plastocyanin-like 3.
+At position 7 to 172, the domain is characterized as PPIase cyclophilin-type.
+At position 6 to 255, the domain is characterized as Glutamine amidotransferase type-1.
+At position 90 to 172, the domain is characterized as PUA.
+At position 246 to 426, the domain is characterized as PCI.
+At position 30 to 143, the domain is characterized as Plastocyanin-like 1.
+At position 172 to 360, the domain is characterized as Plastocyanin-like 2.
+At position 469 to 599, the domain is characterized as Plastocyanin-like 3.
+At position 30 to 79, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 84 to 136, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 151 to 368, the domain is characterized as TLC.
+At position 72 to 218, the domain is characterized as C2.
+At position 575 to 769, the domain is characterized as Ras-GAP.
+At position 31 to 113, the domain is characterized as GOLD.
+At position 146 to 331, the domain is characterized as CheB-type methylesterase.
+At position 153 to 426, the domain is characterized as ABC transporter 1.
+At position 504 to 717, the domain is characterized as ABC transmembrane type-2 1.
+At position 849 to 1101, the domain is characterized as ABC transporter 2.
+At position 1174 to 1388, the domain is characterized as ABC transmembrane type-2 2.
+At position 3 to 142, the domain is characterized as TNase-like 1.
+At position 167 to 312, the domain is characterized as TNase-like 2.
+At position 326 to 464, the domain is characterized as TNase-like 3.
+At position 493 to 626, the domain is characterized as TNase-like 4.
+At position 695 to 755, the domain is characterized as Tudor.
+At position 51 to 129, the domain is characterized as H15.
+At position 16 to 102, the domain is characterized as GIY-YIG.
+At position 21 to 89, the domain is characterized as H15.
+At position 591 to 649, the domain is characterized as RAP.
+At position 31 to 314, the domain is characterized as Septin-type G.
+At position 43 to 132, the domain is characterized as ACB.
+At position 39 to 93, the domain is characterized as SANT.
+At position 82 to 240, the domain is characterized as Thioredoxin.
+At position 113 to 274, the domain is characterized as F5/8 type C.
+At position 6 to 281, the domain is characterized as tr-type G.
+At position 4 to 226, the domain is characterized as Radical SAM core.
+At position 39 to 325, the domain is characterized as Protein kinase.
+At position 9 to 229, the domain is characterized as ATP-grasp.
+At position 25 to 312, the domain is characterized as ABC transmembrane type-1.
+At position 345 to 578, the domain is characterized as ABC transporter.
+At position 254 to 334, the domain is characterized as Toprim.
+At position 206 to 294, the domain is characterized as Protein kinase 1.
+At position 336 to 608, the domain is characterized as BEACH.
+At position 715 to 788, the domain is characterized as Protein kinase 2.
+At position 38 to 169, the domain is characterized as BAH.
+At position 486 to 569, the domain is characterized as RRM.
+At position 224 to 420, the domain is characterized as ATP-grasp 1.
+At position 782 to 975, the domain is characterized as ATP-grasp 2.
+At position 1042 to 1183, the domain is characterized as MGS-like.
+At position 11 to 204, the domain is characterized as Lon N-terminal.
+At position 193 to 273, the domain is characterized as SAND.
+At position 20 to 250, the domain is characterized as ABC transporter.
+At position 104 to 207, the domain is characterized as PPIase FKBP-type.
+At position 57 to 218, the domain is characterized as TNase-like.
+At position 36 to 84, the domain is characterized as PAS.
+At position 87 to 139, the domain is characterized as PAC.
+At position 3 to 184, the domain is characterized as Guanylate kinase-like.
+At position 11 to 226, the domain is characterized as ABC transporter.
+At position 140 to 246, the domain is characterized as Gnk2-homologous 2.
+At position 363 to 640, the domain is characterized as Protein kinase.
+At position 55 to 233, the domain is characterized as Helicase ATP-binding.
+At position 260 to 485, the domain is characterized as Helicase C-terminal.
+At position 18 to 81, the domain is characterized as bZIP.
+At position 19 to 59, the domain is characterized as LRRNT.
+At position 249 to 295, the domain is characterized as LRRCT.
+At position 295 to 382, the domain is characterized as Ig-like.
+At position 427 to 525, the domain is characterized as Fibronectin type-III.
+At position 38 to 171, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 48 to 142, the domain is characterized as Ig-like C2-type 1.
+At position 147 to 243, the domain is characterized as Ig-like C2-type 2.
+At position 249 to 330, the domain is characterized as Ig-like C2-type 3.
+At position 335 to 415, the domain is characterized as Ig-like C2-type 4.
+At position 419 to 515, the domain is characterized as Ig-like C2-type 5.
+At position 52 to 166, the domain is characterized as Expansin-like EG45.
+At position 176 to 255, the domain is characterized as Expansin-like CBD.
+At position 62 to 286, the domain is characterized as Radical SAM core.
+At position 311 to 362, the domain is characterized as GAF.
+At position 77 to 153, the domain is characterized as POTRA.
+At position 3 to 415, the domain is characterized as BRO1.
+At position 22 to 147, the domain is characterized as EamA 1.
+At position 189 to 317, the domain is characterized as EamA 2.
+At position 199 to 260, the domain is characterized as PWWP.
+At position 237 to 473, the domain is characterized as NR LBD.
+At position 22 to 205, the domain is characterized as RabBD.
+At position 619 to 705, the domain is characterized as PDZ.
+At position 756 to 879, the domain is characterized as C2 1.
+At position 1461 to 1579, the domain is characterized as C2 2.
+At position 147 to 177, the domain is characterized as EF-hand 4.
+At position 1 to 58, the domain is characterized as Ig-like C2-type 1.
+At position 69 to 160, the domain is characterized as Ig-like C2-type 2.
+At position 165 to 263, the domain is characterized as Ig-like C2-type 3.
+At position 268 to 355, the domain is characterized as Ig-like C2-type 4.
+At position 360 to 442, the domain is characterized as Ig-like C2-type 5.
+At position 451 to 541, the domain is characterized as Ig-like C2-type 6.
+At position 548 to 643, the domain is characterized as Fibronectin type-III 1.
+At position 645 to 742, the domain is characterized as Fibronectin type-III 2.
+At position 747 to 852, the domain is characterized as Fibronectin type-III 3.
+At position 853 to 952, the domain is characterized as Fibronectin type-III 4.
+At position 953 to 1048, the domain is characterized as Fibronectin type-III 5.
+At position 249 to 565, the domain is characterized as Protein kinase.
+At position 636 to 725, the domain is characterized as BRCT.
+At position 119 to 295, the domain is characterized as Helicase ATP-binding.
+At position 324 to 469, the domain is characterized as Helicase C-terminal.
+At position 4 to 201, the domain is characterized as tr-type G.
+At position 4 to 35, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 268 to 538, the domain is characterized as F-BAR.
+At position 758 to 971, the domain is characterized as Rho-GAP.
+At position 38 to 321, the domain is characterized as ABC transmembrane type-1.
+At position 191 to 220, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 117 to 160, the domain is characterized as LysM.
+At position 782 to 943, the domain is characterized as TLDc.
+At position 831 to 897, the domain is characterized as BTB.
+At position 505 to 541, the domain is characterized as CBM1.
+At position 109 to 184, the domain is characterized as S4 RNA-binding.
+At position 64 to 108, the domain is characterized as LysM.
+At position 112 to 200, the domain is characterized as Ig-like C1-type.
+At position 27 to 205, the domain is characterized as Eph LBD.
+At position 329 to 433, the domain is characterized as Fibronectin type-III 1.
+At position 439 to 530, the domain is characterized as Fibronectin type-III 2.
+At position 614 to 876, the domain is characterized as Protein kinase.
+At position 905 to 969, the domain is characterized as SAM.
+At position 24 to 88, the domain is characterized as HMA.
+At position 159 to 475, the domain is characterized as Protein kinase.
+At position 1138 to 1382, the domain is characterized as Rap-GAP.
+At position 40 to 324, the domain is characterized as Protein kinase.
+At position 124 to 214, the domain is characterized as RRM.
+At position 157 to 242, the domain is characterized as Cadherin 2.
+At position 113 to 199, the domain is characterized as PNT.
+At position 2 to 130, the domain is characterized as Thioredoxin.
+At position 400 to 602, the domain is characterized as PAW.
+At position 7 to 245, the domain is characterized as ABC transporter 1.
+At position 249 to 498, the domain is characterized as ABC transporter 2.
+At position 1 to 64, the domain is characterized as PAS.
+At position 131 to 236, the domain is characterized as HTH LytTR-type.
+At position 27 to 86, the domain is characterized as LIM zinc-binding 1.
+At position 87 to 152, the domain is characterized as LIM zinc-binding 2.
+At position 645 to 715, the domain is characterized as Bromo.
+At position 1085 to 1168, the domain is characterized as PWWP.
+At position 71 to 165, the domain is characterized as Toprim.
+At position 392 to 602, the domain is characterized as Rab-GAP TBC.
+At position 120 to 236, the domain is characterized as Calponin-homology (CH) 1.
+At position 264 to 375, the domain is characterized as Calponin-homology (CH) 2.
+At position 394 to 503, the domain is characterized as Calponin-homology (CH) 3.
+At position 515 to 624, the domain is characterized as Calponin-homology (CH) 4.
+At position 213 to 279, the domain is characterized as SEP.
+At position 337 to 413, the domain is characterized as UBX.
+At position 986 to 1041, the domain is characterized as KASH.
+At position 45 to 353, the domain is characterized as AB hydrolase-1.
+At position 101 to 326, the domain is characterized as Radical SAM core.
+At position 630 to 806, the domain is characterized as PCI.
+At position 29 to 270, the domain is characterized as Peptidase S1.
+At position 668 to 743, the domain is characterized as Smr.
+At position 108 to 191, the domain is characterized as PB1.
+At position 70 to 355, the domain is characterized as Protein kinase.
+At position 135 to 309, the domain is characterized as Helicase ATP-binding.
+At position 338 to 482, the domain is characterized as Helicase C-terminal.
+At position 181 to 228, the domain is characterized as SOCS box.
+At position 216 to 331, the domain is characterized as Calponin-homology (CH).
+At position 1463 to 1597, the domain is characterized as CKK.
+At position 1 to 135, the domain is characterized as IF rod.
+At position 99 to 186, the domain is characterized as PRC barrel.
+At position 50 to 143, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 186 to 216, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 42 to 111, the domain is characterized as SUZ.
+At position 116 to 160, the domain is characterized as SUZ-C.
+At position 54 to 241, the domain is characterized as SEC7.
+At position 259 to 375, the domain is characterized as PH.
+At position 15 to 95, the domain is characterized as RRM.
+At position 121 to 170, the domain is characterized as WAP.
+At position 180 to 281, the domain is characterized as Fibronectin type-III 1.
+At position 286 to 392, the domain is characterized as Fibronectin type-III 2.
+At position 418 to 515, the domain is characterized as Fibronectin type-III 3.
+At position 545 to 652, the domain is characterized as Fibronectin type-III 4.
+At position 158 to 231, the domain is characterized as HTH crp-type.
+At position 185 to 247, the domain is characterized as t-SNARE coiled-coil homology.
+At position 341 to 492, the domain is characterized as N-acetyltransferase.
+At position 44 to 315, the domain is characterized as GH10.
+At position 83 to 318, the domain is characterized as Radical SAM core.
+At position 3 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 199 to 386, the domain is characterized as GMPS ATP-PPase.
+At position 29 to 298, the domain is characterized as CN hydrolase.
+At position 228 to 499, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 156 to 263, the domain is characterized as FAD-binding FR-type.
+At position 40 to 74, the domain is characterized as LRRNT.
+At position 442 to 493, the domain is characterized as LRRCT.
+At position 497 to 596, the domain is characterized as Ig-like C2-type 1.
+At position 601 to 690, the domain is characterized as Ig-like C2-type 2.
+At position 695 to 784, the domain is characterized as Ig-like C2-type 3.
+At position 532 to 566, the domain is characterized as EF-hand 1.
+At position 575 to 608, the domain is characterized as EF-hand 2.
+At position 296 to 435, the domain is characterized as N-acetyltransferase.
+At position 560 to 660, the domain is characterized as tRNA-binding.
+At position 588 to 1010, the domain is characterized as FH2.
+At position 1 to 444, the domain is characterized as Biotin carboxylation.
+At position 200 to 317, the domain is characterized as PX.
+At position 223 to 514, the domain is characterized as Deacetylase sirtuin-type.
+At position 2 to 186, the domain is characterized as Glutamine amidotransferase type-1.
+At position 376 to 807, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1294 to 1598, the domain is characterized as PKS/mFAS DH.
+At position 1645 to 1722, the domain is characterized as Carrier 1.
+At position 1767 to 1844, the domain is characterized as Carrier 2.
+At position 403 to 560, the domain is characterized as N-acetyltransferase.
+At position 353 to 448, the domain is characterized as PFU.
+At position 462 to 717, the domain is characterized as PUL.
+At position 68 to 260, the domain is characterized as tr-type G.
+At position 6 to 124, the domain is characterized as Response regulatory.
+At position 25 to 133, the domain is characterized as Phytocyanin.
+At position 111 to 432, the domain is characterized as G-alpha.
+At position 41 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 139 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 320, the domain is characterized as Fibronectin type-III 1.
+At position 325 to 416, the domain is characterized as Fibronectin type-III 2.
+At position 518 to 790, the domain is characterized as Protein kinase.
+At position 30 to 516, the domain is characterized as Sema.
+At position 131 to 202, the domain is characterized as POTRA.
+At position 252 to 301, the domain is characterized as G-patch.
+At position 577 to 665, the domain is characterized as Ig-like C2-type.
+At position 9 to 155, the domain is characterized as RNase H type-1.
+At position 128 to 234, the domain is characterized as HTH APSES-type.
+At position 99 to 127, the domain is characterized as IQ 1.
+At position 128 to 150, the domain is characterized as IQ 2.
+At position 45 to 74, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 191 to 338, the domain is characterized as MOSC.
+At position 556 to 591, the domain is characterized as EF-hand 2.
+At position 596 to 631, the domain is characterized as EF-hand 3.
+At position 64 to 139, the domain is characterized as Lipoyl-binding.
+At position 172 to 209, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 433 to 865, the domain is characterized as FH2.
+At position 1 to 337, the domain is characterized as SPX.
+At position 78 to 345, the domain is characterized as Pyruvate carboxyltransferase.
+At position 63 to 213, the domain is characterized as Cupin type-1.
+At position 107 to 167, the domain is characterized as LIM zinc-binding 2.
+At position 327 to 488, the domain is characterized as Helicase ATP-binding.
+At position 542 to 702, the domain is characterized as Helicase C-terminal.
+At position 78 to 180, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 156 to 327, the domain is characterized as VWFA.
+At position 42 to 118, the domain is characterized as FAR1 1.
+At position 204 to 280, the domain is characterized as FAR1 2.
+At position 375 to 471, the domain is characterized as MULE.
+At position 168 to 432, the domain is characterized as MHD.
+At position 24 to 101, the domain is characterized as Ubiquitin-like.
+At position 151 to 312, the domain is characterized as FCP1 homology.
+At position 50 to 266, the domain is characterized as Radical SAM core.
+At position 19 to 306, the domain is characterized as tr-type G.
+At position 3 to 135, the domain is characterized as VOC 1.
+At position 166 to 324, the domain is characterized as VOC 2.
+At position 35 to 100, the domain is characterized as J.
+At position 130 to 232, the domain is characterized as Thioredoxin 1.
+At position 454 to 553, the domain is characterized as Thioredoxin 2.
+At position 557 to 662, the domain is characterized as Thioredoxin 3.
+At position 671 to 778, the domain is characterized as Thioredoxin 4.
+At position 8 to 64, the domain is characterized as HTH myb-type 1.
+At position 65 to 116, the domain is characterized as HTH myb-type 2.
+At position 11 to 455, the domain is characterized as Biotin carboxylation.
+At position 130 to 327, the domain is characterized as ATP-grasp.
+At position 524 to 600, the domain is characterized as Biotinyl-binding.
+At position 157 to 404, the domain is characterized as Radical SAM core.
+At position 407 to 486, the domain is characterized as TRAM.
+At position 153 to 188, the domain is characterized as UVR.
+At position 54 to 169, the domain is characterized as SEA.
+At position 197 to 238, the domain is characterized as LDL-receptor class A 1.
+At position 240 to 350, the domain is characterized as CUB 1.
+At position 358 to 520, the domain is characterized as MAM.
+At position 540 to 650, the domain is characterized as CUB 2.
+At position 657 to 695, the domain is characterized as LDL-receptor class A 2.
+At position 694 to 787, the domain is characterized as SRCR.
+At position 801 to 1035, the domain is characterized as Peptidase S1.
+At position 384 to 443, the domain is characterized as LIM zinc-binding 1.
+At position 444 to 503, the domain is characterized as LIM zinc-binding 2.
+At position 504 to 570, the domain is characterized as LIM zinc-binding 3.
+At position 429 to 563, the domain is characterized as Plastocyanin-like 3.
+At position 60 to 135, the domain is characterized as Sm.
+At position 944 to 1110, the domain is characterized as PNPLA.
+At position 94 to 217, the domain is characterized as B12-binding.
+At position 187 to 222, the domain is characterized as Tify.
+At position 970 to 1072, the domain is characterized as Ras-associating.
+At position 1710 to 2000, the domain is characterized as PPM-type phosphatase.
+At position 2058 to 2194, the domain is characterized as Guanylate cyclase.
+At position 1 to 30, the domain is characterized as LCN-type CS-alpha/beta.
+At position 68 to 130, the domain is characterized as BTB.
+At position 42 to 192, the domain is characterized as FPL.
+At position 29 to 104, the domain is characterized as MBD.
+At position 27 to 277, the domain is characterized as Protein kinase.
+At position 22 to 152, the domain is characterized as EamA 1.
+At position 190 to 318, the domain is characterized as EamA 2.
+At position 83 to 183, the domain is characterized as Rhodanese.
+At position 226 to 303, the domain is characterized as RRM 1.
+At position 327 to 407, the domain is characterized as RRM 2.
+At position 446 to 526, the domain is characterized as RRM 3.
+At position 12 to 268, the domain is characterized as Protein kinase.
+At position 2096 to 2227, the domain is characterized as MPN.
+At position 37 to 86, the domain is characterized as F-box.
+At position 2 to 72, the domain is characterized as RRM 1.
+At position 78 to 148, the domain is characterized as RRM 2.
+At position 281 to 372, the domain is characterized as PDZ 1.
+At position 387 to 469, the domain is characterized as PDZ 2.
+At position 308 to 540, the domain is characterized as Glutamine amidotransferase type-1.
+At position 329 to 675, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 309 to 385, the domain is characterized as RRM 1.
+At position 395 to 468, the domain is characterized as RRM 2.
+At position 488 to 562, the domain is characterized as RRM 3.
+At position 574 to 649, the domain is characterized as RRM 4.
+At position 8 to 327, the domain is characterized as Hcy-binding.
+At position 31 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 129 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 310, the domain is characterized as Fibronectin type-III 1.
+At position 315 to 406, the domain is characterized as Fibronectin type-III 2.
+At position 508 to 785, the domain is characterized as Protein kinase.
+At position 21 to 105, the domain is characterized as PAN.
+At position 110 to 186, the domain is characterized as Kringle 1.
+At position 191 to 268, the domain is characterized as Kringle 2.
+At position 283 to 361, the domain is characterized as Kringle 3.
+At position 370 to 448, the domain is characterized as Kringle 4.
+At position 484 to 709, the domain is characterized as Peptidase S1.
+At position 184 to 249, the domain is characterized as HTH luxR-type.
+At position 286 to 329, the domain is characterized as EGF-like.
+At position 109 to 208, the domain is characterized as Glutaredoxin.
+At position 57 to 165, the domain is characterized as PA.
+At position 413 to 463, the domain is characterized as EGF-like 1.
+At position 494 to 540, the domain is characterized as EGF-like 2.
+At position 53 to 201, the domain is characterized as Cupin type-1.
+At position 27 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 313, the domain is characterized as Ig-like C2-type 3.
+At position 324 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 690 to 973, the domain is characterized as Protein kinase.
+At position 163 to 316, the domain is characterized as Plastocyanin-like 2.
+At position 442 to 561, the domain is characterized as Plastocyanin-like 3.
+At position 691 to 973, the domain is characterized as Autotransporter.
+At position 36 to 128, the domain is characterized as PpiC.
+At position 149 to 257, the domain is characterized as CBM21.
+At position 24 to 419, the domain is characterized as Protein kinase.
+At position 18 to 194, the domain is characterized as Helicase ATP-binding.
+At position 364 to 549, the domain is characterized as Helicase C-terminal.
+At position 562 to 656, the domain is characterized as Dicer dsRNA-binding fold.
+At position 897 to 1054, the domain is characterized as RNase III 1.
+At position 1094 to 1270, the domain is characterized as RNase III 2.
+At position 1301 to 1370, the domain is characterized as DRBM.
+At position 107 to 198, the domain is characterized as RRM.
+At position 218 to 253, the domain is characterized as EF-hand 1.
+At position 408 to 443, the domain is characterized as EF-hand 2.
+At position 117 to 395, the domain is characterized as ABC transmembrane type-1 1.
+At position 448 to 695, the domain is characterized as ABC transporter 1.
+At position 751 to 1049, the domain is characterized as ABC transmembrane type-1 2.
+At position 1091 to 1337, the domain is characterized as ABC transporter 2.
+At position 149 to 462, the domain is characterized as IF rod.
+At position 94 to 124, the domain is characterized as KOW.
+At position 7 to 182, the domain is characterized as PNPLA.
+At position 110 to 278, the domain is characterized as Helicase ATP-binding.
+At position 467 to 631, the domain is characterized as Helicase C-terminal.
+At position 242 to 315, the domain is characterized as RRM.
+At position 47 to 174, the domain is characterized as Ricin B-type lectin.
+At position 1 to 66, the domain is characterized as KRAB.
+At position 43 to 163, the domain is characterized as Bulb-type lectin.
+At position 374 to 455, the domain is characterized as PAN.
+At position 322 to 434, the domain is characterized as PLAT.
+At position 165 to 286, the domain is characterized as Calponin-homology (CH).
+At position 972 to 1109, the domain is characterized as CKK.
+At position 267 to 341, the domain is characterized as ACT 1.
+At position 347 to 413, the domain is characterized as ACT 2.
+At position 26 to 286, the domain is characterized as Peptidase S6.
+At position 1140 to 1394, the domain is characterized as Autotransporter.
+At position 292 to 408, the domain is characterized as PAZ.
+At position 577 to 885, the domain is characterized as Piwi.
+At position 580 to 659, the domain is characterized as Carrier.
+At position 1 to 129, the domain is characterized as VOC.
+At position 111 to 310, the domain is characterized as MAGE.
+At position 536 to 838, the domain is characterized as Protein kinase.
+At position 896 to 1026, the domain is characterized as Guanylate cyclase.
+At position 1213 to 1446, the domain is characterized as ABC transporter 2.
+At position 115 to 386, the domain is characterized as Dynamin-type G.
+At position 622 to 713, the domain is characterized as GED.
+At position 19 to 122, the domain is characterized as Ig-like V-type.
+At position 147 to 232, the domain is characterized as Ig-like C2-type 1.
+At position 238 to 322, the domain is characterized as Ig-like C2-type 2.
+At position 327 to 424, the domain is characterized as Ig-like C2-type 3.
+At position 80 to 368, the domain is characterized as ABC transmembrane type-1 1.
+At position 403 to 639, the domain is characterized as ABC transporter 1.
+At position 730 to 1017, the domain is characterized as ABC transmembrane type-1 2.
+At position 1052 to 1289, the domain is characterized as ABC transporter 2.
+At position 1 to 15, the domain is characterized as Ubiquitin-like 1.
+At position 16 to 91, the domain is characterized as Ubiquitin-like 2.
+At position 92 to 167, the domain is characterized as Ubiquitin-like 3.
+At position 86 to 179, the domain is characterized as PH.
+At position 496 to 565, the domain is characterized as PUA.
+At position 34 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 28 to 136, the domain is characterized as Ig-like V-type.
+At position 4 to 76, the domain is characterized as DWNN.
+At position 655 to 734, the domain is characterized as BRCT.
+At position 24 to 59, the domain is characterized as QLQ.
+At position 89 to 133, the domain is characterized as WRC 1.
+At position 307 to 351, the domain is characterized as WRC 2.
+At position 11 to 63, the domain is characterized as F-box.
+At position 101 to 301, the domain is characterized as PNPLA.
+At position 7 to 146, the domain is characterized as DAC.
+At position 363 to 634, the domain is characterized as Protein kinase.
+At position 19 to 135, the domain is characterized as Thioredoxin 1.
+At position 347 to 476, the domain is characterized as Thioredoxin 2.
+At position 261 to 336, the domain is characterized as PUA.
+At position 150 to 201, the domain is characterized as TSP type-1.
+At position 309 to 393, the domain is characterized as Ig-like C2-type.
+At position 735 to 757, the domain is characterized as IQ 1.
+At position 758 to 787, the domain is characterized as IQ 2.
+At position 804 to 833, the domain is characterized as IQ 3.
+At position 929 to 1168, the domain is characterized as MyTH4 1.
+At position 1171 to 1211, the domain is characterized as Ras-associating.
+At position 1173 to 1481, the domain is characterized as FERM 1.
+At position 1479 to 1547, the domain is characterized as SH3.
+At position 1624 to 1772, the domain is characterized as MyTH4 2.
+At position 1778 to 2086, the domain is characterized as FERM 2.
+At position 1325 to 1604, the domain is characterized as Autotransporter.
+At position 155 to 615, the domain is characterized as TBDR beta-barrel.
+At position 117 to 287, the domain is characterized as Era-type G.
+At position 318 to 395, the domain is characterized as KH type-2.
+At position 274 to 499, the domain is characterized as TLDc.
+At position 31 to 147, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 308, the domain is characterized as Plastocyanin-like 2.
+At position 406 to 541, the domain is characterized as Plastocyanin-like 3.
+At position 67 to 184, the domain is characterized as RGS.
+At position 302 to 373, the domain is characterized as RBD 1.
+At position 375 to 445, the domain is characterized as RBD 2.
+At position 498 to 521, the domain is characterized as GoLoco.
+At position 27 to 109, the domain is characterized as Lipoyl-binding.
+At position 569 to 598, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 599 to 626, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 18 to 223, the domain is characterized as Radical SAM core.
+At position 50 to 319, the domain is characterized as PNPLA.
+At position 2 to 77, the domain is characterized as Sm.
+At position 14 to 251, the domain is characterized as ABC transporter 1.
+At position 786 to 870, the domain is characterized as PB1.
+At position 48 to 292, the domain is characterized as PPM-type phosphatase.
+At position 815 to 850, the domain is characterized as EF-hand 1.
+At position 851 to 886, the domain is characterized as EF-hand 2.
+At position 895 to 930, the domain is characterized as EF-hand 3.
+At position 1087 to 1269, the domain is characterized as Ferric oxidoreductase.
+At position 1270 to 1376, the domain is characterized as FAD-binding FR-type.
+At position 42 to 100, the domain is characterized as TCP.
+At position 151 to 172, the domain is characterized as R.
+At position 269 to 302, the domain is characterized as KOW 1.
+At position 416 to 447, the domain is characterized as KOW 2.
+At position 468 to 499, the domain is characterized as KOW 3.
+At position 590 to 623, the domain is characterized as KOW 4.
+At position 700 to 733, the domain is characterized as KOW 5.
+At position 205 to 375, the domain is characterized as PCI.
+At position 14 to 211, the domain is characterized as Lon N-terminal.
+At position 533 to 610, the domain is characterized as GW 1.
+At position 612 to 686, the domain is characterized as GW 2.
+At position 700 to 774, the domain is characterized as GW 3.
+At position 776 to 850, the domain is characterized as GW 4.
+At position 868 to 943, the domain is characterized as GW 5.
+At position 945 to 1020, the domain is characterized as GW 6.
+At position 1023 to 1096, the domain is characterized as GW 7.
+At position 40 to 101, the domain is characterized as LIM zinc-binding 1.
+At position 141 to 205, the domain is characterized as LIM zinc-binding 2.
+At position 206 to 262, the domain is characterized as LIM zinc-binding 3.
+At position 153 to 296, the domain is characterized as Thioredoxin.
+At position 164 to 211, the domain is characterized as PLD phosphodiesterase.
+At position 24 to 409, the domain is characterized as Helicase ATP-binding.
+At position 426 to 589, the domain is characterized as Helicase C-terminal.
+At position 359 to 543, the domain is characterized as N-acetyltransferase.
+At position 264 to 337, the domain is characterized as ACT 1.
+At position 343 to 408, the domain is characterized as ACT 2.
+At position 923 to 1028, the domain is characterized as BRCT.
+At position 124 to 453, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 511 to 827, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 17 to 221, the domain is characterized as ABC transmembrane type-1.
+At position 96 to 172, the domain is characterized as Ubiquitin-like.
+At position 47 to 301, the domain is characterized as AB hydrolase-1.
+At position 3 to 148, the domain is characterized as ADF-H.
+At position 820 to 973, the domain is characterized as DIPSY.
+At position 344 to 400, the domain is characterized as MIR 1.
+At position 410 to 466, the domain is characterized as MIR 2.
+At position 471 to 528, the domain is characterized as MIR 3.
+At position 10 to 77, the domain is characterized as DRBM 1.
+At position 99 to 167, the domain is characterized as DRBM 2.
+At position 209 to 277, the domain is characterized as DRBM 3.
+At position 4 to 81, the domain is characterized as RRM.
+At position 287 to 318, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 142 to 322, the domain is characterized as Helicase ATP-binding.
+At position 354 to 505, the domain is characterized as Helicase C-terminal.
+At position 390 to 559, the domain is characterized as tr-type G.
+At position 28 to 276, the domain is characterized as Protein kinase.
+At position 294 to 334, the domain is characterized as UBA.
+At position 5 to 154, the domain is characterized as UBC core.
+At position 3 to 289, the domain is characterized as DegV.
+At position 82 to 321, the domain is characterized as Lon N-terminal.
+At position 320 to 428, the domain is characterized as CULT.
+At position 3 to 45, the domain is characterized as SpoVT-AbrB.
+At position 589 to 702, the domain is characterized as Calponin-homology (CH).
+At position 216 to 297, the domain is characterized as BCNT-C.
+At position 427 to 478, the domain is characterized as SANT 1.
+At position 610 to 661, the domain is characterized as SANT 2.
+At position 32 to 109, the domain is characterized as Inhibitor I9.
+At position 115 to 624, the domain is characterized as Peptidase S8.
+At position 403 to 481, the domain is characterized as PA.
+At position 55 to 109, the domain is characterized as TCP.
+At position 244 to 306, the domain is characterized as t-SNARE coiled-coil homology.
+At position 14 to 92, the domain is characterized as S1-like.
+At position 30 to 58, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 169 to 234, the domain is characterized as VWFC.
+At position 301 to 392, the domain is characterized as CTCK.
+At position 185 to 411, the domain is characterized as NR LBD.
+At position 1 to 92, the domain is characterized as CARD.
+At position 93 to 162, the domain is characterized as Chitin-binding type R&R.
+At position 589 to 671, the domain is characterized as BRCT.
+At position 62 to 167, the domain is characterized as Cadherin 1.
+At position 168 to 276, the domain is characterized as Cadherin 2.
+At position 277 to 391, the domain is characterized as Cadherin 3.
+At position 392 to 494, the domain is characterized as Cadherin 4.
+At position 495 to 616, the domain is characterized as Cadherin 5.
+At position 361 to 427, the domain is characterized as S4 RNA-binding.
+At position 14 to 105, the domain is characterized as GS beta-grasp.
+At position 112 to 446, the domain is characterized as GS catalytic.
+At position 42 to 120, the domain is characterized as GIY-YIG.
+At position 231 to 266, the domain is characterized as UVR.
+At position 133 to 324, the domain is characterized as ATP-grasp.
+At position 27 to 142, the domain is characterized as PH 1.
+At position 152 to 187, the domain is characterized as EF-hand.
+At position 320 to 464, the domain is characterized as PI-PLC X-box.
+At position 489 to 523, the domain is characterized as PH 2; first part.
+At position 550 to 657, the domain is characterized as SH2 1.
+At position 668 to 756, the domain is characterized as SH2 2.
+At position 791 to 851, the domain is characterized as SH3.
+At position 895 to 931, the domain is characterized as PH 2; second part.
+At position 953 to 1070, the domain is characterized as PI-PLC Y-box.
+At position 1071 to 1194, the domain is characterized as C2.
+At position 293 to 539, the domain is characterized as Glutamine amidotransferase type-1.
+At position 62 to 731, the domain is characterized as Myosin motor.
+At position 734 to 763, the domain is characterized as IQ 1.
+At position 757 to 786, the domain is characterized as IQ 2.
+At position 782 to 811, the domain is characterized as IQ 3.
+At position 805 to 834, the domain is characterized as IQ 4.
+At position 830 to 859, the domain is characterized as IQ 5.
+At position 853 to 882, the domain is characterized as IQ 6.
+At position 1148 to 1452, the domain is characterized as Dilute.
+At position 63 to 315, the domain is characterized as Protein kinase.
+At position 448 to 526, the domain is characterized as POLO box 1.
+At position 547 to 630, the domain is characterized as POLO box 2.
+At position 453 to 662, the domain is characterized as MCM.
+At position 369 to 538, the domain is characterized as tr-type G.
+At position 113 to 332, the domain is characterized as Radical SAM core.
+At position 572 to 759, the domain is characterized as SEC7.
+At position 276 to 437, the domain is characterized as YrdC-like.
+At position 83 to 308, the domain is characterized as Radical SAM core.
+At position 646 to 823, the domain is characterized as Reverse transcriptase.
+At position 919 to 1037, the domain is characterized as RNase H Ty3/gyspy-type.
+At position 1185 to 1350, the domain is characterized as Integrase catalytic.
+At position 153 to 360, the domain is characterized as ATP-grasp.
+At position 10 to 119, the domain is characterized as Calponin-homology (CH) 1.
+At position 128 to 233, the domain is characterized as Calponin-homology (CH) 2.
+At position 15 to 414, the domain is characterized as Helicase ATP-binding.
+At position 55 to 290, the domain is characterized as AB hydrolase-1.
+At position 404 to 606, the domain is characterized as PAW.
+At position 235 to 414, the domain is characterized as PBS-linker 1.
+At position 473 to 652, the domain is characterized as PBS-linker 2.
+At position 671 to 852, the domain is characterized as PBS-linker 3.
+At position 11 to 202, the domain is characterized as RNase H type-2.
+At position 37 to 299, the domain is characterized as Protein kinase.
+At position 408 to 480, the domain is characterized as PAS.
+At position 134 to 432, the domain is characterized as NB-ARC.
+At position 27 to 294, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 25 to 54, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 2 to 88, the domain is characterized as Thioredoxin.
+At position 155 to 230, the domain is characterized as RRM 1.
+At position 284 to 360, the domain is characterized as RRM 2.
+At position 400 to 477, the domain is characterized as RRM 3.
+At position 925 to 1001, the domain is characterized as RRM 4.
+At position 26 to 89, the domain is characterized as S5 DRBM.
+At position 211 to 348, the domain is characterized as TrmE-type G.
+At position 129 to 310, the domain is characterized as Helicase ATP-binding.
+At position 448 to 621, the domain is characterized as Helicase C-terminal.
+At position 654 to 744, the domain is characterized as Dicer dsRNA-binding fold.
+At position 894 to 1028, the domain is characterized as PAZ.
+At position 1052 to 1207, the domain is characterized as RNase III 1.
+At position 1258 to 1424, the domain is characterized as RNase III 2.
+At position 1458 to 1545, the domain is characterized as DRBM.
+At position 20 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 133, the domain is characterized as Gnk2-homologous 1.
+At position 141 to 250, the domain is characterized as Gnk2-homologous 2.
+At position 208 to 378, the domain is characterized as Obg.
+At position 379 to 547, the domain is characterized as OBG-type G.
+At position 577 to 656, the domain is characterized as OCT.
+At position 8 to 447, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 930 to 1220, the domain is characterized as PKS/mFAS DH.
+At position 2410 to 2485, the domain is characterized as Carrier.
+At position 252 to 315, the domain is characterized as bZIP.
+At position 13 to 267, the domain is characterized as uDENN.
+At position 288 to 428, the domain is characterized as cDENN.
+At position 430 to 564, the domain is characterized as dDENN.
+At position 1336 to 1411, the domain is characterized as Death.
+At position 359 to 471, the domain is characterized as BRCT.
+At position 54 to 266, the domain is characterized as AB hydrolase-1.
+At position 107 to 326, the domain is characterized as Radical SAM core.
+At position 34 to 143, the domain is characterized as DM13 1.
+At position 151 to 258, the domain is characterized as DM13 2.
+At position 287 to 419, the domain is characterized as DOMON.
+At position 245 to 558, the domain is characterized as DOT1.
+At position 478 to 647, the domain is characterized as tr-type G.
+At position 28 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 113 to 202, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 377, the domain is characterized as Ig-like C2-type 3.
+At position 380 to 475, the domain is characterized as Ig-like C2-type 4.
+At position 480 to 570, the domain is characterized as Ig-like C2-type 5.
+At position 712 to 1055, the domain is characterized as Protein kinase; inactive.
+At position 128 to 223, the domain is characterized as Rhodanese.
+At position 216 to 371, the domain is characterized as TrmE-type G.
+At position 32 to 142, the domain is characterized as C-type lectin.
+At position 185 to 235, the domain is characterized as DHHC.
+At position 36 to 168, the domain is characterized as MARVEL.
+At position 68 to 288, the domain is characterized as Radical SAM core.
+At position 1 to 429, the domain is characterized as SAM-dependent MTase C5-type.
+At position 95 to 257, the domain is characterized as Protein kinase.
+At position 3 to 175, the domain is characterized as PRELI/MSF1.
+At position 315 to 491, the domain is characterized as CRAL-TRIO.
+At position 518 to 667, the domain is characterized as GOLD.
+At position 11 to 136, the domain is characterized as RNase III.
+At position 20 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 209 to 402, the domain is characterized as GMPS ATP-PPase.
+At position 272 to 460, the domain is characterized as Flavodoxin-like.
+At position 152 to 293, the domain is characterized as SGF29 C-terminal.
+At position 844 to 1112, the domain is characterized as PKS/mFAS DH.
+At position 2113 to 2193, the domain is characterized as Carrier.
+At position 427 to 499, the domain is characterized as ACT-like 1.
+At position 521 to 592, the domain is characterized as ACT-like 2.
+At position 501 to 573, the domain is characterized as HSA.
+At position 785 to 950, the domain is characterized as Helicase ATP-binding.
+At position 1102 to 1263, the domain is characterized as Helicase C-terminal.
+At position 456 to 586, the domain is characterized as RNase H type-1.
+At position 325 to 410, the domain is characterized as PDZ.
+At position 45 to 81, the domain is characterized as Plastocyanin-like 1.
+At position 101 to 178, the domain is characterized as Plastocyanin-like 2.
+At position 240 to 318, the domain is characterized as Plastocyanin-like 3.
+At position 378 to 509, the domain is characterized as Plastocyanin-like 4.
+At position 26 to 69, the domain is characterized as SMB 1.
+At position 66 to 108, the domain is characterized as SMB 2.
+At position 33 to 92, the domain is characterized as 4Fe-4S.
+At position 126 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 163 to 192, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 207 to 237, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 239 to 266, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 270 to 299, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 301 to 330, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 635 to 779, the domain is characterized as N-acetyltransferase.
+At position 317 to 367, the domain is characterized as bHLH.
+At position 1081 to 1381, the domain is characterized as Peptidase M60.
+At position 28 to 396, the domain is characterized as PIPK.
+At position 490 to 673, the domain is characterized as VWFA.
+At position 696 to 715, the domain is characterized as UIM 1.
+At position 766 to 783, the domain is characterized as UIM 2.
+At position 242 to 554, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 645 to 731, the domain is characterized as BRCT.
+At position 180 to 281, the domain is characterized as PpiC 1.
+At position 290 to 390, the domain is characterized as PpiC 2.
+At position 178 to 358, the domain is characterized as CNNM transmembrane.
+At position 377 to 438, the domain is characterized as CBS 1.
+At position 445 to 511, the domain is characterized as CBS 2.
+At position 37 to 128, the domain is characterized as Ig-like C2-type.
+At position 178 to 222, the domain is characterized as EGF-like.
+At position 33 to 66, the domain is characterized as EF-hand 1.
+At position 355 to 632, the domain is characterized as Protein kinase.
+At position 210 to 386, the domain is characterized as Phosphatase tensin-type.
+At position 393 to 522, the domain is characterized as C2 tensin-type.
+At position 186 to 371, the domain is characterized as Glutamine amidotransferase type-1.
+At position 62 to 143, the domain is characterized as C-type lectin.
+At position 12 to 277, the domain is characterized as Protein kinase.
+At position 97 to 279, the domain is characterized as ATP-grasp.
+At position 105 to 344, the domain is characterized as Radical SAM core.
+At position 162 to 316, the domain is characterized as DAGKc.
+At position 37 to 157, the domain is characterized as Thioredoxin.
+At position 91 to 145, the domain is characterized as HTH cro/C1-type.
+At position 276 to 453, the domain is characterized as Helicase ATP-binding.
+At position 477 to 624, the domain is characterized as Helicase C-terminal.
+At position 99 to 318, the domain is characterized as ATP-grasp.
+At position 28 to 149, the domain is characterized as MsrB.
+At position 407 to 435, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 166 to 415, the domain is characterized as ABC transporter 1.
+At position 857 to 1100, the domain is characterized as ABC transporter 2.
+At position 228 to 437, the domain is characterized as Helicase ATP-binding.
+At position 489 to 639, the domain is characterized as Helicase C-terminal.
+At position 35 to 73, the domain is characterized as EGF-like.
+At position 121 to 217, the domain is characterized as Rhodanese.
+At position 111 to 557, the domain is characterized as GBD/FH3.
+At position 1128 to 1544, the domain is characterized as FH2.
+At position 1563 to 1595, the domain is characterized as DAD.
+At position 41 to 155, the domain is characterized as TBDR plug.
+At position 160 to 672, the domain is characterized as TBDR beta-barrel.
+At position 443 to 582, the domain is characterized as PTS EIIA type-2.
+At position 92 to 148, the domain is characterized as J.
+At position 21 to 468, the domain is characterized as Hexokinase.
+At position 173 to 297, the domain is characterized as BTB.
+At position 64 to 146, the domain is characterized as SCAN box.
+At position 155 to 230, the domain is characterized as KRAB.
+At position 3 to 171, the domain is characterized as 3'-5' exonuclease.
+At position 210 to 289, the domain is characterized as HRDC.
+At position 489 to 525, the domain is characterized as CBM1.
+At position 28 to 304, the domain is characterized as Pyruvate carboxyltransferase.
+At position 71 to 252, the domain is characterized as ABC transmembrane type-1.
+At position 406 to 532, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 103 to 330, the domain is characterized as Radical SAM core.
+At position 126 to 194, the domain is characterized as KH.
+At position 8 to 68, the domain is characterized as CBS 1.
+At position 74 to 130, the domain is characterized as CBS 2.
+At position 11 to 203, the domain is characterized as Lon N-terminal.
+At position 591 to 772, the domain is characterized as Lon proteolytic.
+At position 413 to 448, the domain is characterized as EF-hand 2.
+At position 38 to 166, the domain is characterized as SCP.
+At position 198 to 234, the domain is characterized as ShKT.
+At position 27 to 105, the domain is characterized as Death.
+At position 9 to 222, the domain is characterized as YjeF N-terminal.
+At position 232 to 515, the domain is characterized as YjeF C-terminal.
+At position 5 to 134, the domain is characterized as ADF-H.
+At position 16 to 100, the domain is characterized as GS beta-grasp.
+At position 108 to 478, the domain is characterized as GS catalytic.
+At position 39 to 385, the domain is characterized as G-alpha.
+At position 84 to 189, the domain is characterized as FAD-binding FR-type.
+At position 26 to 210, the domain is characterized as NodB homology.
+At position 4 to 230, the domain is characterized as Radical SAM core.
+At position 45 to 88, the domain is characterized as F-box.
+At position 291 to 479, the domain is characterized as Rab-GAP TBC.
+At position 138 to 203, the domain is characterized as Tudor; degenerate.
+At position 11 to 108, the domain is characterized as CRM.
+At position 16 to 124, the domain is characterized as Expansin-like EG45.
+At position 137 to 218, the domain is characterized as Expansin-like CBD.
+At position 11 to 71, the domain is characterized as MADS-box.
+At position 1077 to 1152, the domain is characterized as DEP.
+At position 122 to 153, the domain is characterized as EF-hand 4.
+At position 41 to 84, the domain is characterized as F-box-like.
+At position 355 to 435, the domain is characterized as OCT.
+At position 449 to 577, the domain is characterized as GGDEF.
+At position 132 to 373, the domain is characterized as Radical SAM core.
+At position 63 to 225, the domain is characterized as Thioredoxin.
+At position 90 to 510, the domain is characterized as Peptidase A1.
+At position 319 to 424, the domain is characterized as Saposin B-type.
+At position 2 to 83, the domain is characterized as Disintegrin.
+At position 24 to 139, the domain is characterized as Thioredoxin.
+At position 27 to 215, the domain is characterized as GH16.
+At position 97 to 278, the domain is characterized as tr-type G.
+At position 152 to 193, the domain is characterized as EGF-like.
+At position 43 to 107, the domain is characterized as SH3.
+At position 266 to 330, the domain is characterized as SAM.
+At position 768 to 887, the domain is characterized as PH.
+At position 607 to 781, the domain is characterized as Helicase ATP-binding.
+At position 868 to 1043, the domain is characterized as Helicase C-terminal.
+At position 179 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 226 to 258, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 416 to 690, the domain is characterized as Protein kinase.
+At position 42 to 113, the domain is characterized as KRAB.
+At position 12 to 54, the domain is characterized as CHCH.
+At position 102 to 346, the domain is characterized as ABC transporter 1.
+At position 779 to 1016, the domain is characterized as ABC transporter 2.
+At position 3 to 185, the domain is characterized as DHFR.
+At position 20 to 131, the domain is characterized as MTTase N-terminal.
+At position 155 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 458, the domain is characterized as TRAM.
+At position 228 to 301, the domain is characterized as RRM.
+At position 207 to 279, the domain is characterized as PUA.
+At position 11 to 95, the domain is characterized as GS beta-grasp.
+At position 103 to 467, the domain is characterized as GS catalytic.
+At position 33 to 130, the domain is characterized as BTB.
+At position 4 to 82, the domain is characterized as KRAB.
+At position 62 to 509, the domain is characterized as Biotin carboxylation.
+At position 181 to 378, the domain is characterized as ATP-grasp.
+At position 653 to 728, the domain is characterized as Biotinyl-binding.
+At position 20 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 211 to 409, the domain is characterized as GMPS ATP-PPase.
+At position 525 to 632, the domain is characterized as CBM21.
+At position 46 to 148, the domain is characterized as HD.
+At position 116 to 261, the domain is characterized as PA14.
+At position 28 to 269, the domain is characterized as ABC transporter.
+At position 271 to 624, the domain is characterized as TTL.
+At position 104 to 221, the domain is characterized as Rhodanese.
+At position 83 to 233, the domain is characterized as DAGKc.
+At position 19 to 201, the domain is characterized as Eph LBD.
+At position 322 to 432, the domain is characterized as Fibronectin type-III 1.
+At position 433 to 528, the domain is characterized as Fibronectin type-III 2.
+At position 619 to 882, the domain is characterized as Protein kinase.
+At position 638 to 855, the domain is characterized as Rap-GAP.
+At position 992 to 1068, the domain is characterized as PDZ.
+At position 85 to 136, the domain is characterized as bHLH.
+At position 100 to 152, the domain is characterized as bHLH.
+At position 998 to 1082, the domain is characterized as PB1.
+At position 184 to 246, the domain is characterized as t-SNARE coiled-coil homology.
+At position 137 to 168, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 177 to 206, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 215 to 270, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 169 to 257, the domain is characterized as EH 1.
+At position 201 to 236, the domain is characterized as EF-hand 1.
+At position 458 to 547, the domain is characterized as EH 2.
+At position 491 to 526, the domain is characterized as EF-hand 2.
+At position 1434 to 1451, the domain is characterized as WH2.
+At position 242 to 316, the domain is characterized as U-box.
+At position 209 to 296, the domain is characterized as 5'-3' exonuclease.
+At position 169 to 379, the domain is characterized as ATP-grasp.
+At position 8 to 75, the domain is characterized as Acylphosphatase-like.
+At position 327 to 379, the domain is characterized as TSP type-1.
+At position 30 to 257, the domain is characterized as Peptidase S1.
+At position 353 to 436, the domain is characterized as KH-like.
+At position 128 to 227, the domain is characterized as SSB 2.
+At position 366 to 410, the domain is characterized as FBD.
+At position 288 to 346, the domain is characterized as PWWP.
+At position 478 to 610, the domain is characterized as ADD.
+At position 630 to 908, the domain is characterized as SAM-dependent MTase C5-type.
+At position 25 to 147, the domain is characterized as Ig-like V-type.
+At position 2113 to 2149, the domain is characterized as EGF-like; calcium-binding.
+At position 2161 to 2276, the domain is characterized as C-type lectin.
+At position 2279 to 2339, the domain is characterized as Sushi.
+At position 378 to 474, the domain is characterized as BRCT.
+At position 1 to 124, the domain is characterized as PX.
+At position 250 to 312, the domain is characterized as t-SNARE coiled-coil homology.
+At position 248 to 445, the domain is characterized as GATase cobBQ-type.
+At position 218 to 499, the domain is characterized as FERM.
+At position 1714 to 1989, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 2020 to 2279, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 150 to 208, the domain is characterized as LIM zinc-binding 1.
+At position 209 to 267, the domain is characterized as LIM zinc-binding 2.
+At position 268 to 326, the domain is characterized as LIM zinc-binding 3.
+At position 327 to 386, the domain is characterized as LIM zinc-binding 4.
+At position 13 to 175, the domain is characterized as Ku.
+At position 162 to 273, the domain is characterized as Cytochrome c.
+At position 235 to 298, the domain is characterized as bZIP.
+At position 1594 to 1824, the domain is characterized as Alpha-type protein kinase.
+At position 11 to 41, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 66 to 97, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 99 to 128, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 6 to 98, the domain is characterized as Ig-like 1.
+At position 126 to 225, the domain is characterized as Ig-like 2.
+At position 234 to 330, the domain is characterized as Ig-like 3.
+At position 32 to 99, the domain is characterized as Importin N-terminal.
+At position 102 to 285, the domain is characterized as ATP-grasp.
+At position 1463 to 1633, the domain is characterized as Helicase ATP-binding.
+At position 1805 to 1976, the domain is characterized as Helicase C-terminal.
+At position 294 to 359, the domain is characterized as Mop.
+At position 44 to 158, the domain is characterized as tRNA-binding.
+At position 22 to 190, the domain is characterized as FAD-binding PCMH-type.
+At position 265 to 348, the domain is characterized as Toprim.
+At position 88 to 220, the domain is characterized as GST C-terminal.
+At position 92 to 215, the domain is characterized as PA.
+At position 26 to 65, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 66 to 112, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 119 to 160, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 161 to 209, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 41 to 195, the domain is characterized as PID.
+At position 82 to 242, the domain is characterized as DAC.
+At position 496 to 532, the domain is characterized as CBM1.
+At position 10 to 438, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 930 to 1253, the domain is characterized as PKS/mFAS DH.
+At position 2300 to 2377, the domain is characterized as Carrier.
+At position 38 to 291, the domain is characterized as GH16.
+At position 170 to 409, the domain is characterized as NR LBD.
+At position 12 to 139, the domain is characterized as C-type lectin.
+At position 15 to 296, the domain is characterized as Protein kinase.
+At position 99 to 177, the domain is characterized as PDZ.
+At position 200 to 304, the domain is characterized as Fe2OG dioxygenase.
+At position 361 to 680, the domain is characterized as Transferrin-like 2.
+At position 25 to 188, the domain is characterized as PPIase cyclophilin-type.
+At position 225 to 260, the domain is characterized as EF-hand 1.
+At position 279 to 296, the domain is characterized as EF-hand 2.
+At position 302 to 337, the domain is characterized as EF-hand 3.
+At position 339 to 370, the domain is characterized as EF-hand 4.
+At position 164 to 354, the domain is characterized as CheB-type methylesterase.
+At position 450 to 485, the domain is characterized as EF-hand.
+At position 76 to 173, the domain is characterized as PH.
+At position 24 to 112, the domain is characterized as PPIase FKBP-type.
+At position 1 to 214, the domain is characterized as Radical SAM core.
+At position 30 to 364, the domain is characterized as Protein kinase.
+At position 142 to 211, the domain is characterized as BTB 1.
+At position 247 to 341, the domain is characterized as BTB 2.
+At position 413 to 479, the domain is characterized as BACK.
+At position 44 to 296, the domain is characterized as AB hydrolase-1.
+At position 269 to 424, the domain is characterized as Helicase C-terminal.
+At position 192 to 332, the domain is characterized as Helicase ATP-binding.
+At position 354 to 519, the domain is characterized as Helicase C-terminal.
+At position 1 to 139, the domain is characterized as Obg.
+At position 140 to 309, the domain is characterized as OBG-type G.
+At position 46 to 262, the domain is characterized as Radical SAM core.
+At position 36 to 105, the domain is characterized as S1 motif 1.
+At position 123 to 188, the domain is characterized as S1 motif 2.
+At position 209 to 277, the domain is characterized as S1 motif 3.
+At position 294 to 363, the domain is characterized as S1 motif 4.
+At position 331 to 610, the domain is characterized as ABC transporter 1.
+At position 630 to 959, the domain is characterized as ABC transporter 2.
+At position 35 to 84, the domain is characterized as Myosin N-terminal SH3-like.
+At position 88 to 781, the domain is characterized as Myosin motor.
+At position 781 to 813, the domain is characterized as IQ.
+At position 72 to 171, the domain is characterized as Cytochrome b5 heme-binding.
+At position 14 to 198, the domain is characterized as RNase H type-2.
+At position 44 to 315, the domain is characterized as Septin-type G.
+At position 37 to 322, the domain is characterized as Protein kinase.
+At position 156 to 226, the domain is characterized as POTRA.
+At position 124 to 185, the domain is characterized as CBS 1.
+At position 187 to 243, the domain is characterized as CBS 2.
+At position 1 to 89, the domain is characterized as HPr.
+At position 23 to 167, the domain is characterized as UBC core.
+At position 19 to 137, the domain is characterized as C-type lysozyme.
+At position 209 to 284, the domain is characterized as Carrier.
+At position 31 to 247, the domain is characterized as Radical SAM core.
+At position 515 to 802, the domain is characterized as UvrD-like helicase C-terminal.
+At position 94 to 184, the domain is characterized as K-box.
+At position 264 to 310, the domain is characterized as LysM 1.
+At position 487 to 534, the domain is characterized as LysM 2.
+At position 19 to 139, the domain is characterized as FZ.
+At position 178 to 296, the domain is characterized as NTR.
+At position 43 to 140, the domain is characterized as Core-binding (CB).
+At position 170 to 357, the domain is characterized as Tyr recombinase.
+At position 126 to 333, the domain is characterized as ATP-grasp.
+At position 402 to 480, the domain is characterized as ACT 1.
+At position 481 to 559, the domain is characterized as ACT 2.
+At position 17 to 145, the domain is characterized as Galectin.
+At position 737 to 798, the domain is characterized as SH3 1.
+At position 905 to 963, the domain is characterized as SH3 2.
+At position 994 to 1052, the domain is characterized as SH3 3.
+At position 1066 to 1130, the domain is characterized as SH3 4.
+At position 1147 to 1206, the domain is characterized as SH3 5.
+At position 1229 to 1415, the domain is characterized as DH.
+At position 1454 to 1563, the domain is characterized as PH.
+At position 1571 to 1687, the domain is characterized as C2.
+At position 7 to 330, the domain is characterized as Kinesin motor.
+At position 14 to 208, the domain is characterized as Peptidase M12B.
+At position 216 to 285, the domain is characterized as Disintegrin.
+At position 38 to 182, the domain is characterized as YEATS.
+At position 115 to 443, the domain is characterized as PI3K/PI4K catalytic.
+At position 178 to 228, the domain is characterized as bHLH.
+At position 14 to 209, the domain is characterized as PBC.
+At position 25 to 139, the domain is characterized as Ig-like V-type.
+At position 45 to 391, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 51 to 284, the domain is characterized as Radical SAM core.
+At position 232 to 295, the domain is characterized as LIM zinc-binding 1.
+At position 297 to 357, the domain is characterized as LIM zinc-binding 2.
+At position 360 to 419, the domain is characterized as LIM zinc-binding 3.
+At position 237 to 302, the domain is characterized as PAP-associated.
+At position 681 to 915, the domain is characterized as NR LBD.
+At position 104 to 445, the domain is characterized as Peptidase A1.
+At position 218 to 415, the domain is characterized as GMPS ATP-PPase.
+At position 55 to 165, the domain is characterized as Plastocyanin-like 1.
+At position 227 to 292, the domain is characterized as Plastocyanin-like 2.
+At position 399 to 516, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 43, the domain is characterized as Ferritin-like diiron.
+At position 43 to 97, the domain is characterized as TCP.
+At position 238 to 321, the domain is characterized as RRM 1.
+At position 358 to 436, the domain is characterized as RRM 2.
+At position 479 to 565, the domain is characterized as RRM 3.
+At position 25 to 194, the domain is characterized as PID.
+At position 9 to 167, the domain is characterized as N-acetyltransferase.
+At position 182 to 346, the domain is characterized as SSD.
+At position 164 to 256, the domain is characterized as 5'-3' exonuclease.
+At position 53 to 280, the domain is characterized as Radical SAM core.
+At position 48 to 127, the domain is characterized as PAS.
+At position 216 to 262, the domain is characterized as F-box.
+At position 41 to 118, the domain is characterized as CIDE-N.
+At position 457 to 507, the domain is characterized as DHHC.
+At position 333 to 466, the domain is characterized as RanBD1.
+At position 516 to 568, the domain is characterized as HTH psq-type.
+At position 354 to 570, the domain is characterized as TLDc.
+At position 31 to 142, the domain is characterized as Response regulatory.
+At position 194 to 369, the domain is characterized as Exonuclease.
+At position 485 to 561, the domain is characterized as PDZ.
+At position 34 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 2 to 71, the domain is characterized as HMA.
+At position 225 to 386, the domain is characterized as CP-type G.
+At position 48 to 222, the domain is characterized as EngB-type G.
+At position 221 to 390, the domain is characterized as PCI.
+At position 7 to 239, the domain is characterized as ABC transporter.
+At position 117 to 236, the domain is characterized as PilZ.
+At position 24 to 111, the domain is characterized as UPAR/Ly6 1.
+At position 116 to 208, the domain is characterized as UPAR/Ly6 2.
+At position 215 to 302, the domain is characterized as UPAR/Ly6 3.
+At position 447 to 489, the domain is characterized as CUE.
+At position 42 to 236, the domain is characterized as Lon N-terminal.
+At position 22 to 133, the domain is characterized as Ig-like V-type.
+At position 1 to 165, the domain is characterized as Thioredoxin; atypical.
+At position 49 to 242, the domain is characterized as Protein kinase.
+At position 686 to 880, the domain is characterized as DDHD.
+At position 310 to 668, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 130 to 172, the domain is characterized as DSL.
+At position 173 to 205, the domain is characterized as EGF-like 1.
+At position 203 to 238, the domain is characterized as EGF-like 2.
+At position 240 to 280, the domain is characterized as EGF-like 3.
+At position 284 to 322, the domain is characterized as EGF-like 4.
+At position 325 to 349, the domain is characterized as EGF-like 5; incomplete.
+At position 1 to 77, the domain is characterized as SAMD1-like winged helix (WH).
+At position 95 to 171, the domain is characterized as H15.
+At position 504 to 778, the domain is characterized as MYST-type HAT.
+At position 112 to 326, the domain is characterized as DH.
+At position 39 to 113, the domain is characterized as TFIIS N-terminal.
+At position 130 to 207, the domain is characterized as TFIIS central.
+At position 579 to 655, the domain is characterized as Carrier.
+At position 116 to 203, the domain is characterized as Fibronectin type-III 2.
+At position 204 to 288, the domain is characterized as Fibronectin type-III 3.
+At position 545 to 633, the domain is characterized as Fibronectin type-III 7.
+At position 253 to 461, the domain is characterized as Histidine kinase.
+At position 265 to 328, the domain is characterized as bZIP.
+At position 55 to 116, the domain is characterized as SH3.
+At position 124 to 216, the domain is characterized as SH2.
+At position 234 to 495, the domain is characterized as Protein kinase.
+At position 7 to 97, the domain is characterized as CARD 1.
+At position 110 to 190, the domain is characterized as CARD 2.
+At position 317 to 510, the domain is characterized as Helicase ATP-binding.
+At position 700 to 872, the domain is characterized as Helicase C-terminal.
+At position 893 to 1020, the domain is characterized as RLR CTR.
+At position 122 to 363, the domain is characterized as AB hydrolase-1.
+At position 28 to 64, the domain is characterized as EGF-like 1.
+At position 65 to 106, the domain is characterized as EGF-like 2; calcium-binding.
+At position 107 to 148, the domain is characterized as EGF-like 3; calcium-binding.
+At position 293 to 324, the domain is characterized as EGF-like 4.
+At position 379 to 561, the domain is characterized as Reticulon.
+At position 342 to 576, the domain is characterized as ABC transporter.
+At position 12 to 155, the domain is characterized as Ferritin-like diiron.
+At position 162 to 200, the domain is characterized as Rubredoxin-like.
+At position 92 to 310, the domain is characterized as Histidine kinase.
+At position 229 to 558, the domain is characterized as FERM.
+At position 354 to 457, the domain is characterized as PH.
+At position 15 to 90, the domain is characterized as S1-like.
+At position 70 to 144, the domain is characterized as PAS 1.
+At position 203 to 275, the domain is characterized as PAS 2.
+At position 280 to 319, the domain is characterized as PAC.
+At position 45 to 142, the domain is characterized as PH.
+At position 625 to 817, the domain is characterized as Rab-GAP TBC.
+At position 404 to 481, the domain is characterized as Rhodanese.
+At position 368 to 642, the domain is characterized as Protein kinase.
+At position 395 to 636, the domain is characterized as Fibrinogen C-terminal.
+At position 76 to 234, the domain is characterized as CP-type G.
+At position 140 to 443, the domain is characterized as NB-ARC.
+At position 41 to 108, the domain is characterized as BTB.
+At position 143 to 245, the domain is characterized as BACK.
+At position 46 to 268, the domain is characterized as Peptidase S1.
+At position 199 to 295, the domain is characterized as Ig-like C1-type.
+At position 1 to 113, the domain is characterized as MTTase N-terminal.
+At position 138 to 366, the domain is characterized as Radical SAM core.
+At position 49 to 127, the domain is characterized as MANSC.
+At position 312 to 401, the domain is characterized as PKD 1.
+At position 409 to 498, the domain is characterized as PKD 2.
+At position 504 to 594, the domain is characterized as PKD 3.
+At position 600 to 688, the domain is characterized as PKD 4.
+At position 694 to 785, the domain is characterized as PKD 5.
+At position 42 to 106, the domain is characterized as SH3.
+At position 118 to 380, the domain is characterized as Protein kinase.
+At position 41 to 147, the domain is characterized as Calponin-homology (CH).
+At position 359 to 388, the domain is characterized as IQ 1.
+At position 389 to 418, the domain is characterized as IQ 2.
+At position 418 to 449, the domain is characterized as IQ 3.
+At position 535 to 564, the domain is characterized as IQ 4.
+At position 565 to 594, the domain is characterized as IQ 5.
+At position 655 to 684, the domain is characterized as IQ 6.
+At position 854 to 1077, the domain is characterized as Ras-GAP.
+At position 436 to 525, the domain is characterized as CARD.
+At position 1 to 74, the domain is characterized as S1-like.
+At position 1 to 235, the domain is characterized as LXG.
+At position 507 to 655, the domain is characterized as Helicase C-terminal.
+At position 11 to 45, the domain is characterized as SAP.
+At position 115 to 280, the domain is characterized as PINIT.
+At position 589 to 648, the domain is characterized as KH.
+At position 660 to 732, the domain is characterized as S1 motif.
+At position 116 to 300, the domain is characterized as Rab-GAP TBC.
+At position 425 to 642, the domain is characterized as ABC transporter 1.
+At position 668 to 994, the domain is characterized as ABC transporter 2.
+At position 14 to 31, the domain is characterized as EF-hand 1.
+At position 34 to 52, the domain is characterized as EF-hand 2.
+At position 53 to 88, the domain is characterized as EF-hand 3.
+At position 89 to 124, the domain is characterized as EF-hand 4.
+At position 142 to 177, the domain is characterized as EF-hand 5.
+At position 7 to 351, the domain is characterized as Kinesin motor.
+At position 33 to 216, the domain is characterized as RNase H type-2.
+At position 24 to 259, the domain is characterized as Alpha-carbonic anhydrase.
+At position 111 to 301, the domain is characterized as ATP-grasp.
+At position 2042 to 2107, the domain is characterized as NAC-A/B.
+At position 2148 to 2185, the domain is characterized as UBA.
+At position 188 to 240, the domain is characterized as KH.
+At position 160 to 322, the domain is characterized as OBG-type G.
+At position 100 to 449, the domain is characterized as Peptidase A1.
+At position 99 to 222, the domain is characterized as MPN.
+At position 5 to 204, the domain is characterized as DPCK.
+At position 87 to 115, the domain is characterized as MIT.
+At position 145 to 539, the domain is characterized as Protein kinase.
+At position 124 to 305, the domain is characterized as CP-type G.
+At position 347 to 602, the domain is characterized as Protein kinase.
+At position 603 to 673, the domain is characterized as AGC-kinase C-terminal.
+At position 74 to 220, the domain is characterized as Cupin type-1.
+At position 19 to 90, the domain is characterized as KRAB.
+At position 194 to 409, the domain is characterized as SMP-LTD.
+At position 49 to 356, the domain is characterized as AB hydrolase-1.
+At position 84 to 200, the domain is characterized as RGS.
+At position 165 to 384, the domain is characterized as Radical SAM core.
+At position 65 to 329, the domain is characterized as ABC transporter.
+At position 414 to 623, the domain is characterized as ABC transmembrane type-2.
+At position 29 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 131 to 207, the domain is characterized as Ig-like C2-type 2.
+At position 728 to 783, the domain is characterized as Sushi.
+At position 784 to 827, the domain is characterized as EGF-like; calcium-binding.
+At position 21 to 104, the domain is characterized as Apple 1.
+At position 111 to 194, the domain is characterized as Apple 2.
+At position 201 to 284, the domain is characterized as Apple 3.
+At position 292 to 375, the domain is characterized as Apple 4.
+At position 391 to 626, the domain is characterized as Peptidase S1.
+At position 194 to 256, the domain is characterized as t-SNARE coiled-coil homology.
+At position 64 to 301, the domain is characterized as PABS.
+At position 522 to 591, the domain is characterized as PAS.
+At position 489 to 564, the domain is characterized as PDZ.
+At position 600 to 670, the domain is characterized as SH3.
+At position 722 to 894, the domain is characterized as Guanylate kinase-like.
+At position 86 to 218, the domain is characterized as OmpA-like.
+At position 41 to 93, the domain is characterized as CTLH.
+At position 2 to 151, the domain is characterized as N-acetyltransferase.
+At position 57 to 140, the domain is characterized as PDZ.
+At position 283 to 390, the domain is characterized as PH.
+At position 721 to 989, the domain is characterized as Autotransporter.
+At position 62 to 347, the domain is characterized as Protein kinase.
+At position 29 to 61, the domain is characterized as WW.
+At position 113 to 280, the domain is characterized as PID 1.
+At position 285 to 440, the domain is characterized as PID 2.
+At position 29 to 116, the domain is characterized as GOLD.
+At position 568 to 597, the domain is characterized as IQ.
+At position 595 to 672, the domain is characterized as BAG.
+At position 88 to 166, the domain is characterized as GIY-YIG.
+At position 276 to 311, the domain is characterized as UVR.
+At position 111 to 150, the domain is characterized as LRRCT.
+At position 30 to 157, the domain is characterized as SCP.
+At position 3 to 254, the domain is characterized as Pyruvate carboxyltransferase.
+At position 119 to 236, the domain is characterized as PX.
+At position 46 to 328, the domain is characterized as Protein kinase.
+At position 594 to 678, the domain is characterized as BRCT.
+At position 28 to 102, the domain is characterized as Ig-like.
+At position 167 to 194, the domain is characterized as ITAM.
+At position 361 to 466, the domain is characterized as PDZ 2.
+At position 211 to 258, the domain is characterized as GRAM 1.
+At position 262 to 360, the domain is characterized as PH.
+At position 760 to 826, the domain is characterized as GRAM 2.
+At position 91 to 151, the domain is characterized as Tudor.
+At position 18 to 209, the domain is characterized as KARI N-terminal Rossmann.
+At position 210 to 354, the domain is characterized as KARI C-terminal knotted 1.
+At position 355 to 485, the domain is characterized as KARI C-terminal knotted 2.
+At position 41 to 295, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 31 to 139, the domain is characterized as Glutaredoxin.
+At position 59 to 133, the domain is characterized as RRM 1.
+At position 181 to 257, the domain is characterized as RRM 2.
+At position 338 to 412, the domain is characterized as RRM 3.
+At position 455 to 529, the domain is characterized as RRM 4.
+At position 171 to 358, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 69, the domain is characterized as EF-hand 2.
+At position 368 to 425, the domain is characterized as S4 RNA-binding.
+At position 33 to 320, the domain is characterized as ABC transmembrane type-1 1.
+At position 355 to 591, the domain is characterized as ABC transporter 1.
+At position 686 to 958, the domain is characterized as ABC transmembrane type-1 2.
+At position 993 to 1230, the domain is characterized as ABC transporter 2.
+At position 20 to 187, the domain is characterized as Era-type G.
+At position 218 to 295, the domain is characterized as KH type-2.
+At position 83 to 272, the domain is characterized as VWFA.
+At position 140 to 205, the domain is characterized as BTB.
+At position 781 to 833, the domain is characterized as HTH psq-type.
+At position 351 to 533, the domain is characterized as N-acetyltransferase.
+At position 455 to 577, the domain is characterized as HD.
+At position 696 to 779, the domain is characterized as ACT 1.
+At position 802 to 874, the domain is characterized as ACT 2.
+At position 77 to 172, the domain is characterized as Fibronectin type-III.
+At position 764 to 852, the domain is characterized as Death.
+At position 662 to 776, the domain is characterized as Calponin-homology (CH).
+At position 56 to 131, the domain is characterized as RBD.
+At position 349 to 609, the domain is characterized as Protein kinase.
+At position 267 to 361, the domain is characterized as Ig-like V-type.
+At position 4 to 381, the domain is characterized as Protein kinase.
+At position 31 to 352, the domain is characterized as USP.
+At position 14 to 229, the domain is characterized as ABC transporter.
+At position 227 to 328, the domain is characterized as HD.
+At position 632 to 683, the domain is characterized as GPS.
+At position 156 to 256, the domain is characterized as Fe2OG dioxygenase.
+At position 22 to 109, the domain is characterized as PDZ.
+At position 158 to 267, the domain is characterized as Cadherin 2.
+At position 268 to 388, the domain is characterized as Cadherin 3.
+At position 384 to 495, the domain is characterized as Cadherin 4.
+At position 651 to 668, the domain is characterized as WH2.
+At position 1 to 417, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 877 to 1202, the domain is characterized as PKS/mFAS DH.
+At position 2102 to 2183, the domain is characterized as Carrier.
+At position 375 to 806, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1286 to 1598, the domain is characterized as PKS/mFAS DH.
+At position 1643 to 1720, the domain is characterized as Carrier 1.
+At position 1764 to 1841, the domain is characterized as Carrier 2.
+At position 4 to 111, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 126 to 180, the domain is characterized as AWS.
+At position 182 to 299, the domain is characterized as SET.
+At position 306 to 322, the domain is characterized as Post-SET.
+At position 569 to 601, the domain is characterized as WW.
+At position 165 to 254, the domain is characterized as 5'-3' exonuclease.
+At position 236 to 295, the domain is characterized as SH3.
+At position 173 to 234, the domain is characterized as SH3.
+At position 252 to 316, the domain is characterized as SAM.
+At position 455 to 526, the domain is characterized as PAS.
+At position 209 to 285, the domain is characterized as PUA.
+At position 77 to 138, the domain is characterized as SH3.
+At position 263 to 516, the domain is characterized as Protein kinase.
+At position 231 to 302, the domain is characterized as RRM 1.
+At position 308 to 387, the domain is characterized as RRM 2.
+At position 102 to 271, the domain is characterized as Helicase ATP-binding.
+At position 299 to 460, the domain is characterized as Helicase C-terminal.
+At position 1 to 35, the domain is characterized as EF-hand 1.
+At position 319 to 522, the domain is characterized as Helicase ATP-binding.
+At position 533 to 696, the domain is characterized as Helicase C-terminal.
+At position 9 to 192, the domain is characterized as AMMECR1.
+At position 55 to 155, the domain is characterized as C-type lectin.
+At position 156 to 192, the domain is characterized as EGF-like.
+At position 195 to 256, the domain is characterized as Sushi 1.
+At position 257 to 318, the domain is characterized as Sushi 2.
+At position 79 to 405, the domain is characterized as Peptidase A1.
+At position 596 to 677, the domain is characterized as BRCT.
+At position 247 to 461, the domain is characterized as FAD-binding FR-type.
+At position 38 to 160, the domain is characterized as HIT.
+At position 167 to 198, the domain is characterized as EGF-like 1.
+At position 199 to 229, the domain is characterized as EGF-like 2.
+At position 230 to 260, the domain is characterized as EGF-like 3.
+At position 264 to 352, the domain is characterized as Fibronectin type-III 1.
+At position 353 to 444, the domain is characterized as Fibronectin type-III 2.
+At position 445 to 532, the domain is characterized as Fibronectin type-III 3.
+At position 533 to 623, the domain is characterized as Fibronectin type-III 4.
+At position 624 to 709, the domain is characterized as Fibronectin type-III 5.
+At position 710 to 800, the domain is characterized as Fibronectin type-III 6.
+At position 801 to 886, the domain is characterized as Fibronectin type-III 7.
+At position 887 to 976, the domain is characterized as Fibronectin type-III 8.
+At position 977 to 1063, the domain is characterized as Fibronectin type-III 9.
+At position 1061 to 1278, the domain is characterized as Fibrinogen C-terminal.
+At position 209 to 881, the domain is characterized as Peptidase M13.
+At position 38 to 156, the domain is characterized as SCP.
+At position 131 to 292, the domain is characterized as Exonuclease.
+At position 56 to 131, the domain is characterized as ACT.
+At position 6 to 242, the domain is characterized as PABS.
+At position 1 to 90, the domain is characterized as HotDog ACOT-type 1.
+At position 146 to 252, the domain is characterized as HotDog ACOT-type 2.
+At position 30 to 149, the domain is characterized as Plastocyanin-like 1.
+At position 161 to 328, the domain is characterized as Plastocyanin-like 2.
+At position 372 to 550, the domain is characterized as Plastocyanin-like 3.
+At position 59 to 130, the domain is characterized as KRAB.
+At position 122 to 316, the domain is characterized as ATP-grasp.
+At position 388 to 542, the domain is characterized as MGS-like.
+At position 209 to 401, the domain is characterized as Helicase ATP-binding.
+At position 412 to 573, the domain is characterized as Helicase C-terminal.
+At position 7 to 113, the domain is characterized as RWD.
+At position 37 to 74, the domain is characterized as LRRNT.
+At position 487 to 670, the domain is characterized as Helicase ATP-binding 1.
+At position 697 to 915, the domain is characterized as Helicase C-terminal 1.
+At position 979 to 1288, the domain is characterized as SEC63 1.
+At position 1545 to 1740, the domain is characterized as Helicase C-terminal 2.
+At position 1813 to 2177, the domain is characterized as SEC63 2.
+At position 198 to 256, the domain is characterized as CBS 2.
+At position 283 to 342, the domain is characterized as CBS 3.
+At position 443 to 512, the domain is characterized as CBS 4.
+At position 25 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 150 to 321, the domain is characterized as Helicase ATP-binding.
+At position 348 to 492, the domain is characterized as Helicase C-terminal.
+At position 1304 to 1383, the domain is characterized as DEP.
+At position 758 to 1040, the domain is characterized as Protein kinase.
+At position 269 to 406, the domain is characterized as Flavodoxin-like.
+At position 250 to 418, the domain is characterized as PCI.
+At position 153 to 430, the domain is characterized as Protein kinase.
+At position 4 to 440, the domain is characterized as SAM-dependent MTase C5-type.
+At position 154 to 233, the domain is characterized as Doublecortin 2.
+At position 279 to 316, the domain is characterized as LIM zinc-binding 1.
+At position 399 to 467, the domain is characterized as LIM zinc-binding 3.
+At position 155 to 273, the domain is characterized as Response regulatory.
+At position 626 to 756, the domain is characterized as N-terminal Ras-GEF.
+At position 812 to 1049, the domain is characterized as Ras-GEF.
+At position 51 to 198, the domain is characterized as NAC.
+At position 7 to 253, the domain is characterized as Radical SAM core.
+At position 35 to 72, the domain is characterized as LRRNT.
+At position 173 to 223, the domain is characterized as LRRCT.
+At position 10 to 229, the domain is characterized as Radical SAM core.
+At position 21 to 69, the domain is characterized as F-box.
+At position 396 to 428, the domain is characterized as FBD.
+At position 261 to 296, the domain is characterized as EF-hand 2.
+At position 387 to 422, the domain is characterized as EF-hand 3.
+At position 43 to 101, the domain is characterized as Collagen-like.
+At position 135 to 246, the domain is characterized as C-type lectin.
+At position 359 to 562, the domain is characterized as DPCK.
+At position 97 to 202, the domain is characterized as FAD-binding FR-type.
+At position 329 to 529, the domain is characterized as Protein kinase.
+At position 43 to 157, the domain is characterized as sHSP.
+At position 2 to 135, the domain is characterized as ADF-H.
+At position 112 to 252, the domain is characterized as Ricin B-type lectin.
+At position 23 to 224, the domain is characterized as SET.
+At position 25 to 261, the domain is characterized as Peptidase S1.
+At position 256 to 378, the domain is characterized as CUB.
+At position 7 to 62, the domain is characterized as SANT.
+At position 570 to 837, the domain is characterized as Protein kinase.
+At position 1 to 215, the domain is characterized as Radical SAM core.
+At position 16 to 130, the domain is characterized as CUB 1.
+At position 131 to 172, the domain is characterized as EGF-like; calcium-binding.
+At position 175 to 290, the domain is characterized as CUB 2.
+At position 292 to 356, the domain is characterized as Sushi 1.
+At position 357 to 423, the domain is characterized as Sushi 2.
+At position 438 to 680, the domain is characterized as Peptidase S1.
+At position 50 to 329, the domain is characterized as CN hydrolase.
+At position 1391 to 1963, the domain is characterized as FAT.
+At position 2206 to 2529, the domain is characterized as PI3K/PI4K catalytic.
+At position 2533 to 2565, the domain is characterized as FATC.
+At position 396 to 468, the domain is characterized as HSA.
+At position 793 to 958, the domain is characterized as Helicase ATP-binding.
+At position 1333 to 1486, the domain is characterized as Helicase C-terminal.
+At position 34 to 167, the domain is characterized as Nudix hydrolase.
+At position 3 to 68, the domain is characterized as J.
+At position 707 to 964, the domain is characterized as Protein kinase.
+At position 4 to 118, the domain is characterized as MTTase N-terminal.
+At position 29 to 191, the domain is characterized as Chitin-binding type-4.
+At position 8 to 144, the domain is characterized as N-acetyltransferase.
+At position 227 to 328, the domain is characterized as HTH araC/xylS-type.
+At position 10 to 53, the domain is characterized as Tudor-knot.
+At position 195 to 471, the domain is characterized as MYST-type HAT.
+At position 169 to 469, the domain is characterized as Protein kinase.
+At position 470 to 547, the domain is characterized as AGC-kinase C-terminal.
+At position 21 to 187, the domain is characterized as EngA-type G 1.
+At position 198 to 373, the domain is characterized as EngA-type G 2.
+At position 374 to 457, the domain is characterized as KH-like.
+At position 67 to 255, the domain is characterized as Rho-GAP.
+At position 821 to 934, the domain is characterized as PI3K-RBD.
+At position 1099 to 1271, the domain is characterized as C2 PI3K-type.
+At position 1326 to 1503, the domain is characterized as PIK helical.
+At position 1568 to 1845, the domain is characterized as PI3K/PI4K catalytic.
+At position 39 to 75, the domain is characterized as LRRNT.
+At position 353 to 442, the domain is characterized as Ig-like.
+At position 3 to 104, the domain is characterized as SSB.
+At position 49 to 145, the domain is characterized as Plastocyanin-like.
+At position 83 to 260, the domain is characterized as IRG-type G.
+At position 201 to 264, the domain is characterized as bZIP.
+At position 83 to 267, the domain is characterized as Helicase ATP-binding 1.
+At position 294 to 500, the domain is characterized as Helicase C-terminal 1.
+At position 576 to 849, the domain is characterized as SEC63 1.
+At position 898 to 1073, the domain is characterized as Helicase ATP-binding 2.
+At position 1106 to 1313, the domain is characterized as Helicase C-terminal 2.
+At position 1374 to 1481, the domain is characterized as SEC63 2.
+At position 147 to 405, the domain is characterized as Protein kinase.
+At position 172 to 222, the domain is characterized as HAMP.
+At position 237 to 446, the domain is characterized as Histidine kinase.
+At position 241 to 455, the domain is characterized as FAD-binding FR-type.
+At position 107 to 212, the domain is characterized as Rieske.
+At position 2 to 40, the domain is characterized as EGF-like.
+At position 36 to 254, the domain is characterized as Laminin N-terminal.
+At position 255 to 310, the domain is characterized as Laminin EGF-like 1.
+At position 311 to 373, the domain is characterized as Laminin EGF-like 2.
+At position 374 to 423, the domain is characterized as Laminin EGF-like 3.
+At position 441 to 577, the domain is characterized as NTR.
+At position 149 to 187, the domain is characterized as LRRCT.
+At position 2 to 67, the domain is characterized as HMA.
+At position 13 to 139, the domain is characterized as Arf-GAP.
+At position 643 to 706, the domain is characterized as SAM.
+At position 525 to 791, the domain is characterized as Protein kinase.
+At position 30 to 362, the domain is characterized as BPP.
+At position 102 to 272, the domain is characterized as CP-type G.
+At position 50 to 261, the domain is characterized as ThyX.
+At position 211 to 357, the domain is characterized as YDG.
+At position 432 to 492, the domain is characterized as Pre-SET.
+At position 495 to 639, the domain is characterized as SET.
+At position 654 to 670, the domain is characterized as Post-SET.
+At position 239 to 385, the domain is characterized as Exonuclease.
+At position 40 to 302, the domain is characterized as Pyruvate carboxyltransferase.
+At position 73 to 105, the domain is characterized as LisH.
+At position 25 to 165, the domain is characterized as SprT-like.
+At position 20 to 164, the domain is characterized as CheW-like.
+At position 5 to 60, the domain is characterized as HTH deoR-type.
+At position 5 to 68, the domain is characterized as J.
+At position 69 to 144, the domain is characterized as HTH CENPB-type.
+At position 128 to 226, the domain is characterized as PPIase FKBP-type.
+At position 9 to 182, the domain is characterized as Nudix hydrolase.
+At position 5 to 66, the domain is characterized as HTH asnC-type.
+At position 41 to 284, the domain is characterized as Peptidase S1.
+At position 160 to 338, the domain is characterized as OBG-type G.
+At position 85 to 259, the domain is characterized as Thioredoxin.
+At position 91 to 426, the domain is characterized as Kinesin motor.
+At position 28 to 73, the domain is characterized as F-box.
+At position 438 to 687, the domain is characterized as Protein kinase.
+At position 197 to 594, the domain is characterized as Peptidase S53.
+At position 404 to 498, the domain is characterized as SH2.
+At position 687 to 1003, the domain is characterized as Protein kinase.
+At position 63 to 353, the domain is characterized as tr-type G.
+At position 36 to 192, the domain is characterized as SIS.
+At position 326 to 607, the domain is characterized as ABC transmembrane type-1 1.
+At position 641 to 864, the domain is characterized as ABC transporter 1.
+At position 957 to 1237, the domain is characterized as ABC transmembrane type-1 2.
+At position 1274 to 1508, the domain is characterized as ABC transporter 2.
+At position 45 to 250, the domain is characterized as Helicase ATP-binding.
+At position 284 to 438, the domain is characterized as Helicase C-terminal.
+At position 491 to 544, the domain is characterized as ATP-grasp.
+At position 19 to 277, the domain is characterized as GH16.
+At position 1 to 138, the domain is characterized as N-acetyltransferase.
+At position 106 to 461, the domain is characterized as HAP1 N-terminal.
+At position 42 to 425, the domain is characterized as GH18.
+At position 438 to 498, the domain is characterized as Chitin-binding type-3.
+At position 1 to 103, the domain is characterized as PTS EIIB type-2.
+At position 41 to 138, the domain is characterized as Yippee.
+At position 103 to 132, the domain is characterized as IQ 1.
+At position 926 to 955, the domain is characterized as IQ 2.
+At position 956 to 978, the domain is characterized as IQ 3.
+At position 979 to 1001, the domain is characterized as IQ 4.
+At position 1113 to 1142, the domain is characterized as IQ 5.
+At position 1143 to 1165, the domain is characterized as IQ 6.
+At position 30 to 564, the domain is characterized as PLA2c.
+At position 255 to 290, the domain is characterized as DMA.
+At position 150 to 385, the domain is characterized as Radical SAM core.
+At position 509 to 554, the domain is characterized as KASH.
+At position 2 to 91, the domain is characterized as CARD.
+At position 182 to 466, the domain is characterized as NB-ARC.
+At position 997 to 1066, the domain is characterized as HMA.
+At position 45 to 106, the domain is characterized as Chitin-binding type R&R.
+At position 161 to 249, the domain is characterized as PPIase FKBP-type.
+At position 555 to 716, the domain is characterized as SUN.
+At position 187 to 330, the domain is characterized as FCP1 homology.
+At position 196 to 357, the domain is characterized as SUN.
+At position 606 to 784, the domain is characterized as Helicase ATP-binding.
+At position 811 to 961, the domain is characterized as Helicase C-terminal.
+At position 46 to 108, the domain is characterized as SH3.
+At position 120 to 209, the domain is characterized as SH2.
+At position 233 to 481, the domain is characterized as Protein kinase.
+At position 882 to 911, the domain is characterized as IQ 3.
+At position 37 to 202, the domain is characterized as FAD-binding PCMH-type.
+At position 21 to 59, the domain is characterized as SANT.
+At position 146 to 254, the domain is characterized as BTB.
+At position 1 to 142, the domain is characterized as HTH marR-type.
+At position 46 to 167, the domain is characterized as PX.
+At position 473 to 579, the domain is characterized as SET.
+At position 39 to 372, the domain is characterized as GH10.
+At position 418 to 571, the domain is characterized as CBM3.
+At position 24 to 88, the domain is characterized as LCN-type CS-alpha/beta.
+At position 672 to 760, the domain is characterized as PDZ.
+At position 978 to 1145, the domain is characterized as Guanylate kinase-like.
+At position 21 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 145 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 246 to 348, the domain is characterized as Ig-like C2-type 3.
+At position 471 to 760, the domain is characterized as Protein kinase.
+At position 59 to 346, the domain is characterized as Dynamin-type G.
+At position 1 to 367, the domain is characterized as Trm1 methyltransferase.
+At position 12 to 95, the domain is characterized as GIY-YIG.
+At position 178 to 248, the domain is characterized as PAH 1.
+At position 345 to 415, the domain is characterized as PAH 2.
+At position 504 to 576, the domain is characterized as PAH 3.
+At position 255 to 402, the domain is characterized as Helicase C-terminal.
+At position 231 to 459, the domain is characterized as AB hydrolase-1.
+At position 52 to 178, the domain is characterized as TBDR plug.
+At position 189 to 944, the domain is characterized as TBDR beta-barrel.
+At position 143 to 326, the domain is characterized as tr-type G.
+At position 259 to 341, the domain is characterized as IPT/TIG.
+At position 119 to 666, the domain is characterized as Ferric oxidoreductase.
+At position 147 to 247, the domain is characterized as Fibronectin type-III.
+At position 29 to 260, the domain is characterized as Peptidase S1.
+At position 15 to 701, the domain is characterized as Myosin motor.
+At position 704 to 727, the domain is characterized as IQ 1.
+At position 728 to 749, the domain is characterized as IQ 2.
+At position 750 to 778, the domain is characterized as IQ 3.
+At position 780 to 807, the domain is characterized as IQ 4.
+At position 808 to 837, the domain is characterized as IQ 5.
+At position 923 to 1107, the domain is characterized as TH1.
+At position 214 to 234, the domain is characterized as ELK.
+At position 47 to 243, the domain is characterized as BPL/LPL catalytic.
+At position 491 to 678, the domain is characterized as Helicase C-terminal.
+At position 30 to 105, the domain is characterized as DEP.
+At position 219 to 280, the domain is characterized as G protein gamma.
+At position 295 to 416, the domain is characterized as RGS.
+At position 272 to 440, the domain is characterized as Helicase ATP-binding.
+At position 608 to 784, the domain is characterized as Helicase C-terminal.
+At position 436 to 529, the domain is characterized as PDZ.
+At position 1078 to 1140, the domain is characterized as SAM.
+At position 261 to 342, the domain is characterized as SPOR.
+At position 1 to 75, the domain is characterized as GIY-YIG.
+At position 31 to 219, the domain is characterized as GH11.
+At position 381 to 416, the domain is characterized as EF-hand.
+At position 148 to 477, the domain is characterized as Protein kinase.
+At position 56 to 73, the domain is characterized as WH2.
+At position 50 to 88, the domain is characterized as Collagen-like.
+At position 117 to 334, the domain is characterized as Fibrinogen C-terminal.
+At position 632 to 831, the domain is characterized as Lon proteolytic.
+At position 232 to 478, the domain is characterized as Ku.
+At position 458 to 562, the domain is characterized as CBM2.
+At position 159 to 336, the domain is characterized as OBG-type G.
+At position 356 to 434, the domain is characterized as OCT.
+At position 233 to 463, the domain is characterized as ABC transporter.
+At position 3 to 185, the domain is characterized as Guanylate kinase-like.
+At position 453 to 524, the domain is characterized as RH2.
+At position 479 to 705, the domain is characterized as ABC transporter.
+At position 142 to 430, the domain is characterized as AB hydrolase-1.
+At position 561 to 607, the domain is characterized as EGF-like.
+At position 3 to 70, the domain is characterized as J.
+At position 249 to 435, the domain is characterized as GATase cobBQ-type.
+At position 105 to 211, the domain is characterized as C-type lectin.
+At position 31 to 131, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 230 to 318, the domain is characterized as Ig-like C2-type 3.
+At position 323 to 423, the domain is characterized as Ig-like C2-type 4.
+At position 428 to 520, the domain is characterized as Ig-like C2-type 5.
+At position 524 to 622, the domain is characterized as Fibronectin type-III 1.
+At position 638 to 738, the domain is characterized as Fibronectin type-III 2.
+At position 53 to 120, the domain is characterized as BTB.
+At position 155 to 256, the domain is characterized as BACK.
+At position 168 to 396, the domain is characterized as MIF4G 1.
+At position 571 to 755, the domain is characterized as MIF4G 2.
+At position 774 to 984, the domain is characterized as MIF4G 3.
+At position 166 to 392, the domain is characterized as Sigma-54 factor interaction.
+At position 107 to 277, the domain is characterized as CP-type G.
+At position 120 to 239, the domain is characterized as MRH.
+At position 57 to 368, the domain is characterized as PPM-type phosphatase.
+At position 85 to 242, the domain is characterized as CP-type G.
+At position 158 to 314, the domain is characterized as Helicase ATP-binding.
+At position 393 to 597, the domain is characterized as Helicase C-terminal.
+At position 363 to 434, the domain is characterized as TRAM.
+At position 3 to 74, the domain is characterized as HTH HARE-type.
+At position 1302 to 1664, the domain is characterized as Protein kinase.
+At position 563 to 707, the domain is characterized as MOSC.
+At position 8 to 70, the domain is characterized as J.
+At position 225 to 409, the domain is characterized as FAD-binding PCMH-type.
+At position 169 to 346, the domain is characterized as OBG-type G.
+At position 6 to 450, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 965 to 1280, the domain is characterized as PKS/mFAS DH.
+At position 2556 to 2635, the domain is characterized as Carrier.
+At position 54 to 117, the domain is characterized as SLH 1.
+At position 118 to 181, the domain is characterized as SLH 2.
+At position 182 to 231, the domain is characterized as SLH 3.
+At position 226 to 285, the domain is characterized as SH3.
+At position 45 to 133, the domain is characterized as PPIase FKBP-type.
+At position 27 to 156, the domain is characterized as Thioredoxin.
+At position 11 to 81, the domain is characterized as RRM.
+At position 142 to 388, the domain is characterized as Radical SAM core.
+At position 390 to 453, the domain is characterized as TRAM.
+At position 40 to 127, the domain is characterized as Cadherin 1.
+At position 128 to 240, the domain is characterized as Cadherin 2.
+At position 252 to 357, the domain is characterized as Cadherin 3.
+At position 358 to 462, the domain is characterized as Cadherin 4.
+At position 72 to 194, the domain is characterized as CMP/dCMP-type deaminase.
+At position 116 to 383, the domain is characterized as Protein kinase.
+At position 381 to 441, the domain is characterized as SH3.
+At position 607 to 902, the domain is characterized as Protein kinase.
+At position 119 to 196, the domain is characterized as PDZ.
+At position 11 to 260, the domain is characterized as Lon N-terminal.
+At position 729 to 916, the domain is characterized as Lon proteolytic.
+At position 1781 to 1853, the domain is characterized as RRM.
+At position 86 to 132, the domain is characterized as G-patch.
+At position 230 to 449, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 751 to 785, the domain is characterized as WW.
+At position 341 to 553, the domain is characterized as BPL/LPL catalytic.
+At position 6 to 112, the domain is characterized as HTH APSES-type.
+At position 49 to 134, the domain is characterized as PAN.
+At position 22 to 82, the domain is characterized as SH3.
+At position 84 to 175, the domain is characterized as SH2.
+At position 66 to 282, the domain is characterized as Radical SAM core.
+At position 640 to 709, the domain is characterized as S1 motif.
+At position 23 to 236, the domain is characterized as RNase H type-2.
+At position 7 to 124, the domain is characterized as MATH.
+At position 148 to 215, the domain is characterized as BTB 1.
+At position 304 to 368, the domain is characterized as BTB 2.
+At position 961 to 1127, the domain is characterized as PNPLA.
+At position 75 to 245, the domain is characterized as uDENN.
+At position 268 to 400, the domain is characterized as cDENN.
+At position 402 to 506, the domain is characterized as dDENN.
+At position 112 to 193, the domain is characterized as PRC barrel.
+At position 186 to 269, the domain is characterized as PDZ.
+At position 65 to 109, the domain is characterized as CWF21.
+At position 1372 to 1661, the domain is characterized as Protein kinase.
+At position 43 to 173, the domain is characterized as DOMON.
+At position 180 to 380, the domain is characterized as Cytochrome b561.
+At position 33 to 150, the domain is characterized as FZ.
+At position 178 to 298, the domain is characterized as NTR.
+At position 72 to 337, the domain is characterized as Reverse transcriptase.
+At position 135 to 235, the domain is characterized as HTH LytTR-type.
+At position 319 to 379, the domain is characterized as SAM.
+At position 88 to 214, the domain is characterized as Thioredoxin 1.
+At position 618 to 768, the domain is characterized as Thioredoxin 2.
+At position 46 to 213, the domain is characterized as SprT-like.
+At position 248 to 567, the domain is characterized as Peptidase A1.
+At position 87 to 148, the domain is characterized as SH3.
+At position 154 to 251, the domain is characterized as SH2.
+At position 273 to 526, the domain is characterized as Protein kinase.
+At position 54 to 312, the domain is characterized as Protein kinase.
+At position 355 to 390, the domain is characterized as EF-hand 1.
+At position 391 to 426, the domain is characterized as EF-hand 2.
+At position 427 to 462, the domain is characterized as EF-hand 3.
+At position 463 to 498, the domain is characterized as EF-hand 4.
+At position 379 to 456, the domain is characterized as BAG.
+At position 230 to 265, the domain is characterized as EF-hand 6.
+At position 163 to 479, the domain is characterized as Protein kinase.
+At position 15 to 300, the domain is characterized as Protein kinase.
+At position 22 to 196, the domain is characterized as Exonuclease.
+At position 9 to 252, the domain is characterized as ABC transporter.
+At position 284 to 394, the domain is characterized as DEUBAD.
+At position 87 to 270, the domain is characterized as CRAL-TRIO.
+At position 304 to 399, the domain is characterized as GOLD.
+At position 101 to 402, the domain is characterized as SAM-dependent MTase C5-type.
+At position 754 to 1043, the domain is characterized as Protein kinase.
+At position 1044 to 1144, the domain is characterized as AGC-kinase C-terminal.
+At position 33 to 227, the domain is characterized as GH11.
+At position 250 to 370, the domain is characterized as CBM6 1.
+At position 387 to 507, the domain is characterized as CBM6 2.
+At position 527 to 647, the domain is characterized as CBM6 3.
+At position 10 to 188, the domain is characterized as Ku.
+At position 19 to 65, the domain is characterized as UMA.
+At position 340 to 381, the domain is characterized as UBA 1.
+At position 403 to 449, the domain is characterized as UBA 2.
+At position 20 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1444 to 1534, the domain is characterized as PDZ.
+At position 141 to 468, the domain is characterized as Peptidase S8.
+At position 484 to 595, the domain is characterized as P/Homo B.
+At position 181 to 440, the domain is characterized as Pterin-binding.
+At position 92 to 344, the domain is characterized as Radical SAM core 1.
+At position 555 to 796, the domain is characterized as Radical SAM core 2.
+At position 78 to 137, the domain is characterized as Tudor.
+At position 711 to 1018, the domain is characterized as Protein kinase.
+At position 95 to 175, the domain is characterized as RRM 2.
+At position 377 to 455, the domain is characterized as RRM 3.
+At position 112 to 227, the domain is characterized as C-type lectin.
+At position 1 to 254, the domain is characterized as IMD.
+At position 731 to 748, the domain is characterized as WH2.
+At position 717 to 1013, the domain is characterized as Protein kinase.
+At position 1086 to 1215, the domain is characterized as Guanylate cyclase.
+At position 452 to 648, the domain is characterized as FtsK.
+At position 4 to 106, the domain is characterized as FAD-binding FR-type.
+At position 232 to 317, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 409 to 789, the domain is characterized as USP.
+At position 50 to 234, the domain is characterized as ABC transmembrane type-1.
+At position 26 to 239, the domain is characterized as GH16.
+At position 54 to 417, the domain is characterized as Kinesin motor.
+At position 31 to 186, the domain is characterized as N-acetyltransferase.
+At position 227 to 384, the domain is characterized as TrmE-type G.
+At position 18 to 107, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 253 to 447, the domain is characterized as FAD-binding PCMH-type.
+At position 271 to 366, the domain is characterized as PPIase FKBP-type.
+At position 232 to 328, the domain is characterized as CRM 1.
+At position 350 to 446, the domain is characterized as CRM 2.
+At position 170 to 241, the domain is characterized as Glutaredoxin.
+At position 68 to 271, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 96, the domain is characterized as ADD.
+At position 47 to 148, the domain is characterized as AB hydrolase-1.
+At position 307 to 588, the domain is characterized as ABC transmembrane type-1 1.
+At position 622 to 845, the domain is characterized as ABC transporter 1.
+At position 949 to 1231, the domain is characterized as ABC transmembrane type-1 2.
+At position 1268 to 1502, the domain is characterized as ABC transporter 2.
+At position 217 to 461, the domain is characterized as NR LBD.
+At position 10 to 381, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 861 to 1171, the domain is characterized as PKS/mFAS DH.
+At position 2373 to 2450, the domain is characterized as Carrier.
+At position 481 to 595, the domain is characterized as CFEM.
+At position 43 to 157, the domain is characterized as PX.
+At position 15 to 141, the domain is characterized as CMP/dCMP-type deaminase.
+At position 507 to 820, the domain is characterized as CNH.
+At position 211 to 294, the domain is characterized as HTH OST-type.
+At position 317 to 392, the domain is characterized as RRM.
+At position 32 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 129 to 211, the domain is characterized as Ig-like C2-type 2.
+At position 215 to 302, the domain is characterized as Ig-like C2-type 3.
+At position 1 to 121, the domain is characterized as PINc.
+At position 20 to 322, the domain is characterized as FERM.
+At position 211 to 377, the domain is characterized as Helicase ATP-binding.
+At position 447 to 638, the domain is characterized as Helicase C-terminal.
+At position 106 to 506, the domain is characterized as PPM-type phosphatase.
+At position 61 to 440, the domain is characterized as PRONE.
+At position 4 to 327, the domain is characterized as Kinesin motor.
+At position 43 to 420, the domain is characterized as PIPK.
+At position 25 to 87, the domain is characterized as FHA.
+At position 115 to 190, the domain is characterized as BRCT.
+At position 6 to 133, the domain is characterized as RNase III.
+At position 246 to 338, the domain is characterized as PAZ.
+At position 514 to 834, the domain is characterized as Piwi.
+At position 535 to 607, the domain is characterized as Tudor 1.
+At position 634 to 691, the domain is characterized as Tudor 2.
+At position 811 to 877, the domain is characterized as MBD.
+At position 939 to 1011, the domain is characterized as Pre-SET.
+At position 1014 to 1229, the domain is characterized as SET.
+At position 1238 to 1254, the domain is characterized as Post-SET.
+At position 99 to 291, the domain is characterized as ATP-grasp.
+At position 295 to 337, the domain is characterized as CCT.
+At position 2 to 253, the domain is characterized as Chorismate mutase.
+At position 30 to 309, the domain is characterized as Tyrosine-protein phosphatase.
+At position 8 to 309, the domain is characterized as Hcy-binding.
+At position 218 to 288, the domain is characterized as PAC.
+At position 336 to 657, the domain is characterized as Single-minded C-terminal.
+At position 3 to 285, the domain is characterized as Protein kinase.
+At position 173 to 222, the domain is characterized as bHLH.
+At position 32 to 384, the domain is characterized as Protein kinase.
+At position 316 to 404, the domain is characterized as BRCT 1.
+At position 538 to 629, the domain is characterized as BRCT 2.
+At position 54 to 116, the domain is characterized as LIM zinc-binding 1.
+At position 117 to 179, the domain is characterized as LIM zinc-binding 2.
+At position 247 to 280, the domain is characterized as EGF-like; atypical.
+At position 299 to 381, the domain is characterized as PAN.
+At position 454 to 721, the domain is characterized as Protein kinase.
+At position 2 to 76, the domain is characterized as SH3 1.
+At position 77 to 142, the domain is characterized as SH3 2.
+At position 367 to 427, the domain is characterized as SH3 3.
+At position 1011 to 1176, the domain is characterized as PNPLA.
+At position 26 to 55, the domain is characterized as IQ.
+At position 28 to 253, the domain is characterized as Peptidase S1.
+At position 139 to 227, the domain is characterized as Rieske.
+At position 873 to 936, the domain is characterized as SAM.
+At position 959 to 1164, the domain is characterized as PARP catalytic.
+At position 555 to 742, the domain is characterized as SEC7.
+At position 49 to 476, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 871 to 1155, the domain is characterized as PKS/mFAS DH.
+At position 2016 to 2092, the domain is characterized as Carrier.
+At position 217 to 345, the domain is characterized as OmpA-like.
+At position 4 to 436, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 931 to 1230, the domain is characterized as PKS/mFAS DH.
+At position 2351 to 2428, the domain is characterized as Carrier.
+At position 138 to 341, the domain is characterized as ATP-grasp.
+At position 207 to 384, the domain is characterized as PCI.
+At position 165 to 316, the domain is characterized as JmjC.
+At position 67 to 106, the domain is characterized as EGF-like 1.
+At position 108 to 144, the domain is characterized as EGF-like 2; calcium-binding.
+At position 146 to 182, the domain is characterized as EGF-like 3; calcium-binding.
+At position 184 to 221, the domain is characterized as EGF-like 4; calcium-binding.
+At position 223 to 259, the domain is characterized as EGF-like 5.
+At position 261 to 318, the domain is characterized as EGF-like 6.
+At position 320 to 356, the domain is characterized as EGF-like 7; calcium-binding.
+At position 358 to 394, the domain is characterized as EGF-like 8; calcium-binding.
+At position 396 to 436, the domain is characterized as EGF-like 9.
+At position 431 to 603, the domain is characterized as Laminin G-like 1.
+At position 605 to 641, the domain is characterized as EGF-like 10.
+At position 647 to 805, the domain is characterized as Laminin G-like 2.
+At position 807 to 843, the domain is characterized as EGF-like 11.
+At position 871 to 1054, the domain is characterized as Laminin G-like 3.
+At position 1056 to 1092, the domain is characterized as EGF-like 12.
+At position 1094 to 1130, the domain is characterized as EGF-like 13.
+At position 1134 to 1171, the domain is characterized as EGF-like 14.
+At position 1173 to 1209, the domain is characterized as EGF-like 15.
+At position 22 to 317, the domain is characterized as Protein kinase.
+At position 7 to 145, the domain is characterized as DAC.
+At position 1 to 105, the domain is characterized as SSB.
+At position 123 to 211, the domain is characterized as Ig-like C1-type.
+At position 233 to 308, the domain is characterized as bZIP.
+At position 78 to 267, the domain is characterized as Macro 1.
+At position 293 to 464, the domain is characterized as Macro 2.
+At position 482 to 678, the domain is characterized as PARP catalytic.
+At position 951 to 1096, the domain is characterized as MGS-like.
+At position 33 to 82, the domain is characterized as TSP type-1 1.
+At position 376 to 424, the domain is characterized as TSP type-1 2.
+At position 436 to 493, the domain is characterized as TSP type-1 3.
+At position 522 to 584, the domain is characterized as TSP type-1 4.
+At position 607 to 665, the domain is characterized as TSP type-1 5.
+At position 666 to 729, the domain is characterized as TSP type-1 6.
+At position 788 to 850, the domain is characterized as TSP type-1 7.
+At position 861 to 963, the domain is characterized as Ig-like C2-type 1.
+At position 1164 to 1266, the domain is characterized as Ig-like C2-type 2.
+At position 1286 to 1369, the domain is characterized as Ig-like C2-type 3.
+At position 1395 to 1485, the domain is characterized as Ig-like C2-type 4.
+At position 1545 to 1608, the domain is characterized as TSP type-1 8.
+At position 1666 to 1726, the domain is characterized as TSP type-1 9.
+At position 1726 to 1762, the domain is characterized as PLAC.
+At position 82 to 248, the domain is characterized as Bms1-type G.
+At position 438 to 607, the domain is characterized as tr-type G.
+At position 127 to 204, the domain is characterized as SPOR.
+At position 21 to 351, the domain is characterized as SET.
+At position 384 to 419, the domain is characterized as EF-hand.
+At position 652 to 750, the domain is characterized as Fibronectin type-III 1.
+At position 780 to 869, the domain is characterized as Fibronectin type-III 2.
+At position 880 to 971, the domain is characterized as Fibronectin type-III 3.
+At position 1044 to 1315, the domain is characterized as Protein kinase.
+At position 480 to 607, the domain is characterized as Guanylate cyclase.
+At position 165 to 211, the domain is characterized as F-box.
+At position 361 to 653, the domain is characterized as Protein kinase.
+At position 72 to 230, the domain is characterized as CP-type G.
+At position 23 to 203, the domain is characterized as Thioredoxin.
+At position 567 to 618, the domain is characterized as GPS.
+At position 34 to 356, the domain is characterized as G-alpha.
+At position 180 to 236, the domain is characterized as HAMP.
+At position 268 to 400, the domain is characterized as GGDEF.
+At position 409 to 662, the domain is characterized as EAL.
+At position 15 to 76, the domain is characterized as S4 RNA-binding.
+At position 2 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 579 to 668, the domain is characterized as BRCT.
+At position 23 to 149, the domain is characterized as RNase III.
+At position 417 to 651, the domain is characterized as UmuC.
+At position 169 to 256, the domain is characterized as 5'-3' exonuclease.
+At position 168 to 252, the domain is characterized as Doublecortin 1.
+At position 702 to 800, the domain is characterized as Ricin B-type lectin 1.
+At position 925 to 1015, the domain is characterized as Doublecortin 2.
+At position 1151 to 1266, the domain is characterized as Ricin B-type lectin 2.
+At position 89 to 214, the domain is characterized as GST C-terminal.
+At position 153 to 187, the domain is characterized as SAP.
+At position 324 to 380, the domain is characterized as DEK-C.
+At position 91 to 131, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 132 to 174, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 93 to 137, the domain is characterized as bZIP.
+At position 162 to 382, the domain is characterized as DOG1.
+At position 27 to 216, the domain is characterized as Glutamine amidotransferase type-1.
+At position 217 to 435, the domain is characterized as GMPS ATP-PPase.
+At position 285 to 334, the domain is characterized as bHLH.
+At position 12 to 142, the domain is characterized as MPN.
+At position 698 to 789, the domain is characterized as FDX-ACB.
+At position 88 to 267, the domain is characterized as VWFA.
+At position 31 to 217, the domain is characterized as BPL/LPL catalytic.
+At position 536 to 810, the domain is characterized as Protein kinase.
+At position 8 to 56, the domain is characterized as F-box.
+At position 10 to 79, the domain is characterized as HTH merR-type.
+At position 26 to 130, the domain is characterized as PTS EIIA type-1.
+At position 492 to 668, the domain is characterized as Helicase C-terminal.
+At position 3 to 192, the domain is characterized as RNase H type-2.
+At position 458 to 603, the domain is characterized as Helicase C-terminal.
+At position 807 to 888, the domain is characterized as HRDC.
+At position 231 to 281, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 287 to 337, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 28 to 88, the domain is characterized as LIM zinc-binding 1.
+At position 98 to 148, the domain is characterized as LIM zinc-binding 2.
+At position 155 to 184, the domain is characterized as LIM zinc-binding 3; truncated.
+At position 419 to 474, the domain is characterized as LIM zinc-binding 4.
+At position 730 to 953, the domain is characterized as Rho-GAP.
+At position 65 to 217, the domain is characterized as Cupin type-1.
+At position 387 to 606, the domain is characterized as FtsK.
+At position 10 to 153, the domain is characterized as Jacalin-type lectin.
+At position 890 to 955, the domain is characterized as HP.
+At position 20 to 61, the domain is characterized as UBA 1.
+At position 120 to 140, the domain is characterized as UBA 2.
+At position 204 to 431, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 10 to 349, the domain is characterized as YjeF C-terminal.
+At position 12 to 87, the domain is characterized as GIY-YIG.
+At position 14 to 230, the domain is characterized as ABC transporter.
+At position 50 to 170, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 189 to 297, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 368 to 489, the domain is characterized as MATH.
+At position 21 to 121, the domain is characterized as Ig-like V-type.
+At position 44 to 324, the domain is characterized as GH10.
+At position 25 to 414, the domain is characterized as Helicase ATP-binding.
+At position 1 to 163, the domain is characterized as Peptidase S1.
+At position 1 to 131, the domain is characterized as Jacalin-type lectin 1.
+At position 145 to 289, the domain is characterized as Jacalin-type lectin 2.
+At position 313 to 457, the domain is characterized as Jacalin-type lectin 3.
+At position 10 to 148, the domain is characterized as DAC.
+At position 20 to 128, the domain is characterized as Ig-like.
+At position 49 to 126, the domain is characterized as VWFC 1.
+At position 171 to 280, the domain is characterized as CHRD 1.
+At position 282 to 401, the domain is characterized as CHRD 2.
+At position 402 to 523, the domain is characterized as CHRD 3.
+At position 529 to 649, the domain is characterized as CHRD 4.
+At position 702 to 762, the domain is characterized as VWFC 2.
+At position 782 to 848, the domain is characterized as VWFC 3.
+At position 870 to 930, the domain is characterized as VWFC 4.
+At position 672 to 960, the domain is characterized as ABC transmembrane type-1 2.
+At position 995 to 1233, the domain is characterized as ABC transporter 2.
+At position 15 to 122, the domain is characterized as FAD-binding FR-type.
+At position 293 to 575, the domain is characterized as ABC transmembrane type-1.
+At position 610 to 843, the domain is characterized as ABC transporter.
+At position 35 to 98, the domain is characterized as Kazal-like.
+At position 134 to 160, the domain is characterized as PLD phosphodiesterase 1.
+At position 356 to 383, the domain is characterized as PLD phosphodiesterase 2.
+At position 209 to 313, the domain is characterized as PB1.
+At position 373 to 424, the domain is characterized as FBD.
+At position 56 to 419, the domain is characterized as Protein kinase.
+At position 447 to 652, the domain is characterized as Helicase ATP-binding.
+At position 914 to 1072, the domain is characterized as Helicase C-terminal.
+At position 30 to 199, the domain is characterized as EngA-type G 1.
+At position 227 to 403, the domain is characterized as EngA-type G 2.
+At position 404 to 488, the domain is characterized as KH-like.
+At position 5 to 194, the domain is characterized as Phosphatase tensin-type.
+At position 200 to 337, the domain is characterized as C2 tensin-type.
+At position 1188 to 1588, the domain is characterized as FH2.
+At position 492 to 568, the domain is characterized as Carrier.
+At position 13 to 258, the domain is characterized as Radical SAM core.
+At position 275 to 351, the domain is characterized as Ubiquitin-like.
+At position 28 to 211, the domain is characterized as BPL/LPL catalytic.
+At position 397 to 567, the domain is characterized as tr-type G.
+At position 340 to 491, the domain is characterized as PI-PLC X-box.
+At position 758 to 874, the domain is characterized as PI-PLC Y-box.
+At position 877 to 1002, the domain is characterized as C2.
+At position 1 to 75, the domain is characterized as GST N-terminal.
+At position 72 to 199, the domain is characterized as GST C-terminal.
+At position 844 to 900, the domain is characterized as WHEP-TRS.
+At position 74 to 109, the domain is characterized as EF-hand 1.
+At position 125 to 142, the domain is characterized as EF-hand 2.
+At position 148 to 183, the domain is characterized as EF-hand 3.
+At position 185 to 216, the domain is characterized as EF-hand 4.
+At position 330 to 519, the domain is characterized as Protein kinase.
+At position 1 to 175, the domain is characterized as N-acetyltransferase.
+At position 469 to 729, the domain is characterized as Protein kinase.
+At position 730 to 780, the domain is characterized as AGC-kinase C-terminal.
+At position 24 to 288, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 8 to 282, the domain is characterized as CN hydrolase.
+At position 211 to 311, the domain is characterized as Fe2OG dioxygenase.
+At position 507 to 685, the domain is characterized as Helicase ATP-binding.
+At position 697 to 861, the domain is characterized as Helicase C-terminal.
+At position 12 to 83, the domain is characterized as KRAB.
+At position 260 to 342, the domain is characterized as Toprim.
+At position 2 to 120, the domain is characterized as Response regulatory.
+At position 549 to 682, the domain is characterized as N-acetyltransferase.
+At position 212 to 279, the domain is characterized as BTB.
+At position 120 to 398, the domain is characterized as Protein kinase.
+At position 1015 to 1064, the domain is characterized as KA1.
+At position 190 to 252, the domain is characterized as t-SNARE coiled-coil homology.
+At position 45 to 97, the domain is characterized as TSP type-1.
+At position 360 to 479, the domain is characterized as NTR.
+At position 42 to 154, the domain is characterized as Expansin-like EG45.
+At position 164 to 243, the domain is characterized as Expansin-like CBD.
+At position 196 to 297, the domain is characterized as HTH araC/xylS-type.
+At position 42 to 100, the domain is characterized as HTH cro/C1-type.
+At position 51 to 77, the domain is characterized as PAS.
+At position 102 to 156, the domain is characterized as PAC.
+At position 159 to 224, the domain is characterized as HTH luxR-type.
+At position 899 to 1109, the domain is characterized as START.
+At position 1 to 94, the domain is characterized as FAD-binding FR-type.
+At position 37 to 107, the domain is characterized as Ig-like.
+At position 173 to 200, the domain is characterized as ITAM.
+At position 37 to 296, the domain is characterized as Alpha-carbonic anhydrase.
+At position 5 to 67, the domain is characterized as HTH iclR-type.
+At position 82 to 251, the domain is characterized as IclR-ED.
+At position 47 to 129, the domain is characterized as Lipoyl-binding.
+At position 346 to 506, the domain is characterized as Helicase C-terminal.
+At position 235 to 461, the domain is characterized as CN hydrolase.
+At position 157 to 317, the domain is characterized as CRAL-TRIO.
+At position 7 to 44, the domain is characterized as UBA-like.
+At position 49 to 239, the domain is characterized as DCUN1.
+At position 265 to 556, the domain is characterized as ABC transmembrane type-1.
+At position 590 to 824, the domain is characterized as ABC transporter.
+At position 7 to 172, the domain is characterized as N-acetyltransferase.
+At position 97 to 204, the domain is characterized as PET.
+At position 236 to 299, the domain is characterized as LIM zinc-binding 1.
+At position 301 to 361, the domain is characterized as LIM zinc-binding 2.
+At position 364 to 423, the domain is characterized as LIM zinc-binding 3.
+At position 472 to 642, the domain is characterized as tr-type G.
+At position 572 to 624, the domain is characterized as F-box.
+At position 142 to 380, the domain is characterized as ABC transmembrane type-1 1.
+At position 471 to 697, the domain is characterized as ABC transporter 1.
+At position 752 to 1031, the domain is characterized as ABC transmembrane type-1 2.
+At position 1069 to 1300, the domain is characterized as ABC transporter 2.
+At position 5 to 101, the domain is characterized as SH2.
+At position 209 to 522, the domain is characterized as Protein kinase.
+At position 39 to 168, the domain is characterized as Galectin.
+At position 184 to 450, the domain is characterized as MHD.
+At position 11 to 136, the domain is characterized as Fatty acid hydroxylase.
+At position 426 to 477, the domain is characterized as Rubredoxin-like.
+At position 37 to 75, the domain is characterized as EGF-like.
+At position 82 to 163, the domain is characterized as Kringle.
+At position 180 to 430, the domain is characterized as Peptidase S1.
+At position 368 to 534, the domain is characterized as N-acetyltransferase.
+At position 83 to 264, the domain is characterized as Brix.
+At position 1 to 367, the domain is characterized as TTL.
+At position 10 to 178, the domain is characterized as Era-type G.
+At position 201 to 285, the domain is characterized as KH type-2.
+At position 1 to 20, the domain is characterized as Peptidase M12A.
+At position 27 to 114, the domain is characterized as Ig-like V-type.
+At position 136 to 210, the domain is characterized as Ig-like C2-type.
+At position 21 to 171, the domain is characterized as OCP N-terminal.
+At position 70 to 296, the domain is characterized as RNase H type-2.
+At position 74 to 145, the domain is characterized as HTH iclR-type.
+At position 124 to 365, the domain is characterized as SMP-LTD.
+At position 131 to 368, the domain is characterized as Radical SAM core.
+At position 323 to 391, the domain is characterized as SB.
+At position 164 to 213, the domain is characterized as KH.
+At position 152 to 257, the domain is characterized as FAD-binding FR-type.
+At position 1 to 237, the domain is characterized as Radical SAM core.
+At position 72 to 313, the domain is characterized as AB hydrolase-1.
+At position 37 to 123, the domain is characterized as S4 RNA-binding.
+At position 226 to 509, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 54 to 128, the domain is characterized as RRM 1.
+At position 139 to 217, the domain is characterized as RRM 2.
+At position 260 to 335, the domain is characterized as RRM 3.
+At position 43 to 489, the domain is characterized as Trm1 methyltransferase.
+At position 13 to 66, the domain is characterized as SMP 1.
+At position 130 to 187, the domain is characterized as SMP 2.
+At position 195 to 253, the domain is characterized as SMP 3.
+At position 736 to 1258, the domain is characterized as USP.
+At position 160 to 335, the domain is characterized as Helicase ATP-binding.
+At position 347 to 512, the domain is characterized as Helicase C-terminal.
+At position 45 to 127, the domain is characterized as RRM 1.
+At position 206 to 296, the domain is characterized as RRM 2.
+At position 16 to 65, the domain is characterized as Myosin N-terminal SH3-like.
+At position 70 to 740, the domain is characterized as Myosin motor.
+At position 743 to 772, the domain is characterized as IQ 1.
+At position 766 to 795, the domain is characterized as IQ 2.
+At position 791 to 820, the domain is characterized as IQ 3.
+At position 814 to 843, the domain is characterized as IQ 4.
+At position 839 to 868, the domain is characterized as IQ 5.
+At position 862 to 891, the domain is characterized as IQ 6.
+At position 1168 to 1481, the domain is characterized as Dilute.
+At position 127 to 204, the domain is characterized as UBX.
+At position 30 to 296, the domain is characterized as Dynamin-type G.
+At position 519 to 624, the domain is characterized as PH.
+At position 653 to 744, the domain is characterized as GED.
+At position 60 to 212, the domain is characterized as Flavodoxin-like.
+At position 31 to 108, the domain is characterized as Ubiquitin-like.
+At position 13 to 112, the domain is characterized as PH.
+At position 22 to 69, the domain is characterized as CAP-Gly.
+At position 123 to 456, the domain is characterized as Protein kinase.
+At position 456 to 734, the domain is characterized as Protein kinase.
+At position 2 to 54, the domain is characterized as bHLH.
+At position 93 to 161, the domain is characterized as S4 RNA-binding.
+At position 120 to 433, the domain is characterized as PPM-type phosphatase.
+At position 1158 to 1228, the domain is characterized as Bromo 1.
+At position 1317 to 1412, the domain is characterized as Bromo 2.
+At position 21 to 130, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 798 to 827, the domain is characterized as IQ 1.
+At position 878 to 907, the domain is characterized as IQ 3.
+At position 85 to 177, the domain is characterized as Ig-like C1-type.
+At position 145 to 502, the domain is characterized as PDEase.
+At position 32 to 127, the domain is characterized as Ig-like V-type.
+At position 134 to 238, the domain is characterized as Ig-like C2-type.
+At position 197 to 296, the domain is characterized as Fe2OG dioxygenase.
+At position 26 to 49, the domain is characterized as IQ.
+At position 50 to 78, the domain is characterized as Collagen-like.
+At position 178 to 282, the domain is characterized as Fe2OG dioxygenase.
+At position 98 to 329, the domain is characterized as Radical SAM core.
+At position 8 to 96, the domain is characterized as MtN3/slv 1.
+At position 132 to 215, the domain is characterized as MtN3/slv 2.
+At position 39 to 122, the domain is characterized as Fibronectin type-III 1.
+At position 170 to 266, the domain is characterized as Fibronectin type-III 2.
+At position 270 to 358, the domain is characterized as Fibronectin type-III 3.
+At position 359 to 443, the domain is characterized as Fibronectin type-III 4.
+At position 444 to 527, the domain is characterized as Fibronectin type-III 5.
+At position 528 to 621, the domain is characterized as Fibronectin type-III 6.
+At position 622 to 718, the domain is characterized as Fibronectin type-III 7.
+At position 717 to 803, the domain is characterized as Fibronectin type-III 8.
+At position 942 to 1199, the domain is characterized as Tyrosine-protein phosphatase.
+At position 34 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 142 to 248, the domain is characterized as Gnk2-homologous 2.
+At position 275 to 546, the domain is characterized as Septin-type G.
+At position 1 to 204, the domain is characterized as YjeF N-terminal.
+At position 212 to 488, the domain is characterized as YjeF C-terminal.
+At position 36 to 146, the domain is characterized as Ig-like V-type.
+At position 6 to 70, the domain is characterized as SAM.
+At position 327 to 419, the domain is characterized as PH 1.
+At position 440 to 529, the domain is characterized as PH 2.
+At position 535 to 660, the domain is characterized as Arf-GAP.
+At position 743 to 850, the domain is characterized as PH 3.
+At position 954 to 1139, the domain is characterized as Rho-GAP.
+At position 1172 to 1261, the domain is characterized as Ras-associating.
+At position 1274 to 1396, the domain is characterized as PH 4.
+At position 1717 to 1992, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 2023 to 2282, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 33 to 282, the domain is characterized as AB hydrolase-1.
+At position 13 to 128, the domain is characterized as MTTase N-terminal.
+At position 153 to 382, the domain is characterized as Radical SAM core.
+At position 27 to 279, the domain is characterized as Protein kinase.
+At position 1116 to 1191, the domain is characterized as DEP.
+At position 4 to 73, the domain is characterized as Sm.
+At position 68 to 166, the domain is characterized as AD.
+At position 473 to 486, the domain is characterized as CRIB.
+At position 951 to 1203, the domain is characterized as Protein kinase.
+At position 112 to 181, the domain is characterized as PAN 1.
+At position 185 to 241, the domain is characterized as PAN 2.
+At position 287 to 467, the domain is characterized as Helicase ATP-binding.
+At position 502 to 661, the domain is characterized as Helicase C-terminal.
+At position 120 to 711, the domain is characterized as Lipoxygenase.
+At position 258 to 406, the domain is characterized as Ferric oxidoreductase.
+At position 72 to 369, the domain is characterized as Protein kinase.
+At position 39 to 92, the domain is characterized as Tudor-knot.
+At position 185 to 457, the domain is characterized as MYST-type HAT.
+At position 6 to 169, the domain is characterized as Exonuclease.
+At position 27 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 21 to 222, the domain is characterized as ABC transmembrane type-1.
+At position 158 to 303, the domain is characterized as TRUD.
+At position 1 to 48, the domain is characterized as J.
+At position 504 to 606, the domain is characterized as CXC.
+At position 613 to 728, the domain is characterized as SET.
+At position 4 to 185, the domain is characterized as PHTF.
+At position 27 to 70, the domain is characterized as CUE.
+At position 231 to 400, the domain is characterized as TrmE-type G.
+At position 477 to 513, the domain is characterized as CBM1.
+At position 14 to 177, the domain is characterized as Exonuclease.
+At position 263 to 405, the domain is characterized as Flavodoxin-like.
+At position 1 to 104, the domain is characterized as C2.
+At position 142 to 182, the domain is characterized as EGF-like.
+At position 175 to 280, the domain is characterized as Fe2OG dioxygenase.
+At position 15 to 86, the domain is characterized as PAS.
+At position 161 to 266, the domain is characterized as HTH LytTR-type.
+At position 154 to 191, the domain is characterized as EF-hand 4.
+At position 208 to 336, the domain is characterized as Nudix hydrolase.
+At position 73 to 386, the domain is characterized as Peptidase A1.
+At position 2 to 183, the domain is characterized as Guanylate kinase-like.
+At position 276 to 315, the domain is characterized as UBA.
+At position 405 to 504, the domain is characterized as RWD.
+At position 587 to 756, the domain is characterized as Helicase ATP-binding.
+At position 797 to 968, the domain is characterized as Helicase C-terminal.
+At position 21 to 277, the domain is characterized as Protein kinase.
+At position 4 to 38, the domain is characterized as SAP.
+At position 77 to 198, the domain is characterized as PX.
+At position 48 to 93, the domain is characterized as TSP type-1 1.
+At position 723 to 782, the domain is characterized as TSP type-1 2.
+At position 783 to 842, the domain is characterized as TSP type-1 3.
+At position 845 to 909, the domain is characterized as TSP type-1 4.
+At position 910 to 969, the domain is characterized as TSP type-1 5.
+At position 970 to 1026, the domain is characterized as TSP type-1 6.
+At position 1029 to 1066, the domain is characterized as PLAC.
+At position 33 to 79, the domain is characterized as F-box.
+At position 415 to 795, the domain is characterized as USP.
+At position 34 to 176, the domain is characterized as Peptidase C51.
+At position 40 to 130, the domain is characterized as Link.
+At position 202 to 399, the domain is characterized as Helicase ATP-binding.
+At position 452 to 615, the domain is characterized as Helicase C-terminal.
+At position 1 to 238, the domain is characterized as CN hydrolase.
+At position 94 to 404, the domain is characterized as IF rod.
+At position 609 to 690, the domain is characterized as RWP-RK.
+At position 844 to 927, the domain is characterized as PB1.
+At position 10 to 83, the domain is characterized as ACT.
+At position 63 to 189, the domain is characterized as DUF724.
+At position 33 to 174, the domain is characterized as MPN.
+At position 47 to 269, the domain is characterized as Radical SAM core.
+At position 431 to 565, the domain is characterized as DAGKc.
+At position 152 to 460, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 1 to 66, the domain is characterized as TRAM.
+At position 139 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 28 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 7 to 181, the domain is characterized as Era-type G.
+At position 212 to 290, the domain is characterized as KH type-2.
+At position 60 to 108, the domain is characterized as HTH myb-type 2.
+At position 6 to 170, the domain is characterized as Brix.
+At position 278 to 424, the domain is characterized as SIS 1.
+At position 448 to 596, the domain is characterized as SIS 2.
+At position 469 to 600, the domain is characterized as Ricin B-type lectin.
+At position 112 to 237, the domain is characterized as N-terminal Ras-GEF.
+At position 367 to 629, the domain is characterized as Ras-GEF.
+At position 779 to 866, the domain is characterized as Ras-associating.
+At position 33 to 172, the domain is characterized as WIF.
+At position 208 to 237, the domain is characterized as EGF-like 2.
+At position 237 to 269, the domain is characterized as EGF-like 3.
+At position 270 to 301, the domain is characterized as EGF-like 4.
+At position 302 to 333, the domain is characterized as EGF-like 5.
+At position 1 to 232, the domain is characterized as EAL.
+At position 226 to 413, the domain is characterized as HDOD.
+At position 30 to 128, the domain is characterized as Ig-like V-type.
+At position 930 to 1169, the domain is characterized as MyTH4 1.
+At position 1172 to 1212, the domain is characterized as Ras-associating.
+At position 1174 to 1485, the domain is characterized as FERM 1.
+At position 1480 to 1548, the domain is characterized as SH3.
+At position 1625 to 1773, the domain is characterized as MyTH4 2.
+At position 1779 to 2087, the domain is characterized as FERM 2.
+At position 248 to 475, the domain is characterized as Ku.
+At position 10 to 342, the domain is characterized as Kinesin motor.
+At position 98 to 159, the domain is characterized as KH 1.
+At position 192 to 253, the domain is characterized as KH 2.
+At position 698 to 880, the domain is characterized as Lon proteolytic.
+At position 22 to 142, the domain is characterized as C2 1.
+At position 181 to 305, the domain is characterized as C2 2.
+At position 346 to 474, the domain is characterized as C2 3.
+At position 330 to 482, the domain is characterized as YDG.
+At position 551 to 613, the domain is characterized as Pre-SET.
+At position 616 to 760, the domain is characterized as SET.
+At position 774 to 790, the domain is characterized as Post-SET.
+At position 61 to 207, the domain is characterized as UBC core.
+At position 100 to 163, the domain is characterized as bZIP.
+At position 606 to 670, the domain is characterized as SAM 1.
+At position 678 to 741, the domain is characterized as SAM 2.
+At position 763 to 835, the domain is characterized as SAM 3.
+At position 12 to 262, the domain is characterized as Protein kinase.
+At position 484 to 798, the domain is characterized as Protein kinase.
+At position 68 to 98, the domain is characterized as EF-hand.
+At position 1334 to 1709, the domain is characterized as PIPK.
+At position 545 to 603, the domain is characterized as LIM zinc-binding 1.
+At position 604 to 663, the domain is characterized as LIM zinc-binding 2.
+At position 664 to 723, the domain is characterized as LIM zinc-binding 3.
+At position 301 to 339, the domain is characterized as PLD phosphodiesterase 1.
+At position 610 to 637, the domain is characterized as PLD phosphodiesterase 2.
+At position 60 to 143, the domain is characterized as Saposin B-type 1.
+At position 193 to 277, the domain is characterized as Saposin B-type 2.
+At position 307 to 388, the domain is characterized as Saposin B-type 3.
+At position 399 to 480, the domain is characterized as Saposin B-type 4.
+At position 482 to 518, the domain is characterized as Saposin A-type 2.
+At position 41 to 183, the domain is characterized as RUN.
+At position 534 to 625, the domain is characterized as PH 1.
+At position 683 to 777, the domain is characterized as PH 2.
+At position 79 to 114, the domain is characterized as EF-hand 2.
+At position 115 to 147, the domain is characterized as EF-hand 3.
+At position 28 to 88, the domain is characterized as HTH tetR-type.
+At position 208 to 228, the domain is characterized as ELK.
+At position 1018 to 1093, the domain is characterized as DEP.
+At position 94 to 133, the domain is characterized as Agouti.
+At position 188 to 273, the domain is characterized as KH.
+At position 314 to 407, the domain is characterized as HD.
+At position 285 to 385, the domain is characterized as PpiC 2.
+At position 16 to 378, the domain is characterized as Glutamine amidotransferase type-2.
+At position 40 to 402, the domain is characterized as Protein kinase.
+At position 51 to 248, the domain is characterized as Cupin type-1 1.
+At position 319 to 468, the domain is characterized as Cupin type-1 2.
+At position 117 to 176, the domain is characterized as SUI1.
+At position 409 to 448, the domain is characterized as UBA.
+At position 194 to 306, the domain is characterized as PH.
+At position 139 to 442, the domain is characterized as NB-ARC.
+At position 80 to 171, the domain is characterized as ACB.
+At position 381 to 524, the domain is characterized as GOLD.
+At position 218 to 402, the domain is characterized as GAF.
+At position 695 to 747, the domain is characterized as PAC.
+At position 902 to 1119, the domain is characterized as Histidine kinase.
+At position 27 to 125, the domain is characterized as Ig-like.
+At position 122 to 212, the domain is characterized as RRM.
+At position 318 to 562, the domain is characterized as Clu.
+At position 15 to 131, the domain is characterized as sHSP.
+At position 1332 to 1590, the domain is characterized as Protein kinase.
+At position 42 to 99, the domain is characterized as TRAM.
+At position 18 to 238, the domain is characterized as BAR.
+At position 69 to 121, the domain is characterized as SANT.
+At position 105 to 168, the domain is characterized as S4 RNA-binding.
+At position 178 to 341, the domain is characterized as FCP1 homology.
+At position 619 to 718, the domain is characterized as BRCT.
+At position 174 to 224, the domain is characterized as DHHC.
+At position 44 to 531, the domain is characterized as Sema.
+At position 533 to 585, the domain is characterized as PSI.
+At position 592 to 680, the domain is characterized as Ig-like C2-type.
+At position 204 to 278, the domain is characterized as Ig-like C1-type.
+At position 11 to 86, the domain is characterized as DEP.
+At position 198 to 259, the domain is characterized as G protein gamma.
+At position 280 to 395, the domain is characterized as RGS.
+At position 169 to 221, the domain is characterized as KH.
+At position 50 to 245, the domain is characterized as Lon N-terminal.
+At position 551 to 708, the domain is characterized as STAS.
+At position 134 to 452, the domain is characterized as Protein kinase.
+At position 107 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 35 to 204, the domain is characterized as NAC.
+At position 816 to 955, the domain is characterized as Galectin.
+At position 369 to 540, the domain is characterized as VASt.
+At position 14 to 232, the domain is characterized as Radical SAM core.
+At position 2 to 161, the domain is characterized as N-acetyltransferase.
+At position 662 to 716, the domain is characterized as bHLH.
+At position 21 to 148, the domain is characterized as Plastocyanin-like.
+At position 39 to 324, the domain is characterized as Protein kinase.
+At position 51 to 173, the domain is characterized as HD.
+At position 97 to 378, the domain is characterized as FERM.
+At position 106 to 216, the domain is characterized as EamA.
+At position 73 to 147, the domain is characterized as RRM 1.
+At position 158 to 236, the domain is characterized as RRM 2.
+At position 282 to 356, the domain is characterized as RRM 3.
+At position 287 to 376, the domain is characterized as Rhodanese.
+At position 9 to 187, the domain is characterized as Ku.
+At position 693 to 1017, the domain is characterized as HECT.
+At position 309 to 492, the domain is characterized as PCI.
+At position 601 to 680, the domain is characterized as BRCT.
+At position 6 to 82, the domain is characterized as SAMD1-like winged helix (WH).
+At position 168 to 238, the domain is characterized as Bromo.
+At position 280 to 331, the domain is characterized as PWWP.
+At position 354 to 518, the domain is characterized as SEFIR.
+At position 28 to 68, the domain is characterized as Chitin-binding type-1.
+At position 107 to 410, the domain is characterized as USP.
+At position 279 to 354, the domain is characterized as PUA.
+At position 344 to 397, the domain is characterized as bHLH.
+At position 46 to 116, the domain is characterized as PAH 1.
+At position 130 to 200, the domain is characterized as PAH 2.
+At position 327 to 396, the domain is characterized as PAH 3.
+At position 56 to 276, the domain is characterized as Radical SAM core.
+At position 269 to 308, the domain is characterized as STI1.
+At position 226 to 284, the domain is characterized as PWWP.
+At position 447 to 579, the domain is characterized as ADD.
+At position 599 to 877, the domain is characterized as SAM-dependent MTase C5-type.
+At position 213 to 314, the domain is characterized as Fe2OG dioxygenase.
+At position 224 to 287, the domain is characterized as bZIP.
+At position 32 to 151, the domain is characterized as Bulb-type lectin.
+At position 291 to 327, the domain is characterized as EGF-like; atypical.
+At position 345 to 426, the domain is characterized as PAN.
+At position 523 to 813, the domain is characterized as Protein kinase.
+At position 318 to 521, the domain is characterized as MCM.
+At position 64 to 172, the domain is characterized as MTTase N-terminal.
+At position 200 to 431, the domain is characterized as Radical SAM core.
+At position 431 to 493, the domain is characterized as TRAM.
+At position 144 to 206, the domain is characterized as t-SNARE coiled-coil homology.
+At position 314 to 393, the domain is characterized as G5.
+At position 74 to 191, the domain is characterized as PX.
+At position 9 to 150, the domain is characterized as Clp R.
+At position 250 to 293, the domain is characterized as CUE 2.
+At position 507 to 675, the domain is characterized as Helicase ATP-binding.
+At position 856 to 1008, the domain is characterized as Helicase C-terminal.
+At position 24 to 130, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 141 to 252, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 24 to 69, the domain is characterized as F-box 1.
+At position 523 to 563, the domain is characterized as F-box 2.
+At position 9 to 83, the domain is characterized as ACT.
+At position 193 to 275, the domain is characterized as RCK C-terminal 1.
+At position 277 to 360, the domain is characterized as RCK C-terminal 2.
+At position 37 to 74, the domain is characterized as Myb-like.
+At position 12 to 190, the domain is characterized as Guanylate kinase-like.
+At position 9 to 201, the domain is characterized as YjeF N-terminal.
+At position 203 to 461, the domain is characterized as YjeF C-terminal.
+At position 141 to 176, the domain is characterized as EF-hand 3.
+At position 178 to 213, the domain is characterized as EF-hand 4.
+At position 40 to 85, the domain is characterized as EF-hand 1.
+At position 122 to 156, the domain is characterized as EF-hand 3.
+At position 354 to 437, the domain is characterized as KH-like.
+At position 126 to 294, the domain is characterized as PPIase cyclophilin-type.
+At position 33 to 123, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 149 to 184, the domain is characterized as EF-hand 3.
+At position 197 to 232, the domain is characterized as EF-hand 4.
+At position 240 to 276, the domain is characterized as EF-hand 5.
+At position 2 to 134, the domain is characterized as C2 1.
+At position 161 to 284, the domain is characterized as C2 2.
+At position 328 to 554, the domain is characterized as VWFA.
+At position 107 to 223, the domain is characterized as RGS.
+At position 500 to 735, the domain is characterized as ABC transporter 1.
+At position 1292 to 1527, the domain is characterized as ABC transporter 2.
+At position 18 to 95, the domain is characterized as RRM.
+At position 93 to 154, the domain is characterized as CBS 1.
+At position 158 to 217, the domain is characterized as CBS 2.
+At position 29 to 202, the domain is characterized as VWFA.
+At position 257 to 374, the domain is characterized as Chitin-binding type-2.
+At position 388 to 423, the domain is characterized as EF-hand 1.
+At position 425 to 460, the domain is characterized as EF-hand 2.
+At position 136 to 598, the domain is characterized as Urease.
+At position 146 to 291, the domain is characterized as Jacalin-type lectin 2.
+At position 294 to 439, the domain is characterized as Jacalin-type lectin 3.
+At position 446 to 592, the domain is characterized as Jacalin-type lectin 4.
+At position 271 to 579, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 1 to 92, the domain is characterized as PTS EIIB type-2.
+At position 319 to 408, the domain is characterized as HTH La-type RNA-binding.
+At position 332 to 500, the domain is characterized as tr-type G.
+At position 5 to 120, the domain is characterized as Response regulatory.
+At position 174 to 362, the domain is characterized as CheB-type methylesterase.
+At position 41 to 125, the domain is characterized as PNT.
+At position 2 to 256, the domain is characterized as Radical SAM core.
+At position 79 to 392, the domain is characterized as Peptidase A1.
+At position 69 to 213, the domain is characterized as N-acetyltransferase.
+At position 21 to 274, the domain is characterized as Protein kinase.
+At position 437 to 565, the domain is characterized as N-terminal Ras-GEF.
+At position 712 to 957, the domain is characterized as Ras-GEF.
+At position 126 to 298, the domain is characterized as Helicase ATP-binding.
+At position 328 to 472, the domain is characterized as Helicase C-terminal.
+At position 607 to 936, the domain is characterized as ABC transporter 2.
+At position 4 to 148, the domain is characterized as PPPDE.
+At position 68 to 248, the domain is characterized as tr-type G.
+At position 2 to 178, the domain is characterized as PBS-linker.
+At position 226 to 278, the domain is characterized as CpcD-like.
+At position 140 to 224, the domain is characterized as Ig-like C2-type 2.
+At position 234 to 316, the domain is characterized as Ig-like C2-type 3.
+At position 324 to 414, the domain is characterized as Fibronectin type-III 1.
+At position 419 to 513, the domain is characterized as Fibronectin type-III 2.
+At position 517 to 608, the domain is characterized as Fibronectin type-III 3.
+At position 613 to 707, the domain is characterized as Fibronectin type-III 4.
+At position 711 to 810, the domain is characterized as Fibronectin type-III 5.
+At position 815 to 911, the domain is characterized as Fibronectin type-III 6.
+At position 912 to 1005, the domain is characterized as Fibronectin type-III 7.
+At position 1009 to 1102, the domain is characterized as Fibronectin type-III 8.
+At position 1104 to 1206, the domain is characterized as Fibronectin type-III 9.
+At position 1474 to 1729, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1761 to 2020, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 76 to 213, the domain is characterized as Cupin type-1.
+At position 60 to 246, the domain is characterized as DOC.
+At position 355 to 449, the domain is characterized as BRCT.
+At position 11 to 144, the domain is characterized as HTH marR-type.
+At position 139 to 421, the domain is characterized as ABC transmembrane type-1.
+At position 455 to 694, the domain is characterized as ABC transporter.
+At position 24 to 157, the domain is characterized as Ephrin RBD.
+At position 162 to 266, the domain is characterized as THUMP.
+At position 150 to 437, the domain is characterized as ABC transmembrane type-1.
+At position 472 to 709, the domain is characterized as ABC transporter.
+At position 14 to 106, the domain is characterized as Core-binding (CB).
+At position 127 to 330, the domain is characterized as Tyr recombinase.
+At position 213 to 336, the domain is characterized as OTU.
+At position 65 to 128, the domain is characterized as SAM.
+At position 263 to 353, the domain is characterized as Ras-associating.
+At position 641 to 911, the domain is characterized as Protein kinase.
+At position 280 to 508, the domain is characterized as Rab-GAP TBC.
+At position 119 to 496, the domain is characterized as Protein kinase.
+At position 479 to 714, the domain is characterized as ABC transporter 1.
+At position 1283 to 1516, the domain is characterized as ABC transporter 2.
+At position 4 to 104, the domain is characterized as PH 1.
+At position 139 to 225, the domain is characterized as DEP.
+At position 247 to 353, the domain is characterized as PH 2.
+At position 46 to 339, the domain is characterized as Obg.
+At position 340 to 513, the domain is characterized as OBG-type G.
+At position 8 to 210, the domain is characterized as YjeF N-terminal.
+At position 36 to 92, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 771 to 841, the domain is characterized as Dockerin.
+At position 126 to 202, the domain is characterized as Cytochrome b5 heme-binding.
+At position 10 to 78, the domain is characterized as HTH merR-type.
+At position 46 to 227, the domain is characterized as tr-type G.
+At position 3 to 143, the domain is characterized as DAC.
+At position 192 to 378, the domain is characterized as Glutamine amidotransferase type-1.
+At position 353 to 413, the domain is characterized as S4 RNA-binding.
+At position 15 to 174, the domain is characterized as UBC core.
+At position 36 to 261, the domain is characterized as Cupin type-1 1.
+At position 470 to 616, the domain is characterized as Cupin type-1 2.
+At position 86 to 159, the domain is characterized as K-box.
+At position 56 to 91, the domain is characterized as EF-hand 2.
+At position 8 to 212, the domain is characterized as ABC transporter.
+At position 27 to 272, the domain is characterized as Deacetylase sirtuin-type.
+At position 324 to 516, the domain is characterized as Peptidase M12A.
+At position 539 to 550, the domain is characterized as EGF-like.
+At position 550 to 648, the domain is characterized as CUB.
+At position 8 to 66, the domain is characterized as TRAM.
+At position 143 to 215, the domain is characterized as PAS 1.
+At position 326 to 396, the domain is characterized as PAS 2.
+At position 402 to 445, the domain is characterized as PAC.
+At position 139 to 223, the domain is characterized as EH 2.
+At position 570 to 646, the domain is characterized as Carrier.
+At position 144 to 376, the domain is characterized as Radical SAM core.
+At position 51 to 269, the domain is characterized as Radical SAM core.
+At position 280 to 398, the domain is characterized as Nop.
+At position 120 to 136, the domain is characterized as Post-SET.
+At position 283 to 435, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1212 to 1376, the domain is characterized as PNPLA.
+At position 31 to 135, the domain is characterized as Ig-like V-type.
+At position 309 to 590, the domain is characterized as ABC transmembrane type-1 1.
+At position 624 to 847, the domain is characterized as ABC transporter 1.
+At position 922 to 1204, the domain is characterized as ABC transmembrane type-1 2.
+At position 1241 to 1475, the domain is characterized as ABC transporter 2.
+At position 223 to 250, the domain is characterized as PLD phosphodiesterase 1.
+At position 401 to 428, the domain is characterized as PLD phosphodiesterase 2.
+At position 985 to 1023, the domain is characterized as EGF-like 1.
+At position 1025 to 1063, the domain is characterized as EGF-like 2; calcium-binding.
+At position 145 to 172, the domain is characterized as PLD phosphodiesterase 1.
+At position 373 to 399, the domain is characterized as PLD phosphodiesterase 2.
+At position 14 to 132, the domain is characterized as SCP.
+At position 114 to 330, the domain is characterized as ATP-grasp.
+At position 191 to 386, the domain is characterized as GMPS ATP-PPase.
+At position 43 to 124, the domain is characterized as KH type-2.
+At position 671 to 976, the domain is characterized as Autotransporter.
+At position 8 to 131, the domain is characterized as MsrB.
+At position 706 to 867, the domain is characterized as MOSC.
+At position 33 to 121, the domain is characterized as GOLD.
+At position 47 to 316, the domain is characterized as GH10.
+At position 193 to 296, the domain is characterized as AB hydrolase-1.
+At position 356 to 647, the domain is characterized as Protein kinase.
+At position 263 to 312, the domain is characterized as bHLH.
+At position 378 to 450, the domain is characterized as ACT.
+At position 222 to 341, the domain is characterized as C2 1.
+At position 343 to 470, the domain is characterized as C2 2.
+At position 74 to 168, the domain is characterized as Cytochrome c.
+At position 124 to 232, the domain is characterized as CBM21.
+At position 98 to 283, the domain is characterized as ATP-grasp.
+At position 257 to 505, the domain is characterized as PABS.
+At position 43 to 216, the domain is characterized as EngB-type G.
+At position 49 to 410, the domain is characterized as GH18.
+At position 221 to 283, the domain is characterized as LIM zinc-binding 4.
+At position 40 to 63, the domain is characterized as EF-hand.
+At position 120 to 404, the domain is characterized as Peptidase S1.
+At position 55 to 358, the domain is characterized as USP.
+At position 591 to 864, the domain is characterized as Protein kinase.
+At position 1 to 37, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 38 to 80, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 86 to 126, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 127 to 169, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 503 to 539, the domain is characterized as CBM1.
+At position 128 to 369, the domain is characterized as Radical SAM core.
+At position 47 to 358, the domain is characterized as PPM-type phosphatase.
+At position 138 to 257, the domain is characterized as C-type lectin.
+At position 34 to 111, the domain is characterized as RRM.
+At position 284 to 562, the domain is characterized as Protein kinase.
+At position 2 to 166, the domain is characterized as Exonuclease.
+At position 22 to 98, the domain is characterized as Saposin B-type.
+At position 299 to 351, the domain is characterized as HAMP.
+At position 370 to 606, the domain is characterized as Methyl-accepting transducer.
+At position 1 to 73, the domain is characterized as GST N-terminal.
+At position 79 to 200, the domain is characterized as GST C-terminal.
+At position 10 to 280, the domain is characterized as CheR-type methyltransferase.
+At position 650 to 825, the domain is characterized as TR mART core.
+At position 108 to 402, the domain is characterized as ABC transmembrane type-1.
+At position 439 to 673, the domain is characterized as ABC transporter.
+At position 20 to 152, the domain is characterized as MPN.
+At position 47 to 124, the domain is characterized as IGFBP N-terminal.
+At position 346 to 403, the domain is characterized as VWFC 1.
+At position 413 to 469, the domain is characterized as VWFC 2.
+At position 481 to 510, the domain is characterized as Antistasin-like 1.
+At position 517 to 544, the domain is characterized as Antistasin-like 2.
+At position 551 to 576, the domain is characterized as Antistasin-like 3.
+At position 579 to 604, the domain is characterized as Antistasin-like 4.
+At position 618 to 675, the domain is characterized as VWFC 3.
+At position 689 to 747, the domain is characterized as VWFC 4.
+At position 763 to 821, the domain is characterized as VWFC 5.
+At position 829 to 886, the domain is characterized as VWFC 6.
+At position 529 to 696, the domain is characterized as tr-type G.
+At position 438 to 538, the domain is characterized as C-type lectin.
+At position 779 to 796, the domain is characterized as WH2.
+At position 92 to 150, the domain is characterized as S4 RNA-binding.
+At position 20 to 479, the domain is characterized as Sema.
+At position 1070 to 1160, the domain is characterized as IPT/TIG 1.
+At position 1162 to 1249, the domain is characterized as IPT/TIG 2.
+At position 1252 to 1375, the domain is characterized as IPT/TIG 3.
+At position 32 to 292, the domain is characterized as Protein kinase.
+At position 313 to 347, the domain is characterized as NAF.
+At position 149 to 252, the domain is characterized as Fe2OG dioxygenase.
+At position 49 to 150, the domain is characterized as SRCR 1.
+At position 179 to 293, the domain is characterized as SRCR 2.
+At position 317 to 416, the domain is characterized as SRCR 3.
+At position 426 to 535, the domain is characterized as SRCR 4.
+At position 183 to 356, the domain is characterized as Helicase ATP-binding.
+At position 430 to 572, the domain is characterized as Helicase C-terminal.
+At position 2 to 430, the domain is characterized as BRO1.
+At position 2 to 84, the domain is characterized as Core-binding (CB).
+At position 105 to 291, the domain is characterized as Tyr recombinase.
+At position 176 to 293, the domain is characterized as C2.
+At position 350 to 608, the domain is characterized as Protein kinase.
+At position 609 to 679, the domain is characterized as AGC-kinase C-terminal.
+At position 229 to 271, the domain is characterized as CCT.
+At position 376 to 517, the domain is characterized as TNase-like.
+At position 1376 to 1483, the domain is characterized as HECT.
+At position 394 to 511, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 512 to 615, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 669 to 748, the domain is characterized as POLO box.
+At position 250 to 359, the domain is characterized as DEUBAD.
+At position 563 to 641, the domain is characterized as HSA.
+At position 1049 to 1105, the domain is characterized as SANT.
+At position 11 to 266, the domain is characterized as Pyruvate carboxyltransferase.
+At position 2 to 132, the domain is characterized as RCK N-terminal 1.
+At position 144 to 225, the domain is characterized as RCK C-terminal.
+At position 232 to 356, the domain is characterized as RCK N-terminal 2.
+At position 295 to 886, the domain is characterized as USP.
+At position 153 to 193, the domain is characterized as EGF-like 1.
+At position 305 to 342, the domain is characterized as EGF-like 2; calcium-binding.
+At position 118 to 181, the domain is characterized as bZIP.
+At position 442 to 556, the domain is characterized as Toprim.
+At position 34 to 262, the domain is characterized as Radical SAM core.
+At position 56 to 411, the domain is characterized as SAM-dependent MTase C5-type.
+At position 296 to 437, the domain is characterized as Nudix hydrolase.
+At position 251 to 450, the domain is characterized as GATase cobBQ-type.
+At position 1 to 62, the domain is characterized as Tudor.
+At position 23 to 260, the domain is characterized as PABS.
+At position 21 to 219, the domain is characterized as GH16.
+At position 584 to 686, the domain is characterized as tRNA-binding.
+At position 95 to 164, the domain is characterized as PRC barrel.
+At position 61 to 321, the domain is characterized as GH18.
+At position 112 to 335, the domain is characterized as BURP.
+At position 8 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 69 to 132, the domain is characterized as SAM.
+At position 377 to 457, the domain is characterized as Ras-associating.
+At position 242 to 345, the domain is characterized as Fe2OG dioxygenase.
+At position 10 to 88, the domain is characterized as RRM 1.
+At position 188 to 265, the domain is characterized as RRM 3.
+At position 284 to 362, the domain is characterized as RRM 4.
+At position 489 to 565, the domain is characterized as PABC.
+At position 14 to 141, the domain is characterized as MATH.
+At position 161 to 226, the domain is characterized as BTB.
+At position 4 to 125, the domain is characterized as Peptidase C39.
+At position 158 to 436, the domain is characterized as ABC transmembrane type-1.
+At position 263 to 322, the domain is characterized as SH3.
+At position 19 to 103, the domain is characterized as Ig-like C2-type 1.
+At position 114 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 212 to 319, the domain is characterized as Ig-like C2-type 3.
+At position 375 to 535, the domain is characterized as TIR.
+At position 1544 to 1653, the domain is characterized as BEACH-type PH.
+At position 1667 to 1941, the domain is characterized as BEACH.
+At position 2 to 152, the domain is characterized as Thioredoxin.
+At position 184 to 276, the domain is characterized as 3'-5' exonuclease.
+At position 90 to 210, the domain is characterized as GST C-terminal.
+At position 33 to 160, the domain is characterized as PLAT.
+At position 69 to 136, the domain is characterized as CSD.
+At position 149 to 260, the domain is characterized as Tudor 1.
+At position 386 to 506, the domain is characterized as Tudor 2.
+At position 25 to 164, the domain is characterized as C2 1.
+At position 176 to 303, the domain is characterized as C2 2.
+At position 344 to 563, the domain is characterized as VWFA.
+At position 255 to 396, the domain is characterized as Helicase C-terminal.
+At position 219 to 483, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 41 to 128, the domain is characterized as RRM.
+At position 1 to 50, the domain is characterized as Fibronectin type-II.
+At position 55 to 98, the domain is characterized as Fibronectin type-I 1.
+At position 103 to 145, the domain is characterized as Fibronectin type-I 2.
+At position 146 to 190, the domain is characterized as Fibronectin type-I 3.
+At position 15 to 99, the domain is characterized as Acylphosphatase-like.
+At position 196 to 387, the domain is characterized as YrdC-like.
+At position 3 to 81, the domain is characterized as Carrier.
+At position 1377 to 1634, the domain is characterized as Protein kinase.
+At position 289 to 339, the domain is characterized as bHLH.
+At position 13 to 65, the domain is characterized as Death.
+At position 4 to 71, the domain is characterized as J.
+At position 106 to 248, the domain is characterized as N-acetyltransferase.
+At position 236 to 312, the domain is characterized as RRM 1.
+At position 324 to 403, the domain is characterized as RRM 2.
+At position 59 to 209, the domain is characterized as Cupin type-1.
+At position 2 to 117, the domain is characterized as Response regulatory.
+At position 142 to 247, the domain is characterized as HTH LytTR-type.
+At position 940 to 1094, the domain is characterized as Guanylate cyclase.
+At position 1 to 114, the domain is characterized as ABC transmembrane type-1.
+At position 285 to 384, the domain is characterized as PpiC 2.
+At position 39 to 81, the domain is characterized as PISA.
+At position 236 to 272, the domain is characterized as DFDF.
+At position 20 to 71, the domain is characterized as HTH myb-type 1.
+At position 72 to 126, the domain is characterized as HTH myb-type 2.
+At position 104 to 329, the domain is characterized as Radical SAM core.
+At position 314 to 391, the domain is characterized as SWIB/MDM2.
+At position 321 to 360, the domain is characterized as STI1.
+At position 31 to 285, the domain is characterized as Protein kinase.
+At position 77 to 291, the domain is characterized as Radical SAM core.
+At position 16 to 144, the domain is characterized as PH.
+At position 194 to 298, the domain is characterized as IRS-type PTB.
+At position 26 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 148, the domain is characterized as C-type lectin.
+At position 247 to 399, the domain is characterized as GAF 1.
+At position 431 to 612, the domain is characterized as GAF 2.
+At position 642 to 965, the domain is characterized as PDEase.
+At position 111 to 278, the domain is characterized as PID 1.
+At position 283 to 438, the domain is characterized as PID 2.
+At position 461 to 551, the domain is characterized as SH2.
+At position 564 to 815, the domain is characterized as Protein kinase.
+At position 92 to 280, the domain is characterized as Rab-GAP TBC.
+At position 23 to 225, the domain is characterized as Pentraxin (PTX).
+At position 16 to 143, the domain is characterized as Peptidase C39.
+At position 173 to 455, the domain is characterized as ABC transmembrane type-1.
+At position 489 to 722, the domain is characterized as ABC transporter.
+At position 346 to 410, the domain is characterized as S4 RNA-binding.
+At position 283 to 359, the domain is characterized as PUA.
+At position 251 to 519, the domain is characterized as Protein kinase.
+At position 58 to 255, the domain is characterized as Peptidase M12A.
+At position 250 to 291, the domain is characterized as EGF-like.
+At position 306 to 428, the domain is characterized as CUB.
+At position 26 to 102, the domain is characterized as EF-hand-like.
+At position 103 to 248, the domain is characterized as PI-PLC X-box.
+At position 323 to 439, the domain is characterized as PI-PLC Y-box.
+At position 433 to 566, the domain is characterized as C2.
+At position 71 to 339, the domain is characterized as Protein kinase.
+At position 340 to 415, the domain is characterized as AGC-kinase C-terminal.
+At position 144 to 212, the domain is characterized as HTH crp-type.
+At position 6 to 241, the domain is characterized as ABC transporter.
+At position 67 to 135, the domain is characterized as POTRA.
+At position 27 to 264, the domain is characterized as PABS.
+At position 232 to 464, the domain is characterized as START.
+At position 41 to 482, the domain is characterized as USP.
+At position 17 to 95, the domain is characterized as GIY-YIG.
+At position 20 to 113, the domain is characterized as Ig-like.
+At position 610 to 806, the domain is characterized as Rab-GAP TBC.
+At position 1 to 263, the domain is characterized as Peptidase A1.
+At position 965 to 1056, the domain is characterized as SET.
+At position 836 to 977, the domain is characterized as CID.
+At position 162 to 228, the domain is characterized as DRBM.
+At position 82 to 125, the domain is characterized as CUE.
+At position 27 to 136, the domain is characterized as Ig-like 1.
+At position 142 to 228, the domain is characterized as Ig-like 2.
+At position 241 to 329, the domain is characterized as Ig-like 3.
+At position 334 to 420, the domain is characterized as Ig-like 4.
+At position 430 to 524, the domain is characterized as Fibronectin type-III 1.
+At position 526 to 622, the domain is characterized as Fibronectin type-III 2.
+At position 631 to 742, the domain is characterized as Fibronectin type-III 3.
+At position 751 to 844, the domain is characterized as Fibronectin type-III 4.
+At position 849 to 944, the domain is characterized as Fibronectin type-III 5.
+At position 578 to 756, the domain is characterized as Helicase ATP-binding.
+At position 783 to 933, the domain is characterized as Helicase C-terminal.
+At position 27 to 72, the domain is characterized as WAP; atypical.
+At position 103 to 176, the domain is characterized as PRC barrel.
+At position 47 to 313, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 28 to 615, the domain is characterized as Peptidase M2.
+At position 59 to 243, the domain is characterized as DUF724.
+At position 398 to 444, the domain is characterized as F-box.
+At position 9 to 149, the domain is characterized as SprT-like.
+At position 3 to 31, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 250 to 479, the domain is characterized as VWFA.
+At position 38 to 96, the domain is characterized as Collagen-like.
+At position 129 to 241, the domain is characterized as C-type lectin.
+At position 14 to 100, the domain is characterized as Acylphosphatase-like.
+At position 232 to 485, the domain is characterized as CN hydrolase.
+At position 25 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 59 to 418, the domain is characterized as Protein kinase.
+At position 888 to 1163, the domain is characterized as Protein kinase.
+At position 13 to 129, the domain is characterized as LRAT.
+At position 934 to 1051, the domain is characterized as SET.
+At position 1060 to 1076, the domain is characterized as Post-SET.
+At position 1 to 11, the domain is characterized as Peptidase M12B.
+At position 19 to 105, the domain is characterized as Disintegrin.
+At position 249 to 311, the domain is characterized as t-SNARE coiled-coil homology.
+At position 254 to 336, the domain is characterized as IPT/TIG.
+At position 29 to 280, the domain is characterized as Protein kinase.
+At position 432 to 479, the domain is characterized as SARAH.
+At position 63 to 174, the domain is characterized as Thioredoxin.
+At position 3 to 60, the domain is characterized as Collagen-like 1.
+At position 513 to 571, the domain is characterized as Collagen-like 2.
+At position 661 to 884, the domain is characterized as Fibrillar collagen NC1.
+At position 1 to 154, the domain is characterized as PPIase cyclophilin-type.
+At position 114 to 375, the domain is characterized as Protein kinase.
+At position 274 to 349, the domain is characterized as PUA.
+At position 146 to 355, the domain is characterized as ATP-grasp.
+At position 52 to 275, the domain is characterized as L-type lectin-like.
+At position 263 to 327, the domain is characterized as KH.
+At position 25 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 156 to 244, the domain is characterized as Ig-like C2-type 2.
+At position 253 to 355, the domain is characterized as Ig-like C2-type 3.
+At position 474 to 763, the domain is characterized as Protein kinase.
+At position 4 to 255, the domain is characterized as Pyruvate carboxyltransferase.
+At position 5 to 33, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 59 to 89, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 90 to 119, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 152 to 228, the domain is characterized as RRM 1.
+At position 244 to 322, the domain is characterized as RRM 2.
+At position 515 to 621, the domain is characterized as PH.
+At position 172 to 234, the domain is characterized as TGS.
+At position 127 to 192, the domain is characterized as BTB.
+At position 559 to 611, the domain is characterized as HTH psq-type.
+At position 160 to 529, the domain is characterized as GRAS.
+At position 604 to 857, the domain is characterized as ABC transporter 1.
+At position 923 to 1139, the domain is characterized as ABC transporter 2.
+At position 127 to 243, the domain is characterized as EamA.
+At position 52 to 187, the domain is characterized as RGS.
+At position 202 to 469, the domain is characterized as Protein kinase.
+At position 479 to 544, the domain is characterized as AGC-kinase C-terminal.
+At position 63 to 112, the domain is characterized as LysM.
+At position 560 to 653, the domain is characterized as Big-1 1.
+At position 660 to 753, the domain is characterized as Big-1 2.
+At position 787 to 834, the domain is characterized as BIG2.
+At position 189 to 255, the domain is characterized as S4 RNA-binding 2.
+At position 20 to 50, the domain is characterized as LRRNT.
+At position 293 to 346, the domain is characterized as LRRCT.
+At position 403 to 440, the domain is characterized as EGF-like.
+At position 455 to 543, the domain is characterized as Fibronectin type-III.
+At position 12 to 92, the domain is characterized as NAB.
+At position 344 to 408, the domain is characterized as S4 RNA-binding.
+At position 19 to 90, the domain is characterized as S4 RNA-binding.
+At position 11 to 80, the domain is characterized as Sm.
+At position 617 to 652, the domain is characterized as UVR.
+At position 630 to 704, the domain is characterized as S1 motif.
+At position 171 to 258, the domain is characterized as GIY-YIG.
+At position 22 to 308, the domain is characterized as Dynamin-type G.
+At position 650 to 741, the domain is characterized as GED.
+At position 284 to 487, the domain is characterized as B30.2/SPRY.
+At position 121 to 202, the domain is characterized as PRC barrel.
+At position 109 to 193, the domain is characterized as FAR1.
+At position 327 to 416, the domain is characterized as MULE.
+At position 16 to 304, the domain is characterized as Protein kinase.
+At position 20 to 148, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 28 to 81, the domain is characterized as F-box.
+At position 373 to 423, the domain is characterized as FBD.
+At position 324 to 362, the domain is characterized as UBA.
+At position 151 to 178, the domain is characterized as DAZ.
+At position 102 to 298, the domain is characterized as ATP-grasp.
+At position 24 to 87, the domain is characterized as Kazal-like 1.
+At position 88 to 152, the domain is characterized as Kazal-like 2.
+At position 153 to 207, the domain is characterized as Kazal-like 3.
+At position 45 to 161, the domain is characterized as SCP.
+At position 230 to 494, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 135 to 316, the domain is characterized as Helicase ATP-binding.
+At position 344 to 523, the domain is characterized as Helicase C-terminal.
+At position 5 to 267, the domain is characterized as tr-type G.
+At position 108 to 183, the domain is characterized as RRM.
+At position 209 to 368, the domain is characterized as CID.
+At position 23 to 304, the domain is characterized as ABC transmembrane type-1.
+At position 335 to 570, the domain is characterized as ABC transporter.
+At position 36 to 477, the domain is characterized as Kinesin motor.
+At position 348 to 555, the domain is characterized as MCM.
+At position 8 to 332, the domain is characterized as Protein kinase.
+At position 4 to 257, the domain is characterized as Protein kinase.
+At position 210 to 402, the domain is characterized as Helicase ATP-binding.
+At position 413 to 574, the domain is characterized as Helicase C-terminal.
+At position 6 to 406, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 81 to 146, the domain is characterized as PA.
+At position 23 to 271, the domain is characterized as ABC transporter.
+At position 42 to 459, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 20 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 17 to 140, the domain is characterized as Rhodanese.
+At position 140 to 402, the domain is characterized as Peptidase M66.
+At position 27 to 113, the domain is characterized as IGFBP N-terminal.
+At position 159 to 263, the domain is characterized as Ig-like C2-type.
+At position 164 to 410, the domain is characterized as NB-ARC.
+At position 17 to 130, the domain is characterized as Thioredoxin 1.
+At position 46 to 260, the domain is characterized as Radical SAM core.
+At position 358 to 470, the domain is characterized as PLAT.
+At position 129 to 175, the domain is characterized as F-box.
+At position 117 to 312, the domain is characterized as ATP-grasp.
+At position 221 to 395, the domain is characterized as Helicase ATP-binding.
+At position 406 to 570, the domain is characterized as Helicase C-terminal.
+At position 1160 to 1270, the domain is characterized as Fibronectin type-III.
+At position 34 to 229, the domain is characterized as Helicase ATP-binding.
+At position 263 to 460, the domain is characterized as Helicase C-terminal.
+At position 536 to 847, the domain is characterized as SEC63.
+At position 26 to 264, the domain is characterized as AB hydrolase-1.
+At position 21 to 79, the domain is characterized as Chromo 1.
+At position 117 to 175, the domain is characterized as Chromo 2; shadow subtype.
+At position 50 to 234, the domain is characterized as Laminin G-like.
+At position 292 to 349, the domain is characterized as Collagen-like 1.
+At position 350 to 391, the domain is characterized as Collagen-like 2.
+At position 392 to 433, the domain is characterized as Collagen-like 3.
+At position 474 to 516, the domain is characterized as Collagen-like 4.
+At position 568 to 624, the domain is characterized as Collagen-like 5.
+At position 626 to 678, the domain is characterized as Collagen-like 6.
+At position 728 to 778, the domain is characterized as Collagen-like 7.
+At position 779 to 814, the domain is characterized as Collagen-like 8.
+At position 845 to 903, the domain is characterized as Collagen-like 9.
+At position 904 to 947, the domain is characterized as Collagen-like 10.
+At position 948 to 1004, the domain is characterized as Collagen-like 11.
+At position 101 to 301, the domain is characterized as ATP-grasp.
+At position 12 to 191, the domain is characterized as Guanylate kinase-like.
+At position 89 to 133, the domain is characterized as LysM.
+At position 33 to 82, the domain is characterized as F-box.
+At position 92 to 284, the domain is characterized as B30.2/SPRY.
+At position 34 to 64, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 135 to 409, the domain is characterized as Protein kinase.
+At position 248 to 347, the domain is characterized as Fe2OG dioxygenase.
+At position 132 to 238, the domain is characterized as Rieske.
+At position 164 to 297, the domain is characterized as TIR.
+At position 9 to 62, the domain is characterized as HTH myb-type 1.
+At position 63 to 117, the domain is characterized as HTH myb-type 2.
+At position 34 to 115, the domain is characterized as BTB.
+At position 175 to 277, the domain is characterized as Fibronectin type-III.
+At position 145 to 203, the domain is characterized as TRAM.
+At position 50 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 195 to 297, the domain is characterized as Plastocyanin-like 2.
+At position 387 to 506, the domain is characterized as Plastocyanin-like 3.
+At position 586 to 663, the domain is characterized as BRCT.
+At position 15 to 153, the domain is characterized as SprT-like.
+At position 35 to 52, the domain is characterized as WH2.
+At position 1 to 296, the domain is characterized as FERM.
+At position 1 to 120, the domain is characterized as C2.
+At position 437 to 499, the domain is characterized as FIP-RBD.
+At position 18 to 148, the domain is characterized as VHS.
+At position 9 to 63, the domain is characterized as HTH cro/C1-type.
+At position 99 to 429, the domain is characterized as SAM-dependent MTase C5-type.
+At position 32 to 211, the domain is characterized as BPL/LPL catalytic.
+At position 112 to 249, the domain is characterized as N-terminal Ras-GEF.
+At position 386 to 648, the domain is characterized as Ras-GEF.
+At position 798 to 885, the domain is characterized as Ras-associating.
+At position 166 to 234, the domain is characterized as KRAB.
+At position 3 to 124, the domain is characterized as Response regulatory.
+At position 133 to 198, the domain is characterized as HTH luxR-type.
+At position 42 to 145, the domain is characterized as Cytochrome b5 heme-binding.
+At position 456 to 517, the domain is characterized as Sushi 5.
+At position 518 to 579, the domain is characterized as Sushi 6.
+At position 432 to 642, the domain is characterized as Protein kinase.
+At position 2 to 73, the domain is characterized as J.
+At position 9 to 81, the domain is characterized as Sm.
+At position 15 to 83, the domain is characterized as HTH gntR-type.
+At position 39 to 219, the domain is characterized as Helicase ATP-binding.
+At position 242 to 392, the domain is characterized as Helicase C-terminal.
+At position 9 to 55, the domain is characterized as RPE1 insert.
+At position 33 to 470, the domain is characterized as Kinesin motor.
+At position 325 to 417, the domain is characterized as SH2.
+At position 24 to 82, the domain is characterized as KRAB.
+At position 197 to 217, the domain is characterized as ELK.
+At position 34 to 98, the domain is characterized as BTB.
+At position 32 to 151, the domain is characterized as Thioredoxin 1.
+At position 372 to 491, the domain is characterized as Thioredoxin 2.
+At position 133 to 319, the domain is characterized as CP-type G.
+At position 28 to 204, the domain is characterized as EngB-type G.
+At position 72 to 136, the domain is characterized as HMA 1.
+At position 170 to 234, the domain is characterized as HMA 2.
+At position 160 to 215, the domain is characterized as 5'-3' exonuclease.
+At position 42 to 280, the domain is characterized as ZP.
+At position 175 to 233, the domain is characterized as CTLH.
+At position 183 to 469, the domain is characterized as Protein kinase.
+At position 580 to 640, the domain is characterized as KH.
+At position 650 to 724, the domain is characterized as S1 motif.
+At position 333 to 501, the domain is characterized as tr-type G.
+At position 633 to 692, the domain is characterized as KH.
+At position 704 to 773, the domain is characterized as S1 motif.
+At position 36 to 71, the domain is characterized as EF-hand.
+At position 296 to 385, the domain is characterized as ABM.
+At position 113 to 259, the domain is characterized as Fatty acid hydroxylase.
+At position 476 to 698, the domain is characterized as Histidine kinase.
+At position 720 to 832, the domain is characterized as Response regulatory.
+At position 32 to 143, the domain is characterized as CUB 1.
+At position 153 to 267, the domain is characterized as CUB 2.
+At position 296 to 414, the domain is characterized as NTR.
+At position 232 to 322, the domain is characterized as PA.
+At position 414 to 576, the domain is characterized as Miro 2.
+At position 283 to 339, the domain is characterized as HAMP.
+At position 347 to 575, the domain is characterized as Histidine kinase.
+At position 5 to 85, the domain is characterized as Sm.
+At position 210 to 386, the domain is characterized as Helicase ATP-binding.
+At position 417 to 566, the domain is characterized as Helicase C-terminal.
+At position 140 to 268, the domain is characterized as Nudix hydrolase.
+At position 116 to 238, the domain is characterized as MPN.
+At position 88 to 223, the domain is characterized as GST C-terminal.
+At position 256 to 383, the domain is characterized as CMP/dCMP-type deaminase.
+At position 183 to 235, the domain is characterized as KH.
+At position 20 to 93, the domain is characterized as G protein gamma.
+At position 19 to 382, the domain is characterized as GH18.
+At position 26 to 129, the domain is characterized as HD.
+At position 64 to 188, the domain is characterized as OTU.
+At position 229 to 269, the domain is characterized as UBA-like.
+At position 51 to 127, the domain is characterized as H15.
+At position 153 to 229, the domain is characterized as Cache.
+At position 304 to 356, the domain is characterized as HAMP.
+At position 375 to 611, the domain is characterized as Methyl-accepting transducer.
+At position 42 to 105, the domain is characterized as SH3b 1.
+At position 112 to 172, the domain is characterized as SH3b 2.
+At position 596 to 929, the domain is characterized as Reverse transcriptase.
+At position 18 to 83, the domain is characterized as Chitin-binding type R&R.
+At position 5 to 95, the domain is characterized as ATP-cone.
+At position 187 to 285, the domain is characterized as HTH araC/xylS-type.
+At position 13 to 294, the domain is characterized as Protein kinase.
+At position 32 to 186, the domain is characterized as C-CAP/cofactor C-like.
+At position 13 to 247, the domain is characterized as ABC transporter.
+At position 68 to 125, the domain is characterized as SMP 1.
+At position 133 to 190, the domain is characterized as SMP 2.
+At position 53 to 209, the domain is characterized as PID 1.
+At position 319 to 475, the domain is characterized as PID 2.
+At position 927 to 1121, the domain is characterized as Rab-GAP TBC.
+At position 292 to 377, the domain is characterized as PDZ 1.
+At position 878 to 959, the domain is characterized as PDZ 2.
+At position 773 to 924, the domain is characterized as HNH Cas9-type.
+At position 8 to 165, the domain is characterized as Thioredoxin.
+At position 48 to 118, the domain is characterized as H15.
+At position 30 to 369, the domain is characterized as FERM.
+At position 356 to 526, the domain is characterized as tr-type G.
+At position 238 to 312, the domain is characterized as POU-specific.
+At position 167 to 258, the domain is characterized as CS.
+At position 275 to 387, the domain is characterized as FAD-binding FR-type.
+At position 39 to 155, the domain is characterized as tRNA-binding.
+At position 711 to 804, the domain is characterized as FDX-ACB.
+At position 25 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 138 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 436, the domain is characterized as TRAM.
+At position 63 to 280, the domain is characterized as Radical SAM core.
+At position 211 to 308, the domain is characterized as PH 1.
+At position 361 to 456, the domain is characterized as PH 2.
+At position 125 to 265, the domain is characterized as SIS.
+At position 125 to 160, the domain is characterized as EF-hand 4.
+At position 52 to 116, the domain is characterized as S1 motif 1.
+At position 134 to 199, the domain is characterized as S1 motif 2.
+At position 220 to 288, the domain is characterized as S1 motif 3.
+At position 305 to 375, the domain is characterized as S1 motif 4.
+At position 392 to 462, the domain is characterized as S1 motif 5.
+At position 479 to 548, the domain is characterized as S1 motif 6.
+At position 2 to 108, the domain is characterized as Calponin-homology (CH).
+At position 162 to 225, the domain is characterized as LIM zinc-binding.
+At position 671 to 818, the domain is characterized as bMERB.
+At position 394 to 651, the domain is characterized as Protein kinase.
+At position 4 to 118, the domain is characterized as WH1.
+At position 541 to 616, the domain is characterized as Cytochrome b5 heme-binding.
+At position 656 to 768, the domain is characterized as FAD-binding FR-type.
+At position 33 to 67, the domain is characterized as EF-hand 1.
+At position 68 to 103, the domain is characterized as EF-hand 2.
+At position 111 to 133, the domain is characterized as EF-hand 3.
+At position 299 to 405, the domain is characterized as ERCC4.
+At position 697 to 801, the domain is characterized as Bromo.
+At position 49 to 123, the domain is characterized as RRM 1.
+At position 134 to 212, the domain is characterized as RRM 2.
+At position 255 to 329, the domain is characterized as RRM 3.
+At position 1 to 259, the domain is characterized as NodB homology.
+At position 41 to 134, the domain is characterized as PDZ.
+At position 159 to 267, the domain is characterized as PX.
+At position 271 to 360, the domain is characterized as Ras-associating.
+At position 10 to 115, the domain is characterized as PINc.
+At position 468 to 641, the domain is characterized as tr-type G.
+At position 326 to 613, the domain is characterized as ABC transmembrane type-1 1.
+At position 672 to 905, the domain is characterized as ABC transporter 1.
+At position 1042 to 1308, the domain is characterized as ABC transmembrane type-1 2.
+At position 1345 to 1600, the domain is characterized as ABC transporter 2.
+At position 35 to 190, the domain is characterized as SIS.
+At position 38 to 150, the domain is characterized as tRNA-binding.
+At position 394 to 467, the domain is characterized as B5.
+At position 120 to 275, the domain is characterized as GST C-terminal.
+At position 39 to 318, the domain is characterized as ABC transmembrane type-1.
+At position 361 to 593, the domain is characterized as ABC transporter.
+At position 859 to 935, the domain is characterized as KHA.
+At position 125 to 360, the domain is characterized as Radical SAM core.
+At position 20 to 239, the domain is characterized as Peptidase S1.
+At position 105 to 342, the domain is characterized as Radical SAM core.
+At position 24 to 327, the domain is characterized as Protein kinase.
+At position 329 to 401, the domain is characterized as BTB.
+At position 248 to 409, the domain is characterized as DOD-type homing endonuclease.
+At position 213 to 324, the domain is characterized as HD.
+At position 327 to 402, the domain is characterized as ACT.
+At position 210 to 398, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 274, the domain is characterized as Deacetylase sirtuin-type.
+At position 15 to 79, the domain is characterized as S5 DRBM.
+At position 191 to 275, the domain is characterized as RCK C-terminal 1.
+At position 486 to 539, the domain is characterized as bHLH.
+At position 101 to 147, the domain is characterized as SERTA.
+At position 17 to 243, the domain is characterized as Radical SAM core.
+At position 338 to 495, the domain is characterized as SSD.
+At position 2 to 228, the domain is characterized as Peptidase S1.
+At position 152 to 320, the domain is characterized as GAF.
+At position 536 to 751, the domain is characterized as Histidine kinase.
+At position 411 to 579, the domain is characterized as PA14.
+At position 2 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 117 to 282, the domain is characterized as CRAL-TRIO.
+At position 4 to 207, the domain is characterized as CN hydrolase.
+At position 76 to 171, the domain is characterized as Toprim.
+At position 707 to 898, the domain is characterized as ATP-grasp 2.
+At position 312 to 364, the domain is characterized as TSP type-1.
+At position 32 to 611, the domain is characterized as Peptidase M2.
+At position 653 to 923, the domain is characterized as Protein kinase.
+At position 249 to 503, the domain is characterized as Protein kinase.
+At position 1 to 120, the domain is characterized as FZ.
+At position 458 to 667, the domain is characterized as MCM.
+At position 504 to 630, the domain is characterized as Ricin B-type lectin.
+At position 6 to 121, the domain is characterized as HSR.
+At position 134 to 290, the domain is characterized as Helicase ATP-binding.
+At position 357 to 561, the domain is characterized as Helicase C-terminal.
+At position 268 to 431, the domain is characterized as MAM 1.
+At position 441 to 477, the domain is characterized as LDL-receptor class A.
+At position 482 to 640, the domain is characterized as MAM 2.
+At position 1120 to 1396, the domain is characterized as Protein kinase.
+At position 23 to 83, the domain is characterized as Sushi 1.
+At position 267 to 324, the domain is characterized as Sushi 5.
+At position 329 to 383, the domain is characterized as Sushi 6.
+At position 387 to 444, the domain is characterized as Sushi 7.
+At position 447 to 505, the domain is characterized as Sushi 8.
+At position 507 to 569, the domain is characterized as Sushi 9.
+At position 49 to 127, the domain is characterized as RRM 1.
+At position 137 to 214, the domain is characterized as RRM 2.
+At position 230 to 307, the domain is characterized as RRM 3.
+At position 333 to 470, the domain is characterized as RRM 4.
+At position 659 to 736, the domain is characterized as PABC.
+At position 56 to 131, the domain is characterized as Carrier.
+At position 4 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 51 to 238, the domain is characterized as Rho-GAP.
+At position 135 to 389, the domain is characterized as FAD-binding FR-type.
+At position 145 to 375, the domain is characterized as ABC transmembrane type-2.
+At position 6 to 190, the domain is characterized as GMPS ATP-PPase.
+At position 109 to 198, the domain is characterized as PDZ.
+At position 82 to 165, the domain is characterized as S1 motif.
+At position 8 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 427 to 551, the domain is characterized as B5.
+At position 450 to 498, the domain is characterized as RPE1 insert.
+At position 776 to 869, the domain is characterized as FDX-ACB.
+At position 282 to 564, the domain is characterized as ABC transmembrane type-1 1.
+At position 600 to 821, the domain is characterized as ABC transporter 1.
+At position 901 to 1178, the domain is characterized as ABC transmembrane type-1 2.
+At position 1215 to 1449, the domain is characterized as ABC transporter 2.
+At position 1 to 197, the domain is characterized as Glutamine amidotransferase type-1.
+At position 38 to 226, the domain is characterized as Exonuclease.
+At position 63 to 126, the domain is characterized as CBS 1.
+At position 133 to 190, the domain is characterized as CBS 2.
+At position 233 to 293, the domain is characterized as CBS 3.
+At position 301 to 358, the domain is characterized as CBS 4.
+At position 411 to 498, the domain is characterized as PB1.
+At position 562 to 624, the domain is characterized as KH.
+At position 634 to 703, the domain is characterized as S1 motif.
+At position 102 to 162, the domain is characterized as HTH myb-type.
+At position 6 to 139, the domain is characterized as HIT.
+At position 157 to 257, the domain is characterized as Fe2OG dioxygenase.
+At position 179 to 378, the domain is characterized as Helicase ATP-binding.
+At position 403 to 615, the domain is characterized as Helicase C-terminal.
+At position 492 to 646, the domain is characterized as Helicase C-terminal.
+At position 8 to 66, the domain is characterized as PWWP.
+At position 2 to 75, the domain is characterized as RRM 1.
+At position 81 to 156, the domain is characterized as RRM 2.
+At position 195 to 260, the domain is characterized as KH 1.
+At position 276 to 343, the domain is characterized as KH 2.
+At position 405 to 470, the domain is characterized as KH 3.
+At position 487 to 553, the domain is characterized as KH 4.
+At position 29 to 72, the domain is characterized as P-type.
+At position 7 to 101, the domain is characterized as DMAP1-binding.
+At position 743 to 871, the domain is characterized as BAH 1.
+At position 967 to 1089, the domain is characterized as BAH 2.
+At position 1131 to 1590, the domain is characterized as SAM-dependent MTase C5-type.
+At position 414 to 559, the domain is characterized as MATH.
+At position 61 to 127, the domain is characterized as KH.
+At position 26 to 228, the domain is characterized as DHFR.
+At position 8 to 137, the domain is characterized as RNase III.
+At position 174 to 302, the domain is characterized as GGDEF.
+At position 7 to 74, the domain is characterized as HTH gntR-type.
+At position 29 to 194, the domain is characterized as C-type lectin.
+At position 35 to 142, the domain is characterized as Ig-like V-type 1.
+At position 155 to 262, the domain is characterized as Ig-like V-type 2.
+At position 275 to 382, the domain is characterized as Ig-like V-type 3.
+At position 393 to 500, the domain is characterized as Ig-like V-type 4.
+At position 509 to 616, the domain is characterized as Ig-like V-type 5.
+At position 631 to 695, the domain is characterized as Ig-like C2-type.
+At position 105 to 304, the domain is characterized as ATP-grasp.
+At position 330 to 447, the domain is characterized as SET.
+At position 126 to 319, the domain is characterized as ATP-grasp.
+At position 384 to 416, the domain is characterized as FBD.
+At position 282 to 516, the domain is characterized as ABC transporter 2.
+At position 184 to 269, the domain is characterized as PDZ.
+At position 304 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 404 to 503, the domain is characterized as ERCC4.
+At position 3 to 182, the domain is characterized as UBC core.
+At position 453 to 582, the domain is characterized as C2 2.
+At position 39 to 114, the domain is characterized as KH type-2.
+At position 2 to 161, the domain is characterized as Obg.
+At position 162 to 328, the domain is characterized as OBG-type G.
+At position 2 to 141, the domain is characterized as Thioredoxin.
+At position 77 to 184, the domain is characterized as AB hydrolase-1.
+At position 647 to 812, the domain is characterized as MOSC.
+At position 184 to 281, the domain is characterized as HTH araC/xylS-type.
+At position 45 to 86, the domain is characterized as UBA 1.
+At position 194 to 235, the domain is characterized as UBA 2.
+At position 336 to 663, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 53 to 199, the domain is characterized as Cupin type-1.
+At position 58 to 107, the domain is characterized as HTH myb-type 2.
+At position 148 to 243, the domain is characterized as PpiC.
+At position 30 to 59, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 78 to 246, the domain is characterized as Helicase ATP-binding.
+At position 270 to 443, the domain is characterized as Helicase C-terminal.
+At position 31 to 196, the domain is characterized as SIS.
+At position 327 to 388, the domain is characterized as SH3.
+At position 164 to 542, the domain is characterized as GRAS.
+At position 179 to 277, the domain is characterized as ELM2.
+At position 282 to 334, the domain is characterized as SANT.
+At position 282 to 443, the domain is characterized as PH.
+At position 464 to 584, the domain is characterized as Arf-GAP.
+At position 14 to 93, the domain is characterized as GIY-YIG.
+At position 226 to 426, the domain is characterized as Rho-GAP.
+At position 43 to 150, the domain is characterized as PH 1.
+At position 387 to 483, the domain is characterized as PH 2.
+At position 47 to 354, the domain is characterized as HAP1 N-terminal.
+At position 90 to 168, the domain is characterized as RRM.
+At position 51 to 86, the domain is characterized as ShKT.
+At position 219 to 282, the domain is characterized as FHA.
+At position 88 to 165, the domain is characterized as RRM.
+At position 36 to 86, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 96 to 149, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 158 to 208, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 321 to 423, the domain is characterized as CS 2.
+At position 536 to 1253, the domain is characterized as USP.
+At position 13 to 223, the domain is characterized as YjeF N-terminal.
+At position 297 to 537, the domain is characterized as Glutamine amidotransferase type-1.
+At position 127 to 160, the domain is characterized as EF-hand 4.
+At position 32 to 327, the domain is characterized as Protein kinase.
+At position 366 to 555, the domain is characterized as PID.
+At position 568 to 653, the domain is characterized as PDZ 1.
+At position 659 to 735, the domain is characterized as PDZ 2.
+At position 849 to 1044, the domain is characterized as DH.
+At position 1086 to 1188, the domain is characterized as PH.
+At position 282 to 583, the domain is characterized as Deacetylase sirtuin-type.
+At position 21 to 306, the domain is characterized as GH16.
+At position 43 to 209, the domain is characterized as NHR 1.
+At position 319 to 486, the domain is characterized as NHR 2.
+At position 522 to 688, the domain is characterized as NHR 3.
+At position 718 to 886, the domain is characterized as NHR 4.
+At position 915 to 1087, the domain is characterized as NHR 5.
+At position 1132 to 1295, the domain is characterized as NHR 6.
+At position 120 to 179, the domain is characterized as CBS 1.
+At position 183 to 239, the domain is characterized as CBS 2.
+At position 209 to 378, the domain is characterized as tr-type G.
+At position 19 to 274, the domain is characterized as ABC transporter.
+At position 332 to 543, the domain is characterized as ABC transmembrane type-2.
+At position 520 to 703, the domain is characterized as Flavodoxin-like.
+At position 756 to 1002, the domain is characterized as FAD-binding FR-type.
+At position 1 to 174, the domain is characterized as PXA.
+At position 125 to 191, the domain is characterized as DRBM 1.
+At position 283 to 347, the domain is characterized as DRBM 2.
+At position 414 to 741, the domain is characterized as A to I editase.
+At position 57 to 347, the domain is characterized as ABC transmembrane type-1 1.
+At position 380 to 625, the domain is characterized as ABC transporter 1.
+At position 699 to 986, the domain is characterized as ABC transmembrane type-1 2.
+At position 1021 to 1259, the domain is characterized as ABC transporter 2.
+At position 162 to 200, the domain is characterized as UBA.
+At position 17 to 207, the domain is characterized as RNase H type-2.
+At position 514 to 628, the domain is characterized as SMC hinge.
+At position 401 to 444, the domain is characterized as PAC.
+At position 57 to 338, the domain is characterized as Deacetylase sirtuin-type.
+At position 124 to 484, the domain is characterized as PTS EIIC type-1.
+At position 217 to 280, the domain is characterized as bZIP.
+At position 171 to 340, the domain is characterized as tr-type G.
+At position 152 to 477, the domain is characterized as Kinesin motor.
+At position 62 to 306, the domain is characterized as Velvet.
+At position 45 to 193, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 248, the domain is characterized as PABS.
+At position 193 to 366, the domain is characterized as EngA-type G 2.
+At position 367 to 451, the domain is characterized as KH-like.
+At position 197 to 439, the domain is characterized as ABC transporter 1.
+At position 892 to 1130, the domain is characterized as ABC transporter 2.
+At position 185 to 450, the domain is characterized as Lon N-terminal.
+At position 899 to 1085, the domain is characterized as Lon proteolytic.
+At position 23 to 70, the domain is characterized as F-box.
+At position 104 to 280, the domain is characterized as FBA.
+At position 18 to 96, the domain is characterized as RRM.
+At position 1 to 199, the domain is characterized as Macro.
+At position 358 to 571, the domain is characterized as TLDc.
+At position 555 to 725, the domain is characterized as tr-type G.
+At position 17 to 246, the domain is characterized as tr-type G.
+At position 355 to 439, the domain is characterized as OCT.
+At position 155 to 235, the domain is characterized as RRM Nup35-type.
+At position 10 to 67, the domain is characterized as HTH lysR-type.
+At position 179 to 460, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 84 to 146, the domain is characterized as S4 RNA-binding.
+At position 1642 to 1719, the domain is characterized as Carrier 1.
+At position 1760 to 1837, the domain is characterized as Carrier 2.
+At position 289 to 375, the domain is characterized as PPIase FKBP-type.
+At position 165 to 438, the domain is characterized as ABC transporter 1.
+At position 516 to 729, the domain is characterized as ABC transmembrane type-2 1.
+At position 1163 to 1377, the domain is characterized as ABC transmembrane type-2 2.
+At position 67 to 393, the domain is characterized as ABC transmembrane type-1.
+At position 427 to 639, the domain is characterized as ABC transporter.
+At position 293 to 432, the domain is characterized as SIS 1.
+At position 466 to 607, the domain is characterized as SIS 2.
+At position 17 to 148, the domain is characterized as EamA 1.
+At position 162 to 286, the domain is characterized as EamA 2.
+At position 22 to 660, the domain is characterized as Vitellogenin.
+At position 1442 to 1617, the domain is characterized as VWFD.
+At position 96 to 184, the domain is characterized as PB1.
+At position 35 to 136, the domain is characterized as LOB.
+At position 119 to 172, the domain is characterized as Ig-like C2-type 2.
+At position 1 to 443, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 458 to 701, the domain is characterized as UvrD-like helicase C-terminal.
+At position 340 to 392, the domain is characterized as HTH psq-type.
+At position 12 to 179, the domain is characterized as FAD-binding PCMH-type.
+At position 12 to 86, the domain is characterized as S1-like.
+At position 63 to 98, the domain is characterized as EF-hand 2.
+At position 195 to 230, the domain is characterized as EF-hand 5.
+At position 235 to 270, the domain is characterized as EF-hand 6.
+At position 186 to 230, the domain is characterized as EGF-like.
+At position 228 to 484, the domain is characterized as ZP.
+At position 129 to 164, the domain is characterized as EF-hand.
+At position 572 to 632, the domain is characterized as KH.
+At position 657 to 718, the domain is characterized as S1 motif.
+At position 2 to 27, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 1 to 234, the domain is characterized as ABC transporter.
+At position 26 to 149, the domain is characterized as Avidin-like.
+At position 337 to 414, the domain is characterized as REM-1.
+At position 486 to 547, the domain is characterized as SH3.
+At position 19 to 144, the domain is characterized as CMP/dCMP-type deaminase.
+At position 11 to 452, the domain is characterized as Helicase ATP-binding.
+At position 435 to 569, the domain is characterized as C2 2.
+At position 69 to 285, the domain is characterized as Radical SAM core.
+At position 74 to 153, the domain is characterized as Tudor 1.
+At position 611 to 789, the domain is characterized as Helicase ATP-binding.
+At position 823 to 980, the domain is characterized as Helicase C-terminal.
+At position 1335 to 1394, the domain is characterized as Tudor 2.
+At position 1618 to 1704, the domain is characterized as CS.
+At position 20 to 77, the domain is characterized as PWWP.
+At position 838 to 979, the domain is characterized as CID.
+At position 9 to 111, the domain is characterized as ATP-cone 1.
+At position 118 to 217, the domain is characterized as ATP-cone 2.
+At position 235 to 325, the domain is characterized as ATP-cone 3.
+At position 51 to 125, the domain is characterized as H15.
+At position 225 to 412, the domain is characterized as Glutamine amidotransferase type-1.
+At position 164 to 344, the domain is characterized as Helicase ATP-binding.
+At position 355 to 517, the domain is characterized as Helicase C-terminal.
+At position 22 to 276, the domain is characterized as ABC transporter.
+At position 356 to 566, the domain is characterized as ABC transmembrane type-2.
+At position 143 to 238, the domain is characterized as PB1.
+At position 196 to 231, the domain is characterized as Tify.
+At position 6 to 80, the domain is characterized as Ubiquitin-like.
+At position 109 to 497, the domain is characterized as USP.
+At position 115 to 186, the domain is characterized as PDZ 1.
+At position 199 to 291, the domain is characterized as PDZ 2.
+At position 30 to 353, the domain is characterized as Kinesin motor.
+At position 214 to 374, the domain is characterized as TrmE-type G.
+At position 77 to 251, the domain is characterized as FAD-binding PCMH-type.
+At position 26 to 216, the domain is characterized as Glutamine amidotransferase type-1.
+At position 217 to 415, the domain is characterized as GMPS ATP-PPase.
+At position 297 to 637, the domain is characterized as DOT1.
+At position 216 to 373, the domain is characterized as TrmE-type G.
+At position 3 to 391, the domain is characterized as BRO1.
+At position 45 to 139, the domain is characterized as Ig-like C2-type 1.
+At position 148 to 238, the domain is characterized as Fibronectin type-III.
+At position 261 to 345, the domain is characterized as Ig-like C2-type 2.
+At position 905 to 970, the domain is characterized as HP.
+At position 428 to 583, the domain is characterized as SSD.
+At position 243 to 565, the domain is characterized as NACHT.
+At position 390 to 441, the domain is characterized as bHLH.
+At position 203 to 504, the domain is characterized as Protein kinase.
+At position 26 to 187, the domain is characterized as PPIase cyclophilin-type.
+At position 678 to 713, the domain is characterized as Anaphylatoxin-like.
+At position 1525 to 1671, the domain is characterized as NTR.
+At position 30 to 152, the domain is characterized as CMP/dCMP-type deaminase.
+At position 206 to 439, the domain is characterized as START.
+At position 41 to 149, the domain is characterized as CUB.
+At position 154 to 356, the domain is characterized as Pentraxin (PTX).
+At position 770 to 822, the domain is characterized as GPS.
+At position 11 to 254, the domain is characterized as ABC transporter.
+At position 531 to 581, the domain is characterized as SANT.
+At position 638 to 737, the domain is characterized as CXC.
+At position 752 to 867, the domain is characterized as SET.
+At position 77 to 171, the domain is characterized as Fe2OG dioxygenase.
+At position 150 to 447, the domain is characterized as USP.
+At position 349 to 448, the domain is characterized as BRCT.
+At position 43 to 95, the domain is characterized as KH type-2.
+At position 27 to 133, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 144 to 256, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 31 to 101, the domain is characterized as S1 motif 1.
+At position 116 to 179, the domain is characterized as S1 motif 2.
+At position 200 to 268, the domain is characterized as S1 motif 3.
+At position 285 to 355, the domain is characterized as S1 motif 4.
+At position 372 to 440, the domain is characterized as S1 motif 5.
+At position 457 to 521, the domain is characterized as S1 motif 6.
+At position 351 to 623, the domain is characterized as Protein kinase.
+At position 50 to 344, the domain is characterized as Protein kinase.
+At position 141 to 228, the domain is characterized as Ig-like C2-type.
+At position 256 to 438, the domain is characterized as VWFA.
+At position 452 to 549, the domain is characterized as Cache.
+At position 121 to 203, the domain is characterized as PDZ.
+At position 3 to 80, the domain is characterized as MIT.
+At position 427 to 438, the domain is characterized as EGF-like.
+At position 23 to 314, the domain is characterized as GH18.
+At position 221 to 264, the domain is characterized as CUE.
+At position 486 to 654, the domain is characterized as Helicase ATP-binding.
+At position 835 to 997, the domain is characterized as Helicase C-terminal.
+At position 19 to 120, the domain is characterized as Ig-like V-type 1; required for binding to polymeric IgA and IgM.
+At position 145 to 238, the domain is characterized as Ig-like V-type 2.
+At position 251 to 351, the domain is characterized as Ig-like V-type 3.
+At position 363 to 460, the domain is characterized as Ig-like V-type 4.
+At position 464 to 563, the domain is characterized as Ig-like V-type 5.
+At position 28 to 510, the domain is characterized as Sema.
+At position 862 to 957, the domain is characterized as IPT/TIG 1.
+At position 959 to 1043, the domain is characterized as IPT/TIG 2.
+At position 1046 to 1145, the domain is characterized as IPT/TIG 3.
+At position 1148 to 1234, the domain is characterized as IPT/TIG 4.
+At position 33 to 91, the domain is characterized as Cystatin.
+At position 17 to 88, the domain is characterized as KRAB.
+At position 671 to 868, the domain is characterized as Flavodoxin-like.
+At position 928 to 1167, the domain is characterized as FAD-binding FR-type.
+At position 389 to 814, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1307 to 1627, the domain is characterized as PKS/mFAS DH.
+At position 1684 to 1758, the domain is characterized as Carrier.
+At position 13 to 142, the domain is characterized as Cyclin N-terminal.
+At position 95 to 186, the domain is characterized as SH2.
+At position 25 to 213, the domain is characterized as Reticulon.
+At position 136 to 232, the domain is characterized as PpiC.
+At position 406 to 598, the domain is characterized as DH.
+At position 654 to 754, the domain is characterized as PH.
+At position 72 to 147, the domain is characterized as ACT.
+At position 423 to 498, the domain is characterized as B5.
+At position 724 to 817, the domain is characterized as FDX-ACB.
+At position 420 to 565, the domain is characterized as JmjC.
+At position 178 to 269, the domain is characterized as PPIase FKBP-type.
+At position 9 to 201, the domain is characterized as tr-type G.
+At position 551 to 596, the domain is characterized as G-patch.
+At position 600 to 664, the domain is characterized as R3H.
+At position 45 to 118, the domain is characterized as IGFBP N-terminal.
+At position 121 to 186, the domain is characterized as VWFC.
+At position 215 to 260, the domain is characterized as TSP type-1.
+At position 273 to 347, the domain is characterized as CTCK.
+At position 444 to 508, the domain is characterized as J.
+At position 2 to 148, the domain is characterized as Jacalin-type lectin 1.
+At position 151 to 293, the domain is characterized as Jacalin-type lectin 2.
+At position 295 to 445, the domain is characterized as Jacalin-type lectin 3.
+At position 452 to 595, the domain is characterized as Jacalin-type lectin 4.
+At position 91 to 126, the domain is characterized as EF-hand 1.
+At position 226 to 261, the domain is characterized as EF-hand 3.
+At position 271 to 306, the domain is characterized as EF-hand 4.
+At position 307 to 342, the domain is characterized as EF-hand 5.
+At position 364 to 692, the domain is characterized as GH10.
+At position 700 to 870, the domain is characterized as CBM-cenC 1.
+At position 871 to 1059, the domain is characterized as CBM-cenC 2.
+At position 844 to 909, the domain is characterized as HP.
+At position 737 to 823, the domain is characterized as PI3K-RBD.
+At position 888 to 1036, the domain is characterized as C2 PI3K-type.
+At position 1060 to 1238, the domain is characterized as PIK helical.
+At position 1304 to 1581, the domain is characterized as PI3K/PI4K catalytic.
+At position 31 to 207, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 103, the domain is characterized as Phytocyanin.
+At position 95 to 330, the domain is characterized as Radical SAM core.
+At position 4 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 91 to 162, the domain is characterized as PRC barrel.
+At position 930 to 1022, the domain is characterized as Fibronectin type-III 1.
+At position 1158 to 1252, the domain is characterized as Fibronectin type-III 2.
+At position 341 to 614, the domain is characterized as Protein kinase.
+At position 4 to 90, the domain is characterized as Carrier.
+At position 376 to 543, the domain is characterized as tr-type G.
+At position 121 to 310, the domain is characterized as ATP-grasp.
+At position 163 to 224, the domain is characterized as SH3.
+At position 241 to 305, the domain is characterized as SAM.
+At position 59 to 206, the domain is characterized as Tyrosine-protein phosphatase.
+At position 21 to 123, the domain is characterized as Ig-like.
+At position 132 to 192, the domain is characterized as CBS 1.
+At position 194 to 250, the domain is characterized as CBS 2.
+At position 64 to 104, the domain is characterized as EGF-like.
+At position 61 to 246, the domain is characterized as HD.
+At position 217 to 399, the domain is characterized as FtsK.
+At position 73 to 171, the domain is characterized as Plastocyanin-like.
+At position 8 to 77, the domain is characterized as HTH gntR-type.
+At position 477 to 574, the domain is characterized as SH2.
+At position 45 to 115, the domain is characterized as POTRA.
+At position 13 to 88, the domain is characterized as Sm.
+At position 98 to 314, the domain is characterized as BURP.
+At position 403 to 525, the domain is characterized as RCK N-terminal.
+At position 533 to 614, the domain is characterized as RCK C-terminal.
+At position 1 to 114, the domain is characterized as C2.
+At position 378 to 638, the domain is characterized as Protein kinase.
+At position 639 to 707, the domain is characterized as AGC-kinase C-terminal.
+At position 558 to 826, the domain is characterized as MHD.
+At position 392 to 558, the domain is characterized as N-acetyltransferase.
+At position 52 to 164, the domain is characterized as C-type lectin.
+At position 36 to 320, the domain is characterized as Protein kinase.
+At position 173 to 276, the domain is characterized as Thioredoxin.
+At position 109 to 221, the domain is characterized as DUF1279.
+At position 155 to 316, the domain is characterized as 3'-5' exonuclease.
+At position 627 to 701, the domain is characterized as S1 motif.
+At position 8 to 116, the domain is characterized as SET.
+At position 31 to 81, the domain is characterized as LIM zinc-binding 1.
+At position 90 to 144, the domain is characterized as LIM zinc-binding 2.
+At position 3 to 135, the domain is characterized as Galectin.
+At position 180 to 356, the domain is characterized as EngA-type G 2.
+At position 357 to 437, the domain is characterized as KH-like.
+At position 85 to 383, the domain is characterized as Peptidase A1.
+At position 416 to 532, the domain is characterized as PH.
+At position 576 to 832, the domain is characterized as Protein kinase.
+At position 35 to 416, the domain is characterized as Helicase ATP-binding.
+At position 666 to 701, the domain is characterized as UVR.
+At position 94 to 184, the domain is characterized as CTCK.
+At position 4 to 153, the domain is characterized as N-acetyltransferase.
+At position 60 to 155, the domain is characterized as Fibronectin type-III 1.
+At position 159 to 254, the domain is characterized as Fibronectin type-III 2.
+At position 310 to 398, the domain is characterized as Fibronectin type-III 3.
+At position 401 to 501, the domain is characterized as Fibronectin type-III 4.
+At position 474 to 566, the domain is characterized as Fibronectin type-III 5.
+At position 570 to 665, the domain is characterized as Fibronectin type-III 6.
+At position 670 to 759, the domain is characterized as Fibronectin type-III 7.
+At position 764 to 854, the domain is characterized as Fibronectin type-III 8.
+At position 859 to 948, the domain is characterized as Fibronectin type-III 9.
+At position 953 to 1053, the domain is characterized as Fibronectin type-III 10.
+At position 1058 to 1151, the domain is characterized as Fibronectin type-III 11.
+At position 1156 to 1243, the domain is characterized as Fibronectin type-III 12.
+At position 1248 to 1341, the domain is characterized as Fibronectin type-III 13.
+At position 1345 to 1431, the domain is characterized as Fibronectin type-III 14.
+At position 1435 to 1539, the domain is characterized as Fibronectin type-III 15.
+At position 1544 to 1642, the domain is characterized as Fibronectin type-III 16.
+At position 1647 to 1748, the domain is characterized as Fibronectin type-III 17.
+At position 2006 to 2262, the domain is characterized as Tyrosine-protein phosphatase.
+At position 238 to 473, the domain is characterized as CN hydrolase.
+At position 61 to 224, the domain is characterized as SIS.
+At position 257 to 431, the domain is characterized as GATase cobBQ-type.
+At position 2 to 240, the domain is characterized as GP-PDE.
+At position 223 to 274, the domain is characterized as HAMP.
+At position 293 to 529, the domain is characterized as Methyl-accepting transducer.
+At position 54 to 94, the domain is characterized as EGF-like.
+At position 214 to 345, the domain is characterized as Plus3.
+At position 120 to 358, the domain is characterized as GB1/RHD3-type G.
+At position 100 to 350, the domain is characterized as Protein kinase.
+At position 22 to 131, the domain is characterized as sHSP.
+At position 213 to 593, the domain is characterized as GRAS.
+At position 445 to 619, the domain is characterized as tr-type G.
+At position 73 to 266, the domain is characterized as RNase H type-2.
+At position 1 to 270, the domain is characterized as Lon N-terminal.
+At position 691 to 870, the domain is characterized as Lon proteolytic.
+At position 46 to 247, the domain is characterized as Helicase ATP-binding.
+At position 284 to 434, the domain is characterized as Helicase C-terminal.
+At position 43 to 113, the domain is characterized as SH3.
+At position 46 to 98, the domain is characterized as bHLH.
+At position 55 to 121, the domain is characterized as FAS1.
+At position 7 to 37, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 50 to 81, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 82 to 111, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 83 to 278, the domain is characterized as SMP-LTD.
+At position 1 to 168, the domain is characterized as Miro 1.
+At position 419 to 579, the domain is characterized as Miro 2.
+At position 301 to 365, the domain is characterized as PWWP.
+At position 441 to 500, the domain is characterized as FYR N-terminal.
+At position 504 to 586, the domain is characterized as FYR C-terminal.
+At position 898 to 1016, the domain is characterized as SET.
+At position 1022 to 1038, the domain is characterized as Post-SET.
+At position 591 to 671, the domain is characterized as BRCT.
+At position 55 to 147, the domain is characterized as ARID.
+At position 642 to 709, the domain is characterized as Chromo 1.
+At position 724 to 790, the domain is characterized as Chromo 2.
+At position 823 to 997, the domain is characterized as Helicase ATP-binding.
+At position 1137 to 1288, the domain is characterized as Helicase C-terminal.
+At position 404 to 481, the domain is characterized as REM-1.
+At position 550 to 611, the domain is characterized as SH3.
+At position 119 to 187, the domain is characterized as H15.
+At position 28 to 83, the domain is characterized as Laminin EGF-like 1.
+At position 84 to 130, the domain is characterized as Laminin EGF-like 2.
+At position 139 to 186, the domain is characterized as Laminin EGF-like 3.
+At position 187 to 196, the domain is characterized as Laminin EGF-like 4; first part.
+At position 213 to 381, the domain is characterized as Laminin IV type A.
+At position 382 to 415, the domain is characterized as Laminin EGF-like 4; second part.
+At position 416 to 461, the domain is characterized as Laminin EGF-like 5.
+At position 462 to 516, the domain is characterized as Laminin EGF-like 6.
+At position 517 to 572, the domain is characterized as Laminin EGF-like 7.
+At position 573 to 602, the domain is characterized as Laminin EGF-like 8; truncated.
+At position 297 to 477, the domain is characterized as Rab-GAP TBC.
+At position 14 to 211, the domain is characterized as NYN.
+At position 588 to 869, the domain is characterized as Protein kinase.
+At position 36 to 328, the domain is characterized as Protein kinase.
+At position 77 to 206, the domain is characterized as SEC7.
+At position 265 to 381, the domain is characterized as PH.
+At position 205 to 643, the domain is characterized as Myotubularin phosphatase.
+At position 175 to 288, the domain is characterized as SRCR 2.
+At position 309 to 409, the domain is characterized as SRCR 3.
+At position 419 to 470, the domain is characterized as SRCR 4.
+At position 476 to 579, the domain is characterized as SRCR 5.
+At position 209 to 396, the domain is characterized as Histidine kinase.
+At position 585 to 689, the domain is characterized as tRNA-binding.
+At position 72 to 230, the domain is characterized as Tyrosine-protein phosphatase.
+At position 222 to 370, the domain is characterized as Exonuclease.
+At position 488 to 562, the domain is characterized as RRM 1.
+At position 583 to 662, the domain is characterized as RRM 2.
+At position 10 to 215, the domain is characterized as YjeF N-terminal.
+At position 112 to 403, the domain is characterized as SET.
+At position 15 to 88, the domain is characterized as J.
+At position 106 to 168, the domain is characterized as DPH-type MB.
+At position 25 to 442, the domain is characterized as GH18.
+At position 1 to 196, the domain is characterized as GH16.
+At position 34 to 209, the domain is characterized as Helicase ATP-binding.
+At position 242 to 443, the domain is characterized as Helicase C-terminal.
+At position 60 to 142, the domain is characterized as Lipoyl-binding.
+At position 25 to 124, the domain is characterized as Phytocyanin.
+At position 28 to 240, the domain is characterized as MIF4G.
+At position 226 to 334, the domain is characterized as PX.
+At position 63 to 344, the domain is characterized as Protein kinase.
+At position 326 to 496, the domain is characterized as tr-type G.
+At position 29 to 255, the domain is characterized as Peptidase S1.
+At position 32 to 388, the domain is characterized as IF rod.
+At position 430 to 546, the domain is characterized as LTD.
+At position 37 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 57 to 315, the domain is characterized as Protein kinase.
+At position 358 to 394, the domain is characterized as EF-hand 1.
+At position 395 to 430, the domain is characterized as EF-hand 2.
+At position 431 to 466, the domain is characterized as EF-hand 3.
+At position 467 to 502, the domain is characterized as EF-hand 4.
+At position 6 to 197, the domain is characterized as UmuC.
+At position 116 to 400, the domain is characterized as SET.
+At position 26 to 220, the domain is characterized as Velvet.
+At position 34 to 262, the domain is characterized as Peptidase S1.
+At position 27 to 93, the domain is characterized as S1 motif 1.
+At position 111 to 177, the domain is characterized as S1 motif 2.
+At position 198 to 266, the domain is characterized as S1 motif 3.
+At position 283 to 353, the domain is characterized as S1 motif 4.
+At position 370 to 440, the domain is characterized as S1 motif 5.
+At position 459 to 530, the domain is characterized as S1 motif 6.
+At position 102 to 308, the domain is characterized as Rho-GAP.
+At position 68 to 137, the domain is characterized as POTRA.
+At position 539 to 838, the domain is characterized as Peptidase M60.
+At position 30 to 108, the domain is characterized as Inhibitor I9.
+At position 140 to 656, the domain is characterized as Peptidase S8.
+At position 409 to 504, the domain is characterized as PA.
+At position 3 to 148, the domain is characterized as Toprim.
+At position 158 to 389, the domain is characterized as tr-type G.
+At position 199 to 475, the domain is characterized as Reverse transcriptase.
+At position 17 to 247, the domain is characterized as ABC transporter.
+At position 133 to 429, the domain is characterized as ABC transmembrane type-1.
+At position 465 to 699, the domain is characterized as ABC transporter.
+At position 185 to 220, the domain is characterized as EF-hand 1.
+At position 224 to 259, the domain is characterized as EF-hand 2.
+At position 310 to 460, the domain is characterized as Fe2OG dioxygenase.
+At position 1237 to 1325, the domain is characterized as Toprim.
+At position 28 to 254, the domain is characterized as AB hydrolase-1.
+At position 238 to 327, the domain is characterized as Fibronectin type-III.
+At position 7 to 217, the domain is characterized as ABC transporter 1.
+At position 285 to 512, the domain is characterized as ABC transporter 2.
+At position 1 to 87, the domain is characterized as CARD 1.
+At position 92 to 172, the domain is characterized as CARD 2.
+At position 252 to 431, the domain is characterized as Helicase ATP-binding.
+At position 611 to 777, the domain is characterized as Helicase C-terminal.
+At position 791 to 926, the domain is characterized as RLR CTR.
+At position 30 to 94, the domain is characterized as SH3.
+At position 900 to 1034, the domain is characterized as N-terminal Ras-GEF.
+At position 1068 to 1305, the domain is characterized as Ras-GEF.
+At position 119 to 433, the domain is characterized as Peptidase S8.
+At position 442 to 574, the domain is characterized as P/Homo B.
+At position 454 to 650, the domain is characterized as FtsK.
+At position 36 to 114, the domain is characterized as ACT.
+At position 253 to 439, the domain is characterized as GATase cobBQ-type.
+At position 84 to 144, the domain is characterized as S4 RNA-binding.
+At position 34 to 68, the domain is characterized as EGF-like.
+At position 71 to 108, the domain is characterized as ShKT.
+At position 24 to 662, the domain is characterized as Vitellogenin.
+At position 1389 to 1565, the domain is characterized as VWFD.
+At position 6 to 269, the domain is characterized as PH 1.
+At position 87 to 170, the domain is characterized as PDZ.
+At position 293 to 401, the domain is characterized as PH 2.
+At position 449 to 505, the domain is characterized as SU.
+At position 24 to 435, the domain is characterized as ABC transporter.
+At position 364 to 431, the domain is characterized as TRAM.
+At position 289 to 437, the domain is characterized as N-acetyltransferase.
+At position 182 to 400, the domain is characterized as Lon N-terminal.
+At position 861 to 1049, the domain is characterized as Lon proteolytic.
+At position 494 to 594, the domain is characterized as Chromo 1.
+At position 622 to 697, the domain is characterized as Chromo 2.
+At position 738 to 922, the domain is characterized as Helicase ATP-binding.
+At position 1054 to 1203, the domain is characterized as Helicase C-terminal.
+At position 1 to 230, the domain is characterized as Deacetylase sirtuin-type.
+At position 40 to 77, the domain is characterized as EGF-like 1.
+At position 78 to 118, the domain is characterized as EGF-like 2.
+At position 119 to 156, the domain is characterized as EGF-like 3.
+At position 158 to 195, the domain is characterized as EGF-like 4; calcium-binding.
+At position 197 to 234, the domain is characterized as EGF-like 5.
+At position 236 to 272, the domain is characterized as EGF-like 6; calcium-binding.
+At position 274 to 312, the domain is characterized as EGF-like 7.
+At position 314 to 350, the domain is characterized as EGF-like 8; calcium-binding.
+At position 351 to 389, the domain is characterized as EGF-like 9.
+At position 391 to 429, the domain is characterized as EGF-like 10; calcium-binding.
+At position 431 to 467, the domain is characterized as EGF-like 11; calcium-binding.
+At position 469 to 505, the domain is characterized as EGF-like 12; calcium-binding.
+At position 507 to 543, the domain is characterized as EGF-like 13; calcium-binding.
+At position 545 to 580, the domain is characterized as EGF-like 14; calcium-binding.
+At position 582 to 618, the domain is characterized as EGF-like 15; calcium-binding.
+At position 620 to 655, the domain is characterized as EGF-like 16; calcium-binding.
+At position 657 to 693, the domain is characterized as EGF-like 17; calcium-binding.
+At position 695 to 730, the domain is characterized as EGF-like 18.
+At position 734 to 770, the domain is characterized as EGF-like 19.
+At position 771 to 808, the domain is characterized as EGF-like 20.
+At position 810 to 847, the domain is characterized as EGF-like 21; calcium-binding.
+At position 849 to 885, the domain is characterized as EGF-like 22; calcium-binding.
+At position 887 to 922, the domain is characterized as EGF-like 23; calcium-binding.
+At position 924 to 960, the domain is characterized as EGF-like 24.
+At position 962 to 998, the domain is characterized as EGF-like 25.
+At position 1000 to 1034, the domain is characterized as EGF-like 26.
+At position 1036 to 1082, the domain is characterized as EGF-like 27.
+At position 1084 to 1120, the domain is characterized as EGF-like 28.
+At position 1122 to 1158, the domain is characterized as EGF-like 29; calcium-binding.
+At position 1160 to 1203, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1205 to 1244, the domain is characterized as EGF-like 31.
+At position 1246 to 1287, the domain is characterized as EGF-like 32.
+At position 1289 to 1325, the domain is characterized as EGF-like 33.
+At position 1335 to 1373, the domain is characterized as EGF-like 34.
+At position 2 to 57, the domain is characterized as HTH lacI-type.
+At position 7 to 221, the domain is characterized as tr-type G.
+At position 344 to 410, the domain is characterized as S4 RNA-binding.
+At position 3 to 151, the domain is characterized as N-acetyltransferase.
+At position 1003 to 1223, the domain is characterized as Alpha-type protein kinase.
+At position 153 to 277, the domain is characterized as PH.
+At position 27 to 173, the domain is characterized as FZ.
+At position 157 to 242, the domain is characterized as PPIase FKBP-type.
+At position 634 to 723, the domain is characterized as BRCT.
+At position 3 to 78, the domain is characterized as Ubiquitin-like 1.
+At position 79 to 154, the domain is characterized as Ubiquitin-like 2.
+At position 155 to 230, the domain is characterized as Ubiquitin-like 3.
+At position 231 to 307, the domain is characterized as Ubiquitin-like 4.
+At position 3 to 137, the domain is characterized as ADF-H 1.
+At position 175 to 311, the domain is characterized as ADF-H 2.
+At position 322 to 390, the domain is characterized as SB.
+At position 348 to 590, the domain is characterized as NR LBD.
+At position 233 to 291, the domain is characterized as PH.
+At position 282 to 400, the domain is characterized as C2.
+At position 474 to 668, the domain is characterized as Ras-GAP.
+At position 36 to 543, the domain is characterized as Biotin carboxylation.
+At position 189 to 381, the domain is characterized as ATP-grasp.
+At position 670 to 744, the domain is characterized as Biotinyl-binding.
+At position 1492 to 1831, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1835 to 2150, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 29 to 315, the domain is characterized as FERM.
+At position 617 to 689, the domain is characterized as PDZ.
+At position 753 to 1011, the domain is characterized as Tyrosine-protein phosphatase.
+At position 157 to 380, the domain is characterized as NR LBD.
+At position 295 to 402, the domain is characterized as Ig-like C1-type.
+At position 364 to 386, the domain is characterized as WH2.
+At position 467 to 528, the domain is characterized as J.
+At position 23 to 221, the domain is characterized as GH16.
+At position 27 to 116, the domain is characterized as Ig-like C2-type 1.
+At position 111 to 228, the domain is characterized as Ig-like C2-type 2.
+At position 337 to 418, the domain is characterized as Ig-like C2-type 4.
+At position 214 to 416, the domain is characterized as Peptidase M12B.
+At position 424 to 510, the domain is characterized as Disintegrin.
+At position 656 to 688, the domain is characterized as EGF-like.
+At position 127 to 234, the domain is characterized as Glutaredoxin.
+At position 16 to 76, the domain is characterized as HTH tetR-type.
+At position 32 to 65, the domain is characterized as LRRNT.
+At position 252 to 298, the domain is characterized as LRRCT.
+At position 299 to 386, the domain is characterized as Ig-like.
+At position 424 to 520, the domain is characterized as Fibronectin type-III.
+At position 117 to 284, the domain is characterized as Nudix hydrolase.
+At position 146 to 213, the domain is characterized as GRAM 1.
+At position 293 to 361, the domain is characterized as GRAM 2.
+At position 515 to 702, the domain is characterized as Rab-GAP TBC.
+At position 886 to 921, the domain is characterized as EF-hand.
+At position 75 to 388, the domain is characterized as Peptidase A1.
+At position 1206 to 1304, the domain is characterized as PH 1.
+At position 1386 to 1491, the domain is characterized as PH 2.
+At position 1541 to 1689, the domain is characterized as MyTH4.
+At position 1694 to 2038, the domain is characterized as FERM.
+At position 189 to 249, the domain is characterized as HTH myb-type.
+At position 151 to 231, the domain is characterized as PDZ 2.
+At position 1 to 124, the domain is characterized as PTS EIIA type-4.
+At position 367 to 416, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 462 to 500, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 512 to 556, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 557 to 599, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 605 to 647, the domain is characterized as Beta/gamma crystallin 'Greek key' 5.
+At position 648 to 690, the domain is characterized as Beta/gamma crystallin 'Greek key' 6.
+At position 701 to 737, the domain is characterized as Beta/gamma crystallin 'Greek key' 7.
+At position 738 to 781, the domain is characterized as Beta/gamma crystallin 'Greek key' 8.
+At position 828 to 869, the domain is characterized as Beta/gamma crystallin 'Greek key' 9.
+At position 871 to 1003, the domain is characterized as Ricin B-type lectin.
+At position 313 to 569, the domain is characterized as Glutamine amidotransferase type-1.
+At position 607 to 693, the domain is characterized as BRCT.
+At position 37 to 124, the domain is characterized as RRM.
+At position 77 to 198, the domain is characterized as MsrB.
+At position 507 to 617, the domain is characterized as OCEL.
+At position 60 to 238, the domain is characterized as Eph LBD.
+At position 357 to 467, the domain is characterized as Fibronectin type-III 1.
+At position 468 to 562, the domain is characterized as Fibronectin type-III 2.
+At position 675 to 936, the domain is characterized as Protein kinase.
+At position 965 to 1029, the domain is characterized as SAM.
+At position 157 to 285, the domain is characterized as Fatty acid hydroxylase.
+At position 35 to 331, the domain is characterized as Protein kinase.
+At position 84 to 356, the domain is characterized as AB hydrolase-1.
+At position 503 to 594, the domain is characterized as Big-1 1.
+At position 601 to 691, the domain is characterized as Big-1 2.
+At position 1 to 115, the domain is characterized as Response regulatory.
+At position 161 to 351, the domain is characterized as CheB-type methylesterase.
+At position 200 to 390, the domain is characterized as DH.
+At position 444 to 548, the domain is characterized as PH.
+At position 597 to 741, the domain is characterized as N-terminal Ras-GEF.
+At position 780 to 1019, the domain is characterized as Ras-GEF.
+At position 263 to 383, the domain is characterized as Sox C-terminal.
+At position 43 to 112, the domain is characterized as EamA.
+At position 456 to 662, the domain is characterized as FtsK 1.
+At position 811 to 1000, the domain is characterized as FtsK 2.
+At position 1090 to 1280, the domain is characterized as FtsK 3.
+At position 779 to 853, the domain is characterized as Carrier.
+At position 2 to 232, the domain is characterized as ABC transporter.
+At position 7 to 110, the domain is characterized as IF rod.
+At position 348 to 620, the domain is characterized as Protein kinase.
+At position 245 to 423, the domain is characterized as PCI.
+At position 20 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 229 to 331, the domain is characterized as Ig-like C2-type 3.
+At position 94 to 190, the domain is characterized as BRICHOS.
+At position 39 to 97, the domain is characterized as Chitin-binding type-2.
+At position 18 to 271, the domain is characterized as Protein kinase.
+At position 310 to 336, the domain is characterized as NAF.
+At position 9 to 84, the domain is characterized as ACT.
+At position 107 to 313, the domain is characterized as ATP-grasp.
+At position 674 to 865, the domain is characterized as ATP-grasp 2.
+At position 932 to 1074, the domain is characterized as MGS-like.
+At position 101 to 136, the domain is characterized as Tify.
+At position 455 to 504, the domain is characterized as FHA.
+At position 375 to 552, the domain is characterized as Helicase ATP-binding.
+At position 609 to 758, the domain is characterized as Helicase C-terminal.
+At position 6 to 55, the domain is characterized as Myosin N-terminal SH3-like.
+At position 60 to 729, the domain is characterized as Myosin motor.
+At position 732 to 761, the domain is characterized as IQ 1.
+At position 755 to 784, the domain is characterized as IQ 2.
+At position 780 to 809, the domain is characterized as IQ 3.
+At position 803 to 832, the domain is characterized as IQ 4.
+At position 828 to 857, the domain is characterized as IQ 5.
+At position 851 to 880, the domain is characterized as IQ 6.
+At position 139 to 213, the domain is characterized as POU-specific.
+At position 111 to 189, the domain is characterized as RRM 1.
+At position 199 to 267, the domain is characterized as RRM 2.
+At position 313 to 389, the domain is characterized as RRM 3.
+At position 354 to 403, the domain is characterized as bHLH.
+At position 83 to 330, the domain is characterized as Deacetylase sirtuin-type.
+At position 136 to 226, the domain is characterized as RRM.
+At position 243 to 349, the domain is characterized as Cadherin 3.
+At position 26 to 116, the domain is characterized as BTB.
+At position 251 to 443, the domain is characterized as Helicase ATP-binding.
+At position 605 to 776, the domain is characterized as Helicase C-terminal.
+At position 1 to 93, the domain is characterized as Core-binding (CB).
+At position 114 to 294, the domain is characterized as Tyr recombinase.
+At position 621 to 808, the domain is characterized as DH.
+At position 843 to 973, the domain is characterized as PH.
+At position 995 to 1293, the domain is characterized as CNH.
+At position 180 to 229, the domain is characterized as bHLH.
+At position 344 to 625, the domain is characterized as Protein kinase.
+At position 174 to 440, the domain is characterized as MHD.
+At position 169 to 410, the domain is characterized as Protein kinase.
+At position 87 to 381, the domain is characterized as Protein kinase.
+At position 382 to 452, the domain is characterized as AGC-kinase C-terminal.
+At position 167 to 292, the domain is characterized as Fatty acid hydroxylase.
+At position 4 to 149, the domain is characterized as B12-binding.
+At position 239 to 492, the domain is characterized as Radical SAM core.
+At position 6 to 237, the domain is characterized as Glutamine amidotransferase type-1.
+At position 456 to 584, the domain is characterized as MATH.
+At position 582 to 659, the domain is characterized as BRCT.
+At position 66 to 108, the domain is characterized as Plastocyanin-like 1.
+At position 159 to 349, the domain is characterized as Plastocyanin-like 2.
+At position 460 to 588, the domain is characterized as Plastocyanin-like 3.
+At position 6 to 113, the domain is characterized as HIT.
+At position 37 to 82, the domain is characterized as F-box.
+At position 882 to 952, the domain is characterized as Bromo.
+At position 182 to 221, the domain is characterized as EGF-like.
+At position 156 to 303, the domain is characterized as C2 Aida-type.
+At position 9 to 75, the domain is characterized as Ubiquitin-like.
+At position 27 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 203, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 324, the domain is characterized as Ig-like C2-type 3.
+At position 380 to 540, the domain is characterized as TIR.
+At position 48 to 80, the domain is characterized as Collagen-like.
+At position 84 to 299, the domain is characterized as Fibrinogen C-terminal.
+At position 13 to 98, the domain is characterized as IPT/TIG.
+At position 223 to 357, the domain is characterized as GGDEF.
+At position 87 to 209, the domain is characterized as GST C-terminal.
+At position 426 to 570, the domain is characterized as UBX.
+At position 283 to 515, the domain is characterized as B30.2/SPRY.
+At position 7 to 75, the domain is characterized as PWI.
+At position 561 to 635, the domain is characterized as RRM.
+At position 235 to 297, the domain is characterized as t-SNARE coiled-coil homology.
+At position 104 to 332, the domain is characterized as Radical SAM core.
+At position 70 to 97, the domain is characterized as EF-hand 3.
+At position 98 to 131, the domain is characterized as EF-hand 4.
+At position 86 to 290, the domain is characterized as tr-type G.
+At position 205 to 548, the domain is characterized as Protein kinase.
+At position 587 to 674, the domain is characterized as Thioredoxin.
+At position 26 to 131, the domain is characterized as Glutaredoxin.
+At position 190 to 333, the domain is characterized as FCP1 homology.
+At position 16 to 57, the domain is characterized as F-box.
+At position 1 to 132, the domain is characterized as YDG.
+At position 126 to 290, the domain is characterized as SET.
+At position 163 to 219, the domain is characterized as Pre-SET.
+At position 296 to 312, the domain is characterized as Post-SET.
+At position 60 to 295, the domain is characterized as Radical SAM core.
+At position 293 to 355, the domain is characterized as TRAM.
+At position 358 to 462, the domain is characterized as Rhodanese.
+At position 1 to 252, the domain is characterized as IMD.
+At position 719 to 736, the domain is characterized as WH2.
+At position 2 to 104, the domain is characterized as BMC circularly permuted 1.
+At position 105 to 206, the domain is characterized as BMC circularly permuted 2.
+At position 26 to 156, the domain is characterized as PLAT.
+At position 159 to 857, the domain is characterized as Lipoxygenase.
+At position 11 to 279, the domain is characterized as Protein kinase.
+At position 38 to 152, the domain is characterized as CENP-V/GFA.
+At position 110 to 190, the domain is characterized as KH 1.
+At position 245 to 327, the domain is characterized as KH 2.
+At position 46 to 161, the domain is characterized as Expansin-like EG45.
+At position 171 to 250, the domain is characterized as Expansin-like CBD.
+At position 275 to 389, the domain is characterized as Cadherin 3.
+At position 390 to 494, the domain is characterized as Cadherin 4.
+At position 494 to 610, the domain is characterized as Cadherin 5.
+At position 238 to 486, the domain is characterized as Ku.
+At position 32 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 294 to 533, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 164 to 216, the domain is characterized as KH.
+At position 35 to 118, the domain is characterized as RRM 1.
+At position 126 to 205, the domain is characterized as RRM 2.
+At position 190 to 813, the domain is characterized as USP.
+At position 2 to 213, the domain is characterized as Glutamine amidotransferase type-2.
+At position 66 to 183, the domain is characterized as PDZ GRASP-type 1.
+At position 188 to 276, the domain is characterized as PDZ GRASP-type 2.
+At position 9 to 224, the domain is characterized as Radical SAM core.
+At position 379 to 546, the domain is characterized as Helicase C-terminal.
+At position 946 to 1006, the domain is characterized as Tudor.
+At position 128 to 284, the domain is characterized as CBM21.
+At position 43 to 145, the domain is characterized as HD.
+At position 482 to 556, the domain is characterized as KH.
+At position 585 to 666, the domain is characterized as RWP-RK.
+At position 847 to 926, the domain is characterized as PB1.
+At position 175 to 488, the domain is characterized as IF rod.
+At position 5 to 103, the domain is characterized as ACB.
+At position 648 to 717, the domain is characterized as RBD.
+At position 297 to 470, the domain is characterized as TNase-like.
+At position 592 to 670, the domain is characterized as Carrier.
+At position 141 to 265, the domain is characterized as Nudix hydrolase.
+At position 30 to 130, the domain is characterized as CUB.
+At position 258 to 338, the domain is characterized as U-box.
+At position 62 to 210, the domain is characterized as Cupin type-1.
+At position 38 to 131, the domain is characterized as Ig-like C2-type.
+At position 137 to 232, the domain is characterized as Fibronectin type-III 1.
+At position 237 to 341, the domain is characterized as Fibronectin type-III 2.
+At position 54 to 116, the domain is characterized as SH3.
+At position 122 to 214, the domain is characterized as SH2.
+At position 240 to 493, the domain is characterized as Protein kinase.
+At position 188 to 529, the domain is characterized as Protein kinase.
+At position 43 to 144, the domain is characterized as SRCR 1.
+At position 153 to 257, the domain is characterized as SRCR 2.
+At position 264 to 366, the domain is characterized as SRCR 3.
+At position 382 to 485, the domain is characterized as SRCR 4.
+At position 58 to 383, the domain is characterized as YcaO.
+At position 180 to 265, the domain is characterized as bHLH.
+At position 520 to 639, the domain is characterized as SMC hinge.
+At position 12 to 113, the domain is characterized as FAD-binding FR-type.
+At position 135 to 205, the domain is characterized as KH.
+At position 14 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 164 to 386, the domain is characterized as TRUD.
+At position 289 to 384, the domain is characterized as BEACH-type PH.
+At position 389 to 697, the domain is characterized as BEACH.
+At position 18 to 113, the domain is characterized as EthD.
+At position 175 to 347, the domain is characterized as EngA-type G 2.
+At position 348 to 432, the domain is characterized as KH-like.
+At position 294 to 369, the domain is characterized as PUA.
+At position 144 to 308, the domain is characterized as CRAL-TRIO.
+At position 179 to 262, the domain is characterized as RCK C-terminal 1.
+At position 263 to 346, the domain is characterized as RCK C-terminal 2.
+At position 551 to 600, the domain is characterized as PAP-associated 1.
+At position 1233 to 1286, the domain is characterized as PAP-associated 2.
+At position 598 to 679, the domain is characterized as BRCT.
+At position 111 to 180, the domain is characterized as BTB.
+At position 233 to 327, the domain is characterized as BACK.
+At position 19 to 52, the domain is characterized as CBM1.
+At position 42 to 148, the domain is characterized as Gnk2-homologous 1.
+At position 154 to 260, the domain is characterized as Gnk2-homologous 2.
+At position 344 to 624, the domain is characterized as Protein kinase.
+At position 8 to 135, the domain is characterized as RNase III.
+At position 108 to 411, the domain is characterized as PPM-type phosphatase.
+At position 21 to 180, the domain is characterized as FAD-binding PCMH-type.
+At position 166 to 214, the domain is characterized as PCI.
+At position 6 to 121, the domain is characterized as VOC.
+At position 24 to 278, the domain is characterized as Protein kinase.
+At position 310 to 334, the domain is characterized as NAF.
+At position 22 to 108, the domain is characterized as GIY-YIG.
+At position 417 to 580, the domain is characterized as YDG.
+At position 30 to 198, the domain is characterized as Era-type G.
+At position 221 to 307, the domain is characterized as KH type-2.
+At position 51 to 470, the domain is characterized as Peptidase A1.
+At position 281 to 384, the domain is characterized as Saposin B-type.
+At position 371 to 698, the domain is characterized as HECT.
+At position 26 to 348, the domain is characterized as Asparaginase/glutaminase.
+At position 34 to 151, the domain is characterized as C-type lectin.
+At position 411 to 521, the domain is characterized as PAZ.
+At position 720 to 1023, the domain is characterized as Piwi.
+At position 444 to 518, the domain is characterized as GW 1.
+At position 520 to 594, the domain is characterized as GW 2.
+At position 613 to 687, the domain is characterized as GW 3.
+At position 689 to 763, the domain is characterized as GW 4.
+At position 785 to 860, the domain is characterized as GW 5.
+At position 862 to 937, the domain is characterized as GW 6.
+At position 944 to 1018, the domain is characterized as GW 7.
+At position 27 to 155, the domain is characterized as EamA.
+At position 957 to 1051, the domain is characterized as Peptidase C50.
+At position 76 to 232, the domain is characterized as Helicase ATP-binding.
+At position 307 to 509, the domain is characterized as Helicase C-terminal.
+At position 55 to 227, the domain is characterized as Exonuclease.
+At position 73 to 155, the domain is characterized as Saposin B-type.
+At position 15 to 100, the domain is characterized as GIY-YIG.
+At position 4 to 455, the domain is characterized as BRO1.
+At position 2 to 151, the domain is characterized as RNase H type-1.
+At position 34 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 39 to 332, the domain is characterized as ABC transmembrane type-1.
+At position 389 to 603, the domain is characterized as ABC transporter.
+At position 189 to 450, the domain is characterized as NR LBD.
+At position 218 to 428, the domain is characterized as Peptidase M12B.
+At position 437 to 519, the domain is characterized as Disintegrin.
+At position 520 to 575, the domain is characterized as TSP type-1.
+At position 117 to 341, the domain is characterized as ATP-grasp.
+At position 31 to 174, the domain is characterized as Thioredoxin.
+At position 304 to 406, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 598 to 700, the domain is characterized as tRNA-binding.
+At position 361 to 418, the domain is characterized as S4 RNA-binding.
+At position 24 to 205, the domain is characterized as KARI N-terminal Rossmann.
+At position 206 to 351, the domain is characterized as KARI C-terminal knotted.
+At position 131 to 205, the domain is characterized as POU-specific.
+At position 354 to 662, the domain is characterized as ABC transmembrane type-1 1.
+At position 694 to 935, the domain is characterized as ABC transporter 1.
+At position 1026 to 1345, the domain is characterized as ABC transmembrane type-1 2.
+At position 1381 to 1636, the domain is characterized as ABC transporter 2.
+At position 40 to 203, the domain is characterized as Nudix hydrolase.
+At position 136 to 216, the domain is characterized as RRM 1.
+At position 333 to 410, the domain is characterized as RRM 2.
+At position 414 to 488, the domain is characterized as RRM 3.
+At position 708 to 886, the domain is characterized as SPOC.
+At position 67 to 145, the domain is characterized as RRM 1.
+At position 155 to 232, the domain is characterized as RRM 2.
+At position 248 to 325, the domain is characterized as RRM 3.
+At position 351 to 428, the domain is characterized as RRM 4.
+At position 563 to 644, the domain is characterized as PABC.
+At position 56 to 135, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 108 to 152, the domain is characterized as LysM 1.
+At position 183 to 227, the domain is characterized as LysM 2.
+At position 723 to 843, the domain is characterized as C2.
+At position 458 to 540, the domain is characterized as RRM.
+At position 78 to 377, the domain is characterized as AB hydrolase-1.
+At position 31 to 216, the domain is characterized as FAD-binding PCMH-type.
+At position 163 to 405, the domain is characterized as Radical SAM core.
+At position 23 to 67, the domain is characterized as CAP-Gly.
+At position 63 to 226, the domain is characterized as SIS.
+At position 190 to 256, the domain is characterized as KH.
+At position 316 to 409, the domain is characterized as HD.
+At position 125 to 160, the domain is characterized as EF-hand 2.
+At position 160 to 192, the domain is characterized as EF-hand 3.
+At position 68 to 212, the domain is characterized as SCP.
+At position 186 to 379, the domain is characterized as CheB-type methylesterase.
+At position 338 to 632, the domain is characterized as ABC transmembrane type-1 1.
+At position 664 to 908, the domain is characterized as ABC transporter 1.
+At position 981 to 1282, the domain is characterized as ABC transmembrane type-1 2.
+At position 1323 to 1572, the domain is characterized as ABC transporter 2.
+At position 145 to 532, the domain is characterized as GRAS.
+At position 97 to 155, the domain is characterized as CBS 1.
+At position 159 to 219, the domain is characterized as CBS 2.
+At position 27 to 62, the domain is characterized as EF-hand.
+At position 253 to 342, the domain is characterized as ABM.
+At position 182 to 249, the domain is characterized as SAM.
+At position 99 to 164, the domain is characterized as S4 RNA-binding.
+At position 126 to 339, the domain is characterized as ATP-grasp.
+At position 19 to 111, the domain is characterized as PPIase FKBP-type.
+At position 382 to 399, the domain is characterized as WH2.
+At position 46 to 105, the domain is characterized as TSP type-1 1.
+At position 109 to 181, the domain is characterized as TSP type-1 2.
+At position 183 to 236, the domain is characterized as TSP type-1 3.
+At position 349 to 405, the domain is characterized as TSP type-1 4.
+At position 412 to 499, the domain is characterized as TSP type-1 5.
+At position 501 to 563, the domain is characterized as TSP type-1 6.
+At position 623 to 684, the domain is characterized as TSP type-1 7.
+At position 685 to 758, the domain is characterized as TSP type-1 8.
+At position 760 to 820, the domain is characterized as TSP type-1 9.
+At position 821 to 893, the domain is characterized as TSP type-1 10.
+At position 895 to 948, the domain is characterized as TSP type-1 11.
+At position 949 to 1022, the domain is characterized as TSP type-1 12.
+At position 1024 to 1084, the domain is characterized as TSP type-1 13.
+At position 1085 to 1152, the domain is characterized as TSP type-1 14.
+At position 1154 to 1208, the domain is characterized as TSP type-1 15.
+At position 1209 to 1272, the domain is characterized as TSP type-1 16.
+At position 1274 to 1329, the domain is characterized as TSP type-1 17.
+At position 1330 to 1400, the domain is characterized as TSP type-1 18.
+At position 1402 to 1463, the domain is characterized as TSP type-1 19.
+At position 226 to 368, the domain is characterized as DM10 2.
+At position 431 to 538, the domain is characterized as DM10 3.
+At position 558 to 593, the domain is characterized as EF-hand.
+At position 91 to 152, the domain is characterized as S4 RNA-binding.
+At position 217 to 283, the domain is characterized as J.
+At position 94 to 211, the domain is characterized as AB hydrolase-1.
+At position 391 to 626, the domain is characterized as ABC transporter 1.
+At position 1206 to 1440, the domain is characterized as ABC transporter 2.
+At position 561 to 596, the domain is characterized as EF-hand 1.
+At position 597 to 632, the domain is characterized as EF-hand 2.
+At position 4 to 148, the domain is characterized as ADF-H.
+At position 424 to 465, the domain is characterized as EGF-like 5; calcium-binding.
+At position 1 to 79, the domain is characterized as Cadherin 1.
+At position 80 to 188, the domain is characterized as Cadherin 2.
+At position 189 to 293, the domain is characterized as Cadherin 3.
+At position 294 to 398, the domain is characterized as Cadherin 4.
+At position 399 to 508, the domain is characterized as Cadherin 5.
+At position 515 to 621, the domain is characterized as Cadherin 6.
+At position 18 to 294, the domain is characterized as Protein kinase.
+At position 432 to 524, the domain is characterized as CARD.
+At position 205 to 401, the domain is characterized as Peptidase M12B.
+At position 409 to 495, the domain is characterized as Disintegrin.
+At position 2 to 183, the domain is characterized as tr-type G.
+At position 229 to 412, the domain is characterized as TrmE-type G.
+At position 38 to 131, the domain is characterized as GOLD.
+At position 238 to 529, the domain is characterized as Letm1 RBD.
+At position 656 to 691, the domain is characterized as EF-hand.
+At position 43 to 77, the domain is characterized as RIIa.
+At position 25 to 128, the domain is characterized as Gnk2-homologous 1.
+At position 137 to 250, the domain is characterized as Gnk2-homologous 2.
+At position 353 to 632, the domain is characterized as Protein kinase.
+At position 46 to 224, the domain is characterized as PCI.
+At position 599 to 677, the domain is characterized as BRCT.
+At position 272 to 448, the domain is characterized as Phosphatase tensin-type.
+At position 455 to 566, the domain is characterized as C2 tensin-type.
+At position 93 to 322, the domain is characterized as Radical SAM core.
+At position 86 to 261, the domain is characterized as Bms1-type G.
+At position 77 to 249, the domain is characterized as Helicase ATP-binding.
+At position 260 to 422, the domain is characterized as Helicase C-terminal.
+At position 29 to 414, the domain is characterized as Helicase ATP-binding.
+At position 132 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 218 to 307, the domain is characterized as Ig-like C2-type 3.
+At position 251 to 458, the domain is characterized as Histidine kinase.
+At position 9 to 162, the domain is characterized as Tyrosine-protein phosphatase.
+At position 66 to 250, the domain is characterized as tr-type G.
+At position 106 to 456, the domain is characterized as Peptidase A1.
+At position 25 to 310, the domain is characterized as Protein kinase.
+At position 393 to 455, the domain is characterized as TRAM.
+At position 1244 to 1341, the domain is characterized as Fibronectin type-III 1.
+At position 1346 to 1457, the domain is characterized as Fibronectin type-III 2.
+At position 335 to 601, the domain is characterized as Radical SAM core.
+At position 168 to 286, the domain is characterized as Rhodanese 2.
+At position 611 to 646, the domain is characterized as UVR.
+At position 28 to 249, the domain is characterized as ABC transporter.
+At position 69 to 209, the domain is characterized as Guanylate cyclase 1.
+At position 318 to 438, the domain is characterized as Guanylate cyclase 2.
+At position 450 to 801, the domain is characterized as Kinesin motor.
+At position 58 to 123, the domain is characterized as NAC-A/B.
+At position 158 to 195, the domain is characterized as UBA.
+At position 6 to 137, the domain is characterized as EamA 1.
+At position 150 to 281, the domain is characterized as EamA 2.
+At position 16 to 224, the domain is characterized as YjeF N-terminal.
+At position 217 to 294, the domain is characterized as BCNT-C.
+At position 25 to 270, the domain is characterized as BAR.
+At position 284 to 477, the domain is characterized as Rho-GAP.
+At position 1 to 53, the domain is characterized as DEK-C.
+At position 116 to 193, the domain is characterized as SWIB/MDM2.
+At position 426 to 720, the domain is characterized as Protein kinase.
+At position 5 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 510 to 621, the domain is characterized as SMC hinge.
+At position 161 to 410, the domain is characterized as ABC transporter 1.
+At position 869 to 1112, the domain is characterized as ABC transporter 2.
+At position 68 to 252, the domain is characterized as RNase H type-2.
+At position 138 to 174, the domain is characterized as EF-hand 3.
+At position 104 to 182, the domain is characterized as S4 RNA-binding.
+At position 66 to 144, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 144 to 183, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 281 to 337, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 33 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 213 to 308, the domain is characterized as Ig-like C2-type 3.
+At position 330 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 415 to 523, the domain is characterized as Ig-like C2-type 5.
+At position 599 to 961, the domain is characterized as Protein kinase.
+At position 65 to 246, the domain is characterized as FAD-binding PCMH-type.
+At position 27 to 277, the domain is characterized as AB hydrolase-1.
+At position 1038 to 1310, the domain is characterized as Autotransporter.
+At position 296 to 503, the domain is characterized as MCM.
+At position 7 to 63, the domain is characterized as SpoVT-AbrB 1.
+At position 92 to 135, the domain is characterized as SpoVT-AbrB 2.
+At position 120 to 249, the domain is characterized as Fatty acid hydroxylase.
+At position 3 to 247, the domain is characterized as ABC transporter.
+At position 205 to 723, the domain is characterized as WAPL.
+At position 33 to 74, the domain is characterized as CHCH 1.
+At position 75 to 118, the domain is characterized as CHCH 2.
+At position 33 to 53, the domain is characterized as LRRNT.
+At position 107 to 274, the domain is characterized as Protein kinase.
+At position 409 to 583, the domain is characterized as tr-type G.
+At position 7 to 121, the domain is characterized as MTTase N-terminal.
+At position 379 to 441, the domain is characterized as TRAM.
+At position 1 to 69, the domain is characterized as HTH gntR-type.
+At position 50 to 96, the domain is characterized as Gla.
+At position 88 to 198, the domain is characterized as MTTase N-terminal.
+At position 222 to 459, the domain is characterized as Radical SAM core.
+At position 462 to 531, the domain is characterized as TRAM.
+At position 20 to 106, the domain is characterized as HIG1.
+At position 25 to 262, the domain is characterized as PABS.
+At position 85 to 382, the domain is characterized as USP.
+At position 30 to 61, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 240 to 420, the domain is characterized as Helicase ATP-binding.
+At position 452 to 611, the domain is characterized as Helicase C-terminal.
+At position 61 to 91, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 98 to 131, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 140 to 176, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 184 to 215, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 99 to 302, the domain is characterized as ABC transmembrane type-1.
+At position 214 to 292, the domain is characterized as RRM.
+At position 28 to 328, the domain is characterized as ABC transmembrane type-1.
+At position 360 to 597, the domain is characterized as ABC transporter.
+At position 7 to 134, the domain is characterized as VOC.
+At position 33 to 161, the domain is characterized as EamA 1.
+At position 208 to 334, the domain is characterized as EamA 2.
+At position 38 to 363, the domain is characterized as Kinesin motor.
+At position 511 to 594, the domain is characterized as PB1.
+At position 13 to 77, the domain is characterized as SH3.
+At position 228 to 292, the domain is characterized as SAM.
+At position 776 to 895, the domain is characterized as PH.
+At position 23 to 138, the domain is characterized as MTTase N-terminal.
+At position 162 to 394, the domain is characterized as Radical SAM core.
+At position 391 to 483, the domain is characterized as Disintegrin.
+At position 316 to 413, the domain is characterized as SWIRM.
+At position 33 to 124, the domain is characterized as Cadherin 1.
+At position 125 to 241, the domain is characterized as Cadherin 2.
+At position 242 to 353, the domain is characterized as Cadherin 3.
+At position 368 to 480, the domain is characterized as Cadherin 4.
+At position 481 to 586, the domain is characterized as Cadherin 5.
+At position 586 to 695, the domain is characterized as Cadherin 6.
+At position 695 to 807, the domain is characterized as Cadherin 7.
+At position 809 to 927, the domain is characterized as Cadherin 8.
+At position 929 to 1051, the domain is characterized as Cadherin 9.
+At position 9 to 130, the domain is characterized as C-type lectin.
+At position 30 to 104, the domain is characterized as REM-1.
+At position 115 to 462, the domain is characterized as BRO1.
+At position 500 to 577, the domain is characterized as PDZ.
+At position 134 to 229, the domain is characterized as Rieske.
+At position 24 to 163, the domain is characterized as Jacalin-type lectin 1.
+At position 165 to 309, the domain is characterized as Jacalin-type lectin 2.
+At position 7 to 136, the domain is characterized as EamA 1.
+At position 151 to 281, the domain is characterized as EamA 2.
+At position 88 to 241, the domain is characterized as Cytochrome c.
+At position 123 to 227, the domain is characterized as Rieske.
+At position 37 to 267, the domain is characterized as ABC transporter.
+At position 90 to 160, the domain is characterized as S4 RNA-binding.
+At position 31 to 158, the domain is characterized as ALOG.
+At position 306 to 414, the domain is characterized as SCP2.
+At position 1338 to 1413, the domain is characterized as DEP.
+At position 24 to 244, the domain is characterized as Protein kinase.
+At position 55 to 163, the domain is characterized as HIT.
+At position 37 to 139, the domain is characterized as Gnk2-homologous 1.
+At position 144 to 247, the domain is characterized as Gnk2-homologous 2.
+At position 291 to 355, the domain is characterized as Mop.
+At position 110 to 363, the domain is characterized as NR LBD.
+At position 350 to 436, the domain is characterized as KH-like.
+At position 31 to 129, the domain is characterized as HTH araC/xylS-type.
+At position 46 to 272, the domain is characterized as Radical SAM core.
+At position 602 to 665, the domain is characterized as SH3 2.
+At position 441 to 555, the domain is characterized as Toprim.
+At position 364 to 433, the domain is characterized as BTB.
+At position 664 to 925, the domain is characterized as Protein kinase.
+At position 121 to 232, the domain is characterized as C-type lectin.
+At position 712 to 787, the domain is characterized as Smr.
+At position 17 to 201, the domain is characterized as UmuC.
+At position 223 to 236, the domain is characterized as CRIB.
+At position 534 to 785, the domain is characterized as Protein kinase.
+At position 557 to 677, the domain is characterized as MHD1.
+At position 788 to 895, the domain is characterized as MHD2.
+At position 910 to 1035, the domain is characterized as C2 2.
+At position 37 to 106, the domain is characterized as POTRA.
+At position 41 to 458, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 611 to 744, the domain is characterized as C1q.
+At position 159 to 217, the domain is characterized as LysM.
+At position 14 to 246, the domain is characterized as BAR.
+At position 252 to 442, the domain is characterized as Rho-GAP.
+At position 325 to 360, the domain is characterized as EF-hand 1.
+At position 366 to 401, the domain is characterized as EF-hand 2.
+At position 41 to 114, the domain is characterized as Chitin-binding type R&R.
+At position 91 to 261, the domain is characterized as FAD-binding PCMH-type.
+At position 319 to 523, the domain is characterized as MCM.
+At position 59 to 197, the domain is characterized as Flavodoxin-like.
+At position 230 to 444, the domain is characterized as FAD-binding FR-type.
+At position 92 to 127, the domain is characterized as EF-hand 2.
+At position 87 to 203, the domain is characterized as GST C-terminal.
+At position 4 to 51, the domain is characterized as F-box.
+At position 168 to 306, the domain is characterized as OTU.
+At position 74 to 109, the domain is characterized as Tify.
+At position 143 to 185, the domain is characterized as CCT.
+At position 35 to 356, the domain is characterized as G-alpha.
+At position 241 to 393, the domain is characterized as GAF 1.
+At position 425 to 611, the domain is characterized as GAF 2.
+At position 641 to 964, the domain is characterized as PDEase.
+At position 198 to 307, the domain is characterized as Guanylate cyclase.
+At position 247 to 427, the domain is characterized as PBS-linker 1.
+At position 508 to 684, the domain is characterized as PBS-linker 2.
+At position 703 to 881, the domain is characterized as PBS-linker 3.
+At position 179 to 419, the domain is characterized as Protein kinase.
+At position 200 to 309, the domain is characterized as RRM 1.
+At position 317 to 426, the domain is characterized as RRM 2.
+At position 518 to 752, the domain is characterized as NR LBD.
+At position 7 to 155, the domain is characterized as Nudix hydrolase.
+At position 25 to 285, the domain is characterized as Protein kinase.
+At position 45 to 119, the domain is characterized as H15.
+At position 16 to 100, the domain is characterized as Cytochrome b5 heme-binding.
+At position 256 to 349, the domain is characterized as Toprim.
+At position 492 to 904, the domain is characterized as USP.
+At position 956 to 1126, the domain is characterized as Exonuclease.
+At position 220 to 326, the domain is characterized as HD.
+At position 37 to 120, the domain is characterized as RRM.
+At position 9 to 96, the domain is characterized as Acylphosphatase-like.
+At position 59 to 541, the domain is characterized as A to I editase.
+At position 438 to 744, the domain is characterized as USP.
+At position 52 to 90, the domain is characterized as EGF-like 1.
+At position 92 to 208, the domain is characterized as CUB.
+At position 206 to 244, the domain is characterized as EGF-like 2.
+At position 613 to 656, the domain is characterized as PSI 1.
+At position 665 to 708, the domain is characterized as PSI 2.
+At position 714 to 759, the domain is characterized as PSI 3.
+At position 754 to 872, the domain is characterized as C-type lectin.
+At position 888 to 938, the domain is characterized as PSI 4.
+At position 941 to 1011, the domain is characterized as PSI 5.
+At position 1013 to 1058, the domain is characterized as Laminin EGF-like 1.
+At position 1059 to 1107, the domain is characterized as Laminin EGF-like 2.
+At position 132 to 247, the domain is characterized as C-type lectin.
+At position 755 to 838, the domain is characterized as Smr.
+At position 4 to 86, the domain is characterized as KRAB.
+At position 168 to 273, the domain is characterized as Cadherin.
+At position 725 to 1017, the domain is characterized as Protein kinase.
+At position 508 to 614, the domain is characterized as Calponin-homology (CH).
+At position 686 to 748, the domain is characterized as LIM zinc-binding.
+At position 1053 to 1199, the domain is characterized as bMERB.
+At position 124 to 307, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 138, the domain is characterized as VIT.
+At position 354 to 527, the domain is characterized as VWFA.
+At position 9 to 176, the domain is characterized as TIR.
+At position 197 to 446, the domain is characterized as NB-ARC.
+At position 1 to 76, the domain is characterized as BMV.
+At position 63 to 142, the domain is characterized as Core-binding (CB).
+At position 170 to 376, the domain is characterized as Tyr recombinase.
+At position 221 to 475, the domain is characterized as Peptidase S8.
+At position 5 to 55, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 61 to 111, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 45 to 74, the domain is characterized as IQ.
+At position 688 to 1029, the domain is characterized as HECT.
+At position 3 to 185, the domain is characterized as Miro 1.
+At position 330 to 365, the domain is characterized as EF-hand 2.
+At position 446 to 611, the domain is characterized as Miro 2.
+At position 9 to 255, the domain is characterized as ABC transporter.
+At position 142 to 381, the domain is characterized as Radical SAM core.
+At position 2 to 147, the domain is characterized as N-acetyltransferase.
+At position 55 to 233, the domain is characterized as FAD-binding PCMH-type.
+At position 300 to 405, the domain is characterized as PH.
+At position 355 to 405, the domain is characterized as FBD.
+At position 1 to 109, the domain is characterized as Bulb-type lectin.
+At position 52 to 162, the domain is characterized as HD.
+At position 178 to 257, the domain is characterized as RCK C-terminal 1.
+At position 259 to 341, the domain is characterized as RCK C-terminal 2.
+At position 6 to 91, the domain is characterized as Core-binding (CB).
+At position 112 to 296, the domain is characterized as Tyr recombinase.
+At position 24 to 289, the domain is characterized as Tyrosine-protein phosphatase.
+At position 297 to 532, the domain is characterized as Glutamine amidotransferase type-1.
+At position 9 to 283, the domain is characterized as CN hydrolase.
+At position 58 to 366, the domain is characterized as AB hydrolase-1.
+At position 35 to 503, the domain is characterized as Sema.
+At position 505 to 556, the domain is characterized as PSI.
+At position 565 to 647, the domain is characterized as Ig-like C2-type.
+At position 193 to 283, the domain is characterized as CARD.
+At position 120 to 170, the domain is characterized as DHHC.
+At position 8 to 167, the domain is characterized as Clp R.
+At position 357 to 689, the domain is characterized as Transferrin-like 2.
+At position 30 to 97, the domain is characterized as DRBM 1.
+At position 159 to 227, the domain is characterized as DRBM 2.
+At position 295 to 382, the domain is characterized as PPIase FKBP-type.
+At position 334 to 408, the domain is characterized as HSA.
+At position 842 to 1007, the domain is characterized as Helicase ATP-binding.
+At position 1382 to 1532, the domain is characterized as Helicase C-terminal.
+At position 93 to 194, the domain is characterized as Cyclin N-terminal.
+At position 293 to 385, the domain is characterized as ARID.
+At position 731 to 825, the domain is characterized as REKLES.
+At position 5 to 101, the domain is characterized as DMAP1-binding.
+At position 37 to 296, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 69 to 449, the domain is characterized as Protein kinase.
+At position 593 to 682, the domain is characterized as PH.
+At position 574 to 636, the domain is characterized as FIP-RBD.
+At position 55 to 309, the domain is characterized as GH18.
+At position 419 to 541, the domain is characterized as RCK N-terminal.
+At position 210 to 256, the domain is characterized as GPS.
+At position 48 to 83, the domain is characterized as EF-hand.
+At position 24 to 254, the domain is characterized as Peptidase S1.
+At position 308 to 357, the domain is characterized as FHA.
+At position 24 to 116, the domain is characterized as XRN2-binding (XTBD).
+At position 1395 to 1719, the domain is characterized as PIPK.
+At position 445 to 641, the domain is characterized as FtsK.
+At position 13 to 90, the domain is characterized as Cytochrome b5 heme-binding.
+At position 194 to 261, the domain is characterized as PH.
+At position 153 to 199, the domain is characterized as F-box.
+At position 85 to 161, the domain is characterized as RBD.
+At position 481 to 748, the domain is characterized as Protein kinase.
+At position 437 to 606, the domain is characterized as tr-type G.
+At position 83 to 171, the domain is characterized as S1 motif 1.
+At position 187 to 258, the domain is characterized as S1 motif 2.
+At position 281 to 346, the domain is characterized as S1 motif 3.
+At position 365 to 436, the domain is characterized as S1 motif 4.
+At position 453 to 522, the domain is characterized as S1 motif 5.
+At position 542 to 611, the domain is characterized as S1 motif 6.
+At position 636 to 707, the domain is characterized as S1 motif 7.
+At position 729 to 798, the domain is characterized as S1 motif 8.
+At position 1036 to 1109, the domain is characterized as S1 motif 9.
+At position 1149 to 1222, the domain is characterized as S1 motif 10.
+At position 1230 to 1298, the domain is characterized as S1 motif 11.
+At position 1324 to 1396, the domain is characterized as S1 motif 12.
+At position 13 to 335, the domain is characterized as Kinesin motor.
+At position 181 to 213, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 199 to 254, the domain is characterized as bHLH.
+At position 94 to 346, the domain is characterized as PPM-type phosphatase.
+At position 30 to 112, the domain is characterized as GOLD.
+At position 9 to 59, the domain is characterized as F-box.
+At position 51 to 143, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 71 to 178, the domain is characterized as MTTase N-terminal.
+At position 207 to 438, the domain is characterized as Radical SAM core.
+At position 438 to 500, the domain is characterized as TRAM.
+At position 113 to 150, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 97 to 168, the domain is characterized as PRC barrel.
+At position 142 to 380, the domain is characterized as Radical SAM core.
+At position 382 to 450, the domain is characterized as TRAM.
+At position 7 to 129, the domain is characterized as RCK N-terminal.
+At position 138 to 220, the domain is characterized as RCK C-terminal.
+At position 130 to 372, the domain is characterized as Peptidase S1.
+At position 179 to 232, the domain is characterized as HAMP.
+At position 240 to 453, the domain is characterized as Histidine kinase.
+At position 9 to 147, the domain is characterized as Thioredoxin.
+At position 641 to 705, the domain is characterized as CBS 1.
+At position 738 to 795, the domain is characterized as CBS 2.
+At position 140 to 183, the domain is characterized as CUE.
+At position 10 to 255, the domain is characterized as ABC transporter.
+At position 256 to 314, the domain is characterized as CBS 1.
+At position 316 to 374, the domain is characterized as CBS 2.
+At position 39 to 121, the domain is characterized as KH type-2.
+At position 525 to 803, the domain is characterized as Protein kinase.
+At position 610 to 847, the domain is characterized as ABC transporter.
+At position 26 to 163, the domain is characterized as C2 1.
+At position 341 to 560, the domain is characterized as VWFA.
+At position 9 to 204, the domain is characterized as tr-type G.
+At position 392 to 825, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1322 to 1632, the domain is characterized as PKS/mFAS DH.
+At position 1721 to 1798, the domain is characterized as Carrier.
+At position 23 to 220, the domain is characterized as Peptidase S1.
+At position 1 to 220, the domain is characterized as ABC transporter.
+At position 651 to 882, the domain is characterized as NR LBD.
+At position 32 to 87, the domain is characterized as Kazal-like.
+At position 76 to 200, the domain is characterized as Cyclin N-terminal.
+At position 148 to 269, the domain is characterized as Peptidase C51.
+At position 114 to 192, the domain is characterized as RRM 1.
+At position 217 to 296, the domain is characterized as RRM 2.
+At position 200 to 252, the domain is characterized as HAMP.
+At position 299 to 520, the domain is characterized as Histidine kinase.
+At position 669 to 785, the domain is characterized as Response regulatory.
+At position 822 to 918, the domain is characterized as HPt.
+At position 37 to 180, the domain is characterized as SIS.
+At position 206 to 265, the domain is characterized as CBS 1.
+At position 274 to 329, the domain is characterized as CBS 2.
+At position 28 to 188, the domain is characterized as Helicase ATP-binding.
+At position 10 to 325, the domain is characterized as Deacetylase sirtuin-type.
+At position 30 to 172, the domain is characterized as Nudix hydrolase.
+At position 625 to 842, the domain is characterized as tr-type G.
+At position 14 to 181, the domain is characterized as Era-type G.
+At position 212 to 289, the domain is characterized as KH type-2.
+At position 367 to 605, the domain is characterized as PH.
+At position 626 to 746, the domain is characterized as Arf-GAP.
+At position 11 to 216, the domain is characterized as ABC transporter.
+At position 121 to 303, the domain is characterized as DH.
+At position 290 to 448, the domain is characterized as PH.
+At position 656 to 934, the domain is characterized as Protein kinase.
+At position 276 to 471, the domain is characterized as B30.2/SPRY.
+At position 20 to 169, the domain is characterized as Tyrosine-protein phosphatase.
+At position 83 to 305, the domain is characterized as GB1/RHD3-type G.
+At position 175 to 352, the domain is characterized as EngA-type G 2.
+At position 11 to 321, the domain is characterized as Protein kinase.
+At position 123 to 190, the domain is characterized as COMM.
+At position 92 to 168, the domain is characterized as RRM.
+At position 305 to 406, the domain is characterized as Rieske.
+At position 3 to 236, the domain is characterized as PABS.
+At position 606 to 657, the domain is characterized as SANT 2.
+At position 20 to 349, the domain is characterized as F5/8 type A 1.
+At position 207 to 349, the domain is characterized as Plastocyanin-like 2.
+At position 1683 to 2008, the domain is characterized as F5/8 type A 3.
+At position 1683 to 1845, the domain is characterized as Plastocyanin-like 5.
+At position 1855 to 2008, the domain is characterized as Plastocyanin-like 6.
+At position 2008 to 2156, the domain is characterized as F5/8 type C 1.
+At position 2161 to 2313, the domain is characterized as F5/8 type C 2.
+At position 271 to 406, the domain is characterized as C2 tensin-type.
+At position 35 to 369, the domain is characterized as USP.
+At position 191 to 416, the domain is characterized as Radical SAM core.
+At position 488 to 710, the domain is characterized as Histidine kinase.
+At position 735 to 850, the domain is characterized as Response regulatory.
+At position 106 to 230, the domain is characterized as GST C-terminal.
+At position 82 to 117, the domain is characterized as EF-hand.
+At position 7 to 146, the domain is characterized as MABP.
+At position 210 to 259, the domain is characterized as UMA.
+At position 1 to 27, the domain is characterized as HTH merR-type.
+At position 36 to 254, the domain is characterized as Radical SAM core.
+At position 275 to 446, the domain is characterized as tr-type G.
+At position 26 to 258, the domain is characterized as Peptidase S1.
+At position 145 to 187, the domain is characterized as G-patch.
+At position 63 to 216, the domain is characterized as N-acetyltransferase.
+At position 437 to 511, the domain is characterized as GW 1.
+At position 513 to 587, the domain is characterized as GW 2.
+At position 606 to 680, the domain is characterized as GW 3.
+At position 682 to 756, the domain is characterized as GW 4.
+At position 778 to 853, the domain is characterized as GW 5.
+At position 855 to 930, the domain is characterized as GW 6.
+At position 937 to 1011, the domain is characterized as GW 7.
+At position 20 to 163, the domain is characterized as MPN.
+At position 165 to 391, the domain is characterized as Lon N-terminal.
+At position 865 to 1053, the domain is characterized as Lon proteolytic.
+At position 54 to 286, the domain is characterized as Ferric oxidoreductase.
+At position 287 to 397, the domain is characterized as FAD-binding FR-type.
+At position 116 to 180, the domain is characterized as PAS.
+At position 176 to 240, the domain is characterized as SH3 1.
+At position 268 to 331, the domain is characterized as SH3 2.
+At position 193 to 261, the domain is characterized as Histone-fold.
+At position 5 to 407, the domain is characterized as BRO1.
+At position 186 to 264, the domain is characterized as PDZ 2.
+At position 516 to 584, the domain is characterized as SH3.
+At position 610 to 791, the domain is characterized as Guanylate kinase-like.
+At position 1631 to 1745, the domain is characterized as ZU5.
+At position 47 to 239, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 84, the domain is characterized as GST N-terminal.
+At position 90 to 216, the domain is characterized as GST C-terminal.
+At position 255 to 411, the domain is characterized as EF-1-gamma C-terminal.
+At position 175 to 409, the domain is characterized as NR LBD.
+At position 541 to 602, the domain is characterized as SAM.
+At position 476 to 678, the domain is characterized as FtsK 1.
+At position 858 to 1052, the domain is characterized as FtsK 2.
+At position 1161 to 1354, the domain is characterized as FtsK 3.
+At position 2 to 90, the domain is characterized as DPCK.
+At position 608 to 688, the domain is characterized as BRCT.
+At position 246 to 459, the domain is characterized as Histidine kinase.
+At position 6 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 102 to 173, the domain is characterized as Rieske.
+At position 266 to 501, the domain is characterized as NR LBD.
+At position 199 to 564, the domain is characterized as Peptidase S53.
+At position 2 to 179, the domain is characterized as PBS-linker.
+At position 231 to 286, the domain is characterized as CpcD-like.
+At position 52 to 160, the domain is characterized as Rieske.
+At position 26 to 104, the domain is characterized as GIY-YIG.
+At position 47 to 98, the domain is characterized as HTH psq-type.
+At position 112 to 185, the domain is characterized as HTH CENPB-type.
+At position 233 to 357, the domain is characterized as DDE-1 1.
+At position 410 to 477, the domain is characterized as DDE-1 2.
+At position 144 to 233, the domain is characterized as PPIase FKBP-type.
+At position 421 to 536, the domain is characterized as Toprim.
+At position 109 to 309, the domain is characterized as ATP-grasp.
+At position 449 to 579, the domain is characterized as Thioredoxin.
+At position 7 to 76, the domain is characterized as J.
+At position 200 to 321, the domain is characterized as SET.
+At position 249 to 288, the domain is characterized as LRRCT.
+At position 57 to 96, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 97 to 141, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 147 to 188, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 189 to 231, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 29 to 222, the domain is characterized as Glutamine amidotransferase type-1.
+At position 223 to 415, the domain is characterized as GMPS ATP-PPase.
+At position 168 to 340, the domain is characterized as Helicase ATP-binding.
+At position 418 to 568, the domain is characterized as Helicase C-terminal.
+At position 655 to 715, the domain is characterized as PWWP.
+At position 141 to 220, the domain is characterized as BTB.
+At position 133 to 255, the domain is characterized as EamA 1.
+At position 283 to 411, the domain is characterized as EamA 2.
+At position 1 to 79, the domain is characterized as HIG1.
+At position 1 to 410, the domain is characterized as SMP-LTD.
+At position 25 to 244, the domain is characterized as Peptidase S1.
+At position 207 to 236, the domain is characterized as IQ.
+At position 725 to 800, the domain is characterized as Smr.
+At position 321 to 350, the domain is characterized as IQ 1.
+At position 343 to 372, the domain is characterized as IQ 2.
+At position 24 to 193, the domain is characterized as EngB-type G.
+At position 160 to 209, the domain is characterized as Myosin N-terminal SH3-like.
+At position 213 to 879, the domain is characterized as Myosin motor.
+At position 881 to 910, the domain is characterized as IQ 1.
+At position 904 to 933, the domain is characterized as IQ 2.
+At position 942 to 971, the domain is characterized as IQ 3.
+At position 94 to 410, the domain is characterized as Peptidase A1.
+At position 34 to 166, the domain is characterized as TBDR plug.
+At position 175 to 810, the domain is characterized as TBDR beta-barrel.
+At position 12 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 141, the domain is characterized as ENTH.
+At position 33 to 80, the domain is characterized as SERTA.
+At position 137 to 233, the domain is characterized as HTH araC/xylS-type.
+At position 491 to 746, the domain is characterized as Protein kinase.
+At position 72 to 367, the domain is characterized as Reverse transcriptase.
+At position 14 to 96, the domain is characterized as KRAB.
+At position 192 to 462, the domain is characterized as SMP-LTD.
+At position 384 to 800, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1279 to 1586, the domain is characterized as PKS/mFAS DH.
+At position 1626 to 1703, the domain is characterized as Carrier.
+At position 34 to 178, the domain is characterized as N-acetyltransferase.
+At position 195 to 274, the domain is characterized as RRM.
+At position 75 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 335 to 367, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 369 to 398, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 569 to 898, the domain is characterized as PDEase.
+At position 276 to 349, the domain is characterized as PUA.
+At position 4 to 59, the domain is characterized as HTH myb-type 1.
+At position 60 to 110, the domain is characterized as HTH myb-type 2.
+At position 312 to 398, the domain is characterized as PPIase FKBP-type.
+At position 254 to 596, the domain is characterized as PUM-HD.
+At position 15 to 151, the domain is characterized as VHS.
+At position 178 to 305, the domain is characterized as GAT.
+At position 417 to 532, the domain is characterized as GAE.
+At position 67 to 290, the domain is characterized as Peptidase S1.
+At position 1069 to 1322, the domain is characterized as Glutamine amidotransferase type-1.
+At position 115 to 213, the domain is characterized as Rieske.
+At position 109 to 234, the domain is characterized as RCK N-terminal.
+At position 253 to 338, the domain is characterized as RCK C-terminal.
+At position 46 to 198, the domain is characterized as SIS.
+At position 46 to 117, the domain is characterized as KRAB.
+At position 123 to 452, the domain is characterized as PI3K/PI4K catalytic.
+At position 52 to 141, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 113 to 334, the domain is characterized as Fibrinogen C-terminal.
+At position 197 to 551, the domain is characterized as USP.
+At position 388 to 501, the domain is characterized as PAZ.
+At position 676 to 997, the domain is characterized as Piwi.
+At position 19 to 95, the domain is characterized as GIY-YIG.
+At position 4 to 143, the domain is characterized as ADF-H.
+At position 17 to 81, the domain is characterized as NAC-A/B.
+At position 144 to 182, the domain is characterized as UBA.
+At position 585 to 662, the domain is characterized as Cytochrome b5 heme-binding.
+At position 688 to 815, the domain is characterized as FAD-binding FR-type.
+At position 267 to 325, the domain is characterized as FF 1.
+At position 366 to 420, the domain is characterized as FF 2.
+At position 427 to 481, the domain is characterized as FF 3.
+At position 482 to 548, the domain is characterized as FF 4.
+At position 590 to 763, the domain is characterized as pG1 pseudoGTPase.
+At position 779 to 944, the domain is characterized as pG2 pseudoGTPase.
+At position 1262 to 1449, the domain is characterized as Rho-GAP.
+At position 2 to 91, the domain is characterized as Ig-like C1-type.
+At position 143 to 241, the domain is characterized as CRM 1.
+At position 263 to 359, the domain is characterized as CRM 2.
+At position 13 to 235, the domain is characterized as ThyX.
+At position 254 to 503, the domain is characterized as ABC transporter 2.
+At position 107 to 199, the domain is characterized as PB1.
+At position 57 to 272, the domain is characterized as Radical SAM core.
+At position 99 to 162, the domain is characterized as bHLH.
+At position 360 to 609, the domain is characterized as Protein kinase 1.
+At position 645 to 1018, the domain is characterized as Protein kinase 2.
+At position 251 to 431, the domain is characterized as CNNM transmembrane.
+At position 450 to 511, the domain is characterized as CBS 1.
+At position 518 to 584, the domain is characterized as CBS 2.
+At position 48 to 151, the domain is characterized as Cadherin 1.
+At position 152 to 258, the domain is characterized as Cadherin 2.
+At position 259 to 372, the domain is characterized as Cadherin 3.
+At position 373 to 477, the domain is characterized as Cadherin 4.
+At position 478 to 593, the domain is characterized as Cadherin 5.
+At position 26 to 431, the domain is characterized as FERM.
+At position 450 to 529, the domain is characterized as SH2; atypical.
+At position 589 to 875, the domain is characterized as Protein kinase 1.
+At position 897 to 1176, the domain is characterized as Protein kinase 2.
+At position 224 to 488, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 50 to 229, the domain is characterized as PBS-linker.
+At position 38 to 416, the domain is characterized as Peptidase A1.
+At position 599 to 816, the domain is characterized as Rap-GAP.
+At position 953 to 1031, the domain is characterized as PDZ.
+At position 142 to 314, the domain is characterized as tr-type G.
+At position 448 to 500, the domain is characterized as Collagen-like 1.
+At position 501 to 542, the domain is characterized as Collagen-like 2.
+At position 543 to 594, the domain is characterized as Collagen-like 3.
+At position 681 to 733, the domain is characterized as Collagen-like 4.
+At position 734 to 787, the domain is characterized as Collagen-like 5.
+At position 825 to 882, the domain is characterized as Collagen-like 6.
+At position 884 to 934, the domain is characterized as Collagen-like 7.
+At position 2 to 117, the domain is characterized as PLAT.
+At position 118 to 673, the domain is characterized as Lipoxygenase.
+At position 407 to 436, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 445 to 475, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 48 to 116, the domain is characterized as CSD.
+At position 90 to 245, the domain is characterized as Tyr recombinase.
+At position 757 to 864, the domain is characterized as PH.
+At position 19 to 214, the domain is characterized as RNase H type-2.
+At position 4 to 255, the domain is characterized as ABC transporter 1.
+At position 319 to 537, the domain is characterized as ABC transporter 2.
+At position 37 to 122, the domain is characterized as ACB.
+At position 31 to 304, the domain is characterized as Dynamin-type G.
+At position 535 to 621, the domain is characterized as GED.
+At position 583 to 707, the domain is characterized as C2 2.
+At position 1013 to 1156, the domain is characterized as MHD1.
+At position 1263 to 1405, the domain is characterized as MHD2.
+At position 1419 to 1546, the domain is characterized as C2 3.
+At position 311 to 547, the domain is characterized as NR LBD.
+At position 24 to 86, the domain is characterized as LCN-type CS-alpha/beta.
+At position 165 to 259, the domain is characterized as 5'-3' exonuclease.
+At position 37 to 225, the domain is characterized as GH11.
+At position 375 to 477, the domain is characterized as HTH araC/xylS-type.
+At position 305 to 344, the domain is characterized as EGF-like 2; calcium-binding.
+At position 46 to 110, the domain is characterized as KH 1.
+At position 149 to 217, the domain is characterized as KH 2.
+At position 451 to 521, the domain is characterized as KH 3.
+At position 541 to 610, the domain is characterized as KH 4.
+At position 775 to 839, the domain is characterized as KH 5.
+At position 38 to 164, the domain is characterized as Cadherin 1.
+At position 165 to 265, the domain is characterized as Cadherin 2.
+At position 80 to 153, the domain is characterized as S1 motif.
+At position 11 to 219, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 197 to 398, the domain is characterized as GMPS ATP-PPase.
+At position 102 to 357, the domain is characterized as UmuC.
+At position 44 to 470, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 940 to 1218, the domain is characterized as PKS/mFAS DH.
+At position 1726 to 1801, the domain is characterized as Carrier.
+At position 30 to 87, the domain is characterized as SMP 1.
+At position 96 to 151, the domain is characterized as SMP 2.
+At position 28 to 129, the domain is characterized as Ig-like V-type.
+At position 5 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 73 to 211, the domain is characterized as SCP.
+At position 220 to 408, the domain is characterized as Rab-GAP TBC.
+At position 576 to 611, the domain is characterized as EF-hand 1.
+At position 612 to 647, the domain is characterized as EF-hand 2.
+At position 13 to 190, the domain is characterized as Ku.
+At position 26 to 67, the domain is characterized as CHCH 1.
+At position 68 to 106, the domain is characterized as CHCH 2.
+At position 247 to 475, the domain is characterized as RMT2.
+At position 4 to 223, the domain is characterized as Radical SAM core.
+At position 565 to 624, the domain is characterized as KH.
+At position 634 to 702, the domain is characterized as S1 motif.
+At position 775 to 887, the domain is characterized as MaoC-like.
+At position 499 to 560, the domain is characterized as SH3 1.
+At position 736 to 804, the domain is characterized as SH3 2.
+At position 783 to 860, the domain is characterized as Carrier 1.
+At position 1324 to 1400, the domain is characterized as Carrier 2.
+At position 1858 to 1932, the domain is characterized as Carrier 3.
+At position 65 to 140, the domain is characterized as Rho RNA-BD.
+At position 677 to 706, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 733 to 764, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 3 to 60, the domain is characterized as PUA.
+At position 580 to 808, the domain is characterized as NR LBD.
+At position 525 to 720, the domain is characterized as STAS.
+At position 84 to 145, the domain is characterized as SH3.
+At position 151 to 248, the domain is characterized as SH2.
+At position 196 to 281, the domain is characterized as Ig-like C2-type 1.
+At position 295 to 364, the domain is characterized as Ig-like C2-type 2.
+At position 534 to 803, the domain is characterized as Protein kinase.
+At position 26 to 91, the domain is characterized as SAM.
+At position 471 to 560, the domain is characterized as PDZ 4.
+At position 572 to 657, the domain is characterized as PDZ 5.
+At position 672 to 754, the domain is characterized as PDZ 6.
+At position 988 to 1070, the domain is characterized as PDZ 7.
+At position 39 to 371, the domain is characterized as USP.
+At position 227 to 527, the domain is characterized as MHD.
+At position 109 to 189, the domain is characterized as BAG.
+At position 102 to 192, the domain is characterized as K-box.
+At position 804 to 978, the domain is characterized as PCI.
+At position 383 to 536, the domain is characterized as Nudix hydrolase.
+At position 460 to 632, the domain is characterized as Helicase C-terminal.
+At position 65 to 131, the domain is characterized as KH.
+At position 5 to 261, the domain is characterized as Protein kinase.
+At position 24 to 256, the domain is characterized as Phosphagen kinase C-terminal.
+At position 30 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 11 to 178, the domain is characterized as PPIase cyclophilin-type.
+At position 88 to 193, the domain is characterized as Rieske.
+At position 214 to 280, the domain is characterized as KH.
+At position 3 to 368, the domain is characterized as BRO1.
+At position 744 to 831, the domain is characterized as SUEL-type lectin.
+At position 40 to 110, the domain is characterized as BTB.
+At position 16 to 84, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 62 to 155, the domain is characterized as PH.
+At position 325 to 460, the domain is characterized as DAGKc.
+At position 1143 to 1206, the domain is characterized as SAM.
+At position 34 to 99, the domain is characterized as J.
+At position 373 to 430, the domain is characterized as S4 RNA-binding.
+At position 27 to 211, the domain is characterized as EngB-type G.
+At position 26 to 120, the domain is characterized as PINc.
+At position 85 to 170, the domain is characterized as PNT.
+At position 374 to 408, the domain is characterized as EGF-like 1.
+At position 409 to 440, the domain is characterized as EGF-like 2.
+At position 443 to 480, the domain is characterized as EGF-like 3.
+At position 272 to 335, the domain is characterized as FHA.
+At position 516 to 584, the domain is characterized as PUA.
+At position 72 to 290, the domain is characterized as Radical SAM core.
+At position 48 to 95, the domain is characterized as LysM.
+At position 183 to 306, the domain is characterized as DOD-type homing endonuclease.
+At position 24 to 124, the domain is characterized as Ig-like 1.
+At position 126 to 217, the domain is characterized as Ig-like 2.
+At position 230 to 317, the domain is characterized as Ig-like 3.
+At position 322 to 406, the domain is characterized as Ig-like 4.
+At position 416 to 510, the domain is characterized as Fibronectin type-III 1.
+At position 512 to 608, the domain is characterized as Fibronectin type-III 2.
+At position 613 to 712, the domain is characterized as Fibronectin type-III 3.
+At position 719 to 812, the domain is characterized as Fibronectin type-III 4.
+At position 817 to 912, the domain is characterized as Fibronectin type-III 5.
+At position 328 to 497, the domain is characterized as tr-type G.
+At position 11 to 777, the domain is characterized as Myosin motor.
+At position 1875 to 1930, the domain is characterized as DEK-C.
+At position 85 to 178, the domain is characterized as Rieske.
+At position 34 to 139, the domain is characterized as Ig-like 1.
+At position 247 to 354, the domain is characterized as Ig-like 2.
+At position 203 to 315, the domain is characterized as RRM 1.
+At position 323 to 435, the domain is characterized as RRM 2.
+At position 33 to 214, the domain is characterized as tr-type G.
+At position 140 to 240, the domain is characterized as Gnk2-homologous 2.
+At position 14 to 155, the domain is characterized as MARVEL.
+At position 409 to 479, the domain is characterized as Dockerin.
+At position 102 to 260, the domain is characterized as FCP1 homology.
+At position 111 to 424, the domain is characterized as IF rod.
+At position 9 to 179, the domain is characterized as KaiA N-terminal.
+At position 189 to 297, the domain is characterized as KaiA C-terminal.
+At position 17 to 299, the domain is characterized as ABC transmembrane type-1.
+At position 332 to 567, the domain is characterized as ABC transporter.
+At position 653 to 916, the domain is characterized as Protein kinase.
+At position 313 to 481, the domain is characterized as Helicase ATP-binding.
+At position 651 to 825, the domain is characterized as Helicase C-terminal.
+At position 1 to 100, the domain is characterized as Glutaredoxin.
+At position 3 to 185, the domain is characterized as tr-type G.
+At position 1027 to 1163, the domain is characterized as MGS-like.
+At position 254 to 379, the domain is characterized as TIR.
+At position 34 to 193, the domain is characterized as Cupin type-1 1.
+At position 240 to 401, the domain is characterized as Cupin type-1 2.
+At position 20 to 246, the domain is characterized as Radical SAM core.
+At position 650 to 741, the domain is characterized as Fe2OG dioxygenase.
+At position 13 to 272, the domain is characterized as Protein kinase.
+At position 9 to 214, the domain is characterized as YrdC-like.
+At position 32 to 286, the domain is characterized as Protein kinase.
+At position 77 to 248, the domain is characterized as FAD-binding PCMH-type.
+At position 9 to 126, the domain is characterized as Cystatin 1.
+At position 127 to 243, the domain is characterized as Cystatin 2.
+At position 198 to 257, the domain is characterized as KID.
+At position 300 to 359, the domain is characterized as bZIP.
+At position 653 to 732, the domain is characterized as BRCT.
+At position 233 to 392, the domain is characterized as SSD.
+At position 133 to 250, the domain is characterized as PilZ.
+At position 45 to 385, the domain is characterized as AB hydrolase-1.
+At position 22 to 123, the domain is characterized as PH.
+At position 1023 to 1078, the domain is characterized as BRX.
+At position 165 to 270, the domain is characterized as PRD 1.
+At position 283 to 394, the domain is characterized as PRD 2.
+At position 311 to 593, the domain is characterized as ABC transmembrane type-1 1.
+At position 629 to 853, the domain is characterized as ABC transporter 1.
+At position 947 to 1228, the domain is characterized as ABC transmembrane type-1 2.
+At position 1265 to 1499, the domain is characterized as ABC transporter 2.
+At position 18 to 136, the domain is characterized as EamA 1.
+At position 198 to 326, the domain is characterized as EamA 2.
+At position 199 to 289, the domain is characterized as Death.
+At position 552 to 666, the domain is characterized as Fe2OG dioxygenase.
+At position 36 to 126, the domain is characterized as GOLD.
+At position 164 to 210, the domain is characterized as F-box.
+At position 25 to 103, the domain is characterized as Death.
+At position 151 to 285, the domain is characterized as TIR.
+At position 21 to 73, the domain is characterized as LIM zinc-binding 1.
+At position 82 to 132, the domain is characterized as LIM zinc-binding 2.
+At position 144 to 194, the domain is characterized as LIM zinc-binding 3.
+At position 202 to 255, the domain is characterized as LIM zinc-binding 4.
+At position 264 to 315, the domain is characterized as LIM zinc-binding 5.
+At position 9 to 72, the domain is characterized as HMA.
+At position 216 to 334, the domain is characterized as Nop.
+At position 75 to 163, the domain is characterized as PB1.
+At position 3 to 75, the domain is characterized as Sm.
+At position 27 to 70, the domain is characterized as CHCH.
+At position 171 to 439, the domain is characterized as SF4 helicase; first part.
+At position 333 to 599, the domain is characterized as SF4 helicase; second part.
+At position 348 to 476, the domain is characterized as GGDEF.
+At position 488 to 729, the domain is characterized as EAL.
+At position 432 to 546, the domain is characterized as Toprim.
+At position 39 to 268, the domain is characterized as Radical SAM core.
+At position 294 to 547, the domain is characterized as Glutamine amidotransferase type-1.
+At position 455 to 564, the domain is characterized as RanBD1.
+At position 126 to 320, the domain is characterized as ATP-grasp.
+At position 97 to 191, the domain is characterized as Toprim.
+At position 27 to 375, the domain is characterized as MACPF.
+At position 376 to 408, the domain is characterized as EGF-like.
+At position 397 to 519, the domain is characterized as C2.
+At position 48 to 157, the domain is characterized as sHSP.
+At position 114 to 146, the domain is characterized as LisH.
+At position 153 to 210, the domain is characterized as CTLH.
+At position 17 to 235, the domain is characterized as SET.
+At position 130 to 288, the domain is characterized as MRH.
+At position 21 to 173, the domain is characterized as N-acetyltransferase.
+At position 50 to 150, the domain is characterized as Ig-like V-type.
+At position 209 to 237, the domain is characterized as ITAM.
+At position 211 to 274, the domain is characterized as KH.
+At position 2 to 156, the domain is characterized as Thioredoxin.
+At position 104 to 306, the domain is characterized as ATP-grasp.
+At position 408 to 568, the domain is characterized as PA14.
+At position 355 to 465, the domain is characterized as PLAT.
+At position 85 to 192, the domain is characterized as Calponin-homology (CH).
+At position 27 to 283, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 75 to 197, the domain is characterized as HD.
+At position 1 to 149, the domain is characterized as MGS-like.
+At position 160 to 252, the domain is characterized as Enkurin.
+At position 176 to 187, the domain is characterized as IQ.
+At position 139 to 277, the domain is characterized as EamA 2.
+At position 41 to 130, the domain is characterized as SUEL-type lectin.
+At position 789 to 840, the domain is characterized as GPS.
+At position 58 to 115, the domain is characterized as Chitin-binding type-2 1.
+At position 211 to 268, the domain is characterized as Chitin-binding type-2 2.
+At position 524 to 578, the domain is characterized as Chitin-binding type-2 3.
+At position 79 to 490, the domain is characterized as Peptidase S8.
+At position 144 to 241, the domain is characterized as PpiC.
+At position 282 to 341, the domain is characterized as CBS 1.
+At position 47 to 218, the domain is characterized as MENTAL.
+At position 231 to 444, the domain is characterized as START.
+At position 169 to 258, the domain is characterized as CS.
+At position 276 to 365, the domain is characterized as SGS.
+At position 198 to 365, the domain is characterized as Hflx-type G.
+At position 61 to 289, the domain is characterized as Radical SAM core.
+At position 28 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 217 to 319, the domain is characterized as Ig-like C2-type 2.
+At position 324 to 397, the domain is characterized as Ig-like C2-type 3.
+At position 450 to 545, the domain is characterized as Ig-like C2-type 4.
+At position 548 to 639, the domain is characterized as Ig-like C2-type 5.
+At position 646 to 752, the domain is characterized as Fibronectin type-III 1.
+At position 757 to 854, the domain is characterized as Fibronectin type-III 2.
+At position 859 to 958, the domain is characterized as Fibronectin type-III 3.
+At position 962 to 1056, the domain is characterized as Fibronectin type-III 4.
+At position 1060 to 1155, the domain is characterized as Fibronectin type-III 5.
+At position 1160 to 1255, the domain is characterized as Fibronectin type-III 6.
+At position 1260 to 1360, the domain is characterized as Fibronectin type-III 7.
+At position 1364 to 1458, the domain is characterized as Fibronectin type-III 8.
+At position 1464 to 1567, the domain is characterized as Fibronectin type-III 9.
+At position 1572 to 1672, the domain is characterized as Fibronectin type-III 10.
+At position 1674 to 1774, the domain is characterized as Fibronectin type-III 11.
+At position 1777 to 1873, the domain is characterized as Fibronectin type-III 12.
+At position 1908 to 2010, the domain is characterized as Fibronectin type-III 13.
+At position 1 to 57, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 265 to 326, the domain is characterized as SH3.
+At position 9 to 269, the domain is characterized as Protein kinase 1.
+At position 1131 to 1371, the domain is characterized as Protein kinase 2.
+At position 8 to 409, the domain is characterized as PTS EIIC type-3.
+At position 480 to 583, the domain is characterized as PTS EIIB type-3.
+At position 39 to 153, the domain is characterized as sHSP.
+At position 256 to 401, the domain is characterized as JmjC.
+At position 88 to 332, the domain is characterized as ABC transporter.
+At position 430 to 640, the domain is characterized as ABC transmembrane type-2.
+At position 12 to 104, the domain is characterized as SH2.
+At position 106 to 166, the domain is characterized as SH3 1.
+At position 199 to 260, the domain is characterized as SH3 2.
+At position 69 to 184, the domain is characterized as CUB.
+At position 184 to 282, the domain is characterized as LCCL.
+At position 289 to 446, the domain is characterized as F5/8 type C.
+At position 13 to 148, the domain is characterized as EamA 1.
+At position 171 to 298, the domain is characterized as EamA 2.
+At position 11 to 215, the domain is characterized as tr-type G.
+At position 26 to 190, the domain is characterized as FAD-binding PCMH-type.
+At position 339 to 575, the domain is characterized as PRORP.
+At position 125 to 429, the domain is characterized as USP.
+At position 34 to 75, the domain is characterized as Chitin-binding type-1.
+At position 49 to 331, the domain is characterized as Cupin type-1 1.
+At position 390 to 539, the domain is characterized as Cupin type-1 2.
+At position 145 to 491, the domain is characterized as SAC.
+At position 158 to 338, the domain is characterized as OBG-type G.
+At position 15 to 193, the domain is characterized as Guanylate kinase-like.
+At position 87 to 155, the domain is characterized as POTRA.
+At position 58 to 135, the domain is characterized as KH.
+At position 140 to 208, the domain is characterized as R3H.
+At position 94 to 183, the domain is characterized as HTH araC/xylS-type.
+At position 453 to 884, the domain is characterized as FH2.
+At position 290 to 497, the domain is characterized as MCM.
+At position 549 to 782, the domain is characterized as ABC transporter 1.
+At position 1453 to 1691, the domain is characterized as ABC transporter 2.
+At position 114 to 425, the domain is characterized as IF rod.
+At position 114 to 204, the domain is characterized as RRM.
+At position 61 to 218, the domain is characterized as SSD.
+At position 145 to 219, the domain is characterized as HTH crp-type.
+At position 197 to 388, the domain is characterized as CheB-type methylesterase.
+At position 14 to 307, the domain is characterized as Protein kinase.
+At position 371 to 439, the domain is characterized as Reticulon; atypical.
+At position 116 to 148, the domain is characterized as EF-hand 4.
+At position 358 to 525, the domain is characterized as tr-type G.
+At position 14 to 65, the domain is characterized as GST C-terminal.
+At position 569 to 664, the domain is characterized as SH2.
+At position 24 to 100, the domain is characterized as EthD.
+At position 305 to 401, the domain is characterized as PDZ.
+At position 33 to 354, the domain is characterized as G-alpha.
+At position 429 to 700, the domain is characterized as Protein kinase.
+At position 724 to 796, the domain is characterized as U-box.
+At position 44 to 474, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 971 to 1275, the domain is characterized as PKS/mFAS DH.
+At position 2298 to 2376, the domain is characterized as Carrier.
+At position 26 to 62, the domain is characterized as EGF-like.
+At position 69 to 150, the domain is characterized as Kringle.
+At position 178 to 426, the domain is characterized as Peptidase S1.
+At position 169 to 242, the domain is characterized as Ubiquitin-like.
+At position 34 to 149, the domain is characterized as Calponin-homology (CH).
+At position 730 to 759, the domain is characterized as IQ 1.
+At position 760 to 789, the domain is characterized as IQ 2.
+At position 790 to 819, the domain is characterized as IQ 3.
+At position 820 to 849, the domain is characterized as IQ 4.
+At position 988 to 1221, the domain is characterized as Ras-GAP.
+At position 128 to 257, the domain is characterized as Nudix hydrolase.
+At position 198 to 528, the domain is characterized as Kinesin motor.
+At position 14 to 81, the domain is characterized as CSD.
+At position 1 to 133, the domain is characterized as C2.
+At position 334 to 371, the domain is characterized as PLD phosphodiesterase 1.
+At position 662 to 689, the domain is characterized as PLD phosphodiesterase 2.
+At position 7 to 113, the domain is characterized as PH 1.
+At position 198 to 298, the domain is characterized as PH 2.
+At position 38 to 265, the domain is characterized as SET.
+At position 400 to 435, the domain is characterized as CBM1.
+At position 97 to 402, the domain is characterized as Peptidase A1.
+At position 2 to 50, the domain is characterized as RsgI N-terminal anti-sigma.
+At position 509 to 647, the domain is characterized as GGDEF.
+At position 570 to 714, the domain is characterized as SEC7.
+At position 937 to 1079, the domain is characterized as MGS-like.
+At position 169 to 202, the domain is characterized as WW.
+At position 19 to 80, the domain is characterized as LCN-type CS-alpha/beta.
+At position 237 to 469, the domain is characterized as Peptidase S1.
+At position 4 to 174, the domain is characterized as N-acetyltransferase.
+At position 1 to 190, the domain is characterized as RNase H type-2.
+At position 538 to 946, the domain is characterized as USP.
+At position 1072 to 1199, the domain is characterized as Exonuclease.
+At position 195 to 259, the domain is characterized as OVATE.
+At position 48 to 92, the domain is characterized as bZIP.
+At position 115 to 331, the domain is characterized as DOG1.
+At position 129 to 305, the domain is characterized as Helicase ATP-binding.
+At position 319 to 490, the domain is characterized as Helicase C-terminal.
+At position 20 to 119, the domain is characterized as Thioredoxin 1.
+At position 120 to 267, the domain is characterized as Thioredoxin 2.
+At position 340 to 576, the domain is characterized as PRORP.
+At position 1690 to 1798, the domain is characterized as BEACH-type PH.
+At position 1817 to 2106, the domain is characterized as BEACH.
+At position 1 to 217, the domain is characterized as PDZ.
+At position 54 to 283, the domain is characterized as Radical SAM core.
+At position 29 to 271, the domain is characterized as GB1/RHD3-type G.
+At position 12 to 215, the domain is characterized as ABC transporter.
+At position 40 to 291, the domain is characterized as Protein kinase.
+At position 30 to 512, the domain is characterized as Sema.
+At position 561 to 659, the domain is characterized as Ig-like C2-type.
+At position 26 to 221, the domain is characterized as Lon N-terminal.
+At position 609 to 790, the domain is characterized as Lon proteolytic.
+At position 2 to 195, the domain is characterized as DPCK.
+At position 68 to 292, the domain is characterized as Radical SAM core.
+At position 12 to 181, the domain is characterized as PNPLA.
+At position 577 to 660, the domain is characterized as BRCT.
+At position 584 to 752, the domain is characterized as Helicase ATP-binding.
+At position 953 to 1108, the domain is characterized as Helicase C-terminal.
+At position 10 to 58, the domain is characterized as F-box.
+At position 272 to 377, the domain is characterized as FBD.
+At position 568 to 841, the domain is characterized as Protein kinase.
+At position 842 to 904, the domain is characterized as AGC-kinase C-terminal.
+At position 1139 to 1227, the domain is characterized as PDZ.
+At position 134 to 224, the domain is characterized as PpiC.
+At position 26 to 135, the domain is characterized as Ig-like V-type 1.
+At position 140 to 250, the domain is characterized as Ig-like V-type 2.
+At position 267 to 342, the domain is characterized as Ig-like C2-type 1.
+At position 356 to 435, the domain is characterized as Ig-like C2-type 2.
+At position 442 to 532, the domain is characterized as Ig-like C2-type 3.
+At position 20 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 214 to 406, the domain is characterized as GMPS ATP-PPase.
+At position 58 to 301, the domain is characterized as ABC transporter.
+At position 374 to 633, the domain is characterized as ABC transmembrane type-2.
+At position 91 to 159, the domain is characterized as POTRA.
+At position 20 to 75, the domain is characterized as EF-hand 1.
+At position 113 to 148, the domain is characterized as EF-hand 3.
+At position 604 to 1076, the domain is characterized as Protein kinase.
+At position 32 to 215, the domain is characterized as VWFA 1.
+At position 287 to 472, the domain is characterized as VWFA 2.
+At position 489 to 621, the domain is characterized as C-type lectin.
+At position 103 to 206, the domain is characterized as PH.
+At position 266 to 327, the domain is characterized as SH3.
+At position 23 to 109, the domain is characterized as GIY-YIG.
+At position 33 to 182, the domain is characterized as Tyrosine-protein phosphatase.
+At position 383 to 417, the domain is characterized as SAP.
+At position 1 to 244, the domain is characterized as Deacetylase sirtuin-type.
+At position 45 to 79, the domain is characterized as EF-hand 2.
+At position 95 to 324, the domain is characterized as ABC transmembrane type-1.
+At position 1331 to 1919, the domain is characterized as FAT.
+At position 2093 to 2408, the domain is characterized as PI3K/PI4K catalytic.
+At position 2438 to 2470, the domain is characterized as FATC.
+At position 255 to 307, the domain is characterized as bHLH.
+At position 39 to 131, the domain is characterized as Fibronectin type-III 1.
+At position 158 to 258, the domain is characterized as Fibronectin type-III 2.
+At position 262 to 357, the domain is characterized as Fibronectin type-III 3.
+At position 362 to 457, the domain is characterized as Fibronectin type-III 4.
+At position 1658 to 1752, the domain is characterized as Fibronectin type-III 5.
+At position 142 to 192, the domain is characterized as DHHC.
+At position 267 to 349, the domain is characterized as PUA.
+At position 271 to 306, the domain is characterized as EF-hand 1.
+At position 338 to 359, the domain is characterized as EF-hand 2.
+At position 466 to 501, the domain is characterized as EF-hand 3.
+At position 15 to 82, the domain is characterized as J.
+At position 152 to 461, the domain is characterized as Tyrosine-protein phosphatase.
+At position 119 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 312 to 393, the domain is characterized as Ig-like C2-type 4.
+At position 600 to 682, the domain is characterized as Ig-like C2-type 7.
+At position 794 to 883, the domain is characterized as BRCT 3.
+At position 890 to 978, the domain is characterized as BRCT 4.
+At position 1053 to 1134, the domain is characterized as BRCT 5.
+At position 1155 to 1196, the domain is characterized as BRCT 6.
+At position 274 to 348, the domain is characterized as U-box.
+At position 33 to 357, the domain is characterized as Septin-type G.
+At position 6 to 128, the domain is characterized as PINc.
+At position 6 to 140, the domain is characterized as TCTP.
+At position 47 to 150, the domain is characterized as Expansin-like EG45.
+At position 20 to 152, the domain is characterized as VHS.
+At position 221 to 309, the domain is characterized as GAT.
+At position 21 to 243, the domain is characterized as Peptidase S1.
+At position 144 to 397, the domain is characterized as ABC transporter 1.
+At position 836 to 1084, the domain is characterized as ABC transporter 2.
+At position 121 to 173, the domain is characterized as bHLH.
+At position 1 to 450, the domain is characterized as ADPK.
+At position 75 to 305, the domain is characterized as PPM-type phosphatase.
+At position 224 to 382, the domain is characterized as TrmE-type G.
+At position 25 to 80, the domain is characterized as L27.
+At position 108 to 190, the domain is characterized as PDZ.
+At position 193 to 274, the domain is characterized as Saposin B-type 2.
+At position 310 to 391, the domain is characterized as Saposin B-type 3.
+At position 435 to 516, the domain is characterized as Saposin B-type 4.
+At position 518 to 554, the domain is characterized as Saposin A-type 2.
+At position 97 to 163, the domain is characterized as S4 RNA-binding.
+At position 92 to 289, the domain is characterized as Peptidase M12A.
+At position 297 to 440, the domain is characterized as Ricin B-type lectin.
+At position 101 to 195, the domain is characterized as Plastocyanin-like 1.
+At position 245 to 346, the domain is characterized as Plastocyanin-like 2.
+At position 33 to 359, the domain is characterized as Asparaginase/glutaminase.
+At position 270 to 445, the domain is characterized as B30.2/SPRY.
+At position 704 to 729, the domain is characterized as IQ 1.
+At position 730 to 750, the domain is characterized as IQ 2.
+At position 837 to 866, the domain is characterized as IQ 6.
+At position 952 to 1136, the domain is characterized as TH1.
+At position 24 to 154, the domain is characterized as RNase III.
+At position 181 to 250, the domain is characterized as DRBM.
+At position 372 to 532, the domain is characterized as Helicase C-terminal.
+At position 1 to 164, the domain is characterized as PTS EIIB type-4.
+At position 41 to 150, the domain is characterized as sHSP.
+At position 48 to 119, the domain is characterized as POTRA.
+At position 122 to 423, the domain is characterized as USP.
+At position 28 to 297, the domain is characterized as tr-type G.
+At position 230 to 400, the domain is characterized as PCI.
+At position 86 to 159, the domain is characterized as PAS 1.
+At position 229 to 299, the domain is characterized as PAS 2.
+At position 701 to 889, the domain is characterized as SEC7.
+At position 47 to 123, the domain is characterized as Carrier 1.
+At position 1096 to 1171, the domain is characterized as Carrier 2.
+At position 3 to 95, the domain is characterized as Chorein N-terminal.
+At position 412 to 464, the domain is characterized as SANT.
+At position 2 to 450, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 480 to 746, the domain is characterized as UvrD-like helicase C-terminal.
+At position 80 to 243, the domain is characterized as Bms1-type G.
+At position 134 to 332, the domain is characterized as ATP-grasp.
+At position 28 to 106, the domain is characterized as Ig-like.
+At position 169 to 196, the domain is characterized as ITAM.
+At position 147 to 206, the domain is characterized as BSD 1.
+At position 227 to 278, the domain is characterized as BSD 2.
+At position 32 to 212, the domain is characterized as FAD-binding PCMH-type.
+At position 152 to 263, the domain is characterized as FAD-binding FR-type.
+At position 294 to 355, the domain is characterized as SH3.
+At position 99 to 385, the domain is characterized as tr-type G.
+At position 263 to 316, the domain is characterized as bHLH.
+At position 1721 to 1756, the domain is characterized as EF-hand.
+At position 32 to 108, the domain is characterized as Inhibitor I9.
+At position 128 to 402, the domain is characterized as Peptidase S8.
+At position 11 to 185, the domain is characterized as Exonuclease.
+At position 1 to 254, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 47 to 159, the domain is characterized as sHSP.
+At position 647 to 707, the domain is characterized as HTH myb-type.
+At position 623 to 710, the domain is characterized as BRCT.
+At position 34 to 338, the domain is characterized as tr-type G.
+At position 5 to 41, the domain is characterized as EF-hand 1.
+At position 452 to 524, the domain is characterized as HSA.
+At position 758 to 923, the domain is characterized as Helicase ATP-binding.
+At position 1076 to 1238, the domain is characterized as Helicase C-terminal.
+At position 1436 to 1506, the domain is characterized as Bromo.
+At position 14 to 76, the domain is characterized as Myb-like.
+At position 531 to 644, the domain is characterized as Calponin-homology (CH).
+At position 57 to 343, the domain is characterized as tr-type G.
+At position 49 to 277, the domain is characterized as Protein kinase.
+At position 291 to 373, the domain is characterized as PKD 1.
+At position 375 to 456, the domain is characterized as PKD 2.
+At position 457 to 1349, the domain is characterized as REJ.
+At position 1465 to 1511, the domain is characterized as GPS.
+At position 1573 to 1690, the domain is characterized as PLAT.
+At position 1 to 126, the domain is characterized as Jacalin-type lectin.
+At position 129 to 453, the domain is characterized as Peptidase S8.
+At position 461 to 597, the domain is characterized as P/Homo B.
+At position 625 to 859, the domain is characterized as Fibrillar collagen NC1.
+At position 87 to 304, the domain is characterized as Radical SAM core.
+At position 60 to 161, the domain is characterized as Ig-like C2-type.
+At position 290 to 495, the domain is characterized as Peptidase M12B.
+At position 496 to 585, the domain is characterized as Disintegrin.
+At position 586 to 641, the domain is characterized as TSP type-1 1.
+At position 874 to 922, the domain is characterized as TSP type-1 2.
+At position 927 to 987, the domain is characterized as TSP type-1 3.
+At position 988 to 1048, the domain is characterized as TSP type-1 4.
+At position 1051 to 1115, the domain is characterized as TSP type-1 5.
+At position 1127 to 1181, the domain is characterized as TSP type-1 6.
+At position 1186 to 1223, the domain is characterized as PLAC.
+At position 18 to 141, the domain is characterized as Rhodanese.
+At position 35 to 225, the domain is characterized as Chitin-binding type-4.
+At position 258 to 364, the domain is characterized as CBM2.
+At position 8 to 115, the domain is characterized as Calponin-homology (CH) 1.
+At position 124 to 229, the domain is characterized as Calponin-homology (CH) 2.
+At position 26 to 256, the domain is characterized as Radical SAM core.
+At position 1 to 185, the domain is characterized as RNase H type-2.
+At position 250 to 446, the domain is characterized as Helicase ATP-binding.
+At position 501 to 653, the domain is characterized as Helicase C-terminal.
+At position 22 to 255, the domain is characterized as AB hydrolase-1.
+At position 1 to 242, the domain is characterized as Peptidase S1.
+At position 113 to 485, the domain is characterized as GRAS.
+At position 1 to 57, the domain is characterized as RabBD.
+At position 637 to 762, the domain is characterized as C2 1.
+At position 777 to 906, the domain is characterized as C2 2.
+At position 141 to 176, the domain is characterized as Tify.
+At position 493 to 744, the domain is characterized as EAL.
+At position 424 to 521, the domain is characterized as SWIRM.
+At position 596 to 647, the domain is characterized as SANT.
+At position 142 to 215, the domain is characterized as HTH crp-type.
+At position 631 to 906, the domain is characterized as Protein kinase.
+At position 158 to 295, the domain is characterized as ADD.
+At position 1566 to 1753, the domain is characterized as Helicase ATP-binding.
+At position 2008 to 2188, the domain is characterized as Helicase C-terminal.
+At position 35 to 218, the domain is characterized as tr-type G.
+At position 146 to 221, the domain is characterized as Carrier.
+At position 1121 to 1661, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 705 to 998, the domain is characterized as Protein kinase.
+At position 72 to 246, the domain is characterized as FAD-binding PCMH-type.
+At position 74 to 223, the domain is characterized as PID.
+At position 26 to 147, the domain is characterized as Barwin.
+At position 59 to 248, the domain is characterized as Brix.
+At position 15 to 243, the domain is characterized as Radical SAM core.
+At position 406 to 485, the domain is characterized as B5.
+At position 712 to 814, the domain is characterized as FDX-ACB.
+At position 210 to 334, the domain is characterized as Peptidase C51.
+At position 20 to 139, the domain is characterized as C-type lysozyme.
+At position 243 to 306, the domain is characterized as bZIP.
+At position 372 to 650, the domain is characterized as Radical SAM core.
+At position 77 to 166, the domain is characterized as Ig-like C2-type 1.
+At position 179 to 257, the domain is characterized as Ig-like C2-type 2.
+At position 627 to 881, the domain is characterized as Protein kinase.
+At position 116 to 154, the domain is characterized as CHCH.
+At position 138 to 313, the domain is characterized as Helicase ATP-binding.
+At position 343 to 497, the domain is characterized as Helicase C-terminal.
+At position 123 to 297, the domain is characterized as CRAL-TRIO.
+At position 357 to 459, the domain is characterized as VWFA.
+At position 109 to 417, the domain is characterized as Protein kinase.
+At position 9 to 203, the domain is characterized as tr-type G.
+At position 205 to 257, the domain is characterized as HAMP.
+At position 262 to 333, the domain is characterized as PAS.
+At position 326 to 379, the domain is characterized as PAC.
+At position 383 to 601, the domain is characterized as Histidine kinase.
+At position 26 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 159 to 247, the domain is characterized as Ig-like C2-type 2.
+At position 256 to 358, the domain is characterized as Ig-like C2-type 3.
+At position 477 to 766, the domain is characterized as Protein kinase.
+At position 428 to 555, the domain is characterized as Ricin B-type lectin.
+At position 160 to 326, the domain is characterized as OBG-type G.
+At position 37 to 97, the domain is characterized as CBS 1.
+At position 118 to 181, the domain is characterized as CBS 2.
+At position 194 to 253, the domain is characterized as CBS 3.
+At position 262 to 322, the domain is characterized as CBS 4.
+At position 278 to 452, the domain is characterized as NodB homology.
+At position 97 to 191, the domain is characterized as Plastocyanin-like 1.
+At position 241 to 342, the domain is characterized as Plastocyanin-like 2.
+At position 493 to 609, the domain is characterized as PI-PLC Y-box.
+At position 609 to 736, the domain is characterized as C2.
+At position 137 to 202, the domain is characterized as HTH luxR-type.
+At position 33 to 92, the domain is characterized as Sushi 1.
+At position 93 to 154, the domain is characterized as Sushi 2.
+At position 155 to 219, the domain is characterized as Sushi 3.
+At position 220 to 279, the domain is characterized as Sushi 4.
+At position 280 to 346, the domain is characterized as Sushi 5.
+At position 347 to 412, the domain is characterized as Sushi 6.
+At position 451 to 509, the domain is characterized as Sushi 7.
+At position 90 to 197, the domain is characterized as Cadherin 1.
+At position 198 to 309, the domain is characterized as Cadherin 2.
+At position 310 to 423, the domain is characterized as Cadherin 3.
+At position 424 to 528, the domain is characterized as Cadherin 4.
+At position 529 to 644, the domain is characterized as Cadherin 5.
+At position 66 to 93, the domain is characterized as EF-hand 2.
+At position 118 to 368, the domain is characterized as Radical SAM core.
+At position 2 to 130, the domain is characterized as ADF-H.
+At position 69 to 221, the domain is characterized as N-acetyltransferase.
+At position 9 to 176, the domain is characterized as Thioredoxin.
+At position 1 to 60, the domain is characterized as Peptidase M12B.
+At position 43 to 105, the domain is characterized as t-SNARE coiled-coil homology.
+At position 129 to 159, the domain is characterized as EF-hand 4.
+At position 1 to 97, the domain is characterized as Ig-like 1.
+At position 135 to 227, the domain is characterized as Ig-like 2.
+At position 304 to 392, the domain is characterized as Ig-like 3.
+At position 396 to 502, the domain is characterized as Ig-like 4.
+At position 184 to 309, the domain is characterized as BAH.
+At position 341 to 872, the domain is characterized as SAM-dependent MTase C5-type.
+At position 441 to 504, the domain is characterized as Chromo.
+At position 441 to 653, the domain is characterized as FtsK.
+At position 138 to 177, the domain is characterized as STI1 1.
+At position 537 to 576, the domain is characterized as STI1 2.
+At position 78 to 184, the domain is characterized as C-type lectin.
+At position 17 to 258, the domain is characterized as ABC transporter.
+At position 153 to 212, the domain is characterized as VWFC 1.
+At position 216 to 274, the domain is characterized as VWFC 2.
+At position 197 to 249, the domain is characterized as KH.
+At position 93 to 277, the domain is characterized as ATP-grasp.
+At position 163 to 423, the domain is characterized as ABC transporter 1.
+At position 496 to 721, the domain is characterized as ABC transporter 2.
+At position 1 to 84, the domain is characterized as MIT.
+At position 116 to 436, the domain is characterized as Calpain catalytic.
+At position 95 to 167, the domain is characterized as PRC barrel.
+At position 1 to 337, the domain is characterized as GH10.
+At position 37 to 716, the domain is characterized as Myosin motor.
+At position 720 to 740, the domain is characterized as IQ 1.
+At position 741 to 768, the domain is characterized as IQ 2.
+At position 776 to 962, the domain is characterized as TH1.
+At position 1109 to 1170, the domain is characterized as SH3.
+At position 522 to 645, the domain is characterized as STAS.
+At position 78 to 153, the domain is characterized as Rho RNA-BD.
+At position 68 to 176, the domain is characterized as PX.
+At position 2 to 168, the domain is characterized as Era-type G.
+At position 199 to 279, the domain is characterized as KH type-2.
+At position 344 to 411, the domain is characterized as DRBM 1.
+At position 435 to 546, the domain is characterized as DRBM 2.
+At position 578 to 645, the domain is characterized as DRBM 3.
+At position 690 to 758, the domain is characterized as DRBM 4.
+At position 161 to 337, the domain is characterized as OBG-type G.
+At position 27 to 147, the domain is characterized as Ricin B-type lectin 1.
+At position 118 to 251, the domain is characterized as Ricin B-type lectin 2.
+At position 54 to 160, the domain is characterized as SSB.
+At position 112 to 352, the domain is characterized as Lon N-terminal.
+At position 748 to 932, the domain is characterized as Lon proteolytic.
+At position 89 to 152, the domain is characterized as S5 DRBM.
+At position 14 to 257, the domain is characterized as ABC transporter.
+At position 222 to 460, the domain is characterized as NR LBD.
+At position 37 to 185, the domain is characterized as RNase III.
+At position 211 to 274, the domain is characterized as DRBM.
+At position 204 to 320, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 206, the domain is characterized as N-acetyltransferase.
+At position 5 to 126, the domain is characterized as RCK N-terminal.
+At position 134 to 221, the domain is characterized as RCK C-terminal.
+At position 200 to 369, the domain is characterized as Helicase ATP-binding.
+At position 423 to 584, the domain is characterized as Helicase C-terminal.
+At position 1 to 95, the domain is characterized as PPIase FKBP-type.
+At position 32 to 158, the domain is characterized as Ig-like V-type 1.
+At position 156 to 293, the domain is characterized as Ig-like V-type 2.
+At position 101 to 300, the domain is characterized as ATP-grasp.
+At position 192 to 405, the domain is characterized as MurNAc-LAA.
+At position 311 to 621, the domain is characterized as ABC transmembrane type-1 1.
+At position 651 to 892, the domain is characterized as ABC transporter 1.
+At position 961 to 1251, the domain is characterized as ABC transmembrane type-1 2.
+At position 1285 to 1538, the domain is characterized as ABC transporter 2.
+At position 15 to 173, the domain is characterized as Thioredoxin 1.
+At position 179 to 334, the domain is characterized as Thioredoxin 2.
+At position 25 to 181, the domain is characterized as Helicase ATP-binding.
+At position 370 to 597, the domain is characterized as TRUD.
+At position 446 to 573, the domain is characterized as Ricin B-type lectin.
+At position 173 to 271, the domain is characterized as AB hydrolase-1.
+At position 177 to 236, the domain is characterized as FYR N-terminal.
+At position 237 to 316, the domain is characterized as FYR C-terminal.
+At position 21 to 253, the domain is characterized as Radical SAM core.
+At position 7 to 162, the domain is characterized as Thioredoxin.
+At position 22 to 246, the domain is characterized as Peptidase S1.
+At position 420 to 447, the domain is characterized as KOW 1.
+At position 473 to 506, the domain is characterized as KOW 2.
+At position 595 to 629, the domain is characterized as KOW 3.
+At position 730 to 763, the domain is characterized as KOW 4.
+At position 2 to 131, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 161 to 251, the domain is characterized as 5'-3' exonuclease.
+At position 137 to 242, the domain is characterized as C-type lectin.
+At position 221 to 483, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1017 to 1108, the domain is characterized as ARID.
+At position 546 to 617, the domain is characterized as MBD.
+At position 848 to 913, the domain is characterized as DDT.
+At position 1810 to 1880, the domain is characterized as Bromo.
+At position 160 to 190, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 10 to 72, the domain is characterized as IBB.
+At position 42 to 114, the domain is characterized as TRAM.
+At position 23 to 211, the domain is characterized as CP-type G.
+At position 29 to 213, the domain is characterized as EngB-type G.
+At position 8 to 131, the domain is characterized as FAD-binding FR-type.
+At position 45 to 236, the domain is characterized as Rab-GAP TBC.
+At position 343 to 556, the domain is characterized as TLDc.
+At position 60 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 30 to 417, the domain is characterized as Helicase ATP-binding.
+At position 637 to 672, the domain is characterized as UVR.
+At position 177 to 209, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 192 to 420, the domain is characterized as NR LBD.
+At position 39 to 343, the domain is characterized as Protein kinase.
+At position 242 to 455, the domain is characterized as Histidine kinase.
+At position 35 to 421, the domain is characterized as Helicase ATP-binding.
+At position 668 to 703, the domain is characterized as UVR.
+At position 349 to 382, the domain is characterized as WW 1.
+At position 381 to 414, the domain is characterized as WW 2.
+At position 456 to 489, the domain is characterized as WW 3.
+At position 496 to 529, the domain is characterized as WW 4.
+At position 588 to 922, the domain is characterized as HECT.
+At position 98 to 168, the domain is characterized as MaoC-like.
+At position 157 to 247, the domain is characterized as TonB C-terminal.
+At position 44 to 139, the domain is characterized as sHSP.
+At position 223 to 256, the domain is characterized as WW 1.
+At position 326 to 359, the domain is characterized as WW 2.
+At position 386 to 419, the domain is characterized as WW 3.
+At position 475 to 808, the domain is characterized as HECT.
+At position 321 to 381, the domain is characterized as SAM.
+At position 174 to 249, the domain is characterized as ACT.
+At position 286 to 539, the domain is characterized as Protein kinase.
+At position 5 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 200 to 391, the domain is characterized as GMPS ATP-PPase.
+At position 177 to 381, the domain is characterized as Helicase ATP-binding.
+At position 434 to 583, the domain is characterized as Helicase C-terminal.
+At position 50 to 278, the domain is characterized as Radical SAM core.
+At position 843 to 912, the domain is characterized as BTB.
+At position 1009 to 1245, the domain is characterized as MIF4G.
+At position 356 to 395, the domain is characterized as EGF-like 1.
+At position 396 to 435, the domain is characterized as EGF-like 2; calcium-binding.
+At position 18 to 126, the domain is characterized as HIT.
+At position 80 to 99, the domain is characterized as UIM 1.
+At position 105 to 124, the domain is characterized as UIM 2.
+At position 2 to 216, the domain is characterized as ABC transporter.
+At position 46 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 267 to 356, the domain is characterized as Ig-like C2-type 3.
+At position 361 to 448, the domain is characterized as Ig-like C2-type 4.
+At position 454 to 541, the domain is characterized as Ig-like C2-type 5.
+At position 545 to 626, the domain is characterized as Ig-like C2-type 6.
+At position 649 to 744, the domain is characterized as Fibronectin type-III 1.
+At position 746 to 843, the domain is characterized as Fibronectin type-III 2.
+At position 848 to 950, the domain is characterized as Fibronectin type-III 3.
+At position 954 to 1051, the domain is characterized as Fibronectin type-III 4.
+At position 35 to 231, the domain is characterized as GH11 1.
+At position 285 to 324, the domain is characterized as CBM10 1.
+At position 332 to 371, the domain is characterized as CBM10 2.
+At position 416 to 617, the domain is characterized as GH11 2.
+At position 1 to 14, the domain is characterized as Fibronectin type-III 1.
+At position 17 to 112, the domain is characterized as Fibronectin type-III 2.
+At position 114 to 202, the domain is characterized as Fibronectin type-III 3.
+At position 205 to 295, the domain is characterized as Fibronectin type-III 4.
+At position 296 to 386, the domain is characterized as Fibronectin type-III 5.
+At position 387 to 480, the domain is characterized as Fibronectin type-III 6.
+At position 481 to 572, the domain is characterized as Fibronectin type-III 7.
+At position 573 to 660, the domain is characterized as Fibronectin type-III 8.
+At position 661 to 754, the domain is characterized as Fibronectin type-III 9.
+At position 755 to 841, the domain is characterized as Fibronectin type-III 10.
+At position 842 to 933, the domain is characterized as Fibronectin type-III 11.
+At position 1054 to 1145, the domain is characterized as Fibronectin type-III 12.
+At position 1155 to 1199, the domain is characterized as Fibronectin type-I 1.
+At position 1200 to 1243, the domain is characterized as Fibronectin type-I 2.
+At position 1245 to 1287, the domain is characterized as Fibronectin type-I 3.
+At position 36 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 375 to 544, the domain is characterized as tr-type G.
+At position 4 to 66, the domain is characterized as LCN-type CS-alpha/beta.
+At position 377 to 406, the domain is characterized as IQ.
+At position 59 to 154, the domain is characterized as Fibronectin type-III 1.
+At position 158 to 253, the domain is characterized as Fibronectin type-III 2.
+At position 309 to 397, the domain is characterized as Fibronectin type-III 3.
+At position 400 to 495, the domain is characterized as Fibronectin type-III 4.
+At position 497 to 564, the domain is characterized as Fibronectin type-III 5.
+At position 568 to 663, the domain is characterized as Fibronectin type-III 6.
+At position 668 to 757, the domain is characterized as Fibronectin type-III 7.
+At position 762 to 852, the domain is characterized as Fibronectin type-III 8.
+At position 857 to 946, the domain is characterized as Fibronectin type-III 9.
+At position 951 to 1051, the domain is characterized as Fibronectin type-III 10.
+At position 1056 to 1149, the domain is characterized as Fibronectin type-III 11.
+At position 1154 to 1241, the domain is characterized as Fibronectin type-III 12.
+At position 1246 to 1339, the domain is characterized as Fibronectin type-III 13.
+At position 1343 to 1429, the domain is characterized as Fibronectin type-III 14.
+At position 1433 to 1537, the domain is characterized as Fibronectin type-III 15.
+At position 1542 to 1640, the domain is characterized as Fibronectin type-III 16.
+At position 1645 to 1746, the domain is characterized as Fibronectin type-III 17.
+At position 2004 to 2260, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1158 to 1342, the domain is characterized as DH.
+At position 1375 to 1488, the domain is characterized as PH.
+At position 1494 to 1555, the domain is characterized as SH3.
+At position 160 to 231, the domain is characterized as PPIase FKBP-type.
+At position 1054 to 1143, the domain is characterized as Fibronectin type-III 1.
+At position 1196 to 1302, the domain is characterized as Fibronectin type-III 2.
+At position 26 to 254, the domain is characterized as SET.
+At position 136 to 188, the domain is characterized as HNH.
+At position 221 to 313, the domain is characterized as Olduvai 1.
+At position 314 to 402, the domain is characterized as Olduvai 2.
+At position 405 to 460, the domain is characterized as Olduvai 3.
+At position 461 to 552, the domain is characterized as Olduvai 4.
+At position 555 to 633, the domain is characterized as Olduvai 5.
+At position 178 to 244, the domain is characterized as R3H.
+At position 37 to 159, the domain is characterized as Avidin-like.
+At position 8 to 290, the domain is characterized as Protein kinase.
+At position 38 to 232, the domain is characterized as PBC.
+At position 32 to 120, the domain is characterized as Link.
+At position 23 to 92, the domain is characterized as H15.
+At position 121 to 150, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 160 to 189, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 82 to 131, the domain is characterized as Laminin EGF-like 1.
+At position 132 to 186, the domain is characterized as Laminin EGF-like 2.
+At position 187 to 240, the domain is characterized as Laminin EGF-like 3.
+At position 241 to 255, the domain is characterized as Laminin EGF-like 4; truncated.
+At position 833 to 1035, the domain is characterized as Laminin G-like 1.
+At position 1047 to 1227, the domain is characterized as Laminin G-like 2.
+At position 1234 to 1402, the domain is characterized as Laminin G-like 3.
+At position 1469 to 1640, the domain is characterized as Laminin G-like 4.
+At position 1647 to 1820, the domain is characterized as Laminin G-like 5.
+At position 574 to 679, the domain is characterized as PilZ.
+At position 1 to 239, the domain is characterized as ABC transporter.
+At position 7 to 223, the domain is characterized as tr-type G.
+At position 261 to 331, the domain is characterized as Fibronectin type-III 1.
+At position 445 to 564, the domain is characterized as Fibronectin type-III 2.
+At position 48 to 84, the domain is characterized as EGF-like 1; calcium-binding.
+At position 85 to 126, the domain is characterized as EGF-like 2.
+At position 183 to 409, the domain is characterized as Peptidase S1.
+At position 58 to 77, the domain is characterized as UIM 1.
+At position 82 to 102, the domain is characterized as UIM 2.
+At position 17 to 171, the domain is characterized as Thioredoxin 1.
+At position 177 to 326, the domain is characterized as Thioredoxin 2.
+At position 1 to 56, the domain is characterized as CpcD-like.
+At position 26 to 227, the domain is characterized as ABC transporter.
+At position 18 to 86, the domain is characterized as HTH gntR-type.
+At position 256 to 285, the domain is characterized as IQ.
+At position 361 to 447, the domain is characterized as RRM.
+At position 67 to 102, the domain is characterized as Tify.
+At position 1 to 127, the domain is characterized as RNase H type-1.
+At position 76 to 108, the domain is characterized as LisH.
+At position 19 to 270, the domain is characterized as GH16.
+At position 632 to 1075, the domain is characterized as Biotin carboxylation.
+At position 751 to 948, the domain is characterized as ATP-grasp.
+At position 1754 to 1832, the domain is characterized as Biotinyl-binding.
+At position 457 to 626, the domain is characterized as tr-type G.
+At position 31 to 114, the domain is characterized as Inhibitor I9.
+At position 124 to 407, the domain is characterized as Peptidase S8.
+At position 1 to 140, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 176 to 443, the domain is characterized as SF4 helicase; first part.
+At position 494 to 643, the domain is characterized as DOD-type homing endonuclease.
+At position 606 to 870, the domain is characterized as SF4 helicase; second part.
+At position 32 to 232, the domain is characterized as GH16.
+At position 62 to 185, the domain is characterized as SCP.
+At position 299 to 372, the domain is characterized as SAM.
+At position 25 to 131, the domain is characterized as Gnk2-homologous 1.
+At position 139 to 241, the domain is characterized as Gnk2-homologous 2.
+At position 323 to 578, the domain is characterized as Protein kinase.
+At position 26 to 148, the domain is characterized as MPN.
+At position 14 to 44, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 57 to 314, the domain is characterized as Protein kinase.
+At position 18 to 111, the domain is characterized as CFEM.
+At position 28 to 102, the domain is characterized as RRM 1.
+At position 352 to 434, the domain is characterized as RRM 2.
+At position 56 to 290, the domain is characterized as Radical SAM core.
+At position 4 to 62, the domain is characterized as Flavodoxin-like.
+At position 92 to 248, the domain is characterized as Tyr recombinase.
+At position 84 to 388, the domain is characterized as Protein kinase.
+At position 7 to 55, the domain is characterized as EF-hand.
+At position 124 to 241, the domain is characterized as Calponin-homology (CH) 1.
+At position 269 to 372, the domain is characterized as Calponin-homology (CH) 2.
+At position 393 to 499, the domain is characterized as Calponin-homology (CH) 3.
+At position 514 to 622, the domain is characterized as Calponin-homology (CH) 4.
+At position 153 to 275, the domain is characterized as MPN.
+At position 36 to 147, the domain is characterized as C-type lectin.
+At position 78 to 170, the domain is characterized as Fibronectin type-III.
+At position 164 to 259, the domain is characterized as BRCT.
+At position 305 to 564, the domain is characterized as Glutamine amidotransferase type-1.
+At position 180 to 286, the domain is characterized as Cytochrome c.
+At position 45 to 306, the domain is characterized as ZP.
+At position 347 to 441, the domain is characterized as Helicase C-terminal.
+At position 56 to 249, the domain is characterized as Peptidase M12A.
+At position 124 to 191, the domain is characterized as Sushi 2.
+At position 30 to 131, the domain is characterized as BTB.
+At position 267 to 380, the domain is characterized as N-terminal Ras-GEF.
+At position 385 to 470, the domain is characterized as PDZ.
+At position 606 to 692, the domain is characterized as Ras-associating.
+At position 717 to 944, the domain is characterized as Ras-GEF.
+At position 268 to 449, the domain is characterized as B30.2/SPRY.
+At position 594 to 653, the domain is characterized as KH.
+At position 665 to 737, the domain is characterized as S1 motif.
+At position 1069 to 1320, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 223, the domain is characterized as tr-type G.
+At position 239 to 333, the domain is characterized as Fibronectin type-III 1.
+At position 331 to 429, the domain is characterized as Ig-like.
+At position 539 to 634, the domain is characterized as Fibronectin type-III 2.
+At position 639 to 732, the domain is characterized as Fibronectin type-III 3.
+At position 740 to 833, the domain is characterized as Fibronectin type-III 4.
+At position 24 to 64, the domain is characterized as Saposin A-type.
+At position 64 to 146, the domain is characterized as Saposin B-type 1.
+At position 191 to 268, the domain is characterized as Saposin B-type 2.
+At position 287 to 362, the domain is characterized as Saposin B-type 3.
+At position 168 to 254, the domain is characterized as PPIase FKBP-type.
+At position 590 to 687, the domain is characterized as TAFH.
+At position 426 to 822, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1317 to 1626, the domain is characterized as PKS/mFAS DH.
+At position 1713 to 1789, the domain is characterized as Carrier.
+At position 304 to 350, the domain is characterized as G-patch.
+At position 126 to 394, the domain is characterized as NR LBD.
+At position 1 to 81, the domain is characterized as PET.
+At position 82 to 147, the domain is characterized as LIM zinc-binding 1.
+At position 148 to 207, the domain is characterized as LIM zinc-binding 2.
+At position 200 to 220, the domain is characterized as ELK.
+At position 374 to 441, the domain is characterized as TRAM.
+At position 20 to 160, the domain is characterized as MRH.
+At position 559 to 659, the domain is characterized as tRNA-binding.
+At position 7 to 272, the domain is characterized as Protein kinase.
+At position 416 to 512, the domain is characterized as Ig-like V-type 5.
+At position 24 to 75, the domain is characterized as Tudor-knot.
+At position 163 to 434, the domain is characterized as MYST-type HAT.
+At position 126 to 226, the domain is characterized as Fibronectin type-III 1.
+At position 231 to 329, the domain is characterized as Fibronectin type-III 2.
+At position 333 to 433, the domain is characterized as Fibronectin type-III 3.
+At position 42 to 96, the domain is characterized as EMI.
+At position 99 to 232, the domain is characterized as FAS1 1.
+At position 236 to 367, the domain is characterized as FAS1 2.
+At position 370 to 494, the domain is characterized as FAS1 3.
+At position 498 to 630, the domain is characterized as FAS1 4.
+At position 675 to 958, the domain is characterized as PPM-type phosphatase.
+At position 53 to 144, the domain is characterized as Cyclin N-terminal.
+At position 31 to 76, the domain is characterized as bZIP.
+At position 23 to 148, the domain is characterized as C2.
+At position 11 to 282, the domain is characterized as F-BAR.
+At position 426 to 486, the domain is characterized as SH3.
+At position 1 to 54, the domain is characterized as Kazal-like.
+At position 236 to 357, the domain is characterized as C2 1.
+At position 368 to 501, the domain is characterized as C2 2.
+At position 665 to 743, the domain is characterized as Carrier.
+At position 43 to 123, the domain is characterized as GST N-terminal.
+At position 128 to 259, the domain is characterized as GST C-terminal.
+At position 411 to 499, the domain is characterized as PPIase FKBP-type.
+At position 227 to 287, the domain is characterized as KH.
+At position 353 to 446, the domain is characterized as HD.
+At position 12 to 64, the domain is characterized as HTH myb-type 1.
+At position 65 to 119, the domain is characterized as HTH myb-type 2.
+At position 27 to 490, the domain is characterized as Hexokinase.
+At position 32 to 342, the domain is characterized as Protein kinase.
+At position 562 to 849, the domain is characterized as Protein kinase.
+At position 907 to 1037, the domain is characterized as Guanylate cyclase.
+At position 1 to 51, the domain is characterized as IBB.
+At position 431 to 478, the domain is characterized as SARAH.
+At position 113 to 202, the domain is characterized as HTH La-type RNA-binding.
+At position 203 to 281, the domain is characterized as RRM.
+At position 26 to 363, the domain is characterized as Kinesin motor.
+At position 1479 to 1720, the domain is characterized as VLIG-type G.
+At position 62 to 213, the domain is characterized as Cupin type-1.
+At position 1 to 76, the domain is characterized as TRAM.
+At position 1251 to 1325, the domain is characterized as Carrier 1.
+At position 1785 to 1859, the domain is characterized as Carrier 2.
+At position 174 to 356, the domain is characterized as DH.
+At position 386 to 501, the domain is characterized as PH.
+At position 549 to 603, the domain is characterized as Kazal-like.
+At position 33 to 116, the domain is characterized as MIT.
+At position 195 to 313, the domain is characterized as Rhodanese.
+At position 777 to 1109, the domain is characterized as USP.
+At position 265 to 453, the domain is characterized as Glutamine amidotransferase type-1.
+At position 604 to 796, the domain is characterized as ATP-grasp 1.
+At position 1139 to 1330, the domain is characterized as ATP-grasp 2.
+At position 1396 to 1575, the domain is characterized as MGS-like.
+At position 8 to 138, the domain is characterized as EamA 1.
+At position 151 to 279, the domain is characterized as EamA 2.
+At position 49 to 94, the domain is characterized as Clip.
+At position 109 to 351, the domain is characterized as Peptidase S1.
+At position 30 to 288, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 5 to 146, the domain is characterized as Nudix hydrolase.
+At position 292 to 502, the domain is characterized as NEL.
+At position 1531 to 1754, the domain is characterized as Collagen IV NC1.
+At position 746 to 828, the domain is characterized as SUEL-type lectin.
+At position 223 to 395, the domain is characterized as PCI.
+At position 27 to 413, the domain is characterized as Helicase ATP-binding.
+At position 322 to 416, the domain is characterized as Rieske.
+At position 119 to 279, the domain is characterized as PINIT.
+At position 166 to 273, the domain is characterized as SPR.
+At position 20 to 267, the domain is characterized as ABC transporter.
+At position 207 to 296, the domain is characterized as Ig-like C1-type.
+At position 27 to 74, the domain is characterized as F-box.
+At position 19 to 132, the domain is characterized as FZ.
+At position 91 to 411, the domain is characterized as PPM-type phosphatase.
+At position 811 to 875, the domain is characterized as SAM.
+At position 36 to 82, the domain is characterized as WAP 1.
+At position 83 to 133, the domain is characterized as WAP 2.
+At position 18 to 202, the domain is characterized as UmuC.
+At position 139 to 232, the domain is characterized as PpiC.
+At position 25 to 219, the domain is characterized as GH16.
+At position 14 to 205, the domain is characterized as RNase H type-2.
+At position 26 to 293, the domain is characterized as GH18.
+At position 295 to 365, the domain is characterized as Mop.
+At position 3 to 238, the domain is characterized as ABC transporter.
+At position 114 to 193, the domain is characterized as REM-1 2.
+At position 202 to 283, the domain is characterized as REM-1 3.
+At position 310 to 473, the domain is characterized as C2.
+At position 619 to 878, the domain is characterized as Protein kinase.
+At position 879 to 946, the domain is characterized as AGC-kinase C-terminal.
+At position 368 to 440, the domain is characterized as Bromo 2.
+At position 600 to 682, the domain is characterized as NET.
+At position 205 to 231, the domain is characterized as ShKT.
+At position 133 to 197, the domain is characterized as S1 motif.
+At position 300 to 446, the domain is characterized as KH.
+At position 215 to 307, the domain is characterized as ARID.
+At position 419 to 517, the domain is characterized as REKLES.
+At position 7 to 247, the domain is characterized as PABS.
+At position 409 to 573, the domain is characterized as Helicase ATP-binding.
+At position 598 to 771, the domain is characterized as Helicase C-terminal.
+At position 927 to 1046, the domain is characterized as TFIIS central.
+At position 251 to 442, the domain is characterized as GATase cobBQ-type.
+At position 49 to 192, the domain is characterized as SCP.
+At position 403 to 483, the domain is characterized as Disintegrin.
+At position 564 to 609, the domain is characterized as UBA.
+At position 15 to 140, the domain is characterized as EamA 1.
+At position 164 to 290, the domain is characterized as EamA 2.
+At position 2 to 135, the domain is characterized as ENTH.
+At position 8 to 259, the domain is characterized as Pyruvate carboxyltransferase.
+At position 196 to 361, the domain is characterized as Helicase ATP-binding.
+At position 494 to 645, the domain is characterized as Helicase C-terminal.
+At position 886 to 938, the domain is characterized as SANT.
+At position 229 to 287, the domain is characterized as Plastocyanin-like.
+At position 4 to 127, the domain is characterized as MsrB.
+At position 92 to 161, the domain is characterized as PRC barrel.
+At position 14 to 69, the domain is characterized as Rubredoxin-like.
+At position 56 to 223, the domain is characterized as FCP1 homology.
+At position 294 to 537, the domain is characterized as Glutamine amidotransferase type-1.
+At position 341 to 455, the domain is characterized as Thioredoxin.
+At position 42 to 133, the domain is characterized as Ig-like C2-type.
+At position 86 to 140, the domain is characterized as HTH cro/C1-type.
+At position 3 to 141, the domain is characterized as C2 NT-type.
+At position 12 to 63, the domain is characterized as HTH psq-type.
+At position 75 to 146, the domain is characterized as HTH CENPB-type.
+At position 174 to 375, the domain is characterized as DDE-1.
+At position 209 to 577, the domain is characterized as GRAS.
+At position 2 to 203, the domain is characterized as ABC transporter.
+At position 195 to 276, the domain is characterized as Saposin B-type 2.
+At position 312 to 393, the domain is characterized as Saposin B-type 3.
+At position 406 to 487, the domain is characterized as Saposin B-type 4.
+At position 489 to 525, the domain is characterized as Saposin A-type 2.
+At position 420 to 530, the domain is characterized as STAS.
+At position 92 to 170, the domain is characterized as GIY-YIG.
+At position 280 to 315, the domain is characterized as UVR.
+At position 144 to 244, the domain is characterized as SRCR 1.
+At position 272 to 378, the domain is characterized as CUB 1.
+At position 428 to 528, the domain is characterized as SRCR 2.
+At position 556 to 667, the domain is characterized as CUB 2.
+At position 680 to 780, the domain is characterized as SRCR 3.
+At position 795 to 841, the domain is characterized as CUB 3.
+At position 570 to 631, the domain is characterized as Sushi 7.
+At position 702 to 763, the domain is characterized as Sushi 9.
+At position 40 to 288, the domain is characterized as Peptidase S1.
+At position 1 to 205, the domain is characterized as RNase H type-2.
+At position 3 to 79, the domain is characterized as RRM 1.
+At position 86 to 162, the domain is characterized as RRM 2.
+At position 189 to 259, the domain is characterized as RRM 3.
+At position 67 to 137, the domain is characterized as S1 motif.
+At position 404 to 711, the domain is characterized as Protein kinase.
+At position 282 to 564, the domain is characterized as NB-ARC.
+At position 10 to 92, the domain is characterized as PDZ.
+At position 1190 to 1469, the domain is characterized as ASD2.
+At position 149 to 224, the domain is characterized as Ubiquitin-like.
+At position 39 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 17 to 248, the domain is characterized as tr-type G.
+At position 18 to 93, the domain is characterized as Cytochrome b5 heme-binding.
+At position 535 to 610, the domain is characterized as Cytochrome b5 heme-binding.
+At position 638 to 749, the domain is characterized as FAD-binding FR-type.
+At position 77 to 293, the domain is characterized as Radical SAM core.
+At position 3 to 125, the domain is characterized as C-type lectin.
+At position 37 to 287, the domain is characterized as Protein kinase.
+At position 319 to 439, the domain is characterized as Ricin B-type lectin 1.
+At position 441 to 566, the domain is characterized as Ricin B-type lectin 2.
+At position 898 to 964, the domain is characterized as SAM 1.
+At position 1020 to 1084, the domain is characterized as SAM 2.
+At position 1108 to 1177, the domain is characterized as SAM 3.
+At position 1721 to 1785, the domain is characterized as KH.
+At position 312 to 468, the domain is characterized as PID 2.
+At position 918 to 1112, the domain is characterized as Rab-GAP TBC.
+At position 8 to 62, the domain is characterized as bHLH.
+At position 203 to 276, the domain is characterized as PAS 2.
+At position 45 to 236, the domain is characterized as GH11.
+At position 622 to 651, the domain is characterized as IQ.
+At position 19 to 124, the domain is characterized as Cadherin 1.
+At position 125 to 233, the domain is characterized as Cadherin 2.
+At position 234 to 340, the domain is characterized as Cadherin 3.
+At position 349 to 445, the domain is characterized as Cadherin 4.
+At position 446 to 555, the domain is characterized as Cadherin 5.
+At position 570 to 667, the domain is characterized as Cadherin 6.
+At position 1 to 251, the domain is characterized as Pyruvate carboxyltransferase.
+At position 240 to 401, the domain is characterized as Helicase C-terminal.
+At position 64 to 227, the domain is characterized as SIS.
+At position 260 to 341, the domain is characterized as SPOR.
+At position 38 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 69 to 98, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 154 to 183, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 191 to 220, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 7 to 91, the domain is characterized as Cytochrome b5 heme-binding.
+At position 20 to 224, the domain is characterized as PNPLA.
+At position 13 to 122, the domain is characterized as CBM20 1.
+At position 157 to 270, the domain is characterized as CBM20 2.
+At position 93 to 249, the domain is characterized as Tyrosine-protein phosphatase.
+At position 254 to 453, the domain is characterized as GATase cobBQ-type.
+At position 29 to 130, the domain is characterized as Phytocyanin.
+At position 434 to 659, the domain is characterized as ABC transporter.
+At position 384 to 660, the domain is characterized as Reverse transcriptase.
+At position 274 to 528, the domain is characterized as Protein kinase.
+At position 529 to 583, the domain is characterized as AGC-kinase C-terminal.
+At position 156 to 253, the domain is characterized as Fibronectin type-III.
+At position 3 to 87, the domain is characterized as Core-binding (CB).
+At position 108 to 287, the domain is characterized as Tyr recombinase.
+At position 380 to 553, the domain is characterized as tr-type G.
+At position 348 to 455, the domain is characterized as Calponin-homology (CH).
+At position 131 to 233, the domain is characterized as BACK.
+At position 19 to 306, the domain is characterized as RHD.
+At position 33 to 284, the domain is characterized as AB hydrolase-1.
+At position 15 to 87, the domain is characterized as KRAB.
+At position 46 to 162, the domain is characterized as Plastocyanin-like 1.
+At position 173 to 328, the domain is characterized as Plastocyanin-like 2.
+At position 444 to 586, the domain is characterized as Plastocyanin-like 3.
+At position 531 to 590, the domain is characterized as SH3.
+At position 279 to 337, the domain is characterized as AFP-like.
+At position 238 to 334, the domain is characterized as BEN.
+At position 103 to 153, the domain is characterized as DHHC.
+At position 41 to 59, the domain is characterized as EF-hand 1.
+At position 232 to 395, the domain is characterized as Helicase ATP-binding.
+At position 416 to 589, the domain is characterized as Helicase C-terminal.
+At position 22 to 116, the domain is characterized as UPAR/Ly6.
+At position 12 to 85, the domain is characterized as Sm.
+At position 100 to 177, the domain is characterized as PRC barrel.
+At position 5 to 83, the domain is characterized as ACT.
+At position 27 to 286, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 130 to 331, the domain is characterized as TLC.
+At position 86 to 149, the domain is characterized as bZIP.
+At position 330 to 399, the domain is characterized as BTB.
+At position 92 to 338, the domain is characterized as NR LBD.
+At position 81 to 272, the domain is characterized as ABC transmembrane type-1.
+At position 11 to 70, the domain is characterized as S4 RNA-binding.
+At position 30 to 149, the domain is characterized as C-type lectin.
+At position 237 to 455, the domain is characterized as Fibrinogen C-terminal.
+At position 34 to 107, the domain is characterized as RRM.
+At position 210 to 317, the domain is characterized as Tudor.
+At position 22 to 237, the domain is characterized as tr-type G.
+At position 449 to 960, the domain is characterized as KAP NTPase.
+At position 209 to 439, the domain is characterized as Radical SAM core.
+At position 55 to 140, the domain is characterized as Cytochrome c.
+At position 293 to 366, the domain is characterized as Mop.
+At position 505 to 629, the domain is characterized as STAS.
+At position 73 to 287, the domain is characterized as TLC.
+At position 361 to 383, the domain is characterized as WH2.
+At position 1024 to 1095, the domain is characterized as DRBM.
+At position 1348 to 1513, the domain is characterized as Helicase ATP-binding.
+At position 1585 to 1762, the domain is characterized as Helicase C-terminal.
+At position 4 to 86, the domain is characterized as GST N-terminal.
+At position 88 to 211, the domain is characterized as GST C-terminal.
+At position 54 to 148, the domain is characterized as Rhodanese.
+At position 22 to 219, the domain is characterized as Cytochrome b561.
+At position 109 to 307, the domain is characterized as MAGE.
+At position 333 to 410, the domain is characterized as Death.
+At position 283 to 352, the domain is characterized as Plastocyanin-like.
+At position 828 to 905, the domain is characterized as Carrier.
+At position 149 to 260, the domain is characterized as SET.
+At position 115 to 283, the domain is characterized as tr-type G.
+At position 416 to 443, the domain is characterized as PLD phosphodiesterase 2.
+At position 7 to 91, the domain is characterized as XRN2-binding (XTBD).
+At position 82 to 366, the domain is characterized as ABC transmembrane type-1 1.
+At position 424 to 647, the domain is characterized as ABC transporter 1.
+At position 868 to 1169, the domain is characterized as ABC transmembrane type-1 2.
+At position 1220 to 1453, the domain is characterized as ABC transporter 2.
+At position 73 to 140, the domain is characterized as KH 1.
+At position 165 to 234, the domain is characterized as KH 2.
+At position 340 to 403, the domain is characterized as KH 3.
+At position 349 to 427, the domain is characterized as OCT.
+At position 151 to 237, the domain is characterized as Death.
+At position 246 to 456, the domain is characterized as Peptidase M12B.
+At position 465 to 544, the domain is characterized as Disintegrin.
+At position 823 to 883, the domain is characterized as TSP type-1 2.
+At position 887 to 943, the domain is characterized as TSP type-1 3.
+At position 944 to 997, the domain is characterized as TSP type-1 4.
+At position 1313 to 1366, the domain is characterized as TSP type-1 5.
+At position 1368 to 1422, the domain is characterized as TSP type-1 6.
+At position 1423 to 1471, the domain is characterized as TSP type-1 7.
+At position 1472 to 1532, the domain is characterized as TSP type-1 8.
+At position 1535 to 1575, the domain is characterized as PLAC.
+At position 9 to 121, the domain is characterized as MTTase N-terminal.
+At position 50 to 295, the domain is characterized as Radical SAM core.
+At position 300 to 450, the domain is characterized as JmjC.
+At position 22 to 98, the domain is characterized as PDZ.
+At position 228 to 340, the domain is characterized as PID.
+At position 715 to 832, the domain is characterized as RGS.
+At position 962 to 1032, the domain is characterized as RBD 1.
+At position 1034 to 1104, the domain is characterized as RBD 2.
+At position 1187 to 1209, the domain is characterized as GoLoco.
+At position 349 to 414, the domain is characterized as J.
+At position 16 to 97, the domain is characterized as Lipoyl-binding.
+At position 76 to 143, the domain is characterized as BTB.
+At position 178 to 279, the domain is characterized as BACK.
+At position 17 to 298, the domain is characterized as FERM.
+At position 57 to 135, the domain is characterized as RRM.
+At position 400 to 509, the domain is characterized as SH2.
+At position 504 to 554, the domain is characterized as SOCS box.
+At position 112 to 141, the domain is characterized as IQ.
+At position 45 to 91, the domain is characterized as F-box.
+At position 31 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 227 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 317 to 411, the domain is characterized as Ig-like C2-type 4.
+At position 425 to 511, the domain is characterized as Ig-like C2-type 5.
+At position 533 to 628, the domain is characterized as Fibronectin type-III 1.
+At position 653 to 750, the domain is characterized as Fibronectin type-III 2.
+At position 755 to 849, the domain is characterized as Fibronectin type-III 3.
+At position 120 to 239, the domain is characterized as PilZ.
+At position 1 to 157, the domain is characterized as MGS-like.
+At position 105 to 177, the domain is characterized as HSA.
+At position 459 to 624, the domain is characterized as Helicase ATP-binding.
+At position 995 to 1150, the domain is characterized as Helicase C-terminal.
+At position 930 to 1052, the domain is characterized as MGS-like.
+At position 741 to 827, the domain is characterized as SUEL-type lectin.
+At position 228 to 488, the domain is characterized as Deacetylase sirtuin-type.
+At position 165 to 259, the domain is characterized as Olduvai 1.
+At position 436 to 528, the domain is characterized as Olduvai 2.
+At position 529 to 617, the domain is characterized as Olduvai 3.
+At position 620 to 675, the domain is characterized as Olduvai 4.
+At position 676 to 767, the domain is characterized as Olduvai 5.
+At position 770 to 865, the domain is characterized as Olduvai 6.
+At position 110 to 210, the domain is characterized as PB1.
+At position 86 to 368, the domain is characterized as PPM-type phosphatase.
+At position 65 to 118, the domain is characterized as SANT.
+At position 426 to 582, the domain is characterized as Exonuclease.
+At position 247 to 467, the domain is characterized as Histidine kinase.
+At position 64 to 98, the domain is characterized as EF-hand 1.
+At position 99 to 134, the domain is characterized as EF-hand 2.
+At position 135 to 170, the domain is characterized as EF-hand 3.
+At position 171 to 206, the domain is characterized as EF-hand 4.
+At position 22 to 311, the domain is characterized as ABC transmembrane type-1 1.
+At position 346 to 582, the domain is characterized as ABC transporter 1.
+At position 658 to 946, the domain is characterized as ABC transmembrane type-1 2.
+At position 981 to 1219, the domain is characterized as ABC transporter 2.
+At position 171 to 334, the domain is characterized as CMP/dCMP-type deaminase.
+At position 489 to 552, the domain is characterized as bZIP.
+At position 141 to 340, the domain is characterized as Helicase ATP-binding.
+At position 397 to 548, the domain is characterized as Helicase C-terminal.
+At position 97 to 173, the domain is characterized as PRC barrel.
+At position 230 to 470, the domain is characterized as CN hydrolase.
+At position 35 to 344, the domain is characterized as PPM-type phosphatase.
+At position 1476 to 1744, the domain is characterized as Protein kinase.
+At position 157 to 211, the domain is characterized as Laminin EGF-like 1.
+At position 212 to 274, the domain is characterized as Laminin EGF-like 2.
+At position 275 to 324, the domain is characterized as Laminin EGF-like 3.
+At position 345 to 475, the domain is characterized as NTR.
+At position 87 to 370, the domain is characterized as Protein kinase.
+At position 1 to 187, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 185, the domain is characterized as Macro.
+At position 686 to 775, the domain is characterized as BRCT.
+At position 33 to 315, the domain is characterized as Protein kinase.
+At position 7 to 60, the domain is characterized as SpoVT-AbrB 1.
+At position 32 to 457, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 925 to 1201, the domain is characterized as PKS/mFAS DH.
+At position 1700 to 1774, the domain is characterized as Carrier.
+At position 533 to 608, the domain is characterized as Carrier.
+At position 86 to 267, the domain is characterized as tr-type G.
+At position 671 to 876, the domain is characterized as MRH.
+At position 126 to 366, the domain is characterized as Radical SAM core.
+At position 56 to 123, the domain is characterized as BTB.
+At position 16 to 99, the domain is characterized as PDZ.
+At position 90 to 253, the domain is characterized as Integrase catalytic.
+At position 90 to 188, the domain is characterized as PilZ.
+At position 35 to 296, the domain is characterized as AB hydrolase-1.
+At position 9 to 169, the domain is characterized as N-acetyltransferase.
+At position 26 to 309, the domain is characterized as ABC transmembrane type-1.
+At position 341 to 577, the domain is characterized as ABC transporter.
+At position 25 to 262, the domain is characterized as ABC transporter.
+At position 25 to 104, the domain is characterized as GS beta-grasp.
+At position 111 to 358, the domain is characterized as GS catalytic.
+At position 4 to 184, the domain is characterized as KARI N-terminal Rossmann.
+At position 185 to 330, the domain is characterized as KARI C-terminal knotted.
+At position 153 to 410, the domain is characterized as ABC transporter 1.
+At position 85 to 139, the domain is characterized as HTH cro/C1-type.
+At position 356 to 493, the domain is characterized as YTH.
+At position 1 to 12, the domain is characterized as BTB.
+At position 8 to 119, the domain is characterized as MTTase N-terminal.
+At position 170 to 401, the domain is characterized as Radical SAM core.
+At position 403 to 469, the domain is characterized as TRAM.
+At position 9 to 242, the domain is characterized as PABS.
+At position 202 to 262, the domain is characterized as KH.
+At position 45 to 103, the domain is characterized as Collagen-like.
+At position 127 to 309, the domain is characterized as Helicase ATP-binding.
+At position 339 to 479, the domain is characterized as Helicase C-terminal.
+At position 125 to 271, the domain is characterized as RNase III 1.
+At position 403 to 503, the domain is characterized as RNase III 2.
+At position 1435 to 1540, the domain is characterized as AB hydrolase-1.
+At position 590 to 690, the domain is characterized as tRNA-binding.
+At position 141 to 174, the domain is characterized as EF-hand 3.
+At position 458 to 605, the domain is characterized as Peptidase S59.
+At position 5 to 80, the domain is characterized as Carrier.
+At position 20 to 144, the domain is characterized as FZ.
+At position 178 to 491, the domain is characterized as IF rod.
+At position 35 to 758, the domain is characterized as Myosin motor.
+At position 762 to 782, the domain is characterized as IQ 1.
+At position 1 to 234, the domain is characterized as RMT2.
+At position 503 to 758, the domain is characterized as Protein kinase.
+At position 9 to 128, the domain is characterized as Arf-GAP.
+At position 395 to 447, the domain is characterized as DHHC.
+At position 79 to 200, the domain is characterized as PH.
+At position 232 to 336, the domain is characterized as IRS-type PTB.
+At position 39 to 420, the domain is characterized as Helicase ATP-binding.
+At position 443 to 596, the domain is characterized as Helicase C-terminal.
+At position 640 to 675, the domain is characterized as UVR.
+At position 269 to 473, the domain is characterized as Pentraxin (PTX).
+At position 578 to 660, the domain is characterized as BRCT.
+At position 188 to 241, the domain is characterized as HAMP.
+At position 249 to 463, the domain is characterized as Histidine kinase.
+At position 112 to 208, the domain is characterized as Rieske.
+At position 31 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 24 to 215, the domain is characterized as RNase H type-2.
+At position 177 to 240, the domain is characterized as KH.
+At position 303 to 396, the domain is characterized as HD.
+At position 36 to 149, the domain is characterized as Ig-like V-type 1.
+At position 152 to 241, the domain is characterized as Ig-like V-type 2.
+At position 307 to 506, the domain is characterized as B30.2/SPRY.
+At position 202 to 247, the domain is characterized as SoHo.
+At position 1049 to 1108, the domain is characterized as SH3 1.
+At position 1123 to 1184, the domain is characterized as SH3 2.
+At position 1229 to 1290, the domain is characterized as SH3 3.
+At position 33 to 77, the domain is characterized as SMB.
+At position 43 to 136, the domain is characterized as Fibronectin type-III.
+At position 342 to 415, the domain is characterized as Chitin-binding type R&R.
+At position 9 to 371, the domain is characterized as Kinesin motor.
+At position 158 to 491, the domain is characterized as USP.
+At position 132 to 222, the domain is characterized as PpiC.
+At position 93 to 223, the domain is characterized as C-type lectin.
+At position 145 to 380, the domain is characterized as Radical SAM core.
+At position 83 to 198, the domain is characterized as C-type lectin.
+At position 448 to 515, the domain is characterized as SAM.
+At position 1078 to 1284, the domain is characterized as Rho-GAP.
+At position 1314 to 1521, the domain is characterized as START.
+At position 70 to 269, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 473, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 512 to 806, the domain is characterized as UvrD-like helicase C-terminal.
+At position 77 to 221, the domain is characterized as Flavodoxin-like.
+At position 276 to 515, the domain is characterized as FAD-binding FR-type.
+At position 45 to 85, the domain is characterized as EGF-like 1; calcium-binding.
+At position 86 to 127, the domain is characterized as EGF-like 2; calcium-binding.
+At position 128 to 168, the domain is characterized as EGF-like 3; calcium-binding.
+At position 177 to 213, the domain is characterized as EGF-like 4.
+At position 217 to 252, the domain is characterized as EGF-like 5.
+At position 286 to 321, the domain is characterized as EGF-like 6.
+At position 323 to 363, the domain is characterized as EGF-like 7; calcium-binding.
+At position 364 to 402, the domain is characterized as EGF-like 8; calcium-binding.
+At position 403 to 443, the domain is characterized as EGF-like 9; calcium-binding.
+At position 809 to 921, the domain is characterized as CUB.
+At position 511 to 578, the domain is characterized as DRBM 1.
+At position 620 to 685, the domain is characterized as DRBM 2.
+At position 118 to 401, the domain is characterized as Protein kinase.
+At position 80 to 126, the domain is characterized as SpoVT-AbrB 2.
+At position 16 to 205, the domain is characterized as Radical SAM core.
+At position 47 to 178, the domain is characterized as Guanylate cyclase.
+At position 160 to 296, the domain is characterized as cDENN.
+At position 298 to 375, the domain is characterized as dDENN.
+At position 1443 to 1542, the domain is characterized as Peptidase C50.
+At position 108 to 148, the domain is characterized as EGF-like.
+At position 347 to 440, the domain is characterized as BRCT.
+At position 189 to 258, the domain is characterized as PWWP.
+At position 875 to 993, the domain is characterized as SET.
+At position 1002 to 1018, the domain is characterized as Post-SET.
+At position 35 to 261, the domain is characterized as Glutamine amidotransferase type-2.
+At position 136 to 237, the domain is characterized as HTH LytTR-type.
+At position 420 to 563, the domain is characterized as MATH.
+At position 190 to 383, the domain is characterized as GMPS ATP-PPase.
+At position 375 to 470, the domain is characterized as Fibronectin type-III 1.
+At position 471 to 564, the domain is characterized as Fibronectin type-III 2.
+At position 546 to 744, the domain is characterized as B30.2/SPRY.
+At position 7 to 260, the domain is characterized as ABC transporter 1.
+At position 325 to 551, the domain is characterized as ABC transporter 2.
+At position 3 to 257, the domain is characterized as OBG-type G.
+At position 2 to 78, the domain is characterized as Sm.
+At position 56 to 202, the domain is characterized as Thioredoxin.
+At position 155 to 262, the domain is characterized as Cadherin 1.
+At position 263 to 375, the domain is characterized as Cadherin 2.
+At position 376 to 486, the domain is characterized as Cadherin 3.
+At position 487 to 593, the domain is characterized as Cadherin 4.
+At position 594 to 697, the domain is characterized as Cadherin 5.
+At position 29 to 187, the domain is characterized as GOLD.
+At position 1 to 92, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 101 to 205, the domain is characterized as FAD-binding FR-type.
+At position 210 to 270, the domain is characterized as SH3.
+At position 361 to 459, the domain is characterized as BRCT.
+At position 28 to 144, the domain is characterized as MTTase N-terminal.
+At position 167 to 398, the domain is characterized as Radical SAM core.
+At position 401 to 462, the domain is characterized as TRAM.
+At position 145 to 377, the domain is characterized as Radical SAM core.
+At position 25 to 119, the domain is characterized as Ras-associating.
+At position 179 to 275, the domain is characterized as PTS EIIB type-2.
+At position 310 to 687, the domain is characterized as PTS EIIC type-2.
+At position 89 to 183, the domain is characterized as GS beta-grasp.
+At position 188 to 621, the domain is characterized as GS catalytic.
+At position 27 to 224, the domain is characterized as Rho-GAP.
+At position 237 to 362, the domain is characterized as N-terminal Ras-GEF.
+At position 433 to 663, the domain is characterized as Ras-GEF.
+At position 1 to 279, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 281 to 588, the domain is characterized as UvrD-like helicase C-terminal.
+At position 34 to 225, the domain is characterized as RNase H type-2.
+At position 19 to 61, the domain is characterized as WAP 1.
+At position 62 to 107, the domain is characterized as WAP 2; atypical.
+At position 108 to 150, the domain is characterized as WAP 3.
+At position 83 to 153, the domain is characterized as MBD.
+At position 713 to 763, the domain is characterized as GRIP.
+At position 10 to 190, the domain is characterized as YrdC-like.
+At position 7 to 161, the domain is characterized as MPN.
+At position 5 to 198, the domain is characterized as RNase H type-2.
+At position 121 to 184, the domain is characterized as bZIP.
+At position 55 to 133, the domain is characterized as RRM.
+At position 75 to 141, the domain is characterized as HMA 1.
+At position 153 to 219, the domain is characterized as HMA 2.
+At position 228 to 294, the domain is characterized as HMA 3.
+At position 8 to 51, the domain is characterized as Histone-fold.
+At position 31 to 700, the domain is characterized as PFL.
+At position 707 to 830, the domain is characterized as Glycine radical.
+At position 178 to 307, the domain is characterized as NTR.
+At position 1 to 164, the domain is characterized as Thioredoxin.
+At position 232 to 283, the domain is characterized as LRRCT 1.
+At position 364 to 406, the domain is characterized as LRRNT.
+At position 562 to 613, the domain is characterized as LRRCT 2.
+At position 247 to 282, the domain is characterized as QLQ.
+At position 588 to 661, the domain is characterized as HSA.
+At position 779 to 944, the domain is characterized as Helicase ATP-binding.
+At position 1091 to 1254, the domain is characterized as Helicase C-terminal.
+At position 1568 to 1638, the domain is characterized as Bromo.
+At position 1 to 68, the domain is characterized as Galectin.
+At position 750 to 837, the domain is characterized as SUEL-type lectin.
+At position 7 to 51, the domain is characterized as LEM.
+At position 72 to 245, the domain is characterized as Helicase ATP-binding.
+At position 256 to 416, the domain is characterized as Helicase C-terminal.
+At position 9 to 258, the domain is characterized as UmuC.
+At position 155 to 235, the domain is characterized as RRM.
+At position 110 to 389, the domain is characterized as SET.
+At position 18 to 187, the domain is characterized as EngB-type G.
+At position 127 to 213, the domain is characterized as MtN3/slv 2.
+At position 477 to 545, the domain is characterized as S1 motif 1.
+At position 562 to 632, the domain is characterized as S1 motif 2.
+At position 649 to 716, the domain is characterized as S1 motif 3.
+At position 733 to 802, the domain is characterized as S1 motif 4.
+At position 111 to 270, the domain is characterized as CP-type G.
+At position 178 to 240, the domain is characterized as Sushi 1.
+At position 241 to 302, the domain is characterized as Sushi 2.
+At position 303 to 365, the domain is characterized as Sushi 3.
+At position 366 to 428, the domain is characterized as Sushi 4.
+At position 429 to 487, the domain is characterized as Sushi 5.
+At position 377 to 507, the domain is characterized as DOD-type homing endonuclease.
+At position 4 to 240, the domain is characterized as ABC transporter.
+At position 264 to 278, the domain is characterized as SAP 2.
+At position 107 to 285, the domain is characterized as ATP-grasp.
+At position 11 to 100, the domain is characterized as ABM.
+At position 46 to 316, the domain is characterized as Protein kinase.
+At position 411 to 506, the domain is characterized as B5.
+At position 731 to 824, the domain is characterized as FDX-ACB.
+At position 3 to 58, the domain is characterized as LCN-type CS-alpha/beta.
+At position 144 to 255, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 13 to 107, the domain is characterized as Chorein N-terminal.
+At position 198 to 274, the domain is characterized as KH type-2.
+At position 569 to 672, the domain is characterized as Cadherin 6.
+At position 45 to 113, the domain is characterized as POTRA.
+At position 261 to 311, the domain is characterized as DHHC.
+At position 119 to 190, the domain is characterized as PAS 1.
+At position 335 to 402, the domain is characterized as PAS 2.
+At position 999 to 1251, the domain is characterized as Protein kinase.
+At position 81 to 204, the domain is characterized as Thioredoxin 1.
+At position 416 to 546, the domain is characterized as Thioredoxin 2.
+At position 3 to 149, the domain is characterized as Clp R.
+At position 3 to 189, the domain is characterized as Glutamine amidotransferase type-1.
+At position 190 to 380, the domain is characterized as GMPS ATP-PPase.
+At position 933 to 1067, the domain is characterized as MGS-like.
+At position 229 to 256, the domain is characterized as PLD phosphodiesterase 1.
+At position 407 to 434, the domain is characterized as PLD phosphodiesterase 2.
+At position 79 to 269, the domain is characterized as Glutamine amidotransferase type-1.
+At position 270 to 462, the domain is characterized as GMPS ATP-PPase.
+At position 909 to 1032, the domain is characterized as CBM6.
+At position 21 to 52, the domain is characterized as LRRNT.
+At position 242 to 288, the domain is characterized as LRRCT.
+At position 289 to 375, the domain is characterized as Ig-like.
+At position 421 to 518, the domain is characterized as Fibronectin type-III.
+At position 40 to 492, the domain is characterized as Biotin carboxylation.
+At position 162 to 359, the domain is characterized as ATP-grasp.
+At position 578 to 846, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1115 to 1190, the domain is characterized as Biotinyl-binding.
+At position 64 to 309, the domain is characterized as GB1/RHD3-type G.
+At position 268 to 334, the domain is characterized as LIM zinc-binding.
+At position 175 to 333, the domain is characterized as Cupin type-1 1.
+At position 398 to 571, the domain is characterized as Cupin type-1 2.
+At position 30 to 131, the domain is characterized as CUB.
+At position 215 to 306, the domain is characterized as Ig-like.
+At position 4 to 160, the domain is characterized as N-acetyltransferase.
+At position 916 to 933, the domain is characterized as WH2.
+At position 210 to 393, the domain is characterized as PfpI endopeptidase 2.
+At position 282 to 359, the domain is characterized as PUA.
+At position 56 to 444, the domain is characterized as Helicase ATP-binding.
+At position 461 to 627, the domain is characterized as Helicase C-terminal.
+At position 651 to 686, the domain is characterized as UVR.
+At position 133 to 272, the domain is characterized as Fatty acid hydroxylase.
+At position 1210 to 1443, the domain is characterized as ABC transporter 2.
+At position 5 to 57, the domain is characterized as HTH deoR-type.
+At position 31 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 672 to 912, the domain is characterized as ABC transporter 1.
+At position 15 to 134, the domain is characterized as sHSP.
+At position 42 to 196, the domain is characterized as PID.
+At position 48 to 298, the domain is characterized as GB1/RHD3-type G.
+At position 672 to 949, the domain is characterized as Protein kinase.
+At position 3 to 284, the domain is characterized as DegV.
+At position 2 to 54, the domain is characterized as UBA.
+At position 386 to 463, the domain is characterized as UBX.
+At position 197 to 258, the domain is characterized as CBS 1.
+At position 280 to 340, the domain is characterized as CBS 2.
+At position 355 to 415, the domain is characterized as CBS 3.
+At position 427 to 486, the domain is characterized as CBS 4.
+At position 495 to 514, the domain is characterized as UIM.
+At position 51 to 116, the domain is characterized as NAC-A/B.
+At position 173 to 212, the domain is characterized as UBA.
+At position 620 to 699, the domain is characterized as BRCT.
+At position 43 to 131, the domain is characterized as Ig-like.
+At position 143 to 218, the domain is characterized as Ig-like C2-type.
+At position 229 to 323, the domain is characterized as Ig-like V-type.
+At position 46 to 127, the domain is characterized as RRM 1.
+At position 396 to 474, the domain is characterized as RRM 3.
+At position 5 to 36, the domain is characterized as HNF-p1.
+At position 102 to 197, the domain is characterized as POU-specific atypical.
+At position 1 to 110, the domain is characterized as Calponin-homology (CH).
+At position 152 to 211, the domain is characterized as SH3.
+At position 233 to 413, the domain is characterized as DH.
+At position 435 to 540, the domain is characterized as PH.
+At position 8 to 201, the domain is characterized as AMMECR1.
+At position 95 to 158, the domain is characterized as S4 RNA-binding.
+At position 24 to 129, the domain is characterized as Ig-like.
+At position 692 to 880, the domain is characterized as SEC7.
+At position 224 to 338, the domain is characterized as Ig-like C1-type.
+At position 391 to 413, the domain is characterized as WH2.
+At position 1706 to 1757, the domain is characterized as Kazal-like.
+At position 23 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 23 to 113, the domain is characterized as Ig-like.
+At position 120 to 199, the domain is characterized as RRM.
+At position 387 to 537, the domain is characterized as NTF2.
+At position 566 to 620, the domain is characterized as TAP-C.
+At position 623 to 701, the domain is characterized as BRCT.
+At position 37 to 79, the domain is characterized as CHCH.
+At position 103 to 415, the domain is characterized as IF rod.
+At position 57 to 127, the domain is characterized as U-box.
+At position 238 to 357, the domain is characterized as DOD-type homing endonuclease.
+At position 94 to 170, the domain is characterized as PA.
+At position 37 to 84, the domain is characterized as WAP.
+At position 88 to 138, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 451 to 501, the domain is characterized as DHHC.
+At position 175 to 261, the domain is characterized as 5'-3' exonuclease.
+At position 24 to 342, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 31 to 118, the domain is characterized as Inhibitor I9.
+At position 127 to 410, the domain is characterized as Peptidase S8.
+At position 158 to 231, the domain is characterized as PPIase FKBP-type.
+At position 9 to 235, the domain is characterized as RNase H type-2.
+At position 8 to 51, the domain is characterized as SMB 1.
+At position 52 to 96, the domain is characterized as SMB 2.
+At position 277 to 323, the domain is characterized as F-box.
+At position 23 to 63, the domain is characterized as F-box.
+At position 46 to 288, the domain is characterized as ABC transporter.
+At position 531 to 587, the domain is characterized as Chromo 1.
+At position 601 to 663, the domain is characterized as Chromo 2.
+At position 701 to 878, the domain is characterized as Helicase ATP-binding.
+At position 1008 to 1167, the domain is characterized as Helicase C-terminal.
+At position 199 to 283, the domain is characterized as TonB C-terminal.
+At position 889 to 935, the domain is characterized as F-box.
+At position 148 to 234, the domain is characterized as Ig-like C2-type 1.
+At position 250 to 352, the domain is characterized as Ig-like C2-type 2.
+At position 405 to 558, the domain is characterized as TIR.
+At position 496 to 568, the domain is characterized as U-box.
+At position 112 to 251, the domain is characterized as PPC.
+At position 49 to 315, the domain is characterized as Septin-type G.
+At position 100 to 426, the domain is characterized as Velvet.
+At position 30 to 161, the domain is characterized as RNase III.
+At position 77 to 183, the domain is characterized as HD.
+At position 236 to 413, the domain is characterized as VWFA 2.
+At position 442 to 612, the domain is characterized as VWFA 3.
+At position 628 to 797, the domain is characterized as VWFA 4.
+At position 814 to 987, the domain is characterized as VWFA 5.
+At position 1005 to 1178, the domain is characterized as VWFA 6.
+At position 1194 to 1376, the domain is characterized as VWFA 7.
+At position 1395 to 1446, the domain is characterized as Collagen-like 1.
+At position 1434 to 1490, the domain is characterized as Collagen-like 2.
+At position 1464 to 1520, the domain is characterized as Collagen-like 3.
+At position 1524 to 1580, the domain is characterized as Collagen-like 4.
+At position 1579 to 1629, the domain is characterized as Collagen-like 5.
+At position 1674 to 1729, the domain is characterized as Collagen-like 6.
+At position 1758 to 1965, the domain is characterized as VWFA 8.
+At position 1963 to 2154, the domain is characterized as VWFA 9.
+At position 2291 to 2487, the domain is characterized as VWFA 10.
+At position 599 to 698, the domain is characterized as tRNA-binding.
+At position 58 to 246, the domain is characterized as RNase H type-2.
+At position 5 to 78, the domain is characterized as RRM 1.
+At position 308 to 384, the domain is characterized as RRM 2.
+At position 489 to 560, the domain is characterized as RRM 3.
+At position 599 to 682, the domain is characterized as RRM 4.
+At position 704 to 781, the domain is characterized as RRM 5.
+At position 23 to 143, the domain is characterized as sHSP.
+At position 312 to 436, the domain is characterized as BAH.
+At position 479 to 1017, the domain is characterized as SAM-dependent MTase C5-type.
+At position 584 to 649, the domain is characterized as Chromo.
+At position 331 to 388, the domain is characterized as KASH.
+At position 207 to 307, the domain is characterized as BTB.
+At position 690 to 754, the domain is characterized as SAM 1.
+At position 760 to 828, the domain is characterized as SAM 2.
+At position 837 to 981, the domain is characterized as TIR.
+At position 57 to 100, the domain is characterized as UBA 1.
+At position 108 to 149, the domain is characterized as UBA 2.
+At position 188 to 231, the domain is characterized as UBA 3.
+At position 291 to 622, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 5 to 110, the domain is characterized as SSB.
+At position 3 to 169, the domain is characterized as 3'-5' exonuclease.
+At position 86 to 275, the domain is characterized as Helicase ATP-binding.
+At position 587 to 743, the domain is characterized as Toprim.
+At position 24 to 84, the domain is characterized as SLH.
+At position 101 to 237, the domain is characterized as Fatty acid hydroxylase.
+At position 222 to 288, the domain is characterized as J.
+At position 7 to 134, the domain is characterized as ADF-H.
+At position 11 to 198, the domain is characterized as PPM-type phosphatase.
+At position 69 to 217, the domain is characterized as C2 NT-type.
+At position 120 to 204, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 303, the domain is characterized as Ig-like C2-type 3.
+At position 310 to 396, the domain is characterized as Ig-like C2-type 4.
+At position 405 to 516, the domain is characterized as Ig-like C2-type 5.
+At position 579 to 677, the domain is characterized as Fibronectin type-III 1.
+At position 723 to 821, the domain is characterized as Fibronectin type-III 2.
+At position 826 to 926, the domain is characterized as Fibronectin type-III 3.
+At position 29 to 204, the domain is characterized as FAD-binding PCMH-type.
+At position 52 to 119, the domain is characterized as Rho RNA-BD.
+At position 31 to 125, the domain is characterized as Fibronectin type-III 1.
+At position 127 to 226, the domain is characterized as Fibronectin type-III 2.
+At position 230 to 327, the domain is characterized as Fibronectin type-III 3.
+At position 332 to 425, the domain is characterized as Fibronectin type-III 4.
+At position 497 to 804, the domain is characterized as UvrD-like helicase C-terminal.
+At position 25 to 60, the domain is characterized as EF-hand.
+At position 2 to 55, the domain is characterized as Kazal-like.
+At position 49 to 112, the domain is characterized as HMA 1.
+At position 153 to 220, the domain is characterized as HMA 2.
+At position 259 to 340, the domain is characterized as Toprim.
+At position 87 to 156, the domain is characterized as Chitin-binding type R&R.
+At position 114 to 249, the domain is characterized as Fatty acid hydroxylase.
+At position 48 to 236, the domain is characterized as Reticulon.
+At position 140 to 276, the domain is characterized as Fatty acid hydroxylase.
+At position 21 to 201, the domain is characterized as Guanylate kinase-like.
+At position 42 to 211, the domain is characterized as Phosphatase tensin-type.
+At position 239 to 396, the domain is characterized as C2 tensin-type.
+At position 6 to 69, the domain is characterized as HMA.
+At position 7 to 174, the domain is characterized as PPIase cyclophilin-type.
+At position 23 to 198, the domain is characterized as Exonuclease.
+At position 60 to 120, the domain is characterized as SH3.
+At position 126 to 223, the domain is characterized as SH2.
+At position 244 to 497, the domain is characterized as Protein kinase.
+At position 456 to 665, the domain is characterized as FtsK.
+At position 194 to 264, the domain is characterized as EB1 C-terminal.
+At position 20 to 55, the domain is characterized as EGF-like 1.
+At position 62 to 175, the domain is characterized as CUB.
+At position 176 to 212, the domain is characterized as EGF-like 2; calcium-binding.
+At position 214 to 250, the domain is characterized as EGF-like 3; calcium-binding.
+At position 252 to 288, the domain is characterized as EGF-like 4; calcium-binding.
+At position 290 to 326, the domain is characterized as EGF-like 5; calcium-binding.
+At position 328 to 364, the domain is characterized as EGF-like 6; calcium-binding.
+At position 366 to 402, the domain is characterized as EGF-like 7; calcium-binding.
+At position 404 to 440, the domain is characterized as EGF-like 8; calcium-binding.
+At position 442 to 478, the domain is characterized as EGF-like 9; calcium-binding.
+At position 480 to 516, the domain is characterized as EGF-like 10; calcium-binding.
+At position 518 to 554, the domain is characterized as EGF-like 11; calcium-binding.
+At position 556 to 592, the domain is characterized as EGF-like 12; calcium-binding.
+At position 594 to 630, the domain is characterized as EGF-like 13; calcium-binding.
+At position 632 to 668, the domain is characterized as EGF-like 14; calcium-binding.
+At position 670 to 706, the domain is characterized as EGF-like 15; calcium-binding.
+At position 708 to 744, the domain is characterized as EGF-like 16; calcium-binding.
+At position 746 to 782, the domain is characterized as EGF-like 17; calcium-binding.
+At position 784 to 820, the domain is characterized as EGF-like 18; calcium-binding.
+At position 822 to 858, the domain is characterized as EGF-like 19; calcium-binding.
+At position 860 to 896, the domain is characterized as EGF-like 20.
+At position 898 to 934, the domain is characterized as EGF-like 21; calcium-binding.
+At position 937 to 1056, the domain is characterized as Avidin-like.
+At position 70 to 367, the domain is characterized as Protein kinase.
+At position 116 to 229, the domain is characterized as C-type lectin.
+At position 592 to 669, the domain is characterized as BRCT.
+At position 1321 to 1410, the domain is characterized as PDZ.
+At position 50 to 153, the domain is characterized as Ig-like C2-type 1.
+At position 255 to 344, the domain is characterized as Ig-like C2-type 2.
+At position 345 to 437, the domain is characterized as Ig-like C2-type 3.
+At position 438 to 538, the domain is characterized as Ig-like C2-type 4.
+At position 539 to 638, the domain is characterized as Ig-like C2-type 5.
+At position 641 to 737, the domain is characterized as Fibronectin type-III 1.
+At position 739 to 834, the domain is characterized as Fibronectin type-III 2.
+At position 838 to 932, the domain is characterized as Ig-like C2-type 6.
+At position 935 to 1030, the domain is characterized as Fibronectin type-III 3.
+At position 1048 to 1141, the domain is characterized as Ig-like C2-type 7.
+At position 13 to 70, the domain is characterized as DEK-C.
+At position 65 to 361, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 41 to 432, the domain is characterized as GH18.
+At position 25 to 114, the domain is characterized as SUEL-type lectin.
+At position 692 to 739, the domain is characterized as GPS.
+At position 112 to 298, the domain is characterized as Tyr recombinase.
+At position 24 to 158, the domain is characterized as MATH.
+At position 194 to 261, the domain is characterized as BTB.
+At position 637 to 757, the domain is characterized as SMC hinge.
+At position 145 to 330, the domain is characterized as CheB-type methylesterase.
+At position 1 to 132, the domain is characterized as MGS-like.
+At position 278 to 510, the domain is characterized as ABC transporter 2.
+At position 277 to 497, the domain is characterized as Fibrinogen C-terminal.
+At position 6 to 63, the domain is characterized as PQ-loop.
+At position 161 to 396, the domain is characterized as ABC transmembrane type-2.
+At position 161 to 196, the domain is characterized as EF-hand 4.
+At position 183 to 253, the domain is characterized as Bromo.
+At position 39 to 102, the domain is characterized as bZIP.
+At position 256 to 290, the domain is characterized as SAP.
+At position 12 to 90, the domain is characterized as GIY-YIG.
+At position 45 to 251, the domain is characterized as AIG1-type G.
+At position 16 to 137, the domain is characterized as Arf-GAP.
+At position 16 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 251 to 473, the domain is characterized as ABC transporter 1.
+At position 477 to 696, the domain is characterized as ABC transporter 2.
+At position 22 to 249, the domain is characterized as Laminin N-terminal.
+At position 250 to 312, the domain is characterized as Laminin EGF-like 1.
+At position 313 to 375, the domain is characterized as Laminin EGF-like 2.
+At position 376 to 427, the domain is characterized as Laminin EGF-like 3.
+At position 478 to 530, the domain is characterized as Laminin EGF-like 5.
+At position 531 to 577, the domain is characterized as Laminin EGF-like 6.
+At position 54 to 165, the domain is characterized as PpiC.
+At position 861 to 1038, the domain is characterized as Helicase ATP-binding.
+At position 1095 to 1244, the domain is characterized as Helicase C-terminal.
+At position 329 to 417, the domain is characterized as Ig-like C2-type 1.
+At position 469 to 557, the domain is characterized as Ig-like C2-type 2.
+At position 565 to 657, the domain is characterized as Fibronectin type-III.
+At position 696 to 951, the domain is characterized as Protein kinase.
+At position 1041 to 1130, the domain is characterized as Ig-like C2-type 3.
+At position 90 to 348, the domain is characterized as Protein kinase.
+At position 427 to 462, the domain is characterized as EF-hand 2.
+At position 463 to 497, the domain is characterized as EF-hand 3.
+At position 498 to 533, the domain is characterized as EF-hand 4.
+At position 35 to 317, the domain is characterized as ABC transmembrane type-1.
+At position 350 to 586, the domain is characterized as ABC transporter.
+At position 99 to 206, the domain is characterized as PET.
+At position 239 to 304, the domain is characterized as LIM zinc-binding 1.
+At position 305 to 363, the domain is characterized as LIM zinc-binding 2.
+At position 19 to 61, the domain is characterized as MADS-box.
+At position 6 to 239, the domain is characterized as PABS.
+At position 97 to 144, the domain is characterized as WAP.
+At position 600 to 674, the domain is characterized as RRM.
+At position 28 to 309, the domain is characterized as Brix.
+At position 244 to 307, the domain is characterized as bZIP.
+At position 7 to 129, the domain is characterized as Longin.
+At position 142 to 202, the domain is characterized as v-SNARE coiled-coil homology.
+At position 234 to 527, the domain is characterized as CN hydrolase.
+At position 195 to 494, the domain is characterized as GH10.
+At position 108 to 307, the domain is characterized as MAGE.
+At position 249 to 312, the domain is characterized as bZIP.
+At position 7 to 173, the domain is characterized as 3'-5' exonuclease.
+At position 212 to 293, the domain is characterized as HRDC.
+At position 32 to 301, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 20 to 106, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 265 to 450, the domain is characterized as FAD-binding PCMH-type.
+At position 138 to 200, the domain is characterized as HMA.
+At position 55 to 160, the domain is characterized as sHSP.
+At position 30 to 62, the domain is characterized as LRRNT.
+At position 305 to 356, the domain is characterized as LRRCT.
+At position 409 to 503, the domain is characterized as Fibronectin type-III.
+At position 7 to 187, the domain is characterized as Guanylate kinase-like.
+At position 666 to 840, the domain is characterized as MOSC.
+At position 177 to 408, the domain is characterized as Radical SAM core.
+At position 410 to 482, the domain is characterized as TRAM.
+At position 393 to 548, the domain is characterized as Helicase C-terminal.
+At position 737 to 814, the domain is characterized as ACT 1.
+At position 849 to 926, the domain is characterized as ACT 2.
+At position 220 to 387, the domain is characterized as TrmE-type G.
+At position 54 to 235, the domain is characterized as PCI.
+At position 678 to 1049, the domain is characterized as Protein kinase.
+At position 29 to 72, the domain is characterized as LysM.
+At position 9 to 139, the domain is characterized as ENTH.
+At position 858 to 1100, the domain is characterized as I/LWEQ.
+At position 15 to 315, the domain is characterized as Radical SAM core.
+At position 46 to 75, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 80 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 31 to 287, the domain is characterized as Protein kinase.
+At position 45 to 490, the domain is characterized as Biotin carboxylation.
+At position 163 to 360, the domain is characterized as ATP-grasp.
+At position 622 to 711, the domain is characterized as Biotinyl-binding.
+At position 43 to 97, the domain is characterized as PAS.
+At position 113 to 165, the domain is characterized as PAC.
+At position 24 to 75, the domain is characterized as HTH myb-type 1.
+At position 76 to 131, the domain is characterized as HTH myb-type 2.
+At position 132 to 182, the domain is characterized as HTH myb-type 3.
+At position 55 to 183, the domain is characterized as Runt.
+At position 21 to 118, the domain is characterized as Ig-like V-type.
+At position 122 to 203, the domain is characterized as Ig-like C2-type.
+At position 60 to 204, the domain is characterized as Flavodoxin-like.
+At position 264 to 509, the domain is characterized as FAD-binding FR-type.
+At position 32 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 61 to 91, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 396 to 543, the domain is characterized as Plastocyanin-like 3.
+At position 45 to 101, the domain is characterized as Collagen-like.
+At position 102 to 319, the domain is characterized as Fibrinogen C-terminal.
+At position 175 to 260, the domain is characterized as PPIase FKBP-type.
+At position 28 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 220, the domain is characterized as tr-type G.
+At position 60 to 153, the domain is characterized as Rhodanese.
+At position 175 to 274, the domain is characterized as SWIRM.
+At position 34 to 197, the domain is characterized as Cohesin 1.
+At position 205 to 367, the domain is characterized as Cohesin 2.
+At position 407 to 569, the domain is characterized as Cohesin 3.
+At position 609 to 771, the domain is characterized as Cohesin 4.
+At position 811 to 973, the domain is characterized as Cohesin 5.
+At position 1013 to 1175, the domain is characterized as Cohesin 6.
+At position 1211 to 1375, the domain is characterized as Cohesin 7.
+At position 2067 to 2140, the domain is characterized as SLH 1.
+At position 2141 to 2204, the domain is characterized as SLH 2.
+At position 2211 to 2274, the domain is characterized as SLH 3.
+At position 140 to 426, the domain is characterized as ABC transmembrane type-1.
+At position 460 to 695, the domain is characterized as ABC transporter.
+At position 349 to 404, the domain is characterized as Tudor.
+At position 14 to 238, the domain is characterized as YjeF N-terminal.
+At position 4 to 118, the domain is characterized as C2.
+At position 115 to 614, the domain is characterized as Peptidase S8.
+At position 144 to 394, the domain is characterized as ABC transporter 1.
+At position 845 to 1087, the domain is characterized as ABC transporter 2.
+At position 396 to 483, the domain is characterized as Fibronectin type-III.
+At position 8 to 81, the domain is characterized as Core-binding (CB).
+At position 93 to 253, the domain is characterized as Tyr recombinase.
+At position 148 to 256, the domain is characterized as Fibronectin type-III.
+At position 487 to 523, the domain is characterized as ATP-grasp.
+At position 726 to 881, the domain is characterized as N-acetyltransferase.
+At position 23 to 250, the domain is characterized as ATP-grasp.
+At position 45 to 127, the domain is characterized as Fibronectin type-III 1.
+At position 331 to 428, the domain is characterized as Fibronectin type-III 2.
+At position 431 to 530, the domain is characterized as Fibronectin type-III 3.
+At position 534 to 625, the domain is characterized as Fibronectin type-III 4.
+At position 623 to 715, the domain is characterized as Fibronectin type-III 5.
+At position 720 to 829, the domain is characterized as Fibronectin type-III 6.
+At position 116 to 152, the domain is characterized as Orange.
+At position 11 to 79, the domain is characterized as J.
+At position 504 to 601, the domain is characterized as Ig-like C2-type 6.
+At position 606 to 704, the domain is characterized as Fibronectin type-III 1.
+At position 709 to 806, the domain is characterized as Fibronectin type-III 2.
+At position 811 to 906, the domain is characterized as Fibronectin type-III 3.
+At position 907 to 1000, the domain is characterized as Fibronectin type-III 4.
+At position 31 to 167, the domain is characterized as Ephrin RBD.
+At position 45 to 307, the domain is characterized as ZP.
+At position 81 to 371, the domain is characterized as Radical SAM core.
+At position 395 to 546, the domain is characterized as N-acetyltransferase.
+At position 135 to 648, the domain is characterized as Protein kinase.
+At position 366 to 587, the domain is characterized as Histidine kinase.
+At position 28 to 165, the domain is characterized as ENTH.
+At position 364 to 670, the domain is characterized as Protein kinase.
+At position 791 to 877, the domain is characterized as SUEL-type lectin.
+At position 228 to 376, the domain is characterized as Exonuclease.
+At position 505 to 579, the domain is characterized as RRM 1.
+At position 600 to 679, the domain is characterized as RRM 2.
+At position 55 to 317, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 211 to 249, the domain is characterized as LRRCT.
+At position 558 to 587, the domain is characterized as IQ.
+At position 138 to 229, the domain is characterized as HTH La-type RNA-binding.
+At position 236 to 324, the domain is characterized as RRM.
+At position 145 to 685, the domain is characterized as USP.
+At position 789 to 892, the domain is characterized as DUSP 2.
+At position 185 to 288, the domain is characterized as PpiC 1.
+At position 301 to 399, the domain is characterized as PpiC 2.
+At position 152 to 297, the domain is characterized as TRUD.
+At position 1143 to 1246, the domain is characterized as PH.
+At position 298 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 82 to 127, the domain is characterized as CUE 1.
+At position 175 to 218, the domain is characterized as CUE 2.
+At position 460 to 628, the domain is characterized as Helicase ATP-binding.
+At position 805 to 966, the domain is characterized as Helicase C-terminal.
+At position 121 to 293, the domain is characterized as Helicase ATP-binding.
+At position 360 to 515, the domain is characterized as Helicase C-terminal.
+At position 135 to 249, the domain is characterized as LRAT.
+At position 108 to 137, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 215, the domain is characterized as DegV.
+At position 8 to 107, the domain is characterized as SSB.
+At position 37 to 167, the domain is characterized as Nudix hydrolase.
+At position 23 to 94, the domain is characterized as KRAB.
+At position 39 to 384, the domain is characterized as GH18.
+At position 133 to 376, the domain is characterized as Radical SAM core.
+At position 49 to 195, the domain is characterized as DAGKc.
+At position 1 to 19, the domain is characterized as Peptidase M12B.
+At position 27 to 108, the domain is characterized as Disintegrin.
+At position 2 to 259, the domain is characterized as ABC transporter.
+At position 23 to 265, the domain is characterized as ABC transporter.
+At position 340 to 552, the domain is characterized as ABC transmembrane type-2.
+At position 543 to 607, the domain is characterized as SAM.
+At position 60 to 135, the domain is characterized as ACT.
+At position 249 to 299, the domain is characterized as DHHC.
+At position 19 to 168, the domain is characterized as Tyrosine-protein phosphatase.
+At position 958 to 1124, the domain is characterized as PNPLA.
+At position 306 to 372, the domain is characterized as SH3.
+At position 349 to 446, the domain is characterized as BEN.
+At position 112 to 273, the domain is characterized as CP-type G.
+At position 11 to 239, the domain is characterized as Sigma-54 factor interaction.
+At position 7 to 378, the domain is characterized as Trm1 methyltransferase.
+At position 206 to 446, the domain is characterized as FAD-binding FR-type.
+At position 71 to 236, the domain is characterized as Laminin G-like.
+At position 625 to 679, the domain is characterized as Collagen-like 1.
+At position 688 to 747, the domain is characterized as Collagen-like 2.
+At position 748 to 807, the domain is characterized as Collagen-like 3.
+At position 808 to 867, the domain is characterized as Collagen-like 4.
+At position 871 to 930, the domain is characterized as Collagen-like 5.
+At position 931 to 990, the domain is characterized as Collagen-like 6.
+At position 1003 to 1062, the domain is characterized as Collagen-like 7.
+At position 1066 to 1125, the domain is characterized as Collagen-like 8.
+At position 1126 to 1185, the domain is characterized as Collagen-like 9.
+At position 1192 to 1251, the domain is characterized as Collagen-like 10.
+At position 1258 to 1317, the domain is characterized as Collagen-like 11.
+At position 1318 to 1378, the domain is characterized as Collagen-like 12.
+At position 1382 to 1441, the domain is characterized as Collagen-like 13.
+At position 1442 to 1501, the domain is characterized as Collagen-like 14.
+At position 1502 to 1561, the domain is characterized as Collagen-like 15.
+At position 1562 to 1621, the domain is characterized as Collagen-like 16.
+At position 1660 to 1860, the domain is characterized as Fibrillar collagen NC1.
+At position 107 to 209, the domain is characterized as C-type lectin.
+At position 46 to 81, the domain is characterized as EF-hand 1.
+At position 154 to 248, the domain is characterized as PX; atypical.
+At position 262 to 324, the domain is characterized as SH3.
+At position 375 to 570, the domain is characterized as Rho-GAP.
+At position 101 to 168, the domain is characterized as BTB.
+At position 203 to 305, the domain is characterized as BACK.
+At position 1 to 60, the domain is characterized as AFP-like.
+At position 74 to 387, the domain is characterized as Peptidase A1.
+At position 27 to 98, the domain is characterized as IGFBP N-terminal.
+At position 101 to 167, the domain is characterized as VWFC.
+At position 198 to 243, the domain is characterized as TSP type-1.
+At position 256 to 330, the domain is characterized as CTCK.
+At position 121 to 186, the domain is characterized as Sushi 2.
+At position 213 to 271, the domain is characterized as Chromo.
+At position 407 to 472, the domain is characterized as Pre-SET.
+At position 475 to 601, the domain is characterized as SET.
+At position 617 to 633, the domain is characterized as Post-SET.
+At position 41 to 98, the domain is characterized as Ig-like C2-type 1.
+At position 127 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 22 to 228, the domain is characterized as PNPLA.
+At position 173 to 265, the domain is characterized as DOD-type homing endonuclease.
+At position 451 to 668, the domain is characterized as tr-type G.
+At position 112 to 327, the domain is characterized as START.
+At position 355 to 412, the domain is characterized as S4 RNA-binding.
+At position 7 to 27, the domain is characterized as EF-hand.
+At position 1 to 147, the domain is characterized as RNase H type-1.
+At position 75 to 181, the domain is characterized as C-type lectin.
+At position 42 to 94, the domain is characterized as bHLH.
+At position 464 to 598, the domain is characterized as N-acetyltransferase.
+At position 176 to 260, the domain is characterized as PDZ.
+At position 137 to 411, the domain is characterized as ABC transporter 1.
+At position 489 to 701, the domain is characterized as ABC transmembrane type-2 1.
+At position 798 to 1043, the domain is characterized as ABC transporter 2.
+At position 1115 to 1329, the domain is characterized as ABC transmembrane type-2 2.
+At position 24 to 92, the domain is characterized as LCN-type CS-alpha/beta.
+At position 45 to 363, the domain is characterized as USP.
+At position 672 to 863, the domain is characterized as ATP-grasp 2.
+At position 38 to 156, the domain is characterized as C-type lectin.
+At position 82 to 124, the domain is characterized as JmjN.
+At position 475 to 645, the domain is characterized as JmjC.
+At position 978 to 1329, the domain is characterized as Protein kinase.
+At position 26 to 52, the domain is characterized as LRRNT.
+At position 646 to 699, the domain is characterized as LRRCT.
+At position 755 to 898, the domain is characterized as TIR.
+At position 430 to 537, the domain is characterized as DM10 3.
+At position 25 to 98, the domain is characterized as PAS.
+At position 99 to 153, the domain is characterized as PAC.
+At position 109 to 299, the domain is characterized as Tyr recombinase.
+At position 1 to 332, the domain is characterized as MACPF.
+At position 3 to 122, the domain is characterized as PINc.
+At position 359 to 442, the domain is characterized as KH-like.
+At position 32 to 158, the domain is characterized as MARVEL.
+At position 258 to 482, the domain is characterized as tr-type G.
+At position 55 to 131, the domain is characterized as Carrier.
+At position 6 to 67, the domain is characterized as HTH asnC-type.
+At position 64 to 228, the domain is characterized as Laminin G-like.
+At position 272 to 331, the domain is characterized as VWFC 1.
+At position 397 to 439, the domain is characterized as EGF-like 1.
+At position 440 to 481, the domain is characterized as EGF-like 2; calcium-binding.
+At position 482 to 522, the domain is characterized as EGF-like 3; calcium-binding.
+At position 523 to 553, the domain is characterized as EGF-like 4.
+At position 555 to 601, the domain is characterized as EGF-like 5; calcium-binding.
+At position 602 to 637, the domain is characterized as EGF-like 6; calcium-binding.
+At position 638 to 693, the domain is characterized as VWFC 2.
+At position 698 to 756, the domain is characterized as VWFC 3.
+At position 3 to 230, the domain is characterized as Glutamine amidotransferase type-1.
+At position 89 to 373, the domain is characterized as Protein kinase.
+At position 273 to 370, the domain is characterized as RAMA.
+At position 29 to 327, the domain is characterized as ABC transmembrane type-1.
+At position 359 to 596, the domain is characterized as ABC transporter.
+At position 130 to 208, the domain is characterized as RRM 1.
+At position 227 to 305, the domain is characterized as RRM 2.
+At position 537 to 627, the domain is characterized as RRM 3; atypical.
+At position 3 to 258, the domain is characterized as ABC transporter.
+At position 32 to 121, the domain is characterized as Fibronectin type-III 1.
+At position 224 to 336, the domain is characterized as Fibronectin type-III 2.
+At position 69 to 119, the domain is characterized as bHLH.
+At position 152 to 472, the domain is characterized as Peptidase S8.
+At position 480 to 617, the domain is characterized as P/Homo B.
+At position 84 to 202, the domain is characterized as GST C-terminal.
+At position 342 to 437, the domain is characterized as Fibronectin type-III 1.
+At position 438 to 531, the domain is characterized as Fibronectin type-III 2.
+At position 513 to 711, the domain is characterized as B30.2/SPRY.
+At position 239 to 422, the domain is characterized as Velvet.
+At position 15 to 143, the domain is characterized as VHS.
+At position 258 to 277, the domain is characterized as UIM.
+At position 20 to 235, the domain is characterized as ABC transporter.
+At position 275 to 331, the domain is characterized as CBS 2.
+At position 355 to 416, the domain is characterized as CBS 3.
+At position 79 to 114, the domain is characterized as EF-hand 1.
+At position 166 to 201, the domain is characterized as EF-hand 3.
+At position 203 to 238, the domain is characterized as EF-hand 4.
+At position 244 to 279, the domain is characterized as EF-hand 5.
+At position 280 to 315, the domain is characterized as EF-hand 6.
+At position 212 to 302, the domain is characterized as Ig-like C2-type 3.
+At position 309 to 414, the domain is characterized as Ig-like C2-type 4.
+At position 417 to 502, the domain is characterized as Ig-like C2-type 5.
+At position 510 to 609, the domain is characterized as Fibronectin type-III 1.
+At position 611 to 706, the domain is characterized as Fibronectin type-III 2.
+At position 117 to 201, the domain is characterized as Ig-like C2-type 2.
+At position 202 to 306, the domain is characterized as Ig-like C2-type 3.
+At position 319 to 410, the domain is characterized as Ig-like C2-type 4.
+At position 414 to 517, the domain is characterized as Ig-like C2-type 5.
+At position 593 to 954, the domain is characterized as Protein kinase.
+At position 88 to 214, the domain is characterized as GST C-terminal.
+At position 394 to 563, the domain is characterized as tr-type G.
+At position 39 to 175, the domain is characterized as GH18.
+At position 220 to 412, the domain is characterized as Helicase ATP-binding.
+At position 5 to 214, the domain is characterized as Radical SAM core.
+At position 212 to 313, the domain is characterized as Fe2OG dioxygenase.
+At position 651 to 739, the domain is characterized as BRCT 1.
+At position 807 to 909, the domain is characterized as BRCT 2.
+At position 114 to 309, the domain is characterized as ATP-grasp.
+At position 29 to 116, the domain is characterized as Ig-like C2-type 1.
+At position 127 to 208, the domain is characterized as Ig-like C2-type 2.
+At position 215 to 308, the domain is characterized as Fibronectin type-III 1.
+At position 310 to 403, the domain is characterized as Fibronectin type-III 2.
+At position 505 to 776, the domain is characterized as Protein kinase.
+At position 107 to 229, the domain is characterized as MsrB.
+At position 20 to 73, the domain is characterized as TIL 1.
+At position 80 to 133, the domain is characterized as TIL 2.
+At position 49 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 357 to 534, the domain is characterized as N-acetyltransferase.
+At position 23 to 62, the domain is characterized as CBM1 1.
+At position 63 to 105, the domain is characterized as CBM1 2.
+At position 125 to 165, the domain is characterized as CBM1 3.
+At position 166 to 210, the domain is characterized as CBM1 4.
+At position 150 to 349, the domain is characterized as Peptidase M12A.
+At position 344 to 384, the domain is characterized as EGF-like.
+At position 394 to 510, the domain is characterized as CUB.
+At position 513 to 562, the domain is characterized as TSP type-1.
+At position 527 to 635, the domain is characterized as SMC hinge.
+At position 39 to 348, the domain is characterized as Rab-GAP TBC.
+At position 335 to 434, the domain is characterized as BRCT.
+At position 108 to 170, the domain is characterized as S4 RNA-binding.
+At position 185 to 269, the domain is characterized as Expansin-like CBD.
+At position 479 to 679, the domain is characterized as FtsK.
+At position 1 to 97, the domain is characterized as Plastocyanin-like.
+At position 83 to 487, the domain is characterized as Peptidase A1.
+At position 63 to 211, the domain is characterized as Thioredoxin.
+At position 135 to 255, the domain is characterized as C2 1.
+At position 266 to 399, the domain is characterized as C2 2.
+At position 35 to 199, the domain is characterized as Helicase ATP-binding.
+At position 219 to 398, the domain is characterized as Helicase C-terminal.
+At position 674 to 755, the domain is characterized as ACT 1.
+At position 783 to 850, the domain is characterized as ACT 2.
+At position 53 to 488, the domain is characterized as Sema.
+At position 542 to 627, the domain is characterized as Ig-like C2-type.
+At position 34 to 150, the domain is characterized as C-type lectin.
+At position 406 to 782, the domain is characterized as FH2.
+At position 22 to 106, the domain is characterized as GS beta-grasp.
+At position 114 to 481, the domain is characterized as GS catalytic.
+At position 186 to 369, the domain is characterized as PID.
+At position 522 to 613, the domain is characterized as SH2.
+At position 1807 to 1873, the domain is characterized as KH.
+At position 209 to 280, the domain is characterized as PAS.
+At position 283 to 325, the domain is characterized as PAC.
+At position 475 to 814, the domain is characterized as PDEase.
+At position 29 to 111, the domain is characterized as Lipoyl-binding.
+At position 148 to 193, the domain is characterized as LRRCT.
+At position 194 to 283, the domain is characterized as Ig-like C2-type 1.
+At position 299 to 365, the domain is characterized as Ig-like C2-type 2.
+At position 510 to 781, the domain is characterized as Protein kinase.
+At position 25 to 128, the domain is characterized as Thioredoxin.
+At position 1 to 180, the domain is characterized as Josephin.
+At position 224 to 243, the domain is characterized as UIM 1.
+At position 244 to 263, the domain is characterized as UIM 2.
+At position 331 to 349, the domain is characterized as UIM 3.
+At position 8 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 35 to 116, the domain is characterized as Phosphagen kinase N-terminal 1.
+At position 146 to 382, the domain is characterized as Phosphagen kinase C-terminal 1.
+At position 398 to 479, the domain is characterized as Phosphagen kinase N-terminal 2.
+At position 509 to 746, the domain is characterized as Phosphagen kinase C-terminal 2.
+At position 1 to 141, the domain is characterized as Histidine kinase; second part.
+At position 138 to 367, the domain is characterized as tr-type G.
+At position 324 to 605, the domain is characterized as ABC transmembrane type-1 1.
+At position 639 to 862, the domain is characterized as ABC transporter 1.
+At position 980 to 1260, the domain is characterized as ABC transmembrane type-1 2.
+At position 1297 to 1531, the domain is characterized as ABC transporter 2.
+At position 12 to 691, the domain is characterized as Myosin motor.
+At position 694 to 716, the domain is characterized as IQ 1.
+At position 717 to 746, the domain is characterized as IQ 2.
+At position 773 to 955, the domain is characterized as TH1.
+At position 581 to 684, the domain is characterized as tRNA-binding.
+At position 30 to 107, the domain is characterized as RRM.
+At position 157 to 289, the domain is characterized as GGDEF.
+At position 15 to 184, the domain is characterized as FAD-binding PCMH-type.
+At position 146 to 1017, the domain is characterized as Myosin motor.
+At position 1043 to 1072, the domain is characterized as IQ 2.
+At position 1075 to 1104, the domain is characterized as IQ 3.
+At position 1116 to 1145, the domain is characterized as IQ 4.
+At position 1139 to 1168, the domain is characterized as IQ 5.
+At position 2065 to 2253, the domain is characterized as Rho-GAP.
+At position 509 to 558, the domain is characterized as bHLH.
+At position 11 to 175, the domain is characterized as NAC.
+At position 254 to 344, the domain is characterized as Ig-like.
+At position 31 to 91, the domain is characterized as HTH myb-type.
+At position 40 to 313, the domain is characterized as Dynamin-type G.
+At position 534 to 624, the domain is characterized as GED.
+At position 191 to 370, the domain is characterized as SMP-LTD.
+At position 369 to 489, the domain is characterized as C2 1.
+At position 514 to 639, the domain is characterized as C2 2.
+At position 786 to 908, the domain is characterized as C2 3.
+At position 310 to 344, the domain is characterized as STI1 1.
+At position 386 to 425, the domain is characterized as STI1 2.
+At position 159 to 248, the domain is characterized as 5'-3' exonuclease.
+At position 3 to 97, the domain is characterized as HTH arsR-type.
+At position 298 to 340, the domain is characterized as UBA.
+At position 45 to 160, the domain is characterized as Expansin-like EG45.
+At position 170 to 249, the domain is characterized as Expansin-like CBD.
+At position 539 to 614, the domain is characterized as Cytochrome b5 heme-binding.
+At position 654 to 766, the domain is characterized as FAD-binding FR-type.
+At position 78 to 289, the domain is characterized as PPM-type phosphatase.
+At position 62 to 319, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 32 to 121, the domain is characterized as CARD.
+At position 20 to 158, the domain is characterized as Thioredoxin.
+At position 1 to 235, the domain is characterized as Alpha-carbonic anhydrase.
+At position 225 to 320, the domain is characterized as SH2.
+At position 51 to 280, the domain is characterized as Radical SAM core.
+At position 16 to 178, the domain is characterized as NIDO.
+At position 295 to 324, the domain is characterized as EGF-like.
+At position 435 to 616, the domain is characterized as Thioredoxin.
+At position 36 to 134, the domain is characterized as Cadherin 1.
+At position 139 to 243, the domain is characterized as Cadherin 2.
+At position 248 to 348, the domain is characterized as Cadherin 3.
+At position 353 to 451, the domain is characterized as Cadherin 4.
+At position 29 to 100, the domain is characterized as KRAB.
+At position 132 to 329, the domain is characterized as ATP-grasp.
+At position 170 to 345, the domain is characterized as Helicase ATP-binding.
+At position 500 to 653, the domain is characterized as Helicase C-terminal.
+At position 156 to 348, the domain is characterized as CheB-type methylesterase.
+At position 136 to 338, the domain is characterized as Peptidase M12A.
+At position 340 to 477, the domain is characterized as CUB 1.
+At position 478 to 591, the domain is characterized as CUB 2.
+At position 591 to 631, the domain is characterized as EGF-like 1; calcium-binding.
+At position 634 to 753, the domain is characterized as CUB 3.
+At position 753 to 793, the domain is characterized as EGF-like 2; calcium-binding.
+At position 797 to 909, the domain is characterized as CUB 4.
+At position 910 to 1026, the domain is characterized as CUB 5.
+At position 424 to 591, the domain is characterized as tr-type G.
+At position 1 to 81, the domain is characterized as Helicase ATP-binding.
+At position 106 to 286, the domain is characterized as Helicase C-terminal.
+At position 48 to 152, the domain is characterized as PA.
+At position 247 to 305, the domain is characterized as LIM zinc-binding 1.
+At position 306 to 365, the domain is characterized as LIM zinc-binding 2.
+At position 366 to 424, the domain is characterized as LIM zinc-binding 3.
+At position 1332 to 1470, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1604 to 1746, the domain is characterized as RNase H Ty1/copia-type.
+At position 1 to 213, the domain is characterized as RNase H type-2.
+At position 177 to 507, the domain is characterized as Kinesin motor.
+At position 22 to 129, the domain is characterized as Cadherin 1.
+At position 130 to 238, the domain is characterized as Cadherin 2.
+At position 239 to 346, the domain is characterized as Cadherin 3.
+At position 350 to 453, the domain is characterized as Cadherin 4.
+At position 297 to 334, the domain is characterized as EGF-like 1.
+At position 335 to 380, the domain is characterized as EGF-like 2; calcium-binding.
+At position 527 to 805, the domain is characterized as Protein kinase.
+At position 340 to 396, the domain is characterized as S4 RNA-binding.
+At position 24 to 90, the domain is characterized as Chitin-binding type R&R.
+At position 110 to 190, the domain is characterized as S1 motif.
+At position 1 to 153, the domain is characterized as Thioredoxin.
+At position 430 to 706, the domain is characterized as Protein kinase.
+At position 11 to 261, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 270 to 503, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 7 to 74, the domain is characterized as BTB.
+At position 4 to 373, the domain is characterized as Trm1 methyltransferase.
+At position 28 to 239, the domain is characterized as BURP.
+At position 312 to 487, the domain is characterized as Helicase ATP-binding.
+At position 519 to 664, the domain is characterized as Helicase C-terminal.
+At position 46 to 341, the domain is characterized as ABC transmembrane type-1 1.
+At position 376 to 612, the domain is characterized as ABC transporter 1.
+At position 708 to 995, the domain is characterized as ABC transmembrane type-1 2.
+At position 1029 to 1265, the domain is characterized as ABC transporter 2.
+At position 26 to 60, the domain is characterized as Chitin-binding type-1.
+At position 314 to 391, the domain is characterized as RRM 1.
+At position 395 to 469, the domain is characterized as RRM 2.
+At position 624 to 791, the domain is characterized as SPOC.
+At position 105 to 208, the domain is characterized as PH.
+At position 268 to 329, the domain is characterized as SH3.
+At position 4 to 71, the domain is characterized as PAS.
+At position 136 to 352, the domain is characterized as Histidine kinase.
+At position 121 to 340, the domain is characterized as Radical SAM core.
+At position 1 to 72, the domain is characterized as RRM 1.
+At position 110 to 183, the domain is characterized as RRM 2.
+At position 83 to 211, the domain is characterized as GST C-terminal.
+At position 375 to 463, the domain is characterized as PI3K-RBD.
+At position 635 to 786, the domain is characterized as C2 PI3K-type.
+At position 805 to 981, the domain is characterized as PIK helical.
+At position 1050 to 1328, the domain is characterized as PI3K/PI4K catalytic.
+At position 1365 to 1481, the domain is characterized as PX.
+At position 1504 to 1624, the domain is characterized as C2.
+At position 20 to 131, the domain is characterized as PH.
+At position 2 to 228, the domain is characterized as Glutamine amidotransferase type-1.
+At position 50 to 241, the domain is characterized as Brix.
+At position 1 to 191, the domain is characterized as ATP-grasp.
+At position 3 to 82, the domain is characterized as GS beta-grasp.
+At position 87 to 352, the domain is characterized as GS catalytic.
+At position 43 to 340, the domain is characterized as Dynamin-type G.
+At position 138 to 184, the domain is characterized as F-box.
+At position 442 to 705, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 702 to 760, the domain is characterized as SH3.
+At position 223 to 383, the domain is characterized as TrmE-type G.
+At position 8 to 54, the domain is characterized as F-box.
+At position 65 to 170, the domain is characterized as PH.
+At position 195 to 299, the domain is characterized as IRS-type PTB.
+At position 32 to 126, the domain is characterized as Cystatin.
+At position 418 to 429, the domain is characterized as EGF-like.
+At position 572 to 660, the domain is characterized as GED.
+At position 542 to 571, the domain is characterized as IQ 1.
+At position 601 to 630, the domain is characterized as IQ 2.
+At position 147 to 369, the domain is characterized as SMP-LTD.
+At position 499 to 622, the domain is characterized as HD.
+At position 740 to 822, the domain is characterized as ACT 1.
+At position 851 to 931, the domain is characterized as ACT 2.
+At position 202 to 280, the domain is characterized as HSA.
+At position 354 to 418, the domain is characterized as Myb-like.
+At position 551 to 628, the domain is characterized as PABC.
+At position 180 to 442, the domain is characterized as NPH3.
+At position 634 to 716, the domain is characterized as NET.
+At position 45 to 98, the domain is characterized as bHLH.
+At position 135 to 205, the domain is characterized as PAS 1.
+At position 294 to 360, the domain is characterized as PAS 2.
+At position 366 to 409, the domain is characterized as PAC.
+At position 6 to 61, the domain is characterized as bHLH.
+At position 67 to 123, the domain is characterized as EF-hand 1; degenerate.
+At position 162 to 197, the domain is characterized as EF-hand 3.
+At position 210 to 245, the domain is characterized as EF-hand 4.
+At position 421 to 709, the domain is characterized as Protein kinase.
+At position 7 to 66, the domain is characterized as SpoVT-AbrB 1.
+At position 95 to 138, the domain is characterized as SpoVT-AbrB 2.
+At position 81 to 177, the domain is characterized as Toprim.
+At position 19 to 140, the domain is characterized as Calponin-homology (CH).
+At position 363 to 685, the domain is characterized as Kinesin motor.
+At position 415 to 481, the domain is characterized as KH.
+At position 541 to 634, the domain is characterized as HD.
+At position 296 to 362, the domain is characterized as ACT.
+At position 530 to 673, the domain is characterized as ZU5.
+At position 1 to 218, the domain is characterized as Peptidase S1.
+At position 144 to 180, the domain is characterized as DMA.
+At position 56 to 91, the domain is characterized as EF-hand 1.
+At position 92 to 122, the domain is characterized as EF-hand 2.
+At position 123 to 158, the domain is characterized as EF-hand 3.
+At position 159 to 194, the domain is characterized as EF-hand 4.
+At position 603 to 685, the domain is characterized as BRCT.
+At position 20 to 57, the domain is characterized as EGF-like 1.
+At position 58 to 99, the domain is characterized as EGF-like 2.
+At position 102 to 140, the domain is characterized as EGF-like 3.
+At position 141 to 177, the domain is characterized as EGF-like 4.
+At position 179 to 215, the domain is characterized as EGF-like 5; calcium-binding.
+At position 217 to 254, the domain is characterized as EGF-like 6.
+At position 256 to 292, the domain is characterized as EGF-like 7; calcium-binding.
+At position 294 to 332, the domain is characterized as EGF-like 8; calcium-binding.
+At position 334 to 370, the domain is characterized as EGF-like 9; calcium-binding.
+At position 371 to 409, the domain is characterized as EGF-like 10.
+At position 411 to 449, the domain is characterized as EGF-like 11; calcium-binding.
+At position 451 to 487, the domain is characterized as EGF-like 12; calcium-binding.
+At position 489 to 525, the domain is characterized as EGF-like 13; calcium-binding.
+At position 527 to 563, the domain is characterized as EGF-like 14; calcium-binding.
+At position 565 to 600, the domain is characterized as EGF-like 15; calcium-binding.
+At position 602 to 638, the domain is characterized as EGF-like 16; calcium-binding.
+At position 640 to 675, the domain is characterized as EGF-like 17.
+At position 677 to 713, the domain is characterized as EGF-like 18; calcium-binding.
+At position 715 to 750, the domain is characterized as EGF-like 19; calcium-binding.
+At position 752 to 788, the domain is characterized as EGF-like 20; calcium-binding.
+At position 790 to 826, the domain is characterized as EGF-like 21; calcium-binding.
+At position 828 to 866, the domain is characterized as EGF-like 22.
+At position 868 to 904, the domain is characterized as EGF-like 23; calcium-binding.
+At position 906 to 942, the domain is characterized as EGF-like 24; calcium-binding.
+At position 944 to 980, the domain is characterized as EGF-like 25; calcium-binding.
+At position 982 to 1018, the domain is characterized as EGF-like 26.
+At position 1020 to 1056, the domain is characterized as EGF-like 27; calcium-binding.
+At position 1058 to 1094, the domain is characterized as EGF-like 28.
+At position 1096 to 1142, the domain is characterized as EGF-like 29.
+At position 1144 to 1180, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1182 to 1218, the domain is characterized as EGF-like 31; calcium-binding.
+At position 1220 to 1264, the domain is characterized as EGF-like 32; calcium-binding.
+At position 1266 to 1304, the domain is characterized as EGF-like 33.
+At position 1306 to 1346, the domain is characterized as EGF-like 34.
+At position 1347 to 1383, the domain is characterized as EGF-like 35.
+At position 1386 to 1424, the domain is characterized as EGF-like 36.
+At position 291 to 326, the domain is characterized as EF-hand 2.
+At position 159 to 223, the domain is characterized as bHLH.
+At position 400 to 569, the domain is characterized as tr-type G.
+At position 379 to 795, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1277 to 1584, the domain is characterized as PKS/mFAS DH.
+At position 1626 to 1700, the domain is characterized as Carrier.
+At position 6 to 123, the domain is characterized as WH1.
+At position 233 to 285, the domain is characterized as KBD.
+At position 334 to 442, the domain is characterized as SPR.
+At position 189 to 274, the domain is characterized as RCK C-terminal 1.
+At position 275 to 359, the domain is characterized as RCK C-terminal 2.
+At position 63 to 205, the domain is characterized as DAC.
+At position 607 to 690, the domain is characterized as BRCT.
+At position 20 to 104, the domain is characterized as Rhodanese.
+At position 47 to 112, the domain is characterized as Disintegrin.
+At position 265 to 427, the domain is characterized as PCI.
+At position 1311 to 1400, the domain is characterized as PDZ.
+At position 155 to 333, the domain is characterized as SMP-LTD.
+At position 331 to 452, the domain is characterized as C2 1.
+At position 468 to 618, the domain is characterized as C2 2.
+At position 757 to 879, the domain is characterized as C2 3.
+At position 110 to 148, the domain is characterized as EGF-like 1.
+At position 156 to 193, the domain is characterized as EGF-like 2.
+At position 195 to 229, the domain is characterized as EGF-like 3.
+At position 232 to 271, the domain is characterized as EGF-like 4.
+At position 356 to 494, the domain is characterized as FAS1 1.
+At position 506 to 641, the domain is characterized as FAS1 2.
+At position 728 to 768, the domain is characterized as EGF-like 5.
+At position 818 to 858, the domain is characterized as EGF-like 6.
+At position 861 to 903, the domain is characterized as EGF-like 7.
+At position 904 to 946, the domain is characterized as EGF-like 8.
+At position 947 to 986, the domain is characterized as EGF-like 9.
+At position 988 to 1118, the domain is characterized as FAS1 3.
+At position 1128 to 1253, the domain is characterized as FAS1 4.
+At position 1327 to 1392, the domain is characterized as Laminin EGF-like 1.
+At position 1416 to 1454, the domain is characterized as EGF-like 10.
+At position 1455 to 1496, the domain is characterized as EGF-like 11.
+At position 1497 to 1539, the domain is characterized as EGF-like 12.
+At position 1540 to 1582, the domain is characterized as EGF-like 13.
+At position 1582 to 1708, the domain is characterized as FAS1 5.
+At position 1724 to 1864, the domain is characterized as FAS1 6.
+At position 1966 to 2031, the domain is characterized as Laminin EGF-like 2.
+At position 2056 to 2090, the domain is characterized as EGF-like 14.
+At position 2091 to 2131, the domain is characterized as EGF-like 15.
+At position 2132 to 2174, the domain is characterized as EGF-like 16.
+At position 2206 to 2301, the domain is characterized as Link.
+At position 2322 to 2459, the domain is characterized as FAS1 7.
+At position 8 to 252, the domain is characterized as ABC transporter.
+At position 34 to 192, the domain is characterized as SIS.
+At position 149 to 215, the domain is characterized as PQ-loop 2.
+At position 8 to 90, the domain is characterized as KRAB.
+At position 237 to 423, the domain is characterized as FAD-binding PCMH-type.
+At position 52 to 496, the domain is characterized as ADPK.
+At position 1 to 17, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 121 to 246, the domain is characterized as MRH.
+At position 13 to 281, the domain is characterized as PTS EIID.
+At position 110 to 380, the domain is characterized as NR LBD.
+At position 159 to 216, the domain is characterized as CTLH.
+At position 698 to 733, the domain is characterized as Anaphylatoxin-like.
+At position 1522 to 1664, the domain is characterized as NTR.
+At position 75 to 207, the domain is characterized as ADD.
+At position 100 to 258, the domain is characterized as CP-type G.
+At position 2 to 353, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 164 to 437, the domain is characterized as ABC transporter 1.
+At position 515 to 728, the domain is characterized as ABC transmembrane type-2 1.
+At position 860 to 1112, the domain is characterized as ABC transporter 2.
+At position 1185 to 1399, the domain is characterized as ABC transmembrane type-2 2.
+At position 1 to 119, the domain is characterized as Ig-like 1.
+At position 126 to 218, the domain is characterized as Ig-like 2.
+At position 21 to 189, the domain is characterized as C2 PI3K-type.
+At position 302 to 527, the domain is characterized as PIK helical.
+At position 607 to 886, the domain is characterized as PI3K/PI4K catalytic.
+At position 2 to 85, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 85 to 124, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 144 to 174, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 185 to 216, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 25 to 159, the domain is characterized as NtA.
+At position 193 to 246, the domain is characterized as Kazal-like 1.
+At position 268 to 321, the domain is characterized as Kazal-like 2.
+At position 339 to 393, the domain is characterized as Kazal-like 3.
+At position 409 to 464, the domain is characterized as Kazal-like 4.
+At position 486 to 538, the domain is characterized as Kazal-like 5.
+At position 551 to 603, the domain is characterized as Kazal-like 6.
+At position 616 to 668, the domain is characterized as Kazal-like 7.
+At position 700 to 753, the domain is characterized as Kazal-like 8.
+At position 1144 to 1266, the domain is characterized as SEA.
+At position 1347 to 1383, the domain is characterized as EGF-like 1.
+At position 1388 to 1563, the domain is characterized as Laminin G-like 1.
+At position 1564 to 1601, the domain is characterized as EGF-like 2.
+At position 1603 to 1640, the domain is characterized as EGF-like 3.
+At position 1650 to 1831, the domain is characterized as Laminin G-like 2.
+At position 1832 to 1870, the domain is characterized as EGF-like 4.
+At position 1894 to 2078, the domain is characterized as Laminin G-like 3.
+At position 1 to 73, the domain is characterized as Peptidase S1.
+At position 18 to 78, the domain is characterized as S4 RNA-binding.
+At position 16 to 268, the domain is characterized as Pyruvate carboxyltransferase.
+At position 9 to 111, the domain is characterized as FAD-binding FR-type.
+At position 241 to 324, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 159 to 211, the domain is characterized as KH.
+At position 50 to 105, the domain is characterized as F-box.
+At position 526 to 654, the domain is characterized as SMC hinge.
+At position 286 to 360, the domain is characterized as POU-specific.
+At position 278 to 351, the domain is characterized as KRAB 2.
+At position 18 to 130, the domain is characterized as ASCH.
+At position 107 to 296, the domain is characterized as Macro 1.
+At position 306 to 487, the domain is characterized as Macro 2.
+At position 628 to 850, the domain is characterized as PARP catalytic.
+At position 29 to 80, the domain is characterized as F-box.
+At position 68 to 303, the domain is characterized as Radical SAM core.
+At position 18 to 276, the domain is characterized as Pterin-binding.
+At position 438 to 598, the domain is characterized as SSD.
+At position 49 to 306, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 309 to 555, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 10 to 179, the domain is characterized as PNPLA.
+At position 815 to 1155, the domain is characterized as PUM-HD.
+At position 111 to 312, the domain is characterized as ATP-grasp.
+At position 619 to 683, the domain is characterized as R3H.
+At position 750 to 792, the domain is characterized as G-patch.
+At position 39 to 196, the domain is characterized as PPIase cyclophilin-type.
+At position 173 to 267, the domain is characterized as 5'-3' exonuclease.
+At position 75 to 245, the domain is characterized as Helicase ATP-binding.
+At position 255 to 415, the domain is characterized as Helicase C-terminal.
+At position 506 to 782, the domain is characterized as Protein kinase.
+At position 297 to 333, the domain is characterized as NAF.
+At position 297 to 593, the domain is characterized as Protein kinase.
+At position 145 to 233, the domain is characterized as ASD1.
+At position 543 to 825, the domain is characterized as ASD2.
+At position 221 to 321, the domain is characterized as Fe2OG dioxygenase.
+At position 59 to 281, the domain is characterized as BURP.
+At position 125 to 309, the domain is characterized as Integrase catalytic.
+At position 40 to 100, the domain is characterized as SH3.
+At position 25 to 281, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 295 to 541, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 114 to 386, the domain is characterized as SET.
+At position 118 to 147, the domain is characterized as EF-hand 2.
+At position 18 to 136, the domain is characterized as Response regulatory.
+At position 190 to 387, the domain is characterized as CheB-type methylesterase.
+At position 223 to 282, the domain is characterized as SH3.
+At position 56 to 134, the domain is characterized as RRM 1.
+At position 136 to 218, the domain is characterized as RRM 2.
+At position 231 to 303, the domain is characterized as RRM 3.
+At position 112 to 166, the domain is characterized as MIR 1.
+At position 173 to 223, the domain is characterized as MIR 2.
+At position 230 to 286, the domain is characterized as MIR 3.
+At position 293 to 359, the domain is characterized as MIR 4.
+At position 365 to 421, the domain is characterized as MIR 5.
+At position 105 to 391, the domain is characterized as Peptidase A1.
+At position 43 to 383, the domain is characterized as G-alpha.
+At position 372 to 410, the domain is characterized as EGF-like 10; calcium-binding.
+At position 587 to 671, the domain is characterized as BRCT.
+At position 9 to 198, the domain is characterized as RNase H type-2.
+At position 272 to 356, the domain is characterized as PDZ.
+At position 1 to 59, the domain is characterized as HMA.
+At position 170 to 238, the domain is characterized as KRAB.
+At position 99 to 410, the domain is characterized as PPM-type phosphatase.
+At position 1136 to 1300, the domain is characterized as PNPLA.
+At position 107 to 266, the domain is characterized as CP-type G.
+At position 181 to 421, the domain is characterized as NR LBD.
+At position 158 to 387, the domain is characterized as Radical SAM core.
+At position 1 to 437, the domain is characterized as SMP-LTD.
+At position 9 to 172, the domain is characterized as Ku.
+At position 802 to 867, the domain is characterized as SAM.
+At position 515 to 588, the domain is characterized as SH3.
+At position 15 to 270, the domain is characterized as Protein kinase.
+At position 82 to 203, the domain is characterized as GST C-terminal.
+At position 1 to 89, the domain is characterized as ATP-cone.
+At position 350 to 469, the domain is characterized as C2 1.
+At position 505 to 640, the domain is characterized as C2 2.
+At position 45 to 75, the domain is characterized as EF-hand 1.
+At position 119 to 141, the domain is characterized as EF-hand 3.
+At position 31 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 118 to 205, the domain is characterized as Ig-like C2-type 2.
+At position 220 to 299, the domain is characterized as Ig-like C2-type 3.
+At position 407 to 496, the domain is characterized as Ig-like C2-type 5.
+At position 501 to 590, the domain is characterized as Ig-like C2-type 6.
+At position 597 to 693, the domain is characterized as Fibronectin type-III 1.
+At position 698 to 794, the domain is characterized as Fibronectin type-III 2.
+At position 799 to 898, the domain is characterized as Fibronectin type-III 3.
+At position 1000 to 1099, the domain is characterized as Fibronectin type-III 5.
+At position 1104 to 1202, the domain is characterized as Fibronectin type-III 6.
+At position 1207 to 1304, the domain is characterized as Fibronectin type-III 7.
+At position 1305 to 1402, the domain is characterized as Fibronectin type-III 8.
+At position 1407 to 1504, the domain is characterized as Fibronectin type-III 9.
+At position 1509 to 1626, the domain is characterized as Fibronectin type-III 10.
+At position 1631 to 1727, the domain is characterized as Fibronectin type-III 11.
+At position 1731 to 1826, the domain is characterized as Fibronectin type-III 12.
+At position 1829 to 1928, the domain is characterized as Fibronectin type-III 13.
+At position 24 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 116 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 201 to 305, the domain is characterized as Ig-like C2-type 3.
+At position 318 to 409, the domain is characterized as Ig-like C2-type 4.
+At position 413 to 516, the domain is characterized as Ig-like C2-type 5.
+At position 592 to 953, the domain is characterized as Protein kinase.
+At position 66 to 170, the domain is characterized as PRD 1.
+At position 172 to 284, the domain is characterized as PRD 2.
+At position 69 to 275, the domain is characterized as YjeF N-terminal.
+At position 292 to 507, the domain is characterized as BURP.
+At position 200 to 308, the domain is characterized as Fe2OG dioxygenase.
+At position 35 to 210, the domain is characterized as Helicase ATP-binding.
+At position 654 to 689, the domain is characterized as UVR.
+At position 143 to 245, the domain is characterized as Cadherin 1.
+At position 586 to 680, the domain is characterized as Cadherin 5.
+At position 230 to 294, the domain is characterized as SEP.
+At position 392 to 469, the domain is characterized as UBX.
+At position 4 to 138, the domain is characterized as MSP.
+At position 301 to 355, the domain is characterized as AGC-kinase C-terminal.
+At position 41 to 213, the domain is characterized as Helicase ATP-binding.
+At position 419 to 588, the domain is characterized as Helicase C-terminal.
+At position 616 to 708, the domain is characterized as Dicer dsRNA-binding fold.
+At position 881 to 1028, the domain is characterized as PAZ.
+At position 1262 to 1385, the domain is characterized as RNase III 1.
+At position 1609 to 1767, the domain is characterized as RNase III 2.
+At position 1792 to 1857, the domain is characterized as DRBM.
+At position 152 to 212, the domain is characterized as SH3.
+At position 200 to 317, the domain is characterized as C2 1.
+At position 331 to 452, the domain is characterized as C2 2.
+At position 10 to 87, the domain is characterized as GIY-YIG.
+At position 463 to 652, the domain is characterized as BPL/LPL catalytic.
+At position 12 to 129, the domain is characterized as VOC 1.
+At position 158 to 313, the domain is characterized as VOC 2.
+At position 241 to 389, the domain is characterized as Exonuclease.
+At position 252 to 311, the domain is characterized as SH3.
+At position 336 to 861, the domain is characterized as USP.
+At position 652 to 693, the domain is characterized as UBA 1.
+At position 727 to 767, the domain is characterized as UBA 2.
+At position 76 to 293, the domain is characterized as Radical SAM core.
+At position 114 to 342, the domain is characterized as TLDc.
+At position 363 to 574, the domain is characterized as TLDc.
+At position 179 to 238, the domain is characterized as CBS 2.
+At position 288 to 351, the domain is characterized as bZIP.
+At position 174 to 387, the domain is characterized as FtsK.
+At position 13 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 141 to 170, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 116 to 233, the domain is characterized as Calponin-homology (CH) 1.
+At position 388 to 494, the domain is characterized as Calponin-homology (CH) 3.
+At position 509 to 617, the domain is characterized as Calponin-homology (CH) 4.
+At position 792 to 1024, the domain is characterized as NR LBD.
+At position 139 to 259, the domain is characterized as Calponin-homology (CH) 1.
+At position 287 to 390, the domain is characterized as Calponin-homology (CH) 2.
+At position 411 to 521, the domain is characterized as Calponin-homology (CH) 3.
+At position 534 to 642, the domain is characterized as Calponin-homology (CH) 4.
+At position 49 to 286, the domain is characterized as PABS.
+At position 111 to 377, the domain is characterized as Protein kinase.
+At position 36 to 138, the domain is characterized as Gnk2-homologous 1.
+At position 145 to 251, the domain is characterized as Gnk2-homologous 2.
+At position 207 to 302, the domain is characterized as Fibronectin type-III 1.
+At position 315 to 411, the domain is characterized as Fibronectin type-III 2.
+At position 428 to 518, the domain is characterized as Fibronectin type-III 3.
+At position 530 to 624, the domain is characterized as Fibronectin type-III 4.
+At position 35 to 348, the domain is characterized as GH26.
+At position 544 to 657, the domain is characterized as CRC.
+At position 56 to 251, the domain is characterized as Rho-GAP.
+At position 40 to 121, the domain is characterized as EMI.
+At position 122 to 162, the domain is characterized as EGF-like 1; calcium-binding.
+At position 163 to 203, the domain is characterized as EGF-like 2; calcium-binding.
+At position 287 to 327, the domain is characterized as EGF-like 3; calcium-binding.
+At position 414 to 454, the domain is characterized as EGF-like 4; calcium-binding.
+At position 518 to 554, the domain is characterized as EGF-like 5.
+At position 562 to 597, the domain is characterized as EGF-like 6.
+At position 605 to 640, the domain is characterized as EGF-like 7.
+At position 785 to 816, the domain is characterized as EGF-like 8.
+At position 829 to 859, the domain is characterized as EGF-like 9.
+At position 867 to 903, the domain is characterized as EGF-like 10.
+At position 911 to 946, the domain is characterized as EGF-like 11.
+At position 997 to 1032, the domain is characterized as EGF-like 12.
+At position 1040 to 1075, the domain is characterized as EGF-like 13.
+At position 1083 to 1118, the domain is characterized as EGF-like 14.
+At position 1131 to 1161, the domain is characterized as EGF-like 15.
+At position 1169 to 1204, the domain is characterized as EGF-like 16.
+At position 1256 to 1291, the domain is characterized as EGF-like 17.
+At position 1299 to 1334, the domain is characterized as EGF-like 18.
+At position 1342 to 1377, the domain is characterized as EGF-like 19.
+At position 1390 to 1420, the domain is characterized as EGF-like 20.
+At position 1428 to 1463, the domain is characterized as EGF-like 21.
+At position 69 to 327, the domain is characterized as Protein kinase.
+At position 369 to 404, the domain is characterized as EF-hand 1.
+At position 441 to 476, the domain is characterized as EF-hand 3.
+At position 477 to 511, the domain is characterized as EF-hand 4.
+At position 33 to 100, the domain is characterized as PASTA 1.
+At position 101 to 174, the domain is characterized as PASTA 2.
+At position 180 to 241, the domain is characterized as PASTA 3.
+At position 335 to 370, the domain is characterized as EF-hand 1.
+At position 376 to 411, the domain is characterized as EF-hand 2.
+At position 138 to 371, the domain is characterized as Radical SAM core.
+At position 374 to 434, the domain is characterized as TRAM.
+At position 103 to 167, the domain is characterized as S4 RNA-binding.
+At position 121 to 328, the domain is characterized as ATP-grasp.
+At position 90 to 148, the domain is characterized as S1 motif.
+At position 14 to 238, the domain is characterized as AB hydrolase-1.
+At position 164 to 322, the domain is characterized as Cupin type-1 1.
+At position 381 to 538, the domain is characterized as Cupin type-1 2.
+At position 74 to 246, the domain is characterized as MDFI.
+At position 347 to 641, the domain is characterized as Protein kinase.
+At position 130 to 254, the domain is characterized as CRC.
+At position 94 to 351, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 351 to 600, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 63 to 166, the domain is characterized as FAD-binding FR-type.
+At position 48 to 236, the domain is characterized as RNase H type-2.
+At position 22 to 155, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 185 to 307, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 2 to 179, the domain is characterized as PCI.
+At position 109 to 313, the domain is characterized as ATP-grasp.
+At position 13 to 92, the domain is characterized as Sm.
+At position 132 to 388, the domain is characterized as Olfactomedin-like.
+At position 426 to 503, the domain is characterized as RRM.
+At position 145 to 319, the domain is characterized as CRAL-TRIO.
+At position 129 to 266, the domain is characterized as MPN.
+At position 126 to 213, the domain is characterized as Ig-like C2-type.
+At position 607 to 762, the domain is characterized as MOSC.
+At position 53 to 166, the domain is characterized as Plastocyanin-like 1.
+At position 221 to 290, the domain is characterized as Plastocyanin-like 2.
+At position 416 to 532, the domain is characterized as Plastocyanin-like 3.
+At position 211 to 439, the domain is characterized as NR LBD.
+At position 40 to 78, the domain is characterized as EGF-like 1.
+At position 79 to 119, the domain is characterized as EGF-like 2.
+At position 120 to 157, the domain is characterized as EGF-like 3.
+At position 159 to 196, the domain is characterized as EGF-like 4; calcium-binding.
+At position 198 to 235, the domain is characterized as EGF-like 5.
+At position 237 to 273, the domain is characterized as EGF-like 6; calcium-binding.
+At position 275 to 313, the domain is characterized as EGF-like 7.
+At position 315 to 351, the domain is characterized as EGF-like 8; calcium-binding.
+At position 352 to 390, the domain is characterized as EGF-like 9.
+At position 392 to 430, the domain is characterized as EGF-like 10; calcium-binding.
+At position 432 to 468, the domain is characterized as EGF-like 11; calcium-binding.
+At position 470 to 506, the domain is characterized as EGF-like 12; calcium-binding.
+At position 508 to 544, the domain is characterized as EGF-like 13; calcium-binding.
+At position 546 to 581, the domain is characterized as EGF-like 14; calcium-binding.
+At position 583 to 619, the domain is characterized as EGF-like 15; calcium-binding.
+At position 621 to 656, the domain is characterized as EGF-like 16; calcium-binding.
+At position 658 to 694, the domain is characterized as EGF-like 17; calcium-binding.
+At position 696 to 731, the domain is characterized as EGF-like 18.
+At position 735 to 771, the domain is characterized as EGF-like 19.
+At position 772 to 809, the domain is characterized as EGF-like 20.
+At position 811 to 848, the domain is characterized as EGF-like 21; calcium-binding.
+At position 850 to 886, the domain is characterized as EGF-like 22; calcium-binding.
+At position 888 to 923, the domain is characterized as EGF-like 23; calcium-binding.
+At position 925 to 961, the domain is characterized as EGF-like 24.
+At position 963 to 999, the domain is characterized as EGF-like 25.
+At position 1001 to 1035, the domain is characterized as EGF-like 26.
+At position 1037 to 1083, the domain is characterized as EGF-like 27.
+At position 1085 to 1121, the domain is characterized as EGF-like 28.
+At position 1123 to 1159, the domain is characterized as EGF-like 29; calcium-binding.
+At position 1161 to 1204, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1206 to 1245, the domain is characterized as EGF-like 31.
+At position 1247 to 1288, the domain is characterized as EGF-like 32.
+At position 1290 to 1326, the domain is characterized as EGF-like 33.
+At position 1336 to 1374, the domain is characterized as EGF-like 34.
+At position 218 to 419, the domain is characterized as Helicase ATP-binding.
+At position 456 to 670, the domain is characterized as Helicase C-terminal.
+At position 1 to 98, the domain is characterized as ATP-cone.
+At position 186 to 444, the domain is characterized as Protein kinase.
+At position 487 to 522, the domain is characterized as EF-hand 1.
+At position 523 to 558, the domain is characterized as EF-hand 2.
+At position 559 to 592, the domain is characterized as EF-hand 3.
+At position 593 to 628, the domain is characterized as EF-hand 4.
+At position 94 to 153, the domain is characterized as bHLH.
+At position 73 to 236, the domain is characterized as Cupin type-1 1.
+At position 270 to 414, the domain is characterized as Cupin type-1 2.
+At position 138 to 165, the domain is characterized as PLD phosphodiesterase.
+At position 132 to 383, the domain is characterized as AB hydrolase-1.
+At position 33 to 227, the domain is characterized as Peptidase M12B.
+At position 235 to 318, the domain is characterized as Disintegrin.
+At position 32 to 147, the domain is characterized as GOLD.
+At position 89 to 161, the domain is characterized as PRC barrel.
+At position 7 to 297, the domain is characterized as Helicase ATP-binding.
+At position 386 to 449, the domain is characterized as TRAM.
+At position 146 to 365, the domain is characterized as TRUD.
+At position 92 to 428, the domain is characterized as Velvet.
+At position 59 to 284, the domain is characterized as Radical SAM core.
+At position 499 to 556, the domain is characterized as Chromo 1.
+At position 594 to 655, the domain is characterized as Chromo 2.
+At position 714 to 898, the domain is characterized as Helicase ATP-binding.
+At position 1030 to 1195, the domain is characterized as Helicase C-terminal.
+At position 1 to 32, the domain is characterized as EF-hand 1.
+At position 70 to 105, the domain is characterized as EF-hand 3.
+At position 106 to 131, the domain is characterized as EF-hand 4.
+At position 570 to 647, the domain is characterized as BRCT.
+At position 261 to 446, the domain is characterized as Glutamine amidotransferase type-1.
+At position 53 to 176, the domain is characterized as N-terminal Ras-GEF.
+At position 205 to 436, the domain is characterized as Ras-GEF.
+At position 506 to 532, the domain is characterized as EF-hand 2.
+At position 19 to 131, the domain is characterized as Thioredoxin 1.
+At position 127 to 273, the domain is characterized as Thioredoxin 2.
+At position 196 to 388, the domain is characterized as Glutamine amidotransferase type-1.
+At position 530 to 722, the domain is characterized as ATP-grasp 1.
+At position 1069 to 1260, the domain is characterized as ATP-grasp 2.
+At position 1324 to 1470, the domain is characterized as MGS-like.
+At position 37 to 177, the domain is characterized as C-type lectin.
+At position 190 to 371, the domain is characterized as EngA-type G 2.
+At position 3 to 145, the domain is characterized as Flavodoxin-like.
+At position 234 to 267, the domain is characterized as WW 1.
+At position 280 to 313, the domain is characterized as WW 2.
+At position 394 to 731, the domain is characterized as HECT.
+At position 24 to 142, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 321 to 407, the domain is characterized as PPIase FKBP-type.
+At position 120 to 194, the domain is characterized as RRM 2.
+At position 60 to 161, the domain is characterized as Rieske.
+At position 19 to 98, the domain is characterized as KH type-2.
+At position 19 to 692, the domain is characterized as Myosin motor.
+At position 695 to 724, the domain is characterized as IQ.
+At position 730 to 922, the domain is characterized as TH1.
+At position 1050 to 1107, the domain is characterized as SH3.
+At position 20 to 231, the domain is characterized as HD Cas3-type.
+At position 301 to 504, the domain is characterized as Helicase ATP-binding.
+At position 556 to 735, the domain is characterized as Helicase C-terminal.
+At position 190 to 406, the domain is characterized as BURP.
+At position 876 to 1179, the domain is characterized as Protein kinase.
+At position 43 to 161, the domain is characterized as C-type lectin.
+At position 14 to 82, the domain is characterized as J.
+At position 79 to 192, the domain is characterized as Response regulatory.
+At position 336 to 569, the domain is characterized as TLDc.
+At position 164 to 197, the domain is characterized as EF-hand 3.
+At position 11 to 74, the domain is characterized as SAM.
+At position 10 to 224, the domain is characterized as YjeF N-terminal.
+At position 56 to 112, the domain is characterized as FHA.
+At position 200 to 480, the domain is characterized as Protein kinase.
+At position 735 to 996, the domain is characterized as Protein kinase.
+At position 517 to 859, the domain is characterized as TTL.
+At position 94 to 409, the domain is characterized as IF rod.
+At position 75 to 291, the domain is characterized as Radical SAM core.
+At position 20 to 104, the domain is characterized as Death.
+At position 186 to 454, the domain is characterized as Protein kinase.
+At position 58 to 200, the domain is characterized as EXPERA.
+At position 659 to 697, the domain is characterized as PAP-associated.
+At position 157 to 219, the domain is characterized as t-SNARE coiled-coil homology.
+At position 387 to 526, the domain is characterized as SIS 1.
+At position 559 to 704, the domain is characterized as SIS 2.
+At position 21 to 108, the domain is characterized as HPr.
+At position 21 to 169, the domain is characterized as Thioredoxin 1.
+At position 158 to 301, the domain is characterized as Thioredoxin 2.
+At position 505 to 636, the domain is characterized as Thioredoxin 3.
+At position 66 to 183, the domain is characterized as sHSP.
+At position 189 to 268, the domain is characterized as RRM.
+At position 24 to 99, the domain is characterized as Ubiquitin-like.
+At position 1 to 114, the domain is characterized as Ig-like.
+At position 353 to 452, the domain is characterized as Cadherin 4.
+At position 457 to 562, the domain is characterized as Cadherin 5.
+At position 37 to 181, the domain is characterized as FAS1.
+At position 45 to 240, the domain is characterized as ABC transmembrane type-1.
+At position 65 to 238, the domain is characterized as hSac2.
+At position 159 to 193, the domain is characterized as EF-hand 4.
+At position 27 to 217, the domain is characterized as Ferritin-like diiron.
+At position 188 to 465, the domain is characterized as ZP.
+At position 22 to 125, the domain is characterized as Ig-like V-type.
+At position 7 to 134, the domain is characterized as MTTase N-terminal.
+At position 178 to 409, the domain is characterized as Radical SAM core.
+At position 411 to 492, the domain is characterized as TRAM.
+At position 20 to 158, the domain is characterized as B12-binding.
+At position 319 to 405, the domain is characterized as PDZ 2.
+At position 466 to 546, the domain is characterized as PDZ 3.
+At position 714 to 889, the domain is characterized as Guanylate kinase-like.
+At position 47 to 299, the domain is characterized as CN hydrolase.
+At position 220 to 250, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 294 to 328, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 51 to 196, the domain is characterized as Thioredoxin 1.
+At position 387 to 516, the domain is characterized as Thioredoxin 2.
+At position 46 to 234, the domain is characterized as RNase H type-2.
+At position 230 to 322, the domain is characterized as PA.
+At position 179 to 602, the domain is characterized as GRAS.
+At position 32 to 335, the domain is characterized as PPM-type phosphatase.
+At position 20 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 130 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 216 to 443, the domain is characterized as Rab-GAP TBC.
+At position 43 to 171, the domain is characterized as SCP.
+At position 63 to 169, the domain is characterized as TBDR plug.
+At position 174 to 708, the domain is characterized as TBDR beta-barrel.
+At position 237 to 428, the domain is characterized as GATase cobBQ-type.
+At position 35 to 182, the domain is characterized as Tyrosine-protein phosphatase.
+At position 7 to 82, the domain is characterized as RRM 1.
+At position 109 to 187, the domain is characterized as RRM 2.
+At position 31 to 59, the domain is characterized as LRRNT.
+At position 1185 to 1205, the domain is characterized as WH2 1.
+At position 1225 to 1245, the domain is characterized as WH2 2.
+At position 1313 to 1333, the domain is characterized as WH2 3.
+At position 133 to 163, the domain is characterized as KOW.
+At position 233 to 371, the domain is characterized as VPS9.
+At position 7 to 201, the domain is characterized as DPCK.
+At position 46 to 194, the domain is characterized as Tyrosine-protein phosphatase.
+At position 607 to 686, the domain is characterized as HSA.
+At position 877 to 935, the domain is characterized as Myb-like.
+At position 3 to 265, the domain is characterized as ABC transporter.
+At position 172 to 207, the domain is characterized as Tify.
+At position 17 to 49, the domain is characterized as LisH.
+At position 562 to 609, the domain is characterized as G-patch.
+At position 4 to 168, the domain is characterized as Thioredoxin.
+At position 316 to 590, the domain is characterized as Protein kinase.
+At position 226 to 303, the domain is characterized as HARP 1.
+At position 327 to 398, the domain is characterized as HARP 2.
+At position 445 to 600, the domain is characterized as Helicase ATP-binding.
+At position 716 to 869, the domain is characterized as Helicase C-terminal.
+At position 119 to 297, the domain is characterized as EngB-type G.
+At position 225 to 310, the domain is characterized as RRM.
+At position 34 to 142, the domain is characterized as Ig-like V-type.
+At position 24 to 73, the domain is characterized as UPAR/Ly6.
+At position 1 to 105, the domain is characterized as HPt.
+At position 274 to 526, the domain is characterized as Histidine kinase.
+At position 528 to 663, the domain is characterized as CheW-like.
+At position 54 to 369, the domain is characterized as DOT1.
+At position 2 to 106, the domain is characterized as FAD-binding FR-type.
+At position 262 to 354, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 344 to 403, the domain is characterized as Sushi 1.
+At position 405 to 516, the domain is characterized as CUB 1.
+At position 519 to 580, the domain is characterized as Sushi 2.
+At position 582 to 693, the domain is characterized as CUB 2.
+At position 697 to 756, the domain is characterized as Sushi 3.
+At position 758 to 821, the domain is characterized as Sushi 4.
+At position 825 to 886, the domain is characterized as Sushi 5.
+At position 53 to 220, the domain is characterized as PfpI endopeptidase 1.
+At position 258 to 424, the domain is characterized as PfpI endopeptidase 2.
+At position 402 to 480, the domain is characterized as RRM 3.
+At position 1246 to 1397, the domain is characterized as PINc.
+At position 213 to 257, the domain is characterized as bZIP.
+At position 288 to 502, the domain is characterized as DOG1.
+At position 31 to 217, the domain is characterized as Laminin G-like 1.
+At position 213 to 255, the domain is characterized as EGF-like 1.
+At position 299 to 496, the domain is characterized as Laminin G-like 2.
+At position 503 to 695, the domain is characterized as Laminin G-like 3.
+At position 699 to 736, the domain is characterized as EGF-like 2.
+At position 741 to 914, the domain is characterized as Laminin G-like 4.
+At position 928 to 1103, the domain is characterized as Laminin G-like 5.
+At position 1106 to 1143, the domain is characterized as EGF-like 3.
+At position 1149 to 1347, the domain is characterized as Laminin G-like 6.
+At position 663 to 856, the domain is characterized as ATP-grasp 2.
+At position 923 to 1058, the domain is characterized as MGS-like.
+At position 55 to 236, the domain is characterized as tr-type G.
+At position 147 to 315, the domain is characterized as 3'-5' exonuclease.
+At position 4 to 152, the domain is characterized as Thioredoxin.
+At position 110 to 189, the domain is characterized as PRC barrel.
+At position 205 to 301, the domain is characterized as CRM 1.
+At position 359 to 456, the domain is characterized as CRM 2.
+At position 570 to 670, the domain is characterized as CRM 3.
+At position 146 to 464, the domain is characterized as NB-ARC.
+At position 1714 to 1822, the domain is characterized as BEACH-type PH.
+At position 1841 to 2130, the domain is characterized as BEACH.
+At position 5 to 228, the domain is characterized as tr-type G.
+At position 100 to 459, the domain is characterized as Rab-GAP TBC.
+At position 10 to 109, the domain is characterized as HTH hxlR-type.
+At position 1 to 332, the domain is characterized as PUM-HD.
+At position 35 to 278, the domain is characterized as GB1/RHD3-type G.
+At position 223 to 546, the domain is characterized as Kinesin motor.
+At position 242 to 408, the domain is characterized as RDD.
+At position 884 to 970, the domain is characterized as VRR-NUC.
+At position 288 to 673, the domain is characterized as GRAS.
+At position 28 to 123, the domain is characterized as Ig-like V-type.
+At position 148 to 231, the domain is characterized as Ig-like C2-type 1.
+At position 238 to 333, the domain is characterized as Ig-like C2-type 2.
+At position 655 to 730, the domain is characterized as Biotinyl-binding.
+At position 70 to 261, the domain is characterized as ABC transmembrane type-1.
+At position 5 to 65, the domain is characterized as v-SNARE coiled-coil homology.
+At position 31 to 150, the domain is characterized as sHSP.
+At position 275 to 511, the domain is characterized as PRORP.
+At position 28 to 110, the domain is characterized as Lipoyl-binding.
+At position 15 to 252, the domain is characterized as ABC transporter 1.
+At position 11 to 224, the domain is characterized as ThyX.
+At position 553 to 751, the domain is characterized as VWFA.
+At position 18 to 49, the domain is characterized as KOW.
+At position 39 to 119, the domain is characterized as S1 motif.
+At position 7 to 328, the domain is characterized as YjeF C-terminal.
+At position 45 to 244, the domain is characterized as Radical SAM core.
+At position 19 to 344, the domain is characterized as Kinesin motor.
+At position 353 to 716, the domain is characterized as GH16.
+At position 49 to 105, the domain is characterized as Kazal-like.
+At position 28 to 229, the domain is characterized as Cytochrome b561.
+At position 41 to 91, the domain is characterized as F-box.
+At position 512 to 616, the domain is characterized as Ricin B-type lectin.
+At position 18 to 72, the domain is characterized as BTB 1.
+At position 398 to 485, the domain is characterized as BTB 2.
+At position 1 to 112, the domain is characterized as Peptidase S1.
+At position 110 to 145, the domain is characterized as EF-hand 1.
+At position 155 to 190, the domain is characterized as EF-hand 2.
+At position 372 to 506, the domain is characterized as DAGKc.
+At position 224 to 297, the domain is characterized as RRM.
+At position 126 to 295, the domain is characterized as tr-type G.
+At position 20 to 130, the domain is characterized as Ig-like.
+At position 247 to 318, the domain is characterized as PAS.
+At position 519 to 855, the domain is characterized as PDEase.
+At position 18 to 78, the domain is characterized as HTH tetR-type.
+At position 400 to 459, the domain is characterized as SH3.
+At position 1 to 123, the domain is characterized as CMP/dCMP-type deaminase.
+At position 67 to 254, the domain is characterized as RNase H type-2.
+At position 451 to 726, the domain is characterized as Protein kinase.
+At position 86 to 340, the domain is characterized as ABC transporter.
+At position 21 to 180, the domain is characterized as Ferritin-like diiron.
+At position 49 to 183, the domain is characterized as CMP/dCMP-type deaminase.
+At position 1011 to 1051, the domain is characterized as HNH.
+At position 10 to 129, the domain is characterized as SCP2.
+At position 296 to 468, the domain is characterized as AMMECR1.
+At position 99 to 170, the domain is characterized as SUI1.
+At position 22 to 69, the domain is characterized as CHCH.
+At position 590 to 648, the domain is characterized as CBS 1.
+At position 799 to 859, the domain is characterized as CBS 2.
+At position 84 to 144, the domain is characterized as Myb-like.
+At position 27 to 128, the domain is characterized as CBM2.
+At position 183 to 212, the domain is characterized as CBM10.
+At position 281 to 607, the domain is characterized as GH10.
+At position 1457 to 1682, the domain is characterized as Collagen IV NC1.
+At position 443 to 557, the domain is characterized as Toprim.
+At position 29 to 81, the domain is characterized as F-box.
+At position 203 to 321, the domain is characterized as C2 2.
+At position 360 to 496, the domain is characterized as C2 3.
+At position 1136 to 1262, the domain is characterized as C2 4.
+At position 1310 to 1438, the domain is characterized as C2 5.
+At position 1561 to 1679, the domain is characterized as C2 6.
+At position 1795 to 1943, the domain is characterized as C2 7.
+At position 1 to 51, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 179, the domain is characterized as PBC.
+At position 118 to 293, the domain is characterized as Helicase ATP-binding.
+At position 318 to 466, the domain is characterized as Helicase C-terminal.
+At position 354 to 487, the domain is characterized as KARI C-terminal knotted 2.
+At position 83 to 279, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 21 to 314, the domain is characterized as Protein kinase.
+At position 11 to 73, the domain is characterized as IBB.
+At position 31 to 92, the domain is characterized as Thyroglobulin type-1 1.
+At position 93 to 160, the domain is characterized as Thyroglobulin type-1 2.
+At position 161 to 248, the domain is characterized as Thyroglobulin type-1 3.
+At position 298 to 358, the domain is characterized as Thyroglobulin type-1 4.
+At position 606 to 659, the domain is characterized as Thyroglobulin type-1 5.
+At position 660 to 727, the domain is characterized as Thyroglobulin type-1 6.
+At position 728 to 923, the domain is characterized as Thyroglobulin type-1 7.
+At position 1021 to 1079, the domain is characterized as Thyroglobulin type-1 8.
+At position 1088 to 1147, the domain is characterized as Thyroglobulin type-1 9.
+At position 1148 to 1212, the domain is characterized as Thyroglobulin type-1 10.
+At position 1444 to 1498, the domain is characterized as Thyroglobulin type-1 11.
+At position 133 to 193, the domain is characterized as S4 RNA-binding.
+At position 130 to 440, the domain is characterized as Peptidase S8.
+At position 449 to 583, the domain is characterized as P/Homo B.
+At position 85 to 195, the domain is characterized as GST C-terminal.
+At position 8 to 159, the domain is characterized as N-acetyltransferase.
+At position 219 to 380, the domain is characterized as TrmE-type G.
+At position 36 to 94, the domain is characterized as Cytochrome b5 heme-binding.
+At position 27 to 130, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 234, the domain is characterized as Ig-like C2-type 2.
+At position 242 to 333, the domain is characterized as Ig-like C2-type 3.
+At position 340 to 434, the domain is characterized as Ig-like C2-type 4.
+At position 440 to 540, the domain is characterized as Ig-like C2-type 5.
+At position 544 to 635, the domain is characterized as Ig-like C2-type 6.
+At position 740 to 832, the domain is characterized as Ig-like C2-type 7.
+At position 838 to 939, the domain is characterized as Ig-like C2-type 8.
+At position 943 to 1038, the domain is characterized as Fibronectin type-III.
+At position 776 to 964, the domain is characterized as Reticulon.
+At position 92 to 161, the domain is characterized as BTB.
+At position 196 to 297, the domain is characterized as BACK.
+At position 111 to 205, the domain is characterized as PA.
+At position 120 to 164, the domain is characterized as DSL.
+At position 169 to 210, the domain is characterized as EGF-like.
+At position 37 to 83, the domain is characterized as F-box.
+At position 108 to 168, the domain is characterized as LIM zinc-binding 2.
+At position 25 to 309, the domain is characterized as Protein kinase.
+At position 6 to 234, the domain is characterized as Radical SAM core.
+At position 230 to 381, the domain is characterized as Exonuclease.
+At position 64 to 268, the domain is characterized as ABC transmembrane type-1 1.
+At position 357 to 551, the domain is characterized as ABC transmembrane type-1 2.
+At position 36 to 145, the domain is characterized as Ig-like V-type.
+At position 45 to 160, the domain is characterized as GOLD.
+At position 24 to 182, the domain is characterized as Helicase ATP-binding.
+At position 427 to 593, the domain is characterized as Helicase C-terminal.
+At position 231 to 391, the domain is characterized as TrmE-type G.
+At position 167 to 409, the domain is characterized as GB1/RHD3-type G.
+At position 1 to 66, the domain is characterized as S1 motif 1.
+At position 87 to 155, the domain is characterized as S1 motif 2.
+At position 172 to 242, the domain is characterized as S1 motif 3.
+At position 259 to 329, the domain is characterized as S1 motif 4.
+At position 346 to 378, the domain is characterized as S1 motif 5.
+At position 11 to 260, the domain is characterized as ABC transporter.
+At position 9 to 108, the domain is characterized as BMC circularly permuted.
+At position 537 to 709, the domain is characterized as tr-type G.
+At position 35 to 70, the domain is characterized as LRRNT.
+At position 695 to 781, the domain is characterized as Ig-like C2-type 3.
+At position 182 to 267, the domain is characterized as PPIase FKBP-type.
+At position 93 to 260, the domain is characterized as CRAL-TRIO.
+At position 9 to 76, the domain is characterized as COMM.
+At position 8 to 42, the domain is characterized as EF-hand 1.
+At position 176 to 449, the domain is characterized as ABC transporter 1.
+At position 527 to 740, the domain is characterized as ABC transmembrane type-2 1.
+At position 865 to 1117, the domain is characterized as ABC transporter 2.
+At position 1190 to 1404, the domain is characterized as ABC transmembrane type-2 2.
+At position 41 to 247, the domain is characterized as BPL/LPL catalytic.
+At position 63 to 92, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 102 to 131, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 15 to 72, the domain is characterized as HTH cro/C1-type.
+At position 1523 to 1648, the domain is characterized as MaoC-like.
+At position 79 to 114, the domain is characterized as EF-hand 3.
+At position 115 to 146, the domain is characterized as EF-hand 4.
+At position 169 to 354, the domain is characterized as CheB-type methylesterase.
+At position 433 to 547, the domain is characterized as Toprim.
+At position 23 to 58, the domain is characterized as EF-hand 1.
+At position 59 to 94, the domain is characterized as EF-hand 2.
+At position 132 to 167, the domain is characterized as EF-hand 4.
+At position 631 to 673, the domain is characterized as Chromo 2.
+At position 748 to 932, the domain is characterized as Helicase ATP-binding.
+At position 1064 to 1229, the domain is characterized as Helicase C-terminal.
+At position 431 to 578, the domain is characterized as Thioredoxin.
+At position 20 to 322, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 18 to 196, the domain is characterized as Guanylate kinase-like.
+At position 222 to 299, the domain is characterized as POU-specific.
+At position 3 to 237, the domain is characterized as PABS.
+At position 4 to 350, the domain is characterized as Trm1 methyltransferase.
+At position 539 to 711, the domain is characterized as tr-type G.
+At position 30 to 71, the domain is characterized as WAP 1.
+At position 74 to 122, the domain is characterized as WAP 2.
+At position 132 to 445, the domain is characterized as IF rod.
+At position 52 to 119, the domain is characterized as BTB.
+At position 150 to 250, the domain is characterized as BACK.
+At position 141 to 209, the domain is characterized as Histone-fold.
+At position 265 to 412, the domain is characterized as YDG.
+At position 487 to 548, the domain is characterized as Pre-SET.
+At position 551 to 681, the domain is characterized as SET.
+At position 688 to 704, the domain is characterized as Post-SET.
+At position 184 to 272, the domain is characterized as EH 1.
+At position 216 to 251, the domain is characterized as EF-hand 1.
+At position 471 to 560, the domain is characterized as EH 2.
+At position 504 to 539, the domain is characterized as EF-hand 2.
+At position 1340 to 1357, the domain is characterized as WH2.
+At position 566 to 643, the domain is characterized as Carrier.
+At position 685 to 820, the domain is characterized as C2.
+At position 569 to 628, the domain is characterized as KH.
+At position 638 to 712, the domain is characterized as S1 motif.
+At position 6 to 195, the domain is characterized as Glutamine amidotransferase type-1.
+At position 196 to 392, the domain is characterized as GMPS ATP-PPase.
+At position 68 to 267, the domain is characterized as tr-type G.
+At position 28 to 165, the domain is characterized as Thioredoxin.
+At position 10 to 240, the domain is characterized as Radical SAM core.
+At position 9 to 180, the domain is characterized as CYTH.
+At position 9 to 247, the domain is characterized as ATP-grasp.
+At position 63 to 181, the domain is characterized as Response regulatory.
+At position 682 to 724, the domain is characterized as CCT.
+At position 703 to 900, the domain is characterized as ATP-grasp 2.
+At position 967 to 1104, the domain is characterized as MGS-like.
+At position 27 to 340, the domain is characterized as MACPF.
+At position 562 to 665, the domain is characterized as tRNA-binding.
+At position 2 to 19, the domain is characterized as LCN-type CS-alpha/beta.
+At position 40 to 113, the domain is characterized as H15.
+At position 536 to 670, the domain is characterized as DOD-type homing endonuclease.
+At position 7 to 235, the domain is characterized as ThyX.
+At position 495 to 606, the domain is characterized as PH.
+At position 255 to 444, the domain is characterized as GATase cobBQ-type.
+At position 97 to 288, the domain is characterized as ATP-grasp.
+At position 242 to 316, the domain is characterized as SPOR.
+At position 16 to 114, the domain is characterized as ENT.
+At position 225 to 391, the domain is characterized as TrmE-type G.
+At position 172 to 351, the domain is characterized as Letm1 RBD.
+At position 16 to 111, the domain is characterized as Rieske.
+At position 2 to 85, the domain is characterized as PDZ.
+At position 413 to 472, the domain is characterized as LIM zinc-binding 1.
+At position 472 to 531, the domain is characterized as LIM zinc-binding 2.
+At position 531 to 591, the domain is characterized as LIM zinc-binding 3.
+At position 30 to 173, the domain is characterized as MARVEL.
+At position 14 to 74, the domain is characterized as v-SNARE coiled-coil homology.
+At position 33 to 227, the domain is characterized as TLC.
+At position 83 to 265, the domain is characterized as PID.
+At position 707 to 788, the domain is characterized as BRCT.
+At position 492 to 752, the domain is characterized as Protein kinase.
+At position 827 to 957, the domain is characterized as Guanylate cyclase.
+At position 213 to 276, the domain is characterized as KH.
+At position 339 to 432, the domain is characterized as HD.
+At position 11 to 73, the domain is characterized as MIT.
+At position 21 to 76, the domain is characterized as PAS.
+At position 249 to 485, the domain is characterized as Methyl-accepting transducer.
+At position 53 to 86, the domain is characterized as EGF-like 2.
+At position 172 to 208, the domain is characterized as EGF-like 5.
+At position 210 to 247, the domain is characterized as EGF-like 6.
+At position 293 to 526, the domain is characterized as Fibrillar collagen NC1.
+At position 28 to 70, the domain is characterized as CAP-Gly.
+At position 161 to 312, the domain is characterized as Plastocyanin-like 2.
+At position 429 to 565, the domain is characterized as Plastocyanin-like 3.
+At position 105 to 330, the domain is characterized as Radical SAM core.
+At position 8 to 188, the domain is characterized as Clp R.
+At position 199 to 504, the domain is characterized as Protein kinase.
+At position 668 to 908, the domain is characterized as Dilute.
+At position 63 to 300, the domain is characterized as Grh/CP2 DB.
+At position 4 to 140, the domain is characterized as ADF-H 1.
+At position 176 to 316, the domain is characterized as ADF-H 2.
+At position 1 to 123, the domain is characterized as MSP.
+At position 598 to 677, the domain is characterized as BRCT.
+At position 586 to 761, the domain is characterized as PCI.
+At position 39 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 85 to 116, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 118 to 147, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 3 to 168, the domain is characterized as FeoB-type G.
+At position 176 to 267, the domain is characterized as RRM.
+At position 161 to 405, the domain is characterized as NR LBD.
+At position 182 to 358, the domain is characterized as PNPLA.
+At position 219 to 308, the domain is characterized as Ig-like C1-type.
+At position 9 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 54 to 365, the domain is characterized as Peptidase A1.
+At position 88 to 304, the domain is characterized as RNase H type-2.
+At position 12 to 72, the domain is characterized as HTH myb-type.
+At position 188 to 260, the domain is characterized as Bromo.
+At position 320 to 402, the domain is characterized as NET.
+At position 246 to 349, the domain is characterized as RRM 1.
+At position 366 to 437, the domain is characterized as RRM 2.
+At position 155 to 182, the domain is characterized as PLD phosphodiesterase.
+At position 52 to 125, the domain is characterized as GIY-YIG.
+At position 234 to 269, the domain is characterized as UVR.
+At position 31 to 182, the domain is characterized as N-acetyltransferase.
+At position 583 to 688, the domain is characterized as PH.
+At position 30 to 179, the domain is characterized as MARVEL.
+At position 121 to 206, the domain is characterized as Ig-like C2-type 2.
+At position 638 to 782, the domain is characterized as N-acetyltransferase.
+At position 20 to 125, the domain is characterized as Ig-like V-type.
+At position 17 to 147, the domain is characterized as Galectin 1.
+At position 226 to 354, the domain is characterized as Galectin 2.
+At position 12 to 97, the domain is characterized as GS beta-grasp.
+At position 4 to 59, the domain is characterized as bHLH.
+At position 626 to 701, the domain is characterized as BRCT.
+At position 671 to 758, the domain is characterized as WWE.
+At position 154 to 259, the domain is characterized as CBM21.
+At position 20 to 74, the domain is characterized as MADS-box.
+At position 1 to 93, the domain is characterized as PH.
+At position 136 to 235, the domain is characterized as PB1.
+At position 481 to 665, the domain is characterized as PNPLA.
+At position 223 to 286, the domain is characterized as Ubiquitin-like.
+At position 79 to 121, the domain is characterized as CAP-Gly 1.
+At position 235 to 277, the domain is characterized as CAP-Gly 2.
+At position 46 to 104, the domain is characterized as Chromo.
+At position 189 to 249, the domain is characterized as Pre-SET.
+At position 252 to 375, the domain is characterized as SET.
+At position 405 to 421, the domain is characterized as Post-SET.
+At position 27 to 272, the domain is characterized as AB hydrolase-1.
+At position 63 to 344, the domain is characterized as tr-type G.
+At position 25 to 280, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 25 to 73, the domain is characterized as Myosin N-terminal SH3-like.
+At position 78 to 748, the domain is characterized as Myosin motor.
+At position 774 to 803, the domain is characterized as IQ 1.
+At position 822 to 851, the domain is characterized as IQ 3.
+At position 847 to 876, the domain is characterized as IQ 4.
+At position 870 to 899, the domain is characterized as IQ 5.
+At position 1347 to 1718, the domain is characterized as Dilute.
+At position 424 to 445, the domain is characterized as GoLoco.
+At position 758 to 820, the domain is characterized as SH3.
+At position 115 to 300, the domain is characterized as Rab-GAP TBC.
+At position 27 to 300, the domain is characterized as Protein kinase.
+At position 214 to 291, the domain is characterized as UBX.
+At position 48 to 154, the domain is characterized as Calponin-homology (CH).
+At position 28 to 379, the domain is characterized as Protein kinase.
+At position 248 to 274, the domain is characterized as PLD phosphodiesterase 1.
+At position 487 to 520, the domain is characterized as PLD phosphodiesterase 2.
+At position 277 to 351, the domain is characterized as U-box.
+At position 199 to 364, the domain is characterized as Helicase ATP-binding.
+At position 847 to 899, the domain is characterized as SANT 1.
+At position 950 to 1014, the domain is characterized as SANT 2.
+At position 293 to 417, the domain is characterized as Nop.
+At position 397 to 556, the domain is characterized as PA14.
+At position 68 to 299, the domain is characterized as PABS.
+At position 123 to 248, the domain is characterized as Fatty acid hydroxylase.
+At position 240 to 315, the domain is characterized as Ig-like C2-type 2.
+At position 323 to 410, the domain is characterized as Ig-like C2-type 3.
+At position 418 to 495, the domain is characterized as Ig-like C2-type 4.
+At position 501 to 588, the domain is characterized as Ig-like C2-type 5.
+At position 593 to 675, the domain is characterized as Ig-like C2-type 6.
+At position 206 to 258, the domain is characterized as HAMP.
+At position 263 to 334, the domain is characterized as PAS.
+At position 327 to 380, the domain is characterized as PAC.
+At position 384 to 602, the domain is characterized as Histidine kinase.
+At position 178 to 314, the domain is characterized as DAGKc.
+At position 194 to 451, the domain is characterized as SF4 helicase.
+At position 305 to 368, the domain is characterized as SH3.
+At position 309 to 441, the domain is characterized as ADD.
+At position 462 to 740, the domain is characterized as SAM-dependent MTase C5-type.
+At position 133 to 420, the domain is characterized as ABC transmembrane type-1.
+At position 455 to 692, the domain is characterized as ABC transporter.
+At position 96 to 348, the domain is characterized as Radical SAM core.
+At position 893 to 967, the domain is characterized as RRM.
+At position 32 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 214, the domain is characterized as Ig-like C2-type 2.
+At position 230 to 327, the domain is characterized as Ig-like C2-type 3.
+At position 335 to 421, the domain is characterized as Ig-like C2-type 4.
+At position 428 to 553, the domain is characterized as Ig-like C2-type 5.
+At position 556 to 654, the domain is characterized as Ig-like C2-type 6.
+At position 661 to 747, the domain is characterized as Ig-like C2-type 7.
+At position 827 to 1158, the domain is characterized as Protein kinase.
+At position 5 to 188, the domain is characterized as Guanylate kinase-like.
+At position 566 to 752, the domain is characterized as Reticulon.
+At position 19 to 68, the domain is characterized as F-box.
+At position 270 to 397, the domain is characterized as Ricin B-type lectin 1.
+At position 400 to 523, the domain is characterized as Ricin B-type lectin 2.
+At position 350 to 427, the domain is characterized as OCT.
+At position 41 to 336, the domain is characterized as Protein kinase.
+At position 34 to 269, the domain is characterized as Peptidase S1.
+At position 114 to 305, the domain is characterized as Rab-GAP TBC.
+At position 480 to 539, the domain is characterized as SH3.
+At position 555 to 718, the domain is characterized as RUN.
+At position 1054 to 1324, the domain is characterized as Protein kinase.
+At position 1327 to 1505, the domain is characterized as KEN.
+At position 5 to 148, the domain is characterized as Peptidase C51.
+At position 181 to 363, the domain is characterized as MurNAc-LAA.
+At position 402 to 472, the domain is characterized as SH3b.
+At position 1 to 260, the domain is characterized as SMP-LTD.
+At position 42 to 115, the domain is characterized as U-box.
+At position 311 to 470, the domain is characterized as PPIase cyclophilin-type.
+At position 212 to 406, the domain is characterized as Peptidase M12B.
+At position 414 to 501, the domain is characterized as Disintegrin.
+At position 644 to 698, the domain is characterized as EGF-like.
+At position 9 to 124, the domain is characterized as C-type lectin.
+At position 14 to 267, the domain is characterized as Pyruvate carboxyltransferase.
+At position 163 to 271, the domain is characterized as SEA.
+At position 268 to 366, the domain is characterized as Ig-like 1.
+At position 367 to 464, the domain is characterized as Ig-like 2.
+At position 469 to 559, the domain is characterized as Ig-like 3.
+At position 950 to 1004, the domain is characterized as GPS.
+At position 19 to 345, the domain is characterized as Kinesin motor.
+At position 86 to 137, the domain is characterized as FHA.
+At position 2 to 127, the domain is characterized as C2 1.
+At position 103 to 192, the domain is characterized as PPIase FKBP-type.
+At position 1 to 112, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 174, the domain is characterized as Era-type G.
+At position 599 to 676, the domain is characterized as BRCT.
+At position 34 to 110, the domain is characterized as CIDE-N.
+At position 12 to 338, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 343 to 656, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 12 to 115, the domain is characterized as Longin.
+At position 5 to 379, the domain is characterized as DZF.
+At position 399 to 468, the domain is characterized as DRBM 1.
+At position 520 to 586, the domain is characterized as DRBM 2.
+At position 1 to 132, the domain is characterized as Nudix hydrolase.
+At position 39 to 318, the domain is characterized as tr-type G.
+At position 49 to 273, the domain is characterized as Cache.
+At position 312 to 366, the domain is characterized as HAMP.
+At position 371 to 607, the domain is characterized as Methyl-accepting transducer.
+At position 663 to 832, the domain is characterized as tr-type G.
+At position 7 to 221, the domain is characterized as ABC transporter.
+At position 49 to 78, the domain is characterized as HhH.
+At position 83 to 145, the domain is characterized as CBS 1.
+At position 177 to 234, the domain is characterized as CBS 2.
+At position 12 to 335, the domain is characterized as AB hydrolase-1.
+At position 334 to 398, the domain is characterized as S4 RNA-binding.
+At position 254 to 479, the domain is characterized as BURP.
+At position 71 to 188, the domain is characterized as PX.
+At position 4 to 159, the domain is characterized as Thioredoxin.
+At position 60 to 147, the domain is characterized as RRM.
+At position 248 to 345, the domain is characterized as Fe2OG dioxygenase.
+At position 2127 to 2258, the domain is characterized as MPN.
+At position 106 to 197, the domain is characterized as ARID.
+At position 305 to 398, the domain is characterized as sHSP.
+At position 40 to 331, the domain is characterized as Protein kinase.
+At position 95 to 239, the domain is characterized as PX.
+At position 31 to 134, the domain is characterized as Cytochrome c 1.
+At position 178 to 293, the domain is characterized as Cytochrome c 2.
+At position 317 to 407, the domain is characterized as Cytochrome c 3.
+At position 33 to 198, the domain is characterized as Helicase ATP-binding.
+At position 231 to 429, the domain is characterized as Helicase C-terminal.
+At position 49 to 396, the domain is characterized as Peptidase S8.
+At position 769 to 1045, the domain is characterized as Autotransporter.
+At position 113 to 285, the domain is characterized as Helicase ATP-binding.
+At position 333 to 492, the domain is characterized as Helicase C-terminal.
+At position 25 to 107, the domain is characterized as GOLD.
+At position 10 to 436, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 924 to 1237, the domain is characterized as PKS/mFAS DH.
+At position 2059 to 2136, the domain is characterized as Carrier.
+At position 165 to 238, the domain is characterized as Ubiquitin-like.
+At position 4 to 146, the domain is characterized as Jacalin-type lectin.
+At position 75 to 186, the domain is characterized as PA.
+At position 1 to 95, the domain is characterized as Plastocyanin-like 1.
+At position 101 to 252, the domain is characterized as Plastocyanin-like 2.
+At position 319 to 454, the domain is characterized as Plastocyanin-like 3.
+At position 23 to 220, the domain is characterized as Lon N-terminal.
+At position 9 to 229, the domain is characterized as Peptidase S1.
+At position 43 to 109, the domain is characterized as Importin N-terminal.
+At position 40 to 259, the domain is characterized as Radical SAM core.
+At position 13 to 181, the domain is characterized as PPIase cyclophilin-type.
+At position 6 to 286, the domain is characterized as tr-type G.
+At position 24 to 109, the domain is characterized as PDZ.
+At position 927 to 1023, the domain is characterized as ASD1.
+At position 1659 to 1947, the domain is characterized as ASD2.
+At position 63 to 128, the domain is characterized as NAC-A/B.
+At position 166 to 203, the domain is characterized as UBA.
+At position 574 to 675, the domain is characterized as tRNA-binding.
+At position 66 to 404, the domain is characterized as AB hydrolase-1.
+At position 425 to 484, the domain is characterized as CBS 1.
+At position 486 to 540, the domain is characterized as CBS 2.
+At position 164 to 385, the domain is characterized as Radical SAM core.
+At position 63 to 252, the domain is characterized as KARI N-terminal Rossmann.
+At position 253 to 400, the domain is characterized as KARI C-terminal knotted.
+At position 199 to 291, the domain is characterized as PDZ.
+At position 17 to 251, the domain is characterized as tr-type G.
+At position 986 to 1023, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 1024 to 1067, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 1073 to 1113, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 1114 to 1156, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 1168 to 1213, the domain is characterized as Beta/gamma crystallin 'Greek key' 5.
+At position 1214 to 1256, the domain is characterized as Beta/gamma crystallin 'Greek key' 6.
+At position 1262 to 1302, the domain is characterized as Beta/gamma crystallin 'Greek key' 7.
+At position 1303 to 1345, the domain is characterized as Beta/gamma crystallin 'Greek key' 8.
+At position 1356 to 1393, the domain is characterized as Beta/gamma crystallin 'Greek key' 9.
+At position 1394 to 1437, the domain is characterized as Beta/gamma crystallin 'Greek key' 10.
+At position 1443 to 1483, the domain is characterized as Beta/gamma crystallin 'Greek key' 11.
+At position 1484 to 1525, the domain is characterized as Beta/gamma crystallin 'Greek key' 12.
+At position 1569 to 1659, the domain is characterized as Ricin B-type lectin.
+At position 26 to 329, the domain is characterized as NB-ARC.
+At position 7 to 31, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 77 to 318, the domain is characterized as ABC transporter 1.
+At position 345 to 565, the domain is characterized as ABC transporter 2.
+At position 18 to 119, the domain is characterized as PH.
+At position 29 to 125, the domain is characterized as Fibronectin type-III 1.
+At position 133 to 224, the domain is characterized as Fibronectin type-III 2.
+At position 231 to 329, the domain is characterized as Fibronectin type-III 3.
+At position 333 to 433, the domain is characterized as Fibronectin type-III 4.
+At position 22 to 239, the domain is characterized as tr-type G.
+At position 44 to 158, the domain is characterized as sHSP.
+At position 10 to 272, the domain is characterized as Helicase ATP-binding.
+At position 3 to 51, the domain is characterized as Kazal-like.
+At position 452 to 867, the domain is characterized as FH2.
+At position 279 to 507, the domain is characterized as Peptidase M12B.
+At position 516 to 605, the domain is characterized as Disintegrin.
+At position 192 to 232, the domain is characterized as UBA.
+At position 554 to 614, the domain is characterized as Tudor.
+At position 1 to 162, the domain is characterized as DHFR.
+At position 340 to 617, the domain is characterized as ABC transporter 1.
+At position 637 to 965, the domain is characterized as ABC transporter 2.
+At position 25 to 188, the domain is characterized as MAM.
+At position 190 to 275, the domain is characterized as Ig-like C2-type.
+At position 288 to 383, the domain is characterized as Fibronectin type-III 1.
+At position 485 to 591, the domain is characterized as Fibronectin type-III 3.
+At position 592 to 668, the domain is characterized as Fibronectin type-III 4.
+At position 888 to 1144, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1176 to 1439, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 239 to 401, the domain is characterized as Helicase ATP-binding.
+At position 455 to 609, the domain is characterized as Helicase C-terminal.
+At position 277 to 344, the domain is characterized as SH3.
+At position 45 to 115, the domain is characterized as Rho RNA-BD.
+At position 82 to 204, the domain is characterized as MARVEL.
+At position 16 to 251, the domain is characterized as PABS.
+At position 4 to 195, the domain is characterized as Flavodoxin-like.
+At position 1910 to 2036, the domain is characterized as C-type lectin.
+At position 2039 to 2099, the domain is characterized as Sushi.
+At position 50 to 135, the domain is characterized as Cytochrome c.
+At position 66 to 133, the domain is characterized as POTRA.
+At position 9 to 172, the domain is characterized as FeoB-type G.
+At position 200 to 345, the domain is characterized as YEATS.
+At position 9 to 232, the domain is characterized as Glutamine amidotransferase type-1.
+At position 307 to 586, the domain is characterized as ABC transporter 1.
+At position 606 to 934, the domain is characterized as ABC transporter 2.
+At position 404 to 571, the domain is characterized as tr-type G.
+At position 8 to 70, the domain is characterized as Z-binding 1.
+At position 103 to 166, the domain is characterized as Z-binding 2.
+At position 77 to 399, the domain is characterized as PPM-type phosphatase.
+At position 82 to 366, the domain is characterized as Protein kinase.
+At position 57 to 121, the domain is characterized as BTB.
+At position 363 to 560, the domain is characterized as Lon proteolytic.
+At position 452 to 592, the domain is characterized as Thioredoxin.
+At position 71 to 155, the domain is characterized as PDZ.
+At position 688 to 808, the domain is characterized as PH.
+At position 905 to 1097, the domain is characterized as Rho-GAP.
+At position 416 to 585, the domain is characterized as tr-type G.
+At position 4 to 106, the domain is characterized as BMC circularly permuted 1.
+At position 107 to 211, the domain is characterized as BMC circularly permuted 2.
+At position 336 to 388, the domain is characterized as bHLH.
+At position 25 to 333, the domain is characterized as Protein kinase.
+At position 38 to 84, the domain is characterized as F-box.
+At position 366 to 442, the domain is characterized as RRM.
+At position 4 to 67, the domain is characterized as LCN-type CS-alpha/beta.
+At position 90 to 217, the domain is characterized as GST C-terminal.
+At position 542 to 619, the domain is characterized as PABC.
+At position 102 to 408, the domain is characterized as Peptidase A1.
+At position 80 to 356, the domain is characterized as Protein kinase.
+At position 118 to 314, the domain is characterized as ATP-grasp.
+At position 20 to 84, the domain is characterized as SAM.
+At position 415 to 712, the domain is characterized as Protein kinase.
+At position 277 to 518, the domain is characterized as MHD.
+At position 253 to 433, the domain is characterized as PBS-linker 1.
+At position 514 to 692, the domain is characterized as PBS-linker 2.
+At position 709 to 887, the domain is characterized as PBS-linker 3.
+At position 940 to 1121, the domain is characterized as PBS-linker 4.
+At position 28 to 219, the domain is characterized as TLC.
+At position 10 to 219, the domain is characterized as RNase H type-2.
+At position 77 to 112, the domain is characterized as Tify.
+At position 147 to 189, the domain is characterized as CCT.
+At position 177 to 462, the domain is characterized as Protein kinase.
+At position 1 to 182, the domain is characterized as DHFR.
+At position 445 to 502, the domain is characterized as F-box.
+At position 6 to 279, the domain is characterized as CN hydrolase.
+At position 237 to 425, the domain is characterized as Helicase ATP-binding.
+At position 450 to 603, the domain is characterized as Helicase C-terminal.
+At position 598 to 677, the domain is characterized as Cytochrome c.
+At position 12 to 62, the domain is characterized as Tudor-knot.
+At position 152 to 323, the domain is characterized as MRG.
+At position 1 to 304, the domain is characterized as PTS EIIC type-2.
+At position 81 to 784, the domain is characterized as USP.
+At position 317 to 433, the domain is characterized as PI-PLC Y-box.
+At position 434 to 563, the domain is characterized as C2.
+At position 334 to 395, the domain is characterized as S4 RNA-binding.
+At position 411 to 546, the domain is characterized as Plastocyanin-like 3.
+At position 176 to 288, the domain is characterized as Fe2OG dioxygenase.
+At position 295 to 539, the domain is characterized as B30.2/SPRY.
+At position 30 to 98, the domain is characterized as POTRA.
+At position 1133 to 1366, the domain is characterized as Fibrillar collagen NC1.
+At position 286 to 564, the domain is characterized as ABC transmembrane type-1 1.
+At position 599 to 825, the domain is characterized as ABC transporter 1.
+At position 887 to 1215, the domain is characterized as ABC transmembrane type-1 2.
+At position 1255 to 1488, the domain is characterized as ABC transporter 2.
+At position 137 to 368, the domain is characterized as Radical SAM core.
+At position 371 to 432, the domain is characterized as TRAM.
+At position 40 to 383, the domain is characterized as PH.
+At position 374 to 490, the domain is characterized as C2.
+At position 563 to 757, the domain is characterized as Ras-GAP.
+At position 43 to 76, the domain is characterized as WW 1.
+At position 90 to 123, the domain is characterized as WW 2.
+At position 697 to 817, the domain is characterized as C2.
+At position 285 to 344, the domain is characterized as SH3.
+At position 37 to 138, the domain is characterized as LOB.
+At position 1229 to 1323, the domain is characterized as SH2.
+At position 230 to 378, the domain is characterized as Exonuclease.
+At position 503 to 577, the domain is characterized as RRM 1.
+At position 598 to 677, the domain is characterized as RRM 2.
+At position 22 to 96, the domain is characterized as Ubiquitin-like.
+At position 194 to 233, the domain is characterized as STI1.
+At position 614 to 658, the domain is characterized as UBA.
+At position 2 to 90, the domain is characterized as ABM.
+At position 50 to 85, the domain is characterized as EF-hand 1.
+At position 144 to 173, the domain is characterized as EF-hand 3.
+At position 175 to 210, the domain is characterized as EF-hand 4.
+At position 226 to 251, the domain is characterized as EF-hand 5.
+At position 252 to 287, the domain is characterized as EF-hand 6.
+At position 59 to 255, the domain is characterized as HD.
+At position 6 to 152, the domain is characterized as PINc.
+At position 271 to 369, the domain is characterized as Fe2OG dioxygenase.
+At position 7 to 52, the domain is characterized as SpoVT-AbrB 1.
+At position 11 to 87, the domain is characterized as GST N-terminal.
+At position 45 to 219, the domain is characterized as Helicase ATP-binding.
+At position 246 to 391, the domain is characterized as Helicase C-terminal.
+At position 109 to 155, the domain is characterized as F-box.
+At position 1 to 550, the domain is characterized as SMP-LTD.
+At position 283 to 490, the domain is characterized as Ku.
+At position 595 to 629, the domain is characterized as SAP.
+At position 607 to 781, the domain is characterized as RNase III 1.
+At position 833 to 957, the domain is characterized as RNase III 2.
+At position 984 to 1059, the domain is characterized as DRBM.
+At position 23 to 123, the domain is characterized as Cytochrome c.
+At position 86 to 119, the domain is characterized as Orange.
+At position 211 to 436, the domain is characterized as MIF4G.
+At position 622 to 744, the domain is characterized as MI.
+At position 2 to 126, the domain is characterized as PINc.
+At position 79 to 219, the domain is characterized as PLAT.
+At position 223 to 932, the domain is characterized as Lipoxygenase.
+At position 51 to 340, the domain is characterized as AB hydrolase-1.
+At position 1 to 166, the domain is characterized as SPX.
+At position 717 to 1048, the domain is characterized as GP-PDE.
+At position 6 to 72, the domain is characterized as Cytochrome b5 heme-binding.
+At position 541 to 604, the domain is characterized as bZIP.
+At position 178 to 270, the domain is characterized as Fibronectin type-III 1.
+At position 383 to 479, the domain is characterized as Fibronectin type-III 2.
+At position 63 to 247, the domain is characterized as uDENN.
+At position 273 to 393, the domain is characterized as cDENN.
+At position 395 to 528, the domain is characterized as dDENN.
+At position 172 to 241, the domain is characterized as KH.
+At position 300 to 392, the domain is characterized as HD.
+At position 239 to 340, the domain is characterized as BEN 1.
+At position 384 to 484, the domain is characterized as BEN 2.
+At position 547 to 647, the domain is characterized as BEN 3.
+At position 712 to 813, the domain is characterized as BEN 4.
+At position 156 to 265, the domain is characterized as S1 motif 1.
+At position 283 to 351, the domain is characterized as S1 motif 2.
+At position 362 to 431, the domain is characterized as S1 motif 3.
+At position 352 to 631, the domain is characterized as Protein kinase.
+At position 13 to 158, the domain is characterized as uDENN.
+At position 178 to 348, the domain is characterized as Helicase ATP-binding.
+At position 358 to 518, the domain is characterized as Helicase C-terminal.
+At position 25 to 282, the domain is characterized as OBG-type G.
+At position 303 to 386, the domain is characterized as TGS.
+At position 31 to 93, the domain is characterized as SLH 1.
+At position 94 to 151, the domain is characterized as SLH 2.
+At position 152 to 214, the domain is characterized as SLH 3.
+At position 607 to 667, the domain is characterized as TSP type-1 5.
+At position 703 to 762, the domain is characterized as TSP type-1 6.
+At position 763 to 825, the domain is characterized as TSP type-1 7.
+At position 836 to 938, the domain is characterized as Ig-like C2-type 1.
+At position 1139 to 1241, the domain is characterized as Ig-like C2-type 2.
+At position 1261 to 1352, the domain is characterized as Ig-like C2-type 3.
+At position 1378 to 1468, the domain is characterized as Ig-like C2-type 4.
+At position 1528 to 1591, the domain is characterized as TSP type-1 8.
+At position 1649 to 1709, the domain is characterized as TSP type-1 9.
+At position 1709 to 1745, the domain is characterized as PLAC.
+At position 131 to 207, the domain is characterized as PUA.
+At position 6 to 134, the domain is characterized as RNase III.
+At position 42 to 179, the domain is characterized as Guanylate cyclase 1.
+At position 293 to 418, the domain is characterized as Guanylate cyclase 2.
+At position 5 to 80, the domain is characterized as Sm.
+At position 292 to 347, the domain is characterized as LIM zinc-binding.
+At position 20 to 249, the domain is characterized as RNase H type-2.
+At position 1 to 61, the domain is characterized as KRAB.
+At position 1 to 134, the domain is characterized as CID.
+At position 281 to 344, the domain is characterized as FHA.
+At position 310 to 388, the domain is characterized as RRM 2.
+At position 493 to 565, the domain is characterized as RRM 3.
+At position 617 to 700, the domain is characterized as RRM 4.
+At position 717 to 794, the domain is characterized as RRM 5.
+At position 51 to 123, the domain is characterized as KRAB.
+At position 80 to 254, the domain is characterized as Helicase ATP-binding.
+At position 12 to 90, the domain is characterized as RRM.
+At position 59 to 133, the domain is characterized as U-box.
+At position 706 to 796, the domain is characterized as HTH La-type RNA-binding.
+At position 30 to 264, the domain is characterized as ABC transporter.
+At position 37 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 113, the domain is characterized as Glutaredoxin.
+At position 26 to 56, the domain is characterized as EF-hand 1.
+At position 93 to 156, the domain is characterized as EF-hand 3; atypical; contains an insert of 28 residues.
+At position 165 to 200, the domain is characterized as EF-hand 4.
+At position 293 to 440, the domain is characterized as Ferric oxidoreductase.
+At position 441 to 577, the domain is characterized as FAD-binding FR-type.
+At position 7 to 207, the domain is characterized as AMMECR1.
+At position 14 to 128, the domain is characterized as Response regulatory.
+At position 64 to 250, the domain is characterized as tr-type G.
+At position 4 to 80, the domain is characterized as SH3.
+At position 109 to 291, the domain is characterized as Rho-GAP.
+At position 326 to 421, the domain is characterized as SH2 1.
+At position 618 to 712, the domain is characterized as SH2 2.
+At position 36 to 71, the domain is characterized as EF-hand 1.
+At position 75 to 106, the domain is characterized as EF-hand 2.
+At position 64 to 160, the domain is characterized as Ig-like C2-type 1.
+At position 166 to 253, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 342, the domain is characterized as Ig-like C2-type 3.
+At position 347 to 440, the domain is characterized as Ig-like C2-type 4.
+At position 450 to 531, the domain is characterized as Ig-like C2-type 5.
+At position 558 to 652, the domain is characterized as Fibronectin type-III 1.
+At position 671 to 766, the domain is characterized as Fibronectin type-III 2.
+At position 771 to 869, the domain is characterized as Fibronectin type-III 3.
+At position 4 to 280, the domain is characterized as DegV.
+At position 153 to 400, the domain is characterized as NR LBD.
+At position 126 to 369, the domain is characterized as Radical SAM core.
+At position 30 to 77, the domain is characterized as SERTA.
+At position 18 to 151, the domain is characterized as Ephrin RBD.
+At position 25 to 146, the domain is characterized as CUB 1.
+At position 154 to 265, the domain is characterized as CUB 2.
+At position 276 to 519, the domain is characterized as ZP.
+At position 40 to 153, the domain is characterized as tRNA-binding.
+At position 78 to 120, the domain is characterized as CAP-Gly 1.
+At position 231 to 273, the domain is characterized as CAP-Gly 2.
+At position 32 to 445, the domain is characterized as GRAS.
+At position 112 to 289, the domain is characterized as Rho-GAP.
+At position 324 to 419, the domain is characterized as SH2 1.
+At position 616 to 710, the domain is characterized as SH2 2.
+At position 165 to 390, the domain is characterized as tr-type G.
+At position 131 to 319, the domain is characterized as Helicase ATP-binding.
+At position 350 to 539, the domain is characterized as Helicase C-terminal.
+At position 607 to 665, the domain is characterized as RAP.
+At position 43 to 83, the domain is characterized as EGF-like 1; calcium-binding.
+At position 84 to 125, the domain is characterized as EGF-like 2; calcium-binding.
+At position 126 to 162, the domain is characterized as EGF-like 3; calcium-binding.
+At position 175 to 211, the domain is characterized as EGF-like 4.
+At position 215 to 250, the domain is characterized as EGF-like 5.
+At position 284 to 319, the domain is characterized as EGF-like 6.
+At position 321 to 361, the domain is characterized as EGF-like 7; calcium-binding.
+At position 362 to 400, the domain is characterized as EGF-like 8; calcium-binding.
+At position 401 to 441, the domain is characterized as EGF-like 9; calcium-binding.
+At position 807 to 919, the domain is characterized as CUB.
+At position 53 to 212, the domain is characterized as TNase-like.
+At position 8 to 198, the domain is characterized as Peptidase M12B.
+At position 7 to 228, the domain is characterized as ABC transporter.
+At position 121 to 170, the domain is characterized as UPAR/Ly6.
+At position 158 to 732, the domain is characterized as TBDR beta-barrel.
+At position 290 to 367, the domain is characterized as SWIB/MDM2.
+At position 204 to 256, the domain is characterized as bHLH.
+At position 2 to 129, the domain is characterized as Response regulatory.
+At position 32 to 420, the domain is characterized as Helicase ATP-binding.
+At position 643 to 678, the domain is characterized as UVR.
+At position 411 to 460, the domain is characterized as bHLH.
+At position 452 to 511, the domain is characterized as Collagen-like 1.
+At position 7 to 139, the domain is characterized as HTH marR-type.
+At position 25 to 104, the domain is characterized as Pentapeptide repeat 1.
+At position 117 to 191, the domain is characterized as Pentapeptide repeat 2.
+At position 11 to 91, the domain is characterized as PDZ 1.
+At position 7 to 148, the domain is characterized as RNase H type-1.
+At position 37 to 295, the domain is characterized as Protein kinase.
+At position 26 to 196, the domain is characterized as Helicase ATP-binding.
+At position 235 to 435, the domain is characterized as Helicase C-terminal.
+At position 520 to 626, the domain is characterized as CBM20.
+At position 204 to 259, the domain is characterized as LRRCT.
+At position 260 to 361, the domain is characterized as Ig-like C2-type.
+At position 363 to 419, the domain is characterized as FHA.
+At position 36 to 114, the domain is characterized as RRM 1.
+At position 124 to 201, the domain is characterized as RRM 2.
+At position 215 to 292, the domain is characterized as RRM 3.
+At position 318 to 395, the domain is characterized as RRM 4.
+At position 739 to 819, the domain is characterized as ERCC4.
+At position 243 to 433, the domain is characterized as GATase cobBQ-type.
+At position 224 to 339, the domain is characterized as N-terminal Ras-GEF.
+At position 412 to 640, the domain is characterized as Ras-GEF.
+At position 368 to 578, the domain is characterized as NR LBD.
+At position 960 to 1051, the domain is characterized as SH2.
+At position 1063 to 1318, the domain is characterized as Protein kinase.
+At position 156 to 377, the domain is characterized as Radical SAM core.
+At position 411 to 616, the domain is characterized as Helicase ATP-binding.
+At position 627 to 790, the domain is characterized as Helicase C-terminal.
+At position 673 to 888, the domain is characterized as Rho-GAP.
+At position 570 to 658, the domain is characterized as GED.
+At position 16 to 60, the domain is characterized as UBA.
+At position 271 to 336, the domain is characterized as SH3.
+At position 10 to 440, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 944 to 1267, the domain is characterized as PKS/mFAS DH.
+At position 2346 to 2423, the domain is characterized as Carrier.
+At position 1 to 431, the domain is characterized as SMP-LTD.
+At position 37 to 85, the domain is characterized as F-box.
+At position 2 to 412, the domain is characterized as Helicase ATP-binding.
+At position 12 to 132, the domain is characterized as VOC 1.
+At position 162 to 313, the domain is characterized as VOC 2.
+At position 154 to 344, the domain is characterized as CheB-type methylesterase.
+At position 102 to 279, the domain is characterized as TLC.
+At position 6 to 29, the domain is characterized as Peptidase M12B.
+At position 92 to 159, the domain is characterized as BTB.
+At position 194 to 296, the domain is characterized as BACK.
+At position 281 to 472, the domain is characterized as PNPLA.
+At position 30 to 74, the domain is characterized as PSI.
+At position 132 to 310, the domain is characterized as VWFA.
+At position 981 to 1086, the domain is characterized as Calx-beta.
+At position 1131 to 1220, the domain is characterized as Fibronectin type-III 1.
+At position 1224 to 1323, the domain is characterized as Fibronectin type-III 2.
+At position 1526 to 1621, the domain is characterized as Fibronectin type-III 3.
+At position 1639 to 1735, the domain is characterized as Fibronectin type-III 4.
+At position 361 to 534, the domain is characterized as Helicase ATP-binding.
+At position 561 to 719, the domain is characterized as Helicase C-terminal.
+At position 60 to 368, the domain is characterized as tr-type G.
+At position 30 to 174, the domain is characterized as MARVEL.
+At position 23 to 52, the domain is characterized as LRRNT.
+At position 300 to 348, the domain is characterized as LRRCT.
+At position 96 to 147, the domain is characterized as bHLH.
+At position 249 to 417, the domain is characterized as PCI.
+At position 36 to 233, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 466, the domain is characterized as Sema.
+At position 803 to 893, the domain is characterized as IPT/TIG 1.
+At position 895 to 980, the domain is characterized as IPT/TIG 2.
+At position 983 to 1092, the domain is characterized as IPT/TIG 3.
+At position 292 to 410, the domain is characterized as Nop.
+At position 74 to 244, the domain is characterized as VWFA.
+At position 256 to 338, the domain is characterized as IPT/TIG.
+At position 34 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 35 to 141, the domain is characterized as Ig-like V-type.
+At position 145 to 234, the domain is characterized as Ig-like C2-type 1.
+At position 327 to 411, the domain is characterized as Ig-like C2-type 3.
+At position 98 to 194, the domain is characterized as Plastocyanin-like 1.
+At position 404 to 526, the domain is characterized as Plastocyanin-like 2.
+At position 36 to 99, the domain is characterized as Fibronectin type-III 1.
+At position 100 to 195, the domain is characterized as Fibronectin type-III 2.
+At position 199 to 294, the domain is characterized as Fibronectin type-III 3.
+At position 350 to 438, the domain is characterized as Fibronectin type-III 4.
+At position 441 to 539, the domain is characterized as Fibronectin type-III 5.
+At position 514 to 606, the domain is characterized as Fibronectin type-III 6.
+At position 610 to 705, the domain is characterized as Fibronectin type-III 7.
+At position 710 to 799, the domain is characterized as Fibronectin type-III 8.
+At position 804 to 894, the domain is characterized as Fibronectin type-III 9.
+At position 899 to 988, the domain is characterized as Fibronectin type-III 10.
+At position 993 to 1093, the domain is characterized as Fibronectin type-III 11.
+At position 1098 to 1190, the domain is characterized as Fibronectin type-III 12.
+At position 1192 to 1282, the domain is characterized as Fibronectin type-III 13.
+At position 1287 to 1380, the domain is characterized as Fibronectin type-III 14.
+At position 1384 to 1470, the domain is characterized as Fibronectin type-III 15.
+At position 1474 to 1578, the domain is characterized as Fibronectin type-III 16.
+At position 1583 to 1681, the domain is characterized as Fibronectin type-III 17.
+At position 1686 to 1787, the domain is characterized as Fibronectin type-III 18.
+At position 2036 to 2292, the domain is characterized as Tyrosine-protein phosphatase.
+At position 167 to 581, the domain is characterized as Protein kinase.
+At position 121 to 271, the domain is characterized as Tyrosine-protein phosphatase.
+At position 8 to 78, the domain is characterized as PAH 1.
+At position 94 to 164, the domain is characterized as PAH 2.
+At position 283 to 351, the domain is characterized as PAH 3.
+At position 415 to 449, the domain is characterized as ShKT.
+At position 35 to 165, the domain is characterized as TsaA-like.
+At position 243 to 435, the domain is characterized as PNPLA.
+At position 354 to 415, the domain is characterized as S4 RNA-binding.
+At position 266 to 341, the domain is characterized as PUA.
+At position 30 to 236, the domain is characterized as Reticulon.
+At position 176 to 220, the domain is characterized as DSL.
+At position 225 to 253, the domain is characterized as EGF-like 1.
+At position 256 to 284, the domain is characterized as EGF-like 2.
+At position 291 to 324, the domain is characterized as EGF-like 3.
+At position 331 to 362, the domain is characterized as EGF-like 4; calcium-binding.
+At position 369 to 401, the domain is characterized as EGF-like 5.
+At position 408 to 439, the domain is characterized as EGF-like 6.
+At position 446 to 477, the domain is characterized as EGF-like 7; calcium-binding.
+At position 484 to 515, the domain is characterized as EGF-like 8.
+At position 123 to 185, the domain is characterized as t-SNARE coiled-coil homology.
+At position 110 to 160, the domain is characterized as DHHC.
+At position 496 to 559, the domain is characterized as bZIP.
+At position 39 to 116, the domain is characterized as Inhibitor I9.
+At position 121 to 606, the domain is characterized as Peptidase S8.
+At position 91 to 171, the domain is characterized as ACT 1.
+At position 206 to 276, the domain is characterized as ACT 2.
+At position 26 to 247, the domain is characterized as ABC transporter.
+At position 162 to 362, the domain is characterized as Helicase ATP-binding.
+At position 421 to 565, the domain is characterized as Helicase C-terminal.
+At position 103 to 302, the domain is characterized as ATP-grasp.
+At position 39 to 138, the domain is characterized as Phytocyanin.
+At position 278 to 514, the domain is characterized as NR LBD.
+At position 1 to 128, the domain is characterized as RNase H type-1.
+At position 233 to 447, the domain is characterized as DHFR.
+At position 31 to 158, the domain is characterized as PLAT.
+At position 268 to 365, the domain is characterized as BEN.
+At position 47 to 316, the domain is characterized as Septin-type G.
+At position 7 to 115, the domain is characterized as STAS.
+At position 51 to 316, the domain is characterized as Protein kinase.
+At position 527 to 584, the domain is characterized as Collagen-like 2.
+At position 567 to 623, the domain is characterized as Collagen-like 3.
+At position 728 to 781, the domain is characterized as Collagen-like 4.
+At position 1427 to 1482, the domain is characterized as Collagen-like 5.
+At position 1481 to 1539, the domain is characterized as Collagen-like 6.
+At position 4 to 275, the domain is characterized as Pyruvate carboxyltransferase.
+At position 676 to 731, the domain is characterized as DEK-C.
+At position 77 to 221, the domain is characterized as UBC core.
+At position 59 to 254, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 141, the domain is characterized as Rhodanese 1.
+At position 176 to 292, the domain is characterized as Rhodanese 2.
+At position 504 to 579, the domain is characterized as PUA.
+At position 35 to 113, the domain is characterized as Inhibitor I9.
+At position 125 to 398, the domain is characterized as Peptidase S8.
+At position 161 to 285, the domain is characterized as GST C-terminal.
+At position 134 to 191, the domain is characterized as VWFC 1.
+At position 192 to 251, the domain is characterized as VWFC 2.
+At position 313 to 370, the domain is characterized as VWFC 4.
+At position 371 to 425, the domain is characterized as VWFC 5.
+At position 426 to 485, the domain is characterized as VWFC 6.
+At position 486 to 544, the domain is characterized as VWFC 7.
+At position 545 to 602, the domain is characterized as VWFC 8.
+At position 603 to 661, the domain is characterized as VWFC 9.
+At position 665 to 724, the domain is characterized as VWFC 10.
+At position 725 to 781, the domain is characterized as VWFC 11.
+At position 782 to 840, the domain is characterized as VWFC 12.
+At position 841 to 902, the domain is characterized as VWFC 13.
+At position 903 to 958, the domain is characterized as VWFC 14.
+At position 959 to 1016, the domain is characterized as VWFC 15.
+At position 1017 to 1084, the domain is characterized as VWFC 16.
+At position 1085 to 1144, the domain is characterized as VWFC 17.
+At position 1148 to 1208, the domain is characterized as VWFC 18.
+At position 1212 to 1388, the domain is characterized as VWFD.
+At position 1489 to 1542, the domain is characterized as TIL.
+At position 35 to 180, the domain is characterized as PLAT.
+At position 183 to 886, the domain is characterized as Lipoxygenase.
+At position 301 to 588, the domain is characterized as Protein kinase.
+At position 91 to 350, the domain is characterized as Protein kinase.
+At position 351 to 426, the domain is characterized as AGC-kinase C-terminal.
+At position 48 to 112, the domain is characterized as HMA.
+At position 1 to 33, the domain is characterized as LDL-receptor class A 1.
+At position 36 to 74, the domain is characterized as LDL-receptor class A 2.
+At position 77 to 113, the domain is characterized as LDL-receptor class A 3.
+At position 116 to 154, the domain is characterized as LDL-receptor class A 4.
+At position 167 to 203, the domain is characterized as LDL-receptor class A 5.
+At position 206 to 242, the domain is characterized as LDL-receptor class A 6.
+At position 246 to 285, the domain is characterized as LDL-receptor class A 7.
+At position 285 to 324, the domain is characterized as EGF-like 1.
+At position 325 to 357, the domain is characterized as EGF-like 2; calcium-binding.
+At position 78 to 200, the domain is characterized as PLAT.
+At position 203 to 899, the domain is characterized as Lipoxygenase.
+At position 122 to 216, the domain is characterized as Rhodanese.
+At position 7 to 58, the domain is characterized as HTH psq-type.
+At position 16 to 269, the domain is characterized as F-BAR.
+At position 607 to 670, the domain is characterized as SH3.
+At position 117 to 336, the domain is characterized as Radical SAM core.
+At position 27 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 124 to 218, the domain is characterized as Ig-like C2-type 2.
+At position 32 to 98, the domain is characterized as BTB.
+At position 16 to 134, the domain is characterized as MTTase N-terminal.
+At position 157 to 387, the domain is characterized as Radical SAM core.
+At position 390 to 452, the domain is characterized as TRAM.
+At position 62 to 218, the domain is characterized as N-acetyltransferase.
+At position 233 to 502, the domain is characterized as CN hydrolase.
+At position 1509 to 2066, the domain is characterized as FAT.
+At position 2184 to 2508, the domain is characterized as PI3K/PI4K catalytic.
+At position 2485 to 2517, the domain is characterized as FATC.
+At position 50 to 90, the domain is characterized as Fibronectin type-I 1.
+At position 95 to 138, the domain is characterized as Fibronectin type-I 2.
+At position 139 to 182, the domain is characterized as Fibronectin type-I 3.
+At position 184 to 228, the domain is characterized as Fibronectin type-I 4.
+At position 229 to 273, the domain is characterized as Fibronectin type-I 5.
+At position 306 to 345, the domain is characterized as Fibronectin type-I 6.
+At position 355 to 403, the domain is characterized as Fibronectin type-II 1.
+At position 415 to 463, the domain is characterized as Fibronectin type-II 2.
+At position 468 to 511, the domain is characterized as Fibronectin type-I 7.
+At position 516 to 558, the domain is characterized as Fibronectin type-I 8.
+At position 559 to 602, the domain is characterized as Fibronectin type-I 9.
+At position 610 to 702, the domain is characterized as Fibronectin type-III 1.
+At position 722 to 812, the domain is characterized as Fibronectin type-III 2.
+At position 813 to 904, the domain is characterized as Fibronectin type-III 3.
+At position 909 to 998, the domain is characterized as Fibronectin type-III 4.
+At position 999 to 1088, the domain is characterized as Fibronectin type-III 5.
+At position 1089 to 1175, the domain is characterized as Fibronectin type-III 6.
+At position 1176 to 1270, the domain is characterized as Fibronectin type-III 7.
+At position 1271 to 1359, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1360 to 1452, the domain is characterized as Fibronectin type-III 9.
+At position 1453 to 1540, the domain is characterized as Fibronectin type-III 10.
+At position 1541 to 1634, the domain is characterized as Fibronectin type-III 11.
+At position 1635 to 1726, the domain is characterized as Fibronectin type-III 12.
+At position 1727 to 1814, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1815 to 1908, the domain is characterized as Fibronectin type-III 14.
+At position 1909 to 1995, the domain is characterized as Fibronectin type-III 15.
+At position 1996 to 2086, the domain is characterized as Fibronectin type-III 16.
+At position 2194 to 2288, the domain is characterized as Fibronectin type-III 17.
+At position 2295 to 2339, the domain is characterized as Fibronectin type-I 10.
+At position 2340 to 2382, the domain is characterized as Fibronectin type-I 11.
+At position 2384 to 2427, the domain is characterized as Fibronectin type-I 12.
+At position 6 to 201, the domain is characterized as Peptidase M12B.
+At position 139 to 219, the domain is characterized as RRM 1.
+At position 337 to 414, the domain is characterized as RRM 2.
+At position 418 to 492, the domain is characterized as RRM 3.
+At position 711 to 889, the domain is characterized as SPOC.
+At position 226 to 431, the domain is characterized as PCI.
+At position 254 to 442, the domain is characterized as GATase cobBQ-type.
+At position 187 to 236, the domain is characterized as GRAM 1.
+At position 238 to 336, the domain is characterized as PH.
+At position 570 to 636, the domain is characterized as GRAM 2.
+At position 68 to 253, the domain is characterized as Reticulon.
+At position 87 to 277, the domain is characterized as Rab-GAP TBC.
+At position 449 to 546, the domain is characterized as SWIRM.
+At position 618 to 669, the domain is characterized as SANT.
+At position 1045 to 1528, the domain is characterized as FAT.
+At position 1746 to 2091, the domain is characterized as PI3K/PI4K catalytic.
+At position 2281 to 2313, the domain is characterized as FATC.
+At position 17 to 281, the domain is characterized as Protein kinase.
+At position 365 to 422, the domain is characterized as L27 1.
+At position 428 to 479, the domain is characterized as L27 2.
+At position 545 to 620, the domain is characterized as PDZ.
+At position 633 to 717, the domain is characterized as SH3.
+At position 774 to 946, the domain is characterized as Guanylate kinase-like.
+At position 152 to 274, the domain is characterized as MPN.
+At position 15 to 117, the domain is characterized as PH.
+At position 155 to 259, the domain is characterized as IRS-type PTB.
+At position 22 to 103, the domain is characterized as Core-binding (CB).
+At position 124 to 304, the domain is characterized as Tyr recombinase.
+At position 32 to 110, the domain is characterized as GIY-YIG.
+At position 44 to 93, the domain is characterized as bHLH.
+At position 210 to 451, the domain is characterized as Peptidase S1.
+At position 178 to 346, the domain is characterized as JmjC.
+At position 1059 to 1105, the domain is characterized as F-box.
+At position 619 to 708, the domain is characterized as BRCT.
+At position 186 to 241, the domain is characterized as Myb-like.
+At position 561 to 639, the domain is characterized as TFIIS N-terminal.
+At position 10 to 109, the domain is characterized as PINc.
+At position 2 to 119, the domain is characterized as TRM112.
+At position 366 to 425, the domain is characterized as PAP-associated.
+At position 73 to 281, the domain is characterized as SMP-LTD.
+At position 141 to 243, the domain is characterized as PPIase FKBP-type.
+At position 51 to 396, the domain is characterized as GH10.
+At position 1327 to 1444, the domain is characterized as SET.
+At position 1453 to 1468, the domain is characterized as Post-SET.
+At position 21 to 101, the domain is characterized as GST N-terminal.
+At position 106 to 234, the domain is characterized as GST C-terminal.
+At position 56 to 292, the domain is characterized as Radical SAM core.
+At position 5 to 191, the domain is characterized as Prephenate dehydratase.
+At position 205 to 282, the domain is characterized as ACT.
+At position 464 to 884, the domain is characterized as FH2.
+At position 24 to 144, the domain is characterized as Bulb-type lectin.
+At position 334 to 416, the domain is characterized as PAN.
+At position 527 to 816, the domain is characterized as Protein kinase.
+At position 212 to 264, the domain is characterized as HAMP.
+At position 269 to 505, the domain is characterized as Methyl-accepting transducer.
+At position 145 to 209, the domain is characterized as S1 motif.
+At position 312 to 379, the domain is characterized as KH.
+At position 2 to 94, the domain is characterized as RRM 1.
+At position 345 to 423, the domain is characterized as RRM 2.
+At position 532 to 604, the domain is characterized as RRM 3.
+At position 663 to 746, the domain is characterized as RRM 4.
+At position 763 to 840, the domain is characterized as RRM 5.
+At position 84 to 413, the domain is characterized as Asparaginase/glutaminase.
+At position 104 to 304, the domain is characterized as ATP-grasp.
+At position 111 to 170, the domain is characterized as CBS 1.
+At position 174 to 230, the domain is characterized as CBS 2.
+At position 11 to 289, the domain is characterized as F-BAR.
+At position 542 to 603, the domain is characterized as SH3 1.
+At position 658 to 721, the domain is characterized as SH3 2.
+At position 149 to 353, the domain is characterized as ATP-grasp.
+At position 177 to 240, the domain is characterized as bZIP.
+At position 351 to 430, the domain is characterized as Ubiquitin-like 1.
+At position 431 to 507, the domain is characterized as Ubiquitin-like 2.
+At position 275 to 488, the domain is characterized as ELMO.
+At position 98 to 297, the domain is characterized as MAGE.
+At position 31 to 134, the domain is characterized as Cadherin 1.
+At position 582 to 679, the domain is characterized as Cadherin 6.
+At position 57 to 243, the domain is characterized as BPL/LPL catalytic.
+At position 3 to 55, the domain is characterized as F-box.
+At position 34 to 188, the domain is characterized as SIS.
+At position 693 to 773, the domain is characterized as ACT 1.
+At position 800 to 873, the domain is characterized as ACT 2.
+At position 194 to 392, the domain is characterized as Peptidase M12B.
+At position 400 to 484, the domain is characterized as Disintegrin.
+At position 223 to 482, the domain is characterized as Olfactomedin-like.
+At position 537 to 666, the domain is characterized as MPN.
+At position 127 to 377, the domain is characterized as Radical SAM core.
+At position 336 to 397, the domain is characterized as S4 RNA-binding.
+At position 47 to 146, the domain is characterized as Ig-like V-type.
+At position 144 to 228, the domain is characterized as Ig-like C2-type.
+At position 20 to 96, the domain is characterized as Cytochrome b5 heme-binding.
+At position 97 to 311, the domain is characterized as TLC.
+At position 1 to 187, the domain is characterized as Macro.
+At position 297 to 445, the domain is characterized as CRAL-TRIO.
+At position 423 to 495, the domain is characterized as PAS.
+At position 7 to 116, the domain is characterized as MaoC-like.
+At position 142 to 356, the domain is characterized as BURP.
+At position 221 to 377, the domain is characterized as TrmE-type G.
+At position 522 to 585, the domain is characterized as bZIP.
+At position 218 to 375, the domain is characterized as TrmE-type G.
+At position 20 to 120, the domain is characterized as Ig-like.
+At position 106 to 345, the domain is characterized as Radical SAM core.
+At position 84 to 138, the domain is characterized as bHLH.
+At position 159 to 349, the domain is characterized as OBG-type G.
+At position 114 to 191, the domain is characterized as PRC barrel.
+At position 22 to 199, the domain is characterized as EngB-type G.
+At position 389 to 502, the domain is characterized as PAZ.
+At position 668 to 959, the domain is characterized as Piwi.
+At position 150 to 412, the domain is characterized as Protein kinase.
+At position 455 to 491, the domain is characterized as EF-hand 1.
+At position 492 to 527, the domain is characterized as EF-hand 2.
+At position 528 to 567, the domain is characterized as EF-hand 3.
+At position 570 to 599, the domain is characterized as EF-hand 4.
+At position 8 to 60, the domain is characterized as Myosin N-terminal SH3-like.
+At position 69 to 762, the domain is characterized as Myosin motor.
+At position 765 to 794, the domain is characterized as IQ 1.
+At position 788 to 817, the domain is characterized as IQ 2.
+At position 813 to 842, the domain is characterized as IQ 3.
+At position 836 to 865, the domain is characterized as IQ 4.
+At position 861 to 890, the domain is characterized as IQ 5.
+At position 884 to 913, the domain is characterized as IQ 6.
+At position 1496 to 1773, the domain is characterized as Dilute.
+At position 2 to 187, the domain is characterized as RNase H type-2.
+At position 14 to 283, the domain is characterized as tr-type G.
+At position 136 to 422, the domain is characterized as Tyr recombinase Flp-type.
+At position 502 to 807, the domain is characterized as Protein kinase.
+At position 808 to 874, the domain is characterized as AGC-kinase C-terminal.
+At position 8 to 55, the domain is characterized as RPE1 insert.
+At position 310 to 359, the domain is characterized as bHLH.
+At position 74 to 130, the domain is characterized as CBS 1.
+At position 252 to 310, the domain is characterized as CBS 2.
+At position 130 to 364, the domain is characterized as NR LBD.
+At position 106 to 138, the domain is characterized as EGF-like 1.
+At position 274 to 328, the domain is characterized as TB 1.
+At position 352 to 392, the domain is characterized as EGF-like 2; calcium-binding.
+At position 400 to 452, the domain is characterized as TB 2.
+At position 571 to 612, the domain is characterized as EGF-like 3.
+At position 613 to 656, the domain is characterized as EGF-like 4; calcium-binding.
+At position 657 to 699, the domain is characterized as EGF-like 5; calcium-binding.
+At position 741 to 781, the domain is characterized as EGF-like 6; calcium-binding.
+At position 782 to 822, the domain is characterized as EGF-like 7; calcium-binding.
+At position 823 to 861, the domain is characterized as EGF-like 8; calcium-binding.
+At position 863 to 905, the domain is characterized as EGF-like 9; calcium-binding.
+At position 914 to 968, the domain is characterized as TB 3.
+At position 990 to 1032, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1033 to 1072, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1086 to 1136, the domain is characterized as TB 4.
+At position 1204 to 1231, the domain is characterized as EGF-like 12; calcium-binding.
+At position 251 to 286, the domain is characterized as DMA.
+At position 794 to 925, the domain is characterized as Ricin B-type lectin.
+At position 49 to 340, the domain is characterized as YjeF C-terminal.
+At position 140 to 316, the domain is characterized as TNase-like.
+At position 30 to 200, the domain is characterized as Helicase ATP-binding.
+At position 223 to 365, the domain is characterized as Helicase C-terminal.
+At position 370 to 519, the domain is characterized as MATH.
+At position 1 to 86, the domain is characterized as FAD-binding FR-type.
+At position 579 to 852, the domain is characterized as Protein kinase.
+At position 53 to 340, the domain is characterized as tr-type G.
+At position 139 to 443, the domain is characterized as NB-ARC.
+At position 21 to 140, the domain is characterized as DSCP-N.
+At position 184 to 206, the domain is characterized as Follistatin-like 1.
+At position 220 to 243, the domain is characterized as Follistatin-like 2.
+At position 267 to 289, the domain is characterized as Follistatin-like 3.
+At position 297 to 319, the domain is characterized as Follistatin-like 4.
+At position 331 to 359, the domain is characterized as Follistatin-like 5.
+At position 394 to 416, the domain is characterized as Follistatin-like 6.
+At position 122 to 199, the domain is characterized as Sm.
+At position 163 to 446, the domain is characterized as ABC transmembrane type-1.
+At position 479 to 718, the domain is characterized as ABC transporter.
+At position 158 to 218, the domain is characterized as KH.
+At position 285 to 378, the domain is characterized as HD.
+At position 359 to 426, the domain is characterized as S4 RNA-binding.
+At position 18 to 135, the domain is characterized as Glutaredoxin.
+At position 128 to 212, the domain is characterized as PB1.
+At position 183 to 256, the domain is characterized as HTH crp-type.
+At position 2 to 91, the domain is characterized as CS.
+At position 6 to 73, the domain is characterized as Trm1 methyltransferase.
+At position 159 to 617, the domain is characterized as TBDR beta-barrel.
+At position 278 to 478, the domain is characterized as ERCC4.
+At position 5 to 250, the domain is characterized as Radical SAM core.
+At position 315 to 482, the domain is characterized as tr-type G.
+At position 37 to 208, the domain is characterized as Helicase ATP-binding.
+At position 232 to 379, the domain is characterized as Helicase C-terminal.
+At position 70 to 190, the domain is characterized as PINc.
+At position 104 to 377, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 746 to 921, the domain is characterized as Helicase ATP-binding.
+At position 944 to 1093, the domain is characterized as Helicase C-terminal.
+At position 1283 to 1363, the domain is characterized as HRDC.
+At position 84 to 140, the domain is characterized as AWS.
+At position 142 to 259, the domain is characterized as SET.
+At position 266 to 282, the domain is characterized as Post-SET.
+At position 558 to 592, the domain is characterized as WW.
+At position 115 to 257, the domain is characterized as Clp R.
+At position 532 to 567, the domain is characterized as UVR.
+At position 242 to 411, the domain is characterized as tr-type G.
+At position 59 to 187, the domain is characterized as Thioredoxin.
+At position 82 to 255, the domain is characterized as Helicase ATP-binding.
+At position 283 to 428, the domain is characterized as Helicase C-terminal.
+At position 246 to 297, the domain is characterized as SANT.
+At position 458 to 540, the domain is characterized as PDZ.
+At position 23 to 155, the domain is characterized as Cyclin N-terminal.
+At position 422 to 541, the domain is characterized as PH.
+At position 583 to 839, the domain is characterized as Protein kinase.
+At position 296 to 434, the domain is characterized as N-acetyltransferase.
+At position 95 to 266, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 318, the domain is characterized as 5'-3' exonuclease.
+At position 319 to 531, the domain is characterized as 3'-5' exonuclease.
+At position 20 to 120, the domain is characterized as Ig-like V-type.
+At position 449 to 627, the domain is characterized as Helicase ATP-binding.
+At position 638 to 802, the domain is characterized as Helicase C-terminal.
+At position 25 to 131, the domain is characterized as VOC 1.
+At position 167 to 282, the domain is characterized as VOC 2.
+At position 54 to 169, the domain is characterized as DOMON.
+At position 176 to 255, the domain is characterized as Cytochrome b561.
+At position 4 to 117, the domain is characterized as VOC.
+At position 55 to 119, the domain is characterized as Ubiquitin-like.
+At position 335 to 412, the domain is characterized as RRM 4.
+At position 537 to 618, the domain is characterized as PABC.
+At position 18 to 234, the domain is characterized as ABC transporter.
+At position 230 to 290, the domain is characterized as CBS 1.
+At position 312 to 370, the domain is characterized as CBS 2.
+At position 385 to 447, the domain is characterized as CBS 3.
+At position 459 to 517, the domain is characterized as CBS 4.
+At position 435 to 774, the domain is characterized as HECT.
+At position 135 to 333, the domain is characterized as ATP-grasp.
+At position 18 to 116, the domain is characterized as Phytocyanin.
+At position 249 to 366, the domain is characterized as C2.
+At position 398 to 604, the domain is characterized as Rho-GAP.
+At position 67 to 139, the domain is characterized as S1 motif.
+At position 151 to 217, the domain is characterized as KH.
+At position 375 to 438, the domain is characterized as bZIP.
+At position 114 to 321, the domain is characterized as ATP-grasp.
+At position 335 to 381, the domain is characterized as G-patch.
+At position 416 to 579, the domain is characterized as Miro 2.
+At position 134 to 310, the domain is characterized as Helicase ATP-binding.
+At position 324 to 484, the domain is characterized as Helicase C-terminal.
+At position 9 to 87, the domain is characterized as GIY-YIG.
+At position 191 to 226, the domain is characterized as UVR.
+At position 490 to 547, the domain is characterized as F-box.
+At position 76 to 389, the domain is characterized as Peptidase A1.
+At position 16 to 369, the domain is characterized as TROVE.
+At position 277 to 305, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 59 to 147, the domain is characterized as BRCT.
+At position 279 to 460, the domain is characterized as UmuC.
+At position 144 to 224, the domain is characterized as Ubiquitin-like.
+At position 246 to 326, the domain is characterized as BAG.
+At position 106 to 292, the domain is characterized as Tyr recombinase.
+At position 7 to 59, the domain is characterized as HTH myb-type 1.
+At position 60 to 114, the domain is characterized as HTH myb-type 2.
+At position 315 to 366, the domain is characterized as GRIP.
+At position 301 to 457, the domain is characterized as PNPLA.
+At position 84 to 369, the domain is characterized as Protein kinase.
+At position 385 to 570, the domain is characterized as Guanylate kinase-like.
+At position 147 to 334, the domain is characterized as CheB-type methylesterase.
+At position 22 to 139, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 262, the domain is characterized as Ig-like C2-type 2.
+At position 406 to 527, the domain is characterized as Ig-like C2-type 4.
+At position 678 to 800, the domain is characterized as Ig-like C2-type 6.
+At position 810 to 934, the domain is characterized as Ig-like C2-type 7.
+At position 951 to 1067, the domain is characterized as Ig-like C2-type 8.
+At position 184 to 264, the domain is characterized as KH.
+At position 10 to 265, the domain is characterized as Protein kinase.
+At position 24 to 217, the domain is characterized as Pentraxin (PTX).
+At position 129 to 227, the domain is characterized as PPIase FKBP-type.
+At position 11 to 222, the domain is characterized as YjeF N-terminal.
+At position 10 to 212, the domain is characterized as YjeF N-terminal.
+At position 18 to 95, the domain is characterized as GIY-YIG.
+At position 146 to 241, the domain is characterized as TAFH.
+At position 168 to 347, the domain is characterized as Helicase ATP-binding.
+At position 380 to 524, the domain is characterized as Helicase C-terminal.
+At position 3 to 232, the domain is characterized as Glutamine amidotransferase type-1.
+At position 57 to 227, the domain is characterized as Helicase ATP-binding.
+At position 88 to 218, the domain is characterized as C-type lectin.
+At position 3 to 200, the domain is characterized as ABC transporter.
+At position 25 to 83, the domain is characterized as HTH cro/C1-type.
+At position 6 to 206, the domain is characterized as ABC transporter.
+At position 90 to 233, the domain is characterized as GST C-terminal.
+At position 1 to 186, the domain is characterized as KARI N-terminal Rossmann.
+At position 91 to 237, the domain is characterized as Clp R.
+At position 20 to 42, the domain is characterized as F-box.
+At position 2 to 133, the domain is characterized as CID.
+At position 504 to 592, the domain is characterized as PDZ.
+At position 988 to 1051, the domain is characterized as SAM.
+At position 55 to 119, the domain is characterized as Sushi 1.
+At position 120 to 179, the domain is characterized as Sushi 2.
+At position 178 to 239, the domain is characterized as Sushi 3.
+At position 241 to 304, the domain is characterized as Sushi 4.
+At position 525 to 576, the domain is characterized as LRRCT.
+At position 1370 to 1543, the domain is characterized as Helicase ATP-binding.
+At position 1725 to 1877, the domain is characterized as Helicase C-terminal.
+At position 54 to 455, the domain is characterized as Glutamine amidotransferase type-2.
+At position 70 to 151, the domain is characterized as Core-binding (CB).
+At position 173 to 379, the domain is characterized as Tyr recombinase.
+At position 220 to 357, the domain is characterized as GAF 1.
+At position 389 to 528, the domain is characterized as GAF 2.
+At position 558 to 882, the domain is characterized as PDEase.
+At position 24 to 85, the domain is characterized as TRAM.
+At position 749 to 805, the domain is characterized as WHEP-TRS 1.
+At position 822 to 878, the domain is characterized as WHEP-TRS 2.
+At position 900 to 956, the domain is characterized as WHEP-TRS 3.
+At position 48 to 277, the domain is characterized as Radical SAM core.
+At position 225 to 451, the domain is characterized as Lon N-terminal.
+At position 450 to 559, the domain is characterized as CULT.
+At position 5 to 92, the domain is characterized as Ig-like C1-type.
+At position 112 to 295, the domain is characterized as Integrase catalytic.
+At position 22 to 91, the domain is characterized as KH type-2.
+At position 431 to 546, the domain is characterized as Toprim.
+At position 8 to 204, the domain is characterized as tr-type G.
+At position 200 to 379, the domain is characterized as ABC transmembrane type-1 1.
+At position 523 to 703, the domain is characterized as ABC transmembrane type-1 2.
+At position 622 to 695, the domain is characterized as S1 motif.
+At position 344 to 421, the domain is characterized as OCT.
+At position 293 to 361, the domain is characterized as Mop.
+At position 404 to 469, the domain is characterized as SAM.
+At position 242 to 360, the domain is characterized as C2 1.
+At position 452 to 569, the domain is characterized as C2 2.
+At position 603 to 724, the domain is characterized as C2 3.
+At position 1 to 435, the domain is characterized as Protein kinase 1.
+At position 1418 to 1488, the domain is characterized as Bromo 1.
+At position 1446 to 1891, the domain is characterized as Protein kinase 2.
+At position 1541 to 1611, the domain is characterized as Bromo 2.
+At position 315 to 454, the domain is characterized as JmjC.
+At position 8 to 134, the domain is characterized as MH1.
+At position 222 to 418, the domain is characterized as MH2.
+At position 30 to 138, the domain is characterized as Thioredoxin.
+At position 345 to 422, the domain is characterized as OCT.
+At position 51 to 156, the domain is characterized as Expansin-like EG45.
+At position 171 to 254, the domain is characterized as Expansin-like CBD.
+At position 95 to 163, the domain is characterized as POTRA.
+At position 23 to 168, the domain is characterized as Ferritin-like diiron.
+At position 169 to 202, the domain is characterized as Rubredoxin-like.
+At position 1 to 96, the domain is characterized as FAD-binding PCMH-type.
+At position 12 to 333, the domain is characterized as Kinesin motor.
+At position 773 to 836, the domain is characterized as SAM.
+At position 43 to 113, the domain is characterized as KH type-2.
+At position 35 to 209, the domain is characterized as Helicase ATP-binding.
+At position 240 to 388, the domain is characterized as Helicase C-terminal.
+At position 2 to 165, the domain is characterized as EngA-type G 1.
+At position 192 to 270, the domain is characterized as RRM.
+At position 23 to 273, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 270 to 464, the domain is characterized as MH2.
+At position 707 to 868, the domain is characterized as MOSC.
+At position 1 to 186, the domain is characterized as YrdC-like.
+At position 47 to 164, the domain is characterized as PX.
+At position 5 to 131, the domain is characterized as PINc.
+At position 58 to 201, the domain is characterized as SIS.
+At position 227 to 284, the domain is characterized as CBS 1.
+At position 292 to 337, the domain is characterized as CBS 2.
+At position 372 to 471, the domain is characterized as PFU.
+At position 537 to 798, the domain is characterized as PUL.
+At position 354 to 432, the domain is characterized as OCT.
+At position 13 to 243, the domain is characterized as ABC transporter.
+At position 1533 to 1812, the domain is characterized as Autotransporter.
+At position 185 to 261, the domain is characterized as Biotinyl-binding.
+At position 196 to 463, the domain is characterized as SF4 helicase.
+At position 25 to 99, the domain is characterized as IGFBP N-terminal.
+At position 102 to 168, the domain is characterized as VWFC.
+At position 199 to 244, the domain is characterized as TSP type-1.
+At position 258 to 332, the domain is characterized as CTCK.
+At position 77 to 302, the domain is characterized as Radical SAM core.
+At position 21 to 124, the domain is characterized as Ig-like V-type.
+At position 414 to 587, the domain is characterized as tr-type G.
+At position 26 to 150, the domain is characterized as Thioredoxin 1.
+At position 346 to 489, the domain is characterized as Thioredoxin 2.
+At position 37 to 235, the domain is characterized as VWFA 1.
+At position 615 to 805, the domain is characterized as VWFA 2.
+At position 829 to 1021, the domain is characterized as VWFA 3.
+At position 10 to 48, the domain is characterized as MtN3/slv 1.
+At position 110 to 191, the domain is characterized as MtN3/slv 2.
+At position 35 to 241, the domain is characterized as Velvet.
+At position 95 to 154, the domain is characterized as Collagen-like 2.
+At position 155 to 191, the domain is characterized as Collagen-like 3.
+At position 397 to 514, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 515 to 618, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 672 to 751, the domain is characterized as POLO box.
+At position 87 to 294, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 130 to 179, the domain is characterized as bHLH.
+At position 9 to 72, the domain is characterized as TGS.
+At position 22 to 295, the domain is characterized as Septin-type G.
+At position 43 to 231, the domain is characterized as Rho-GAP.
+At position 304 to 611, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 234 to 304, the domain is characterized as Kringle.
+At position 319 to 356, the domain is characterized as LDL-receptor class A 1.
+At position 355 to 435, the domain is characterized as PAN.
+At position 433 to 585, the domain is characterized as SRCR 1.
+At position 557 to 594, the domain is characterized as LDL-receptor class A 2.
+At position 598 to 694, the domain is characterized as SRCR 2.
+At position 713 to 947, the domain is characterized as Peptidase S1.
+At position 30 to 210, the domain is characterized as BPL/LPL catalytic.
+At position 138 to 256, the domain is characterized as Response regulatory.
+At position 449 to 621, the domain is characterized as tr-type G.
+At position 3 to 231, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 41, the domain is characterized as Disintegrin.
+At position 16 to 236, the domain is characterized as Peptidase S1.
+At position 251 to 367, the domain is characterized as SET.
+At position 339 to 509, the domain is characterized as Helicase C-terminal.
+At position 159 to 325, the domain is characterized as OBG-type G.
+At position 11 to 181, the domain is characterized as FAD-binding PCMH-type.
+At position 4 to 162, the domain is characterized as Obg.
+At position 163 to 329, the domain is characterized as OBG-type G.
+At position 281 to 399, the domain is characterized as Nop.
+At position 23 to 95, the domain is characterized as UPAR/Ly6.
+At position 27 to 180, the domain is characterized as Bulb-type lectin.
+At position 311 to 348, the domain is characterized as EGF-like.
+At position 368 to 447, the domain is characterized as PAN.
+At position 537 to 822, the domain is characterized as Protein kinase.
+At position 289 to 556, the domain is characterized as ABC transmembrane type-1 1.
+At position 602 to 834, the domain is characterized as ABC transporter 1.
+At position 919 to 1199, the domain is characterized as ABC transmembrane type-1 2.
+At position 1236 to 1567, the domain is characterized as ABC transporter 2.
+At position 11 to 143, the domain is characterized as ENTH.
+At position 175 to 194, the domain is characterized as UIM 1.
+At position 206 to 225, the domain is characterized as UIM 2.
+At position 2 to 457, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 9 to 132, the domain is characterized as MsrB.
+At position 35 to 151, the domain is characterized as FZ.
+At position 127 to 162, the domain is characterized as EF-hand 2.
+At position 333 to 372, the domain is characterized as PLD phosphodiesterase 1.
+At position 663 to 690, the domain is characterized as PLD phosphodiesterase 2.
+At position 29 to 103, the domain is characterized as IGFBP N-terminal.
+At position 106 to 172, the domain is characterized as VWFC.
+At position 203 to 248, the domain is characterized as TSP type-1.
+At position 260 to 334, the domain is characterized as CTCK.
+At position 7 to 68, the domain is characterized as LIM zinc-binding 1.
+At position 77 to 139, the domain is characterized as LIM zinc-binding 2.
+At position 141 to 197, the domain is characterized as LIM zinc-binding 3.
+At position 562 to 693, the domain is characterized as AXH.
+At position 46 to 210, the domain is characterized as Exonuclease.
+At position 33 to 172, the domain is characterized as GOLD.
+At position 69 to 169, the domain is characterized as SRCR 1.
+At position 200 to 300, the domain is characterized as SRCR 2.
+At position 355 to 455, the domain is characterized as SRCR 3.
+At position 484 to 584, the domain is characterized as SRCR 4.
+At position 70 to 342, the domain is characterized as Septin-type G.
+At position 44 to 98, the domain is characterized as Kazal-like.
+At position 11 to 188, the domain is characterized as Josephin.
+At position 247 to 338, the domain is characterized as PDZ 1.
+At position 420 to 505, the domain is characterized as PDZ 2.
+At position 15 to 381, the domain is characterized as Protein kinase.
+At position 10 to 151, the domain is characterized as RNase H type-1.
+At position 115 to 330, the domain is characterized as START.
+At position 3 to 242, the domain is characterized as KaiC.
+At position 268 to 557, the domain is characterized as ABC transmembrane type-1 1.
+At position 593 to 821, the domain is characterized as ABC transporter 1.
+At position 918 to 1202, the domain is characterized as ABC transmembrane type-1 2.
+At position 1239 to 1473, the domain is characterized as ABC transporter 2.
+At position 8 to 130, the domain is characterized as RNase III.
+At position 157 to 227, the domain is characterized as DRBM.
+At position 159 to 389, the domain is characterized as Radical SAM core.
+At position 392 to 455, the domain is characterized as TRAM.
+At position 208 to 649, the domain is characterized as Myotubularin phosphatase.
+At position 193 to 361, the domain is characterized as PCI.
+At position 41 to 269, the domain is characterized as Peptidase S1.
+At position 14 to 53, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 54 to 100, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 149 to 197, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 25 to 77, the domain is characterized as bHLH.
+At position 96 to 129, the domain is characterized as Orange.
+At position 71 to 114, the domain is characterized as CHCH.
+At position 360 to 407, the domain is characterized as G-patch.
+At position 142 to 184, the domain is characterized as P-type.
+At position 189 to 462, the domain is characterized as ZP.
+At position 26 to 66, the domain is characterized as Chitin-binding type-1.
+At position 27 to 90, the domain is characterized as IGFBP N-terminal.
+At position 76 to 134, the domain is characterized as Kazal-like.
+At position 365 to 450, the domain is characterized as PDZ.
+At position 20 to 141, the domain is characterized as Thioredoxin.
+At position 187 to 265, the domain is characterized as RRM.
+At position 9 to 236, the domain is characterized as RNase H type-2.
+At position 172 to 201, the domain is characterized as GS.
+At position 202 to 492, the domain is characterized as Protein kinase.
+At position 619 to 717, the domain is characterized as tRNA-binding.
+At position 42 to 82, the domain is characterized as EGF-like.
+At position 189 to 295, the domain is characterized as RRM.
+At position 9 to 78, the domain is characterized as PAN 1.
+At position 82 to 138, the domain is characterized as PAN 2.
+At position 45 to 223, the domain is characterized as BPL/LPL catalytic.
+At position 430 to 569, the domain is characterized as Thioredoxin.
+At position 9 to 233, the domain is characterized as Glutamine amidotransferase type-1.
+At position 276 to 435, the domain is characterized as Helicase C-terminal.
+At position 64 to 245, the domain is characterized as FAD-binding PCMH-type.
+At position 232 to 464, the domain is characterized as Peptidase S1.
+At position 23 to 278, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 642 to 677, the domain is characterized as UVR.
+At position 269 to 304, the domain is characterized as EF-hand.
+At position 382 to 520, the domain is characterized as PI-PLC X-box.
+At position 590 to 709, the domain is characterized as PI-PLC Y-box.
+At position 713 to 862, the domain is characterized as C2.
+At position 13 to 44, the domain is characterized as HNF-p1.
+At position 78 to 173, the domain is characterized as POU-specific atypical.
+At position 60 to 173, the domain is characterized as OmpA-like.
+At position 23 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 30 to 250, the domain is characterized as Peptidase S1.
+At position 84 to 301, the domain is characterized as Radical SAM core.
+At position 614 to 675, the domain is characterized as SAM.
+At position 25 to 189, the domain is characterized as PI-PLC X-box.
+At position 1 to 324, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 282 to 597, the domain is characterized as UvrD-like helicase C-terminal.
+At position 229 to 314, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 96 to 241, the domain is characterized as PPC.
+At position 18 to 354, the domain is characterized as Kinesin motor.
+At position 539 to 709, the domain is characterized as tr-type G.
+At position 26 to 215, the domain is characterized as GH16.
+At position 68 to 440, the domain is characterized as Peptidase S8.
+At position 454 to 619, the domain is characterized as P/Homo B.
+At position 1149 to 1224, the domain is characterized as DEP.
+At position 165 to 275, the domain is characterized as Fe2OG dioxygenase.
+At position 128 to 313, the domain is characterized as Integrase catalytic.
+At position 289 to 490, the domain is characterized as Helicase ATP-binding.
+At position 26 to 301, the domain is characterized as GH18.
+At position 322 to 342, the domain is characterized as ELK.
+At position 95 to 347, the domain is characterized as PPM-type phosphatase.
+At position 34 to 141, the domain is characterized as WH1.
+At position 203 to 216, the domain is characterized as CRIB.
+At position 405 to 422, the domain is characterized as WH2 1.
+At position 433 to 450, the domain is characterized as WH2 2.
+At position 71 to 396, the domain is characterized as Protein kinase.
+At position 2 to 152, the domain is characterized as UBC core.
+At position 157 to 216, the domain is characterized as OVATE.
+At position 37 to 79, the domain is characterized as PISA.
+At position 130 to 405, the domain is characterized as NR LBD.
+At position 7 to 129, the domain is characterized as MTTase N-terminal.
+At position 183 to 414, the domain is characterized as Radical SAM core.
+At position 416 to 510, the domain is characterized as TRAM.
+At position 220 to 348, the domain is characterized as OmpA-like.
+At position 294 to 532, the domain is characterized as Glutamine amidotransferase type-1.
+At position 18 to 143, the domain is characterized as Arf-GAP.
+At position 102 to 182, the domain is characterized as KH 1.
+At position 237 to 319, the domain is characterized as KH 2.
+At position 601 to 694, the domain is characterized as BRCT 3.
+At position 703 to 779, the domain is characterized as BRCT 4.
+At position 866 to 947, the domain is characterized as BRCT 5.
+At position 970 to 1059, the domain is characterized as BRCT 6.
+At position 218 to 366, the domain is characterized as TrmE-type G.
+At position 45 to 105, the domain is characterized as HTH iclR-type.
+At position 120 to 291, the domain is characterized as IclR-ED.
+At position 172 to 186, the domain is characterized as F-box; atypical.
+At position 339 to 389, the domain is characterized as SANT.
+At position 428 to 532, the domain is characterized as CXC.
+At position 544 to 659, the domain is characterized as SET.
+At position 27 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 115 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 54 to 153, the domain is characterized as PH.
+At position 18 to 132, the domain is characterized as Ig-like C2-type 1.
+At position 141 to 232, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 347, the domain is characterized as Ig-like C2-type 3.
+At position 400 to 556, the domain is characterized as TIR.
+At position 596 to 683, the domain is characterized as Thioredoxin.
+At position 547 to 641, the domain is characterized as SH2.
+At position 261 to 310, the domain is characterized as bHLH.
+At position 80 to 134, the domain is characterized as MADS-box.
+At position 182 to 257, the domain is characterized as SPOR.
+At position 106 to 339, the domain is characterized as Radical SAM core.
+At position 2 to 197, the domain is characterized as tr-type G.
+At position 47 to 231, the domain is characterized as Helicase ATP-binding.
+At position 260 to 461, the domain is characterized as Helicase C-terminal.
+At position 380 to 414, the domain is characterized as SAP.
+At position 431 to 545, the domain is characterized as Toprim.
+At position 111 to 302, the domain is characterized as Rab-GAP TBC.
+At position 552 to 715, the domain is characterized as RUN.
+At position 34 to 124, the domain is characterized as GOLD.
+At position 1 to 338, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 276 to 579, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 64, the domain is characterized as SH3b 1.
+At position 72 to 140, the domain is characterized as SH3b 2.
+At position 148 to 268, the domain is characterized as NlpC/P60.
+At position 38 to 154, the domain is characterized as MTTase N-terminal.
+At position 178 to 413, the domain is characterized as Radical SAM core.
+At position 393 to 443, the domain is characterized as DHHC.
+At position 311 to 350, the domain is characterized as STI1.
+At position 64 to 215, the domain is characterized as Cupin type-1.
+At position 74 to 146, the domain is characterized as KRAB.
+At position 59 to 130, the domain is characterized as RRM 1.
+At position 132 to 210, the domain is characterized as RRM 2.
+At position 221 to 299, the domain is characterized as RRM 3.
+At position 179 to 341, the domain is characterized as PCI.
+At position 182 to 222, the domain is characterized as EGF-like; calcium-binding.
+At position 261 to 516, the domain is characterized as ZP.
+At position 73 to 181, the domain is characterized as PX.
+At position 341 to 480, the domain is characterized as JmjC.
+At position 351 to 587, the domain is characterized as TLDc.
+At position 110 to 231, the domain is characterized as MPN.
+At position 140 to 244, the domain is characterized as HTH LytTR-type.
+At position 99 to 129, the domain is characterized as KOW.
+At position 914 to 943, the domain is characterized as IQ 2.
+At position 31 to 197, the domain is characterized as Helicase ATP-binding.
+At position 224 to 411, the domain is characterized as Helicase C-terminal.
+At position 4 to 64, the domain is characterized as MADS-box.
+At position 236 to 465, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 2 to 57, the domain is characterized as CpcD-like.
+At position 433 to 618, the domain is characterized as Lon proteolytic.
+At position 2 to 153, the domain is characterized as Thioredoxin.
+At position 102 to 797, the domain is characterized as REJ.
+At position 1114 to 1231, the domain is characterized as PLAT.
+At position 3 to 103, the domain is characterized as Cystatin.
+At position 47 to 125, the domain is characterized as RRM.
+At position 340 to 485, the domain is characterized as Helicase C-terminal.
+At position 96 to 204, the domain is characterized as FAD-binding FR-type.
+At position 223 to 424, the domain is characterized as Pentraxin (PTX).
+At position 197 to 391, the domain is characterized as Peptidase M12B.
+At position 399 to 480, the domain is characterized as Disintegrin.
+At position 185 to 455, the domain is characterized as NR LBD.
+At position 200 to 386, the domain is characterized as Hflx-type G.
+At position 278 to 377, the domain is characterized as Fibronectin type-III 1.
+At position 381 to 473, the domain is characterized as Fibronectin type-III 2.
+At position 477 to 570, the domain is characterized as Fibronectin type-III 3.
+At position 574 to 669, the domain is characterized as Fibronectin type-III 4.
+At position 673 to 765, the domain is characterized as Fibronectin type-III 5.
+At position 766 to 859, the domain is characterized as Fibronectin type-III 6.
+At position 871 to 957, the domain is characterized as Fibronectin type-III 7.
+At position 958 to 1052, the domain is characterized as Fibronectin type-III 8.
+At position 1056 to 1153, the domain is characterized as Fibronectin type-III 9.
+At position 139 to 441, the domain is characterized as NB-ARC.
+At position 6 to 93, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 235 to 421, the domain is characterized as FAD-binding PCMH-type.
+At position 153 to 467, the domain is characterized as NB-ARC.
+At position 586 to 648, the domain is characterized as KH.
+At position 657 to 729, the domain is characterized as S1 motif.
+At position 315 to 367, the domain is characterized as HAMP 1.
+At position 409 to 462, the domain is characterized as HAMP 2.
+At position 481 to 717, the domain is characterized as Methyl-accepting transducer.
+At position 330 to 445, the domain is characterized as Ferric oxidoreductase.
+At position 465 to 583, the domain is characterized as FAD-binding FR-type.
+At position 272 to 354, the domain is characterized as BCNT-C.
+At position 12 to 261, the domain is characterized as ABC transporter.
+At position 304 to 346, the domain is characterized as CAP-Gly 1.
+At position 423 to 465, the domain is characterized as CAP-Gly 2.
+At position 566 to 679, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 680 to 792, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 864 to 942, the domain is characterized as POLO box.
+At position 6 to 163, the domain is characterized as Obg.
+At position 164 to 344, the domain is characterized as OBG-type G.
+At position 362 to 442, the domain is characterized as OCT.
+At position 214 to 248, the domain is characterized as WW 1.
+At position 595 to 629, the domain is characterized as WW 2.
+At position 6 to 151, the domain is characterized as Toprim.
+At position 251 to 430, the domain is characterized as Helicase ATP-binding.
+At position 610 to 776, the domain is characterized as Helicase C-terminal.
+At position 794 to 925, the domain is characterized as RLR CTR.
+At position 52 to 106, the domain is characterized as TCP.
+At position 194 to 294, the domain is characterized as Fe2OG dioxygenase.
+At position 224 to 403, the domain is characterized as SSD.
+At position 40 to 140, the domain is characterized as FAD-binding FR-type.
+At position 95 to 154, the domain is characterized as CBS 1.
+At position 155 to 215, the domain is characterized as CBS 2.
+At position 27 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 156 to 249, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 360, the domain is characterized as Ig-like C2-type 3.
+At position 483 to 772, the domain is characterized as Protein kinase.
+At position 11 to 251, the domain is characterized as ABC transporter.
+At position 7 to 333, the domain is characterized as Helicase ATP-binding.
+At position 189 to 284, the domain is characterized as PpiC.
+At position 21 to 359, the domain is characterized as Protein kinase.
+At position 23 to 372, the domain is characterized as TTL.
+At position 687 to 945, the domain is characterized as Protein kinase.
+At position 194 to 253, the domain is characterized as SH3.
+At position 284 to 468, the domain is characterized as DH.
+At position 499 to 606, the domain is characterized as PH.
+At position 222 to 380, the domain is characterized as TrmE-type G.
+At position 124 to 175, the domain is characterized as DHHC.
+At position 71 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 196 to 263, the domain is characterized as SCA7.
+At position 485 to 551, the domain is characterized as SAM.
+At position 62 to 122, the domain is characterized as MADS-box.
+At position 1 to 84, the domain is characterized as Ubiquitin-like.
+At position 404 to 444, the domain is characterized as UBA.
+At position 429 to 789, the domain is characterized as Protein kinase.
+At position 31 to 231, the domain is characterized as FBA.
+At position 117 to 168, the domain is characterized as SANT.
+At position 374 to 472, the domain is characterized as SWIRM.
+At position 579 to 711, the domain is characterized as MPN.
+At position 63 to 102, the domain is characterized as EGF-like 1.
+At position 114 to 145, the domain is characterized as EGF-like 2.
+At position 140 to 174, the domain is characterized as EGF-like 3.
+At position 175 to 204, the domain is characterized as EGF-like 4.
+At position 205 to 233, the domain is characterized as EGF-like 5.
+At position 228 to 262, the domain is characterized as EGF-like 6.
+At position 364 to 395, the domain is characterized as EGF-like 7.
+At position 17 to 104, the domain is characterized as Rhodanese.
+At position 47 to 298, the domain is characterized as Protein kinase.
+At position 513 to 687, the domain is characterized as N-acetyltransferase.
+At position 73 to 125, the domain is characterized as bHLH.
+At position 10 to 429, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 858 to 1145, the domain is characterized as PKS/mFAS DH.
+At position 2280 to 2362, the domain is characterized as Carrier.
+At position 152 to 271, the domain is characterized as PAZ.
+At position 442 to 753, the domain is characterized as Piwi.
+At position 62 to 407, the domain is characterized as TTL.
+At position 624 to 706, the domain is characterized as BRCT.
+At position 411 to 495, the domain is characterized as B5.
+At position 1 to 100, the domain is characterized as PTS EIIB type-3.
+At position 33 to 236, the domain is characterized as Eph LBD.
+At position 368 to 485, the domain is characterized as Fibronectin type-III 1.
+At position 486 to 581, the domain is characterized as Fibronectin type-III 2.
+At position 669 to 918, the domain is characterized as Protein kinase.
+At position 947 to 1011, the domain is characterized as SAM.
+At position 63 to 137, the domain is characterized as RRM 1.
+At position 148 to 226, the domain is characterized as RRM 2.
+At position 269 to 344, the domain is characterized as RRM 3.
+At position 227 to 391, the domain is characterized as PCI.
+At position 107 to 319, the domain is characterized as ATP-grasp.
+At position 263 to 337, the domain is characterized as ACT 1.
+At position 343 to 415, the domain is characterized as ACT 2.
+At position 19 to 453, the domain is characterized as CN hydrolase.
+At position 1 to 59, the domain is characterized as Kazal-like.
+At position 175 to 225, the domain is characterized as DHHC.
+At position 39 to 186, the domain is characterized as F5/8 type C.
+At position 20 to 313, the domain is characterized as Protein kinase.
+At position 231 to 493, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 125 to 196, the domain is characterized as POTRA.
+At position 30 to 80, the domain is characterized as Tudor-knot.
+At position 150 to 318, the domain is characterized as MRG.
+At position 138 to 217, the domain is characterized as SPOR.
+At position 4 to 53, the domain is characterized as Myosin N-terminal SH3-like.
+At position 60 to 731, the domain is characterized as Myosin motor.
+At position 733 to 755, the domain is characterized as IQ 1.
+At position 756 to 778, the domain is characterized as IQ 2.
+At position 781 to 803, the domain is characterized as IQ 3.
+At position 804 to 826, the domain is characterized as IQ 4.
+At position 829 to 851, the domain is characterized as IQ 5.
+At position 852 to 874, the domain is characterized as IQ 6.
+At position 1162 to 1459, the domain is characterized as Dilute.
+At position 19 to 69, the domain is characterized as UBA.
+At position 333 to 413, the domain is characterized as UBX.
+At position 85 to 170, the domain is characterized as PSP1 C-terminal.
+At position 43 to 228, the domain is characterized as VWFA.
+At position 235 to 281, the domain is characterized as TSP type-1.
+At position 103 to 298, the domain is characterized as ATP-grasp.
+At position 301 to 436, the domain is characterized as Fido.
+At position 47 to 352, the domain is characterized as AB hydrolase-1.
+At position 375 to 431, the domain is characterized as CBS 1.
+At position 440 to 492, the domain is characterized as CBS 2.
+At position 80 to 241, the domain is characterized as CP-type G.
+At position 261 to 339, the domain is characterized as PDZ.
+At position 33 to 167, the domain is characterized as MOSC.
+At position 689 to 775, the domain is characterized as SUEL-type lectin.
+At position 11 to 134, the domain is characterized as MPN.
+At position 5 to 171, the domain is characterized as PRELI/MSF1.
+At position 243 to 389, the domain is characterized as Exonuclease.
+At position 16 to 191, the domain is characterized as Tyrosine-protein phosphatase.
+At position 120 to 177, the domain is characterized as F-box.
+At position 284 to 459, the domain is characterized as Helicase ATP-binding.
+At position 487 to 632, the domain is characterized as Helicase C-terminal.
+At position 41 to 124, the domain is characterized as ACT.
+At position 57 to 87, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 109 to 233, the domain is characterized as RCK N-terminal.
+At position 246 to 331, the domain is characterized as RCK C-terminal.
+At position 586 to 664, the domain is characterized as BRCT.
+At position 154 to 272, the domain is characterized as PAZ.
+At position 473 to 756, the domain is characterized as Piwi.
+At position 189 to 321, the domain is characterized as Fe2OG dioxygenase.
+At position 823 to 1142, the domain is characterized as F5/8 type A 3.
+At position 823 to 991, the domain is characterized as Plastocyanin-like 5.
+At position 1000 to 1142, the domain is characterized as Plastocyanin-like 6.
+At position 1146 to 1297, the domain is characterized as F5/8 type C 1.
+At position 1302 to 1456, the domain is characterized as F5/8 type C 2.
+At position 27 to 227, the domain is characterized as RNase H type-2.
+At position 28 to 175, the domain is characterized as VOC.
+At position 415 to 551, the domain is characterized as Plastocyanin-like 3.
+At position 55 to 224, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 55, the domain is characterized as HTH gntR-type.
+At position 2 to 129, the domain is characterized as RNase III.
+At position 283 to 519, the domain is characterized as PIK helical.
+At position 604 to 870, the domain is characterized as PI3K/PI4K catalytic.
+At position 71 to 106, the domain is characterized as EF-hand 1.
+At position 281 to 369, the domain is characterized as EH 1.
+At position 313 to 348, the domain is characterized as EF-hand 1.
+At position 821 to 910, the domain is characterized as EH 2.
+At position 854 to 889, the domain is characterized as EF-hand 2.
+At position 1748 to 1765, the domain is characterized as WH2.
+At position 127 to 267, the domain is characterized as Fatty acid hydroxylase.
+At position 136 to 406, the domain is characterized as Protein kinase.
+At position 97 to 330, the domain is characterized as Radical SAM core.
+At position 29 to 98, the domain is characterized as POTRA.
+At position 455 to 513, the domain is characterized as Collagen-like 1.
+At position 544 to 603, the domain is characterized as Collagen-like 2.
+At position 493 to 557, the domain is characterized as DRBM 5.
+At position 434 to 516, the domain is characterized as RRM.
+At position 62 to 335, the domain is characterized as Dynamin-type G.
+At position 566 to 654, the domain is characterized as GED.
+At position 116 to 195, the domain is characterized as Cytochrome c 1.
+At position 205 to 286, the domain is characterized as Cytochrome c 2.
+At position 352 to 589, the domain is characterized as NR LBD.
+At position 39 to 119, the domain is characterized as KRAB.
+At position 25 to 198, the domain is characterized as PI-PLC X-box.
+At position 324 to 378, the domain is characterized as MIR 1.
+At position 388 to 448, the domain is characterized as MIR 2.
+At position 459 to 514, the domain is characterized as MIR 3.
+At position 87 to 285, the domain is characterized as Laminin G-like.
+At position 5 to 66, the domain is characterized as Acylphosphatase-like.
+At position 225 to 346, the domain is characterized as OTU.
+At position 486 to 546, the domain is characterized as Tudor.
+At position 72 to 140, the domain is characterized as ACT 1.
+At position 21 to 258, the domain is characterized as Peptidase S1.
+At position 10 to 97, the domain is characterized as PDZ 1.
+At position 291 to 369, the domain is characterized as PDZ 2.
+At position 493 to 574, the domain is characterized as PDZ 3.
+At position 588 to 653, the domain is characterized as SH3.
+At position 679 to 860, the domain is characterized as Guanylate kinase-like.
+At position 177 to 268, the domain is characterized as CS.
+At position 98 to 289, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 69 to 308, the domain is characterized as ABC transporter.
+At position 388 to 594, the domain is characterized as ABC transmembrane type-2.
+At position 476 to 589, the domain is characterized as C-type lectin.
+At position 5 to 335, the domain is characterized as Kinesin motor.
+At position 8 to 116, the domain is characterized as MaoC-like.
+At position 27 to 151, the domain is characterized as PX.
+At position 1273 to 1494, the domain is characterized as Rap-GAP.
+At position 28 to 91, the domain is characterized as bZIP.
+At position 46 to 151, the domain is characterized as PH.
+At position 159 to 353, the domain is characterized as Rho-GAP.
+At position 125 to 313, the domain is characterized as Tyr recombinase.
+At position 230 to 402, the domain is characterized as TrmE-type G.
+At position 500 to 605, the domain is characterized as CBM20.
+At position 129 to 386, the domain is characterized as PPM-type phosphatase.
+At position 95 to 178, the domain is characterized as PDZ.
+At position 143 to 280, the domain is characterized as PH 1.
+At position 305 to 417, the domain is characterized as PH 2.
+At position 464 to 520, the domain is characterized as SU.
+At position 341 to 440, the domain is characterized as BRCT.
+At position 1266 to 1558, the domain is characterized as Protein kinase.
+At position 54 to 172, the domain is characterized as MTTase N-terminal.
+At position 429 to 491, the domain is characterized as TRAM.
+At position 996 to 1209, the domain is characterized as FtsK.
+At position 30 to 84, the domain is characterized as Clip.
+At position 137 to 390, the domain is characterized as Peptidase S1.
+At position 188 to 351, the domain is characterized as PCI.
+At position 21 to 156, the domain is characterized as N-acetyltransferase.
+At position 124 to 311, the domain is characterized as ATP-grasp.
+At position 1 to 342, the domain is characterized as Myosin motor.
+At position 345 to 374, the domain is characterized as IQ.
+At position 21 to 466, the domain is characterized as Hexokinase.
+At position 609 to 684, the domain is characterized as BRCT.
+At position 79 to 122, the domain is characterized as SpoVT-AbrB 2.
+At position 81 to 241, the domain is characterized as Exonuclease.
+At position 145 to 480, the domain is characterized as PPM-type phosphatase.
+At position 21 to 162, the domain is characterized as Ig-like V-type.
+At position 1 to 290, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 283 to 588, the domain is characterized as UvrD-like helicase C-terminal.
+At position 96 to 290, the domain is characterized as ATP-grasp.
+At position 332 to 368, the domain is characterized as UBA.
+At position 17 to 190, the domain is characterized as Era-type G.
+At position 221 to 303, the domain is characterized as KH type-2.
+At position 48 to 148, the domain is characterized as SRCR 1.
+At position 155 to 255, the domain is characterized as SRCR 2.
+At position 262 to 362, the domain is characterized as SRCR 3.
+At position 369 to 469, the domain is characterized as SRCR 4.
+At position 476 to 576, the domain is characterized as SRCR 5.
+At position 583 to 683, the domain is characterized as SRCR 6.
+At position 690 to 790, the domain is characterized as SRCR 7.
+At position 795 to 895, the domain is characterized as SRCR 8.
+At position 900 to 1000, the domain is characterized as SRCR 9.
+At position 1036 to 1136, the domain is characterized as SRCR 10.
+At position 1141 to 1243, the domain is characterized as SRCR 11.
+At position 1246 to 1346, the domain is characterized as SRCR 12.
+At position 107 to 397, the domain is characterized as PPM-type phosphatase.
+At position 785 to 1038, the domain is characterized as Protein kinase.
+At position 31 to 167, the domain is characterized as C-type lectin.
+At position 240 to 280, the domain is characterized as EGF-like 1.
+At position 283 to 323, the domain is characterized as EGF-like 2.
+At position 324 to 362, the domain is characterized as EGF-like 3; calcium-binding.
+At position 364 to 404, the domain is characterized as EGF-like 4.
+At position 403 to 439, the domain is characterized as EGF-like 5.
+At position 440 to 480, the domain is characterized as EGF-like 6; calcium-binding.
+At position 110 to 365, the domain is characterized as Protein kinase.
+At position 410 to 445, the domain is characterized as EF-hand 1.
+At position 448 to 479, the domain is characterized as EF-hand 2.
+At position 480 to 515, the domain is characterized as EF-hand 3.
+At position 521 to 554, the domain is characterized as EF-hand 4.
+At position 26 to 325, the domain is characterized as Protein kinase.
+At position 340 to 417, the domain is characterized as REM-1.
+At position 480 to 541, the domain is characterized as SH3.
+At position 435 to 515, the domain is characterized as HRDC.
+At position 261 to 434, the domain is characterized as tr-type G.
+At position 274 to 348, the domain is characterized as PUA.
+At position 38 to 242, the domain is characterized as Peptidase S1.
+At position 2 to 207, the domain is characterized as ThyX.
+At position 365 to 469, the domain is characterized as tRNA-binding.
+At position 753 to 789, the domain is characterized as EGF-like 20.
+At position 1021 to 1057, the domain is characterized as EGF-like 27.
+At position 1145 to 1181, the domain is characterized as EGF-like 30.
+At position 43 to 181, the domain is characterized as Thioredoxin.
+At position 41 to 129, the domain is characterized as RRM.
+At position 6 to 229, the domain is characterized as tr-type G.
+At position 15 to 116, the domain is characterized as AB hydrolase-1.
+At position 3 to 147, the domain is characterized as NAC.
+At position 8 to 207, the domain is characterized as YjeF N-terminal.
+At position 215 to 466, the domain is characterized as YjeF C-terminal.
+At position 7 to 76, the domain is characterized as S1-like.
+At position 58 to 137, the domain is characterized as S1 motif.
+At position 421 to 535, the domain is characterized as Toprim.
+At position 991 to 1067, the domain is characterized as Carrier.
+At position 32 to 151, the domain is characterized as C-type lectin.
+At position 10 to 124, the domain is characterized as Response regulatory.
+At position 147 to 376, the domain is characterized as Sigma-54 factor interaction.
+At position 153 to 308, the domain is characterized as C1q.
+At position 5 to 83, the domain is characterized as TFIIS N-terminal.
+At position 153 to 268, the domain is characterized as TFIIS central.
+At position 169 to 350, the domain is characterized as OBG-type G.
+At position 124 to 322, the domain is characterized as Peptidase M12A.
+At position 317 to 357, the domain is characterized as EGF-like.
+At position 366 to 469, the domain is characterized as CUB.
+At position 525 to 566, the domain is characterized as TSP type-1.
+At position 237 to 328, the domain is characterized as Fibronectin type-III.
+At position 1 to 107, the domain is characterized as Ig-like.
+At position 42 to 157, the domain is characterized as tRNA-binding.
+At position 417 to 491, the domain is characterized as B5.
+At position 745 to 839, the domain is characterized as FDX-ACB.
+At position 39 to 359, the domain is characterized as FERM.
+At position 425 to 683, the domain is characterized as Protein kinase.
+At position 22 to 263, the domain is characterized as ABC transporter.
+At position 44 to 122, the domain is characterized as BTB.
+At position 570 to 703, the domain is characterized as C1q.
+At position 22 to 73, the domain is characterized as Clip.
+At position 97 to 350, the domain is characterized as Peptidase S1.
+At position 17 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 149 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 246 to 346, the domain is characterized as Ig-like C2-type 3.
+At position 464 to 752, the domain is characterized as Protein kinase.
+At position 7 to 126, the domain is characterized as Longin.
+At position 137 to 197, the domain is characterized as v-SNARE coiled-coil homology.
+At position 151 to 178, the domain is characterized as PLD phosphodiesterase.
+At position 405 to 463, the domain is characterized as SOCS box.
+At position 383 to 436, the domain is characterized as HTH myb-type.
+At position 435 to 513, the domain is characterized as Myb-like.
+At position 85 to 161, the domain is characterized as Lipoyl-binding 1.
+At position 212 to 288, the domain is characterized as Lipoyl-binding 2.
+At position 330 to 367, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 3 to 59, the domain is characterized as DPH-type MB.
+At position 1 to 49, the domain is characterized as Myosin N-terminal SH3-like.
+At position 53 to 724, the domain is characterized as Myosin motor.
+At position 574 to 642, the domain is characterized as SH2.
+At position 154 to 206, the domain is characterized as KH.
+At position 43 to 110, the domain is characterized as SH3.
+At position 151 to 241, the domain is characterized as SH2.
+At position 283 to 535, the domain is characterized as Protein kinase.
+At position 13 to 120, the domain is characterized as HIT.
+At position 465 to 581, the domain is characterized as HD.
+At position 719 to 804, the domain is characterized as ACT 1.
+At position 827 to 899, the domain is characterized as ACT 2.
+At position 160 to 248, the domain is characterized as 5'-3' exonuclease.
+At position 141 to 383, the domain is characterized as Fibrinogen C-terminal.
+At position 208 to 594, the domain is characterized as GRAS.
+At position 65 to 192, the domain is characterized as THUMP.
+At position 307 to 353, the domain is characterized as F-box 1.
+At position 679 to 726, the domain is characterized as F-box 2.
+At position 1116 to 1244, the domain is characterized as N-terminal Ras-GEF.
+At position 1317 to 1548, the domain is characterized as Ras-GEF.
+At position 133 to 380, the domain is characterized as Radical SAM core.
+At position 2 to 78, the domain is characterized as HTH rpiR-type.
+At position 122 to 261, the domain is characterized as SIS.
+At position 38 to 488, the domain is characterized as Hexokinase.
+At position 173 to 248, the domain is characterized as RRM 1.
+At position 270 to 346, the domain is characterized as RRM 2.
+At position 186 to 258, the domain is characterized as Bromo.
+At position 389 to 470, the domain is characterized as NET.
+At position 214 to 337, the domain is characterized as Fatty acid hydroxylase.
+At position 251 to 378, the domain is characterized as Guanylate cyclase.
+At position 18 to 257, the domain is characterized as ABC transporter.
+At position 13 to 203, the domain is characterized as HORMA.
+At position 40 to 118, the domain is characterized as Kringle.
+At position 15 to 99, the domain is characterized as GS beta-grasp.
+At position 107 to 474, the domain is characterized as GS catalytic.
+At position 10 to 151, the domain is characterized as Clp R.
+At position 296 to 451, the domain is characterized as Helicase C-terminal.
+At position 227 to 300, the domain is characterized as KRAB.
+At position 168 to 207, the domain is characterized as Disintegrin; truncated.
+At position 5 to 348, the domain is characterized as Kinesin motor.
+At position 523 to 590, the domain is characterized as FHA.
+At position 190 to 273, the domain is characterized as RCK C-terminal 1.
+At position 281 to 365, the domain is characterized as RCK C-terminal 2.
+At position 7 to 136, the domain is characterized as ENTH.
+At position 673 to 914, the domain is characterized as I/LWEQ.
+At position 33 to 59, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 347 to 402, the domain is characterized as LRRNT.
+At position 489 to 538, the domain is characterized as LRRCT.
+At position 407 to 576, the domain is characterized as tr-type G.
+At position 666 to 719, the domain is characterized as Myb-like.
+At position 8 to 272, the domain is characterized as Pyruvate carboxyltransferase.
+At position 181 to 244, the domain is characterized as bZIP.
+At position 1 to 686, the domain is characterized as Myosin motor.
+At position 689 to 712, the domain is characterized as IQ 1.
+At position 713 to 733, the domain is characterized as IQ 2.
+At position 735 to 764, the domain is characterized as IQ 3.
+At position 279 to 335, the domain is characterized as CBS 1.
+At position 340 to 395, the domain is characterized as CBS 2.
+At position 24 to 83, the domain is characterized as AFP-like.
+At position 60 to 236, the domain is characterized as VWFA.
+At position 346 to 541, the domain is characterized as Helicase ATP-binding.
+At position 568 to 712, the domain is characterized as Helicase C-terminal.
+At position 108 to 225, the domain is characterized as PilZ.
+At position 185 to 230, the domain is characterized as bZIP.
+At position 254 to 355, the domain is characterized as DOG1.
+At position 49 to 264, the domain is characterized as Radical SAM core.
+At position 55 to 215, the domain is characterized as PID.
+At position 117 to 185, the domain is characterized as H15.
+At position 28 to 419, the domain is characterized as Helicase ATP-binding.
+At position 411 to 496, the domain is characterized as PDZ 1.
+At position 533 to 618, the domain is characterized as PDZ 2.
+At position 207 to 270, the domain is characterized as KH.
+At position 333 to 427, the domain is characterized as HD.
+At position 1 to 212, the domain is characterized as CN hydrolase.
+At position 385 to 819, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1312 to 1618, the domain is characterized as PKS/mFAS DH.
+At position 1685 to 1762, the domain is characterized as Carrier.
+At position 13 to 87, the domain is characterized as Ubiquitin-like.
+At position 192 to 229, the domain is characterized as STI1 1.
+At position 230 to 261, the domain is characterized as STI1 2.
+At position 393 to 440, the domain is characterized as STI1 3.
+At position 444 to 476, the domain is characterized as STI1 4.
+At position 553 to 598, the domain is characterized as UBA.
+At position 662 to 871, the domain is characterized as FtsK.
+At position 33 to 221, the domain is characterized as GH11.
+At position 642 to 848, the domain is characterized as Rho-GAP.
+At position 878 to 1085, the domain is characterized as START.
+At position 7 to 51, the domain is characterized as F-box.
+At position 198 to 298, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 56, the domain is characterized as bZIP.
+At position 35 to 154, the domain is characterized as Bulb-type lectin.
+At position 288 to 324, the domain is characterized as EGF-like; atypical.
+At position 343 to 425, the domain is characterized as PAN.
+At position 500 to 785, the domain is characterized as Protein kinase.
+At position 18 to 129, the domain is characterized as PINc.
+At position 167 to 403, the domain is characterized as Radical SAM core.
+At position 406 to 477, the domain is characterized as TRAM.
+At position 3 to 132, the domain is characterized as PH.
+At position 211 to 271, the domain is characterized as SH3.
+At position 276 to 366, the domain is characterized as SH2.
+At position 400 to 653, the domain is characterized as Protein kinase.
+At position 41 to 437, the domain is characterized as GRAS.
+At position 137 to 172, the domain is characterized as EF-hand 2.
+At position 291 to 313, the domain is characterized as EF-hand 3.
+At position 323 to 358, the domain is characterized as EF-hand 4.
+At position 359 to 394, the domain is characterized as EF-hand 5.
+At position 349 to 415, the domain is characterized as S4 RNA-binding.
+At position 71 to 277, the domain is characterized as YjeF N-terminal.
+At position 44 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 139 to 202, the domain is characterized as Ig-like C2-type 2.
+At position 126 to 161, the domain is characterized as EF-hand 4.
+At position 6 to 280, the domain is characterized as Protein kinase.
+At position 107 to 225, the domain is characterized as MTTase N-terminal.
+At position 251 to 518, the domain is characterized as Radical SAM core.
+At position 521 to 589, the domain is characterized as TRAM.
+At position 133 to 200, the domain is characterized as SCA7.
+At position 70 to 226, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 112, the domain is characterized as Calponin-homology (CH).
+At position 163 to 222, the domain is characterized as SH3.
+At position 250 to 430, the domain is characterized as DH.
+At position 452 to 557, the domain is characterized as PH.
+At position 9 to 114, the domain is characterized as FAD-binding FR-type.
+At position 254 to 337, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 72 to 344, the domain is characterized as CN hydrolase.
+At position 50 to 163, the domain is characterized as Expansin-like EG45.
+At position 173 to 252, the domain is characterized as Expansin-like CBD.
+At position 269 to 604, the domain is characterized as MHD.
+At position 174 to 304, the domain is characterized as TRUD.
+At position 374 to 437, the domain is characterized as SH3.
+At position 31 to 78, the domain is characterized as F-box.
+At position 56 to 201, the domain is characterized as Helicase ATP-binding.
+At position 212 to 373, the domain is characterized as Helicase C-terminal.
+At position 161 to 240, the domain is characterized as RRM.
+At position 4 to 120, the domain is characterized as VOC.
+At position 623 to 708, the domain is characterized as Fibronectin type-III.
+At position 1295 to 1518, the domain is characterized as NodB homology.
+At position 2111 to 2223, the domain is characterized as Cohesin.
+At position 109 to 223, the domain is characterized as sHSP.
+At position 84 to 322, the domain is characterized as Lon N-terminal.
+At position 321 to 429, the domain is characterized as CULT.
+At position 50 to 128, the domain is characterized as RRM.
+At position 28 to 267, the domain is characterized as Peptidase S1.
+At position 12 to 92, the domain is characterized as MtN3/slv 1.
+At position 135 to 440, the domain is characterized as NB-ARC.
+At position 20 to 154, the domain is characterized as Bulb-type lectin.
+At position 285 to 321, the domain is characterized as EGF-like.
+At position 339 to 426, the domain is characterized as PAN.
+At position 532 to 819, the domain is characterized as Protein kinase.
+At position 2131 to 2194, the domain is characterized as HP.
+At position 82 to 117, the domain is characterized as QLQ.
+At position 151 to 195, the domain is characterized as WRC.
+At position 30 to 296, the domain is characterized as ABC transmembrane type-1.
+At position 376 to 605, the domain is characterized as ABC transporter.
+At position 202 to 470, the domain is characterized as Pterin-binding.
+At position 214 to 313, the domain is characterized as Fe2OG dioxygenase.
+At position 619 to 700, the domain is characterized as BRCT.
+At position 47 to 137, the domain is characterized as CTCK.
+At position 2 to 211, the domain is characterized as RNase H type-2.
+At position 1 to 82, the domain is characterized as Ig-like C2-type.
+At position 84 to 179, the domain is characterized as Ig-like V-type.
+At position 23 to 279, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 7 to 43, the domain is characterized as WW.
+At position 156 to 185, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 27 to 200, the domain is characterized as BPL/LPL catalytic.
+At position 130 to 306, the domain is characterized as Helicase ATP-binding.
+At position 335 to 484, the domain is characterized as Helicase C-terminal.
+At position 337 to 570, the domain is characterized as ABC transporter.
+At position 383 to 425, the domain is characterized as CCT.
+At position 15 to 105, the domain is characterized as PDZ GRASP-type 1.
+At position 111 to 199, the domain is characterized as PDZ GRASP-type 2.
+At position 7 to 182, the domain is characterized as Era-type G.
+At position 144 to 216, the domain is characterized as Bromo.
+At position 320 to 401, the domain is characterized as NET.
+At position 67 to 228, the domain is characterized as CP-type G.
+At position 64 to 358, the domain is characterized as Protein kinase.
+At position 359 to 462, the domain is characterized as AGC-kinase C-terminal.
+At position 51 to 114, the domain is characterized as bZIP.
+At position 25 to 313, the domain is characterized as Protein kinase.
+At position 1138 to 1425, the domain is characterized as CNH.
+At position 1 to 88, the domain is characterized as SMP-LTD.
+At position 101 to 307, the domain is characterized as ATP-grasp.
+At position 144 to 208, the domain is characterized as KH 1.
+At position 233 to 299, the domain is characterized as KH 2.
+At position 322 to 386, the domain is characterized as KH 3.
+At position 424 to 491, the domain is characterized as KH 4.
+At position 49 to 137, the domain is characterized as Cystatin 1.
+At position 156 to 202, the domain is characterized as Cystatin 2.
+At position 303 to 327, the domain is characterized as NAF.
+At position 8 to 157, the domain is characterized as C2 NT-type.
+At position 1037 to 1142, the domain is characterized as Calponin-homology (CH).
+At position 1349 to 1501, the domain is characterized as bMERB.
+At position 489 to 581, the domain is characterized as PB1.
+At position 342 to 441, the domain is characterized as Rhodanese.
+At position 1 to 103, the domain is characterized as Pyrin.
+At position 196 to 513, the domain is characterized as NACHT.
+At position 10 to 365, the domain is characterized as Kinesin motor.
+At position 77 to 120, the domain is characterized as CUE.
+At position 10 to 52, the domain is characterized as CHCH.
+At position 165 to 270, the domain is characterized as Fe2OG dioxygenase.
+At position 289 to 826, the domain is characterized as USP.
+At position 117 to 334, the domain is characterized as ATP-grasp.
+At position 455 to 603, the domain is characterized as N-acetyltransferase.
+At position 112 to 330, the domain is characterized as Era-type G.
+At position 360 to 437, the domain is characterized as KH type-2.
+At position 32 to 270, the domain is characterized as AB hydrolase-1.
+At position 41 to 265, the domain is characterized as Peptidase S1.
+At position 482 to 758, the domain is characterized as Reverse transcriptase.
+At position 349 to 807, the domain is characterized as Myotubularin phosphatase.
+At position 572 to 750, the domain is characterized as Helicase ATP-binding.
+At position 761 to 927, the domain is characterized as Helicase C-terminal.
+At position 80 to 324, the domain is characterized as GB1/RHD3-type G.
+At position 99 to 169, the domain is characterized as Myb-like.
+At position 7 to 58, the domain is characterized as SpoVT-AbrB 1.
+At position 87 to 130, the domain is characterized as SpoVT-AbrB 2.
+At position 47 to 144, the domain is characterized as RRM.
+At position 26 to 108, the domain is characterized as IGFBP N-terminal.
+At position 157 to 232, the domain is characterized as Thyroglobulin type-1.
+At position 19 to 96, the domain is characterized as Cytochrome c.
+At position 8 to 223, the domain is characterized as Radical SAM core.
+At position 34 to 116, the domain is characterized as Inhibitor I9.
+At position 37 to 220, the domain is characterized as FAD-binding PCMH-type.
+At position 622 to 722, the domain is characterized as tRNA-binding.
+At position 55 to 183, the domain is characterized as GGDEF.
+At position 266 to 302, the domain is characterized as CBM1.
+At position 45 to 387, the domain is characterized as IF rod.
+At position 435 to 550, the domain is characterized as LTD.
+At position 748 to 816, the domain is characterized as BTB.
+At position 107 to 328, the domain is characterized as Radical SAM core.
+At position 257 to 451, the domain is characterized as PCI.
+At position 159 to 249, the domain is characterized as Rhodanese.
+At position 714 to 792, the domain is characterized as BRCT.
+At position 26 to 62, the domain is characterized as CBM1.
+At position 169 to 286, the domain is characterized as Rhodanese.
+At position 322 to 465, the domain is characterized as Tyrosine-protein phosphatase.
+At position 141 to 176, the domain is characterized as EF-hand 2.
+At position 176 to 208, the domain is characterized as EF-hand 3.
+At position 32 to 143, the domain is characterized as CFEM 1.
+At position 223 to 334, the domain is characterized as CFEM 2.
+At position 393 to 504, the domain is characterized as CFEM 3.
+At position 555 to 666, the domain is characterized as CFEM 4.
+At position 110 to 359, the domain is characterized as Protein kinase.
+At position 116 to 205, the domain is characterized as EH 1.
+At position 149 to 184, the domain is characterized as EF-hand 1.
+At position 465 to 554, the domain is characterized as EH 2.
+At position 498 to 533, the domain is characterized as EF-hand 2.
+At position 1338 to 1355, the domain is characterized as WH2.
+At position 61 to 187, the domain is characterized as PX.
+At position 285 to 335, the domain is characterized as bHLH.
+At position 1 to 211, the domain is characterized as Protein kinase.
+At position 423 to 607, the domain is characterized as C2 DOCK-type.
+At position 1211 to 1622, the domain is characterized as DOCKER.
+At position 10 to 151, the domain is characterized as Tyrosine-protein phosphatase.
+At position 61 to 241, the domain is characterized as TR mART core.
+At position 30 to 345, the domain is characterized as G-alpha.
+At position 3 to 47, the domain is characterized as WAP.
+At position 154 to 258, the domain is characterized as FAD-binding FR-type.
+At position 185 to 308, the domain is characterized as GST C-terminal.
+At position 947 to 1113, the domain is characterized as PNPLA.
+At position 30 to 80, the domain is characterized as Myosin N-terminal SH3-like.
+At position 84 to 785, the domain is characterized as Myosin motor.
+At position 788 to 817, the domain is characterized as IQ.
+At position 28 to 242, the domain is characterized as GB1/RHD3-type G.
+At position 171 to 206, the domain is characterized as EF-hand 1.
+At position 215 to 250, the domain is characterized as EF-hand 2.
+At position 336 to 495, the domain is characterized as Ferric oxidoreductase.
+At position 534 to 657, the domain is characterized as FAD-binding FR-type.
+At position 34 to 346, the domain is characterized as AB hydrolase-1.
+At position 105 to 293, the domain is characterized as CP-type G.
+At position 626 to 688, the domain is characterized as S1 motif.
+At position 293 to 523, the domain is characterized as TLDc.
+At position 11 to 232, the domain is characterized as ABC transporter.
+At position 506 to 684, the domain is characterized as Helicase ATP-binding.
+At position 705 to 872, the domain is characterized as Helicase C-terminal.
+At position 237 to 385, the domain is characterized as Helicase C-terminal.
+At position 91 to 230, the domain is characterized as Cyclin N-terminal.
+At position 68 to 315, the domain is characterized as Protein kinase.
+At position 8 to 89, the domain is characterized as NAB.
+At position 5 to 235, the domain is characterized as Glutamine amidotransferase type-1.
+At position 121 to 388, the domain is characterized as Radical SAM core.
+At position 528 to 578, the domain is characterized as SANT.
+At position 628 to 732, the domain is characterized as CXC.
+At position 747 to 862, the domain is characterized as SET.
+At position 274 to 349, the domain is characterized as B5.
+At position 21 to 102, the domain is characterized as Chorismate mutase.
+At position 38 to 330, the domain is characterized as tr-type G.
+At position 115 to 285, the domain is characterized as PITH.
+At position 65 to 113, the domain is characterized as F-box.
+At position 2 to 437, the domain is characterized as PTS EIIC type-2.
+At position 167 to 342, the domain is characterized as Helicase ATP-binding.
+At position 370 to 519, the domain is characterized as Helicase C-terminal.
+At position 218 to 411, the domain is characterized as Helicase ATP-binding.
+At position 422 to 584, the domain is characterized as Helicase C-terminal.
+At position 401 to 482, the domain is characterized as Disintegrin.
+At position 7 to 46, the domain is characterized as F-box.
+At position 74 to 118, the domain is characterized as LysM.
+At position 24 to 189, the domain is characterized as Reelin.
+At position 190 to 383, the domain is characterized as Spondin.
+At position 437 to 490, the domain is characterized as TSP type-1 1.
+At position 496 to 550, the domain is characterized as TSP type-1 2.
+At position 553 to 606, the domain is characterized as TSP type-1 3.
+At position 609 to 661, the domain is characterized as TSP type-1 4.
+At position 663 to 716, the domain is characterized as TSP type-1 5.
+At position 749 to 801, the domain is characterized as TSP type-1 6.
+At position 326 to 423, the domain is characterized as PDZ.
+At position 285 to 449, the domain is characterized as Hflx-type G.
+At position 18 to 178, the domain is characterized as Tyrosine-protein phosphatase.
+At position 169 to 255, the domain is characterized as PPIase FKBP-type.
+At position 14 to 59, the domain is characterized as F-box.
+At position 3 to 278, the domain is characterized as tr-type G.
+At position 3 to 194, the domain is characterized as RNase H type-2.
+At position 143 to 310, the domain is characterized as Helicase ATP-binding.
+At position 321 to 498, the domain is characterized as Helicase C-terminal.
+At position 118 to 159, the domain is characterized as JmjN.
+At position 185 to 279, the domain is characterized as ARID.
+At position 476 to 695, the domain is characterized as JmjC.
+At position 39 to 132, the domain is characterized as WSC.
+At position 400 to 481, the domain is characterized as Disintegrin.
+At position 10 to 85, the domain is characterized as Sm.
+At position 635 to 780, the domain is characterized as MOSC.
+At position 30 to 302, the domain is characterized as PPM-type phosphatase.
+At position 242 to 343, the domain is characterized as BEN 1.
+At position 387 to 487, the domain is characterized as BEN 2.
+At position 548 to 650, the domain is characterized as BEN 3.
+At position 715 to 816, the domain is characterized as BEN 4.
+At position 6 to 56, the domain is characterized as CHCH.
+At position 637 to 776, the domain is characterized as C2.
+At position 437 to 628, the domain is characterized as Glutamine amidotransferase type-1.
+At position 33 to 143, the domain is characterized as HD.
+At position 32 to 111, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 194, the domain is characterized as Ig-like C2-type 2.
+At position 201 to 286, the domain is characterized as Ig-like C2-type 3.
+At position 31 to 222, the domain is characterized as BPL/LPL catalytic.
+At position 198 to 241, the domain is characterized as LysM 2.
+At position 318 to 361, the domain is characterized as LysM 3.
+At position 405 to 523, the domain is characterized as NlpC/P60.
+At position 102 to 176, the domain is characterized as RRM 1.
+At position 193 to 270, the domain is characterized as RRM 2.
+At position 382 to 478, the domain is characterized as RRM 3.
+At position 495 to 583, the domain is characterized as RRM 4.
+At position 15 to 84, the domain is characterized as DRBM 1.
+At position 101 to 170, the domain is characterized as DRBM 2.
+At position 248 to 434, the domain is characterized as GATase cobBQ-type.
+At position 171 to 258, the domain is characterized as 5'-3' exonuclease.
+At position 78 to 238, the domain is characterized as CP-type G.
+At position 21 to 248, the domain is characterized as RNase H type-2.
+At position 10 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 267 to 336, the domain is characterized as PAP-associated.
+At position 188 to 292, the domain is characterized as Fe2OG dioxygenase.
+At position 297 to 332, the domain is characterized as EF-hand 1.
+At position 337 to 372, the domain is characterized as EF-hand 2.
+At position 176 to 283, the domain is characterized as Cadherin 1.
+At position 284 to 398, the domain is characterized as Cadherin 2.
+At position 399 to 513, the domain is characterized as Cadherin 3.
+At position 514 to 621, the domain is characterized as Cadherin 4.
+At position 620 to 728, the domain is characterized as Cadherin 5.
+At position 303 to 383, the domain is characterized as B5.
+At position 18 to 165, the domain is characterized as Thioredoxin.
+At position 56 to 241, the domain is characterized as BPL/LPL catalytic.
+At position 233 to 310, the domain is characterized as BCNT-C.
+At position 121 to 220, the domain is characterized as Ig-like 2.
+At position 229 to 325, the domain is characterized as Ig-like 3.
+At position 10 to 109, the domain is characterized as EH 1.
+At position 43 to 78, the domain is characterized as EF-hand 1.
+At position 129 to 225, the domain is characterized as EH 2.
+At position 300 to 398, the domain is characterized as EH 3.
+At position 333 to 368, the domain is characterized as EF-hand 2.
+At position 788 to 828, the domain is characterized as UBA.
+At position 69 to 331, the domain is characterized as Protein kinase.
+At position 48 to 145, the domain is characterized as Plastocyanin-like.
+At position 3 to 130, the domain is characterized as Thioredoxin.
+At position 45 to 140, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 159 to 203, the domain is characterized as LysM.
+At position 134 to 172, the domain is characterized as LRRCT.
+At position 14 to 74, the domain is characterized as HTH myb-type.
+At position 2 to 87, the domain is characterized as HPr.
+At position 1 to 297, the domain is characterized as SAM-dependent MTase C5-type.
+At position 518 to 713, the domain is characterized as STAS.
+At position 64 to 209, the domain is characterized as Cadherin 1.
+At position 210 to 320, the domain is characterized as Cadherin 2.
+At position 321 to 535, the domain is characterized as Cadherin 3.
+At position 536 to 639, the domain is characterized as Cadherin 4.
+At position 640 to 742, the domain is characterized as Cadherin 5.
+At position 746 to 863, the domain is characterized as Cadherin 6.
+At position 123 to 160, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 19 to 74, the domain is characterized as HTH cro/C1-type.
+At position 119 to 404, the domain is characterized as Protein kinase.
+At position 452 to 589, the domain is characterized as Thioredoxin.
+At position 428 to 464, the domain is characterized as CBM1.
+At position 679 to 797, the domain is characterized as CNA-B 1.
+At position 798 to 907, the domain is characterized as CNA-B 2.
+At position 908 to 1018, the domain is characterized as CNA-B 3.
+At position 1019 to 1129, the domain is characterized as CNA-B 4.
+At position 39 to 99, the domain is characterized as LIM zinc-binding.
+At position 217 to 382, the domain is characterized as CRAL-TRIO.
+At position 21 to 203, the domain is characterized as tr-type G.
+At position 155 to 273, the domain is characterized as C2.
+At position 66 to 268, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 114, the domain is characterized as VWFA.
+At position 130 to 219, the domain is characterized as Fibronectin type-III 1.
+At position 220 to 310, the domain is characterized as Fibronectin type-III 2.
+At position 311 to 401, the domain is characterized as Fibronectin type-III 3.
+At position 402 to 490, the domain is characterized as Fibronectin type-III 4.
+At position 491 to 585, the domain is characterized as Fibronectin type-III 5.
+At position 586 to 639, the domain is characterized as Fibronectin type-III 6.
+At position 1444 to 1668, the domain is characterized as Collagen IV NC1.
+At position 134 to 228, the domain is characterized as WSC.
+At position 580 to 632, the domain is characterized as LRRCT.
+At position 692 to 837, the domain is characterized as TIR.
+At position 7 to 36, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 172 to 203, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 205 to 234, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 30 to 475, the domain is characterized as Biotin carboxylation.
+At position 148 to 345, the domain is characterized as ATP-grasp.
+At position 624 to 699, the domain is characterized as Biotinyl-binding.
+At position 586 to 665, the domain is characterized as KIX.
+At position 1104 to 1176, the domain is characterized as Bromo.
+At position 1324 to 1701, the domain is characterized as CBP/p300-type HAT.
+At position 104 to 299, the domain is characterized as ATP-grasp.
+At position 23 to 104, the domain is characterized as RRM.
+At position 611 to 686, the domain is characterized as BRCT.
+At position 118 to 297, the domain is characterized as FAD-binding PCMH-type.
+At position 5 to 187, the domain is characterized as Guanylate kinase-like.
+At position 128 to 456, the domain is characterized as SAC.
+At position 566 to 692, the domain is characterized as G8.
+At position 143 to 309, the domain is characterized as Helicase ATP-binding.
+At position 390 to 570, the domain is characterized as Helicase C-terminal.
+At position 29 to 313, the domain is characterized as Protein kinase.
+At position 81 to 229, the domain is characterized as C2 NT-type.
+At position 24 to 114, the domain is characterized as ARID.
+At position 372 to 463, the domain is characterized as ELM2.
+At position 391 to 483, the domain is characterized as Fibronectin type-III 1.
+At position 484 to 576, the domain is characterized as Fibronectin type-III 2.
+At position 653 to 912, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 944 to 1228, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 111 to 130, the domain is characterized as HhH.
+At position 61 to 114, the domain is characterized as SANT.
+At position 347 to 437, the domain is characterized as SWIRM.
+At position 1 to 240, the domain is characterized as Deacetylase sirtuin-type.
+At position 53 to 236, the domain is characterized as MIF4G.
+At position 331 to 453, the domain is characterized as MI.
+At position 228 to 509, the domain is characterized as YjeF C-terminal.
+At position 227 to 477, the domain is characterized as CN hydrolase.
+At position 24 to 255, the domain is characterized as Radical SAM core.
+At position 353 to 459, the domain is characterized as ERCC4.
+At position 82 to 222, the domain is characterized as GST C-terminal.
+At position 390 to 412, the domain is characterized as WH2.
+At position 146 to 217, the domain is characterized as SANT.
+At position 80 to 248, the domain is characterized as TNase-like.
+At position 95 to 256, the domain is characterized as TNase-like.
+At position 119 to 358, the domain is characterized as NR LBD.
+At position 36 to 292, the domain is characterized as Peptidase S1.
+At position 5 to 95, the domain is characterized as Ig-like.
+At position 66 to 216, the domain is characterized as Flavodoxin-like.
+At position 269 to 546, the domain is characterized as FAD-binding FR-type.
+At position 44 to 235, the domain is characterized as DH.
+At position 266 to 387, the domain is characterized as PH.
+At position 416 to 491, the domain is characterized as DEP 1.
+At position 518 to 592, the domain is characterized as DEP 2.
+At position 620 to 698, the domain is characterized as PDZ.
+At position 210 to 259, the domain is characterized as EGF-like 2.
+At position 377 to 414, the domain is characterized as EGF-like 3.
+At position 519 to 557, the domain is characterized as EGF-like 4.
+At position 559 to 600, the domain is characterized as EGF-like 5.
+At position 287 to 411, the domain is characterized as MATH.
+At position 9 to 88, the domain is characterized as RRM 1.
+At position 108 to 185, the domain is characterized as RRM 2.
+At position 320 to 420, the domain is characterized as DOD-type homing endonuclease.
+At position 23 to 99, the domain is characterized as SAMD1-like winged helix (WH).
+At position 443 to 511, the domain is characterized as SAM.
+At position 384 to 444, the domain is characterized as LIM zinc-binding.
+At position 152 to 342, the domain is characterized as CheB-type methylesterase.
+At position 28 to 87, the domain is characterized as CBS 1.
+At position 91 to 156, the domain is characterized as CBS 2.
+At position 163 to 193, the domain is characterized as EF-hand 4.
+At position 85 to 174, the domain is characterized as EH 1.
+At position 118 to 153, the domain is characterized as EF-hand 1.
+At position 492 to 581, the domain is characterized as EH 2.
+At position 525 to 560, the domain is characterized as EF-hand 2.
+At position 1474 to 1491, the domain is characterized as WH2.
+At position 48 to 92, the domain is characterized as UBA.
+At position 593 to 675, the domain is characterized as BRCT.
+At position 79 to 402, the domain is characterized as Peptidase A1.
+At position 14 to 112, the domain is characterized as Chorein N-terminal.
+At position 22 to 103, the domain is characterized as Ig-like C2-type.
+At position 105 to 203, the domain is characterized as Ig-like V-type.
+At position 236 to 331, the domain is characterized as Ig-like C2-type 2.
+At position 18 to 290, the domain is characterized as CN hydrolase.
+At position 210 to 370, the domain is characterized as TrmE-type G.
+At position 60 to 97, the domain is characterized as LRRNT.
+At position 168 to 196, the domain is characterized as IQ 1.
+At position 197 to 218, the domain is characterized as IQ 2.
+At position 44 to 123, the domain is characterized as PB1.
+At position 362 to 622, the domain is characterized as Protein kinase.
+At position 35 to 179, the domain is characterized as Toprim.
+At position 69 to 259, the domain is characterized as ABC transmembrane type-1.
+At position 17 to 358, the domain is characterized as Kinesin motor.
+At position 269 to 366, the domain is characterized as PDZ.
+At position 14 to 177, the domain is characterized as Helicase ATP-binding.
+At position 195 to 368, the domain is characterized as Helicase C-terminal.
+At position 71 to 269, the domain is characterized as Laminin G-like.
+At position 20 to 153, the domain is characterized as SIS.
+At position 123 to 323, the domain is characterized as ATP-grasp.
+At position 242 to 361, the domain is characterized as PAZ.
+At position 532 to 843, the domain is characterized as Piwi.
+At position 610 to 711, the domain is characterized as tRNA-binding.
+At position 8 to 45, the domain is characterized as F-box.
+At position 62 to 167, the domain is characterized as HD.
+At position 28 to 171, the domain is characterized as GAF.
+At position 212 to 345, the domain is characterized as GGDEF.
+At position 354 to 609, the domain is characterized as EAL.
+At position 26 to 366, the domain is characterized as Transferrin-like 1.
+At position 372 to 621, the domain is characterized as Transferrin-like 2.
+At position 439 to 553, the domain is characterized as Toprim.
+At position 367 to 398, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 98 to 337, the domain is characterized as NR LBD.
+At position 278 to 466, the domain is characterized as PPIase cyclophilin-type.
+At position 4 to 91, the domain is characterized as BMC.
+At position 491 to 539, the domain is characterized as LysM.
+At position 28 to 106, the domain is characterized as Sm.
+At position 291 to 389, the domain is characterized as PpiC 2.
+At position 254 to 470, the domain is characterized as Histidine kinase.
+At position 41 to 143, the domain is characterized as HD.
+At position 14 to 355, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 364 to 685, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 149 to 247, the domain is characterized as Ig-like C2-type 2.
+At position 256 to 347, the domain is characterized as Ig-like C2-type 3.
+At position 354 to 448, the domain is characterized as Ig-like C2-type 4.
+At position 454 to 554, the domain is characterized as Ig-like C2-type 5.
+At position 558 to 649, the domain is characterized as Ig-like C2-type 6.
+At position 754 to 846, the domain is characterized as Ig-like C2-type 7.
+At position 852 to 953, the domain is characterized as Ig-like C2-type 8.
+At position 957 to 1052, the domain is characterized as Fibronectin type-III.
+At position 13 to 115, the domain is characterized as Calponin-homology (CH).
+At position 173 to 243, the domain is characterized as EB1 C-terminal.
+At position 424 to 596, the domain is characterized as tr-type G.
+At position 131 to 303, the domain is characterized as ATP-grasp.
+At position 6 to 126, the domain is characterized as Peptidase C39.
+At position 464 to 657, the domain is characterized as ABC transporter.
+At position 52 to 87, the domain is characterized as EF-hand 1.
+At position 121 to 156, the domain is characterized as EF-hand 2.
+At position 479 to 741, the domain is characterized as Reverse transcriptase.
+At position 1 to 72, the domain is characterized as Ubiquitin-like.
+At position 434 to 472, the domain is characterized as UBA.
+At position 114 to 260, the domain is characterized as PA14.
+At position 71 to 137, the domain is characterized as G protein gamma.
+At position 981 to 1276, the domain is characterized as Autotransporter.
+At position 359 to 449, the domain is characterized as Fibronectin type-III 1.
+At position 583 to 675, the domain is characterized as Fibronectin type-III 2.
+At position 677 to 787, the domain is characterized as Fibronectin type-III 3.
+At position 102 to 223, the domain is characterized as MPN.
+At position 24 to 106, the domain is characterized as CBS 1.
+At position 122 to 196, the domain is characterized as CBS 2.
+At position 210 to 281, the domain is characterized as CBS 3.
+At position 297 to 352, the domain is characterized as CBS 4.
+At position 22 to 238, the domain is characterized as ABC transporter.
+At position 945 to 1296, the domain is characterized as Protein kinase.
+At position 261 to 309, the domain is characterized as RPE1 insert.
+At position 39 to 124, the domain is characterized as Core-binding (CB).
+At position 152 to 327, the domain is characterized as Tyr recombinase.
+At position 156 to 332, the domain is characterized as Helicase ATP-binding.
+At position 346 to 516, the domain is characterized as Helicase C-terminal.
+At position 720 to 958, the domain is characterized as NR LBD.
+At position 172 to 263, the domain is characterized as CS.
+At position 280 to 392, the domain is characterized as FAD-binding FR-type.
+At position 196 to 280, the domain is characterized as TonB C-terminal.
+At position 192 to 241, the domain is characterized as bHLH.
+At position 1 to 127, the domain is characterized as VOC.
+At position 299 to 460, the domain is characterized as FCP1 homology.
+At position 6 to 222, the domain is characterized as Radical SAM core.
+At position 403 to 609, the domain is characterized as Helicase ATP-binding.
+At position 620 to 783, the domain is characterized as Helicase C-terminal.
+At position 274 to 652, the domain is characterized as USP.
+At position 408 to 477, the domain is characterized as Disintegrin.
+At position 360 to 595, the domain is characterized as NR LBD.
+At position 201 to 278, the domain is characterized as SWIB/MDM2.
+At position 20 to 224, the domain is characterized as L-type lectin-like.
+At position 108 to 301, the domain is characterized as ATP-grasp.
+At position 2 to 46, the domain is characterized as LysM.
+At position 155 to 341, the domain is characterized as CheB-type methylesterase.
+At position 34 to 162, the domain is characterized as FAS1 1.
+At position 463 to 604, the domain is characterized as FAS1 2.
+At position 606 to 744, the domain is characterized as FAS1 3.
+At position 149 to 235, the domain is characterized as PDZ 1.
+At position 244 to 330, the domain is characterized as PDZ 2.
+At position 404 to 484, the domain is characterized as PDZ 3.
+At position 519 to 589, the domain is characterized as SH3.
+At position 659 to 834, the domain is characterized as Guanylate kinase-like.
+At position 3 to 130, the domain is characterized as RNase III.
+At position 157 to 228, the domain is characterized as DRBM.
+At position 160 to 848, the domain is characterized as Peptidase M13.
+At position 331 to 508, the domain is characterized as PCI.
+At position 408 to 668, the domain is characterized as Protein kinase.
+At position 669 to 737, the domain is characterized as AGC-kinase C-terminal.
+At position 31 to 214, the domain is characterized as YjeF N-terminal.
+At position 216 to 474, the domain is characterized as YjeF C-terminal.
+At position 16 to 107, the domain is characterized as Core-binding (CB).
+At position 128 to 315, the domain is characterized as Tyr recombinase.
+At position 235 to 404, the domain is characterized as PCI.
+At position 129 to 279, the domain is characterized as 3'-5' exonuclease.
+At position 6 to 129, the domain is characterized as Thioredoxin.
+At position 21 to 84, the domain is characterized as F-box.
+At position 358 to 409, the domain is characterized as FBD.
+At position 4 to 87, the domain is characterized as GIY-YIG.
+At position 26 to 79, the domain is characterized as WAP.
+At position 108 to 159, the domain is characterized as Kazal-like.
+At position 186 to 279, the domain is characterized as Ig-like C2-type.
+At position 299 to 351, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 359 to 409, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 409 to 540, the domain is characterized as NTR.
+At position 239 to 517, the domain is characterized as Protein kinase.
+At position 1 to 226, the domain is characterized as ABC transporter.
+At position 81 to 162, the domain is characterized as SH2.
+At position 207 to 255, the domain is characterized as SOCS box.
+At position 123 to 198, the domain is characterized as J.
+At position 228 to 532, the domain is characterized as SEC63.
+At position 172 to 363, the domain is characterized as CheB-type methylesterase.
+At position 747 to 821, the domain is characterized as PAS 2.
+At position 901 to 1118, the domain is characterized as Histidine kinase.
+At position 39 to 68, the domain is characterized as HhH.
+At position 50 to 264, the domain is characterized as Radical SAM core.
+At position 37 to 145, the domain is characterized as Fibronectin type-III 1.
+At position 153 to 248, the domain is characterized as Fibronectin type-III 2.
+At position 352 to 390, the domain is characterized as EGF-like 1.
+At position 395 to 573, the domain is characterized as Laminin G-like 1.
+At position 574 to 611, the domain is characterized as EGF-like 2.
+At position 618 to 797, the domain is characterized as Laminin G-like 2.
+At position 793 to 829, the domain is characterized as EGF-like 3.
+At position 836 to 1015, the domain is characterized as Laminin G-like 3.
+At position 38 to 153, the domain is characterized as sHSP.
+At position 50 to 112, the domain is characterized as SH3.
+At position 15 to 267, the domain is characterized as Pterin-binding.
+At position 78 to 230, the domain is characterized as Tyrosine-protein phosphatase.
+At position 22 to 136, the domain is characterized as CUB 1.
+At position 137 to 178, the domain is characterized as EGF-like; calcium-binding.
+At position 181 to 296, the domain is characterized as CUB 2.
+At position 298 to 362, the domain is characterized as Sushi 1.
+At position 363 to 430, the domain is characterized as Sushi 2.
+At position 445 to 687, the domain is characterized as Peptidase S1.
+At position 29 to 338, the domain is characterized as GH18.
+At position 159 to 281, the domain is characterized as Ferric oxidoreductase.
+At position 300 to 418, the domain is characterized as FAD-binding FR-type.
+At position 212 to 274, the domain is characterized as t-SNARE coiled-coil homology.
+At position 173 to 399, the domain is characterized as NR LBD.
+At position 393 to 597, the domain is characterized as Histidine kinase.
+At position 4 to 89, the domain is characterized as Carrier.
+At position 262 to 348, the domain is characterized as Toprim.
+At position 96 to 171, the domain is characterized as Smr.
+At position 196 to 387, the domain is characterized as GMPS ATP-PPase.
+At position 595 to 697, the domain is characterized as tRNA-binding.
+At position 711 to 792, the domain is characterized as ACT 1.
+At position 24 to 123, the domain is characterized as Gnk2-homologous 1.
+At position 133 to 246, the domain is characterized as Gnk2-homologous 2.
+At position 345 to 624, the domain is characterized as Protein kinase.
+At position 254 to 476, the domain is characterized as Ku.
+At position 17 to 239, the domain is characterized as ThyX.
+At position 112 to 274, the domain is characterized as JmjC.
+At position 4 to 119, the domain is characterized as PpiC.
+At position 28 to 239, the domain is characterized as MARVEL.
+At position 383 to 705, the domain is characterized as Peptidase S8.
+At position 714 to 852, the domain is characterized as P/Homo B.
+At position 11 to 131, the domain is characterized as GAF.
+At position 158 to 381, the domain is characterized as Histidine kinase.
+At position 608 to 782, the domain is characterized as PCI.
+At position 46 to 135, the domain is characterized as Cystatin 1.
+At position 152 to 214, the domain is characterized as Cystatin 2.
+At position 1 to 88, the domain is characterized as ENT.
+At position 332 to 395, the domain is characterized as bZIP.
+At position 56 to 96, the domain is characterized as EGF-like.
+At position 2 to 237, the domain is characterized as ABC transporter 1.
+At position 247 to 491, the domain is characterized as ABC transporter 2.
+At position 17 to 161, the domain is characterized as uDENN.
+At position 173 to 340, the domain is characterized as cDENN.
+At position 342 to 575, the domain is characterized as dDENN.
+At position 107 to 167, the domain is characterized as SH3.
+At position 173 to 263, the domain is characterized as SH2.
+At position 288 to 539, the domain is characterized as Protein kinase.
+At position 8 to 105, the domain is characterized as DMAP1-binding.
+At position 667 to 791, the domain is characterized as BAH 1.
+At position 883 to 1011, the domain is characterized as BAH 2.
+At position 1054 to 1513, the domain is characterized as SAM-dependent MTase C5-type.
+At position 45 to 323, the domain is characterized as GH10.
+At position 56 to 115, the domain is characterized as SH3 1.
+At position 322 to 456, the domain is characterized as ZU5.
+At position 656 to 726, the domain is characterized as SH3 2.
+At position 465 to 566, the domain is characterized as CBM20.
+At position 103 to 176, the domain is characterized as Ubiquitin-like.
+At position 177 to 531, the domain is characterized as USP.
+At position 431 to 619, the domain is characterized as VWFA.
+At position 162 to 284, the domain is characterized as C-type lectin.
+At position 1 to 69, the domain is characterized as TGS.
+At position 7 to 70, the domain is characterized as SAM.
+At position 118 to 249, the domain is characterized as Fatty acid hydroxylase.
+At position 9 to 95, the domain is characterized as Core-binding (CB).
+At position 116 to 296, the domain is characterized as Tyr recombinase.
+At position 42 to 131, the domain is characterized as ACB.
+At position 171 to 357, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 61, the domain is characterized as HTH lacI-type.
+At position 261 to 333, the domain is characterized as Fibronectin type-III 1.
+At position 447 to 566, the domain is characterized as Fibronectin type-III 2.
+At position 146 to 203, the domain is characterized as CBS 2.
+At position 35 to 126, the domain is characterized as Fibronectin type-III 1.
+At position 148 to 240, the domain is characterized as Fibronectin type-III 2.
+At position 619 to 709, the domain is characterized as BRCT.
+At position 51 to 125, the domain is characterized as Rho RNA-BD.
+At position 14 to 284, the domain is characterized as PTS EIID.
+At position 13 to 91, the domain is characterized as RRM 1.
+At position 100 to 179, the domain is characterized as RRM 2.
+At position 338 to 566, the domain is characterized as ABC transporter 2.
+At position 10 to 140, the domain is characterized as B12-binding.
+At position 877 to 986, the domain is characterized as MSP.
+At position 173 to 227, the domain is characterized as Laminin EGF-like 1.
+At position 228 to 277, the domain is characterized as Laminin EGF-like 2.
+At position 298 to 442, the domain is characterized as NTR.
+At position 4 to 142, the domain is characterized as DAC.
+At position 192 to 354, the domain is characterized as TRUD.
+At position 333 to 577, the domain is characterized as NR LBD.
+At position 40 to 179, the domain is characterized as sHSP.
+At position 6 to 207, the domain is characterized as ABC transporter.
+At position 321 to 491, the domain is characterized as tr-type G.
+At position 195 to 244, the domain is characterized as bHLH.
+At position 23 to 364, the domain is characterized as Transferrin-like 1.
+At position 371 to 676, the domain is characterized as Transferrin-like 2.
+At position 35 to 110, the domain is characterized as EamA.
+At position 218 to 454, the domain is characterized as Ras-GEF.
+At position 2 to 78, the domain is characterized as Carrier 1.
+At position 1054 to 1130, the domain is characterized as Carrier 2.
+At position 79 to 163, the domain is characterized as Core-binding (CB).
+At position 186 to 392, the domain is characterized as Tyr recombinase.
+At position 77 to 198, the domain is characterized as C-type lectin.
+At position 140 to 301, the domain is characterized as PX.
+At position 113 to 247, the domain is characterized as Fatty acid hydroxylase.
+At position 133 to 335, the domain is characterized as ATP-grasp.
+At position 21 to 210, the domain is characterized as RNase H type-2.
+At position 4 to 371, the domain is characterized as Trm1 methyltransferase.
+At position 81 to 153, the domain is characterized as RRM 1.
+At position 155 to 236, the domain is characterized as RRM 2.
+At position 33 to 181, the domain is characterized as Nudix hydrolase.
+At position 96 to 254, the domain is characterized as Upf1 CH-rich.
+At position 267 to 599, the domain is characterized as USP.
+At position 19 to 126, the domain is characterized as XRN2-binding (XTBD).
+At position 452 to 527, the domain is characterized as DRBM.
+At position 282 to 324, the domain is characterized as EGF-like 1.
+At position 588 to 628, the domain is characterized as EGF-like 2.
+At position 889 to 930, the domain is characterized as EGF-like 3.
+At position 1203 to 1244, the domain is characterized as EGF-like 4.
+At position 1248 to 1286, the domain is characterized as LDL-receptor class A 1.
+At position 1287 to 1323, the domain is characterized as LDL-receptor class A 2.
+At position 1325 to 1361, the domain is characterized as LDL-receptor class A 3.
+At position 240 to 318, the domain is characterized as RRM.
+At position 245 to 426, the domain is characterized as SSD.
+At position 62 to 240, the domain is characterized as Eph LBD.
+At position 359 to 469, the domain is characterized as Fibronectin type-III 1.
+At position 470 to 564, the domain is characterized as Fibronectin type-III 2.
+At position 677 to 938, the domain is characterized as Protein kinase.
+At position 967 to 1005, the domain is characterized as SAM.
+At position 942 to 1094, the domain is characterized as Rieske; atypical.
+At position 25 to 381, the domain is characterized as IF rod.
+At position 445 to 562, the domain is characterized as LTD.
+At position 57 to 193, the domain is characterized as C1q.
+At position 127 to 500, the domain is characterized as PRONE.
+At position 72 to 259, the domain is characterized as B30.2/SPRY.
+At position 290 to 322, the domain is characterized as LisH.
+At position 328 to 385, the domain is characterized as CTLH.
+At position 48 to 194, the domain is characterized as FPL.
+At position 158 to 483, the domain is characterized as Peptidase S8.
+At position 491 to 627, the domain is characterized as P/Homo B.
+At position 129 to 246, the domain is characterized as PX.
+At position 383 to 484, the domain is characterized as HD.
+At position 108 to 164, the domain is characterized as EutK-Ctail.
+At position 136 to 206, the domain is characterized as FISNA.
+At position 216 to 532, the domain is characterized as NACHT.
+At position 30 to 119, the domain is characterized as SUEL-type lectin.
+At position 713 to 760, the domain is characterized as GPS.
+At position 98 to 270, the domain is characterized as Helicase ATP-binding.
+At position 298 to 442, the domain is characterized as Helicase C-terminal.
+At position 18 to 170, the domain is characterized as N-acetyltransferase 1.
+At position 176 to 333, the domain is characterized as N-acetyltransferase 2.
+At position 1136 to 1552, the domain is characterized as FAT.
+At position 1808 to 2192, the domain is characterized as PI3K/PI4K catalytic.
+At position 2312 to 2344, the domain is characterized as FATC.
+At position 1877 to 1912, the domain is characterized as EF-hand.
+At position 48 to 165, the domain is characterized as MTTase N-terminal.
+At position 188 to 430, the domain is characterized as Radical SAM core.
+At position 433 to 496, the domain is characterized as TRAM.
+At position 44 to 353, the domain is characterized as PPM-type phosphatase.
+At position 5 to 164, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 181 to 253, the domain is characterized as RRM.
+At position 10 to 61, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 13 to 72, the domain is characterized as Tudor-knot.
+At position 172 to 521, the domain is characterized as MRG.
+At position 131 to 298, the domain is characterized as Nudix hydrolase.
+At position 18 to 103, the domain is characterized as ACB.
+At position 468 to 667, the domain is characterized as FtsK.
+At position 3 to 124, the domain is characterized as TsaA-like.
+At position 142 to 233, the domain is characterized as ARID.
+At position 336 to 434, the domain is characterized as sHSP.
+At position 454 to 504, the domain is characterized as DHHC.
+At position 10 to 228, the domain is characterized as DHFR.
+At position 276 to 475, the domain is characterized as B30.2/SPRY.
+At position 20 to 133, the domain is characterized as FZ.
+At position 40 to 124, the domain is characterized as PNT.
+At position 225 to 555, the domain is characterized as USP.
+At position 66 to 101, the domain is characterized as EF-hand 2.
+At position 11 to 355, the domain is characterized as Kinesin motor.
+At position 60 to 108, the domain is characterized as EGF-like 2.
+At position 108 to 148, the domain is characterized as EGF-like 3.
+At position 151 to 175, the domain is characterized as EGF-like 4; truncated.
+At position 37 to 191, the domain is characterized as SIS.
+At position 17 to 492, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 541 to 838, the domain is characterized as UvrD-like helicase C-terminal.
+At position 351 to 417, the domain is characterized as S4 RNA-binding.
+At position 29 to 107, the domain is characterized as GIY-YIG.
+At position 217 to 252, the domain is characterized as UVR.
+At position 28 to 270, the domain is characterized as ABC transporter.
+At position 275 to 348, the domain is characterized as RRM 1.
+At position 360 to 433, the domain is characterized as RRM 2.
+At position 213 to 373, the domain is characterized as Helicase C-terminal.
+At position 8 to 117, the domain is characterized as Ig-like C1-type.
+At position 512 to 1044, the domain is characterized as Histidine kinase.
+At position 1245 to 1366, the domain is characterized as Response regulatory.
+At position 44 to 497, the domain is characterized as ADPK.
+At position 585 to 686, the domain is characterized as tRNA-binding.
+At position 55 to 115, the domain is characterized as Chromo.
+At position 7 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 151 to 180, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 47, the domain is characterized as Disintegrin.
+At position 345 to 409, the domain is characterized as S4 RNA-binding.
+At position 273 to 335, the domain is characterized as SAM.
+At position 61 to 201, the domain is characterized as HD.
+At position 5 to 174, the domain is characterized as Era-type G.
+At position 475 to 488, the domain is characterized as CRIB.
+At position 953 to 1205, the domain is characterized as Protein kinase.
+At position 47 to 190, the domain is characterized as SCP.
+At position 27 to 68, the domain is characterized as Chitin-binding type-1.
+At position 133 to 314, the domain is characterized as ELMO.
+At position 38 to 189, the domain is characterized as Thioredoxin.
+At position 408 to 493, the domain is characterized as PDZ 1.
+At position 529 to 614, the domain is characterized as PDZ 2.
+At position 12 to 254, the domain is characterized as ABC transporter.
+At position 29 to 238, the domain is characterized as GH16.
+At position 1 to 138, the domain is characterized as Peptidase S1.
+At position 6 to 89, the domain is characterized as GIY-YIG.
+At position 3 to 99, the domain is characterized as Cystatin.
+At position 6 to 98, the domain is characterized as CARD.
+At position 233 to 392, the domain is characterized as W2.
+At position 552 to 788, the domain is characterized as ABC transporter.
+At position 471 to 573, the domain is characterized as PDZ 1.
+At position 622 to 721, the domain is characterized as PDZ 2.
+At position 184 to 361, the domain is characterized as EngA-type G 2.
+At position 362 to 446, the domain is characterized as KH-like.
+At position 776 to 853, the domain is characterized as Carrier 1.
+At position 1826 to 1902, the domain is characterized as Carrier 2.
+At position 5 to 46, the domain is characterized as EGF-like.
+At position 471 to 643, the domain is characterized as SSD.
+At position 496 to 531, the domain is characterized as EF-hand 1.
+At position 528 to 563, the domain is characterized as EF-hand 2.
+At position 985 to 1047, the domain is characterized as FIP-RBD.
+At position 9 to 106, the domain is characterized as EH 1.
+At position 134 to 224, the domain is characterized as EH 2.
+At position 259 to 348, the domain is characterized as EH 3.
+At position 292 to 327, the domain is characterized as EF-hand 4.
+At position 135 to 419, the domain is characterized as Protein kinase.
+At position 96 to 160, the domain is characterized as Sushi 2.
+At position 223 to 285, the domain is characterized as Sushi 4.
+At position 379 to 537, the domain is characterized as SEFIR.
+At position 370 to 454, the domain is characterized as SWIB/MDM2.
+At position 478 to 551, the domain is characterized as SUI1.
+At position 178 to 405, the domain is characterized as Radical SAM core.
+At position 124 to 192, the domain is characterized as KH.
+At position 69 to 167, the domain is characterized as GTD-binding.
+At position 193 to 354, the domain is characterized as SUN.
+At position 575 to 831, the domain is characterized as Protein kinase.
+At position 141 to 218, the domain is characterized as RRM.
+At position 5 to 125, the domain is characterized as MSP.
+At position 607 to 719, the domain is characterized as CNA-B 1.
+At position 720 to 829, the domain is characterized as CNA-B 2.
+At position 830 to 940, the domain is characterized as CNA-B 3.
+At position 212 to 396, the domain is characterized as Helicase ATP-binding.
+At position 433 to 566, the domain is characterized as Helicase C-terminal.
+At position 365 to 401, the domain is characterized as EGF-like 1.
+At position 436 to 473, the domain is characterized as EGF-like 2.
+At position 4 to 114, the domain is characterized as VOC.
+At position 106 to 276, the domain is characterized as Helicase ATP-binding.
+At position 287 to 455, the domain is characterized as Helicase C-terminal.
+At position 221 to 289, the domain is characterized as HTH OST-type 2.
+At position 330 to 399, the domain is characterized as HTH OST-type 3.
+At position 500 to 557, the domain is characterized as Tudor 1.
+At position 689 to 746, the domain is characterized as Tudor 2.
+At position 29 to 130, the domain is characterized as GOLD.
+At position 86 to 323, the domain is characterized as PABS.
+At position 2294 to 2533, the domain is characterized as I/LWEQ.
+At position 63 to 126, the domain is characterized as PWWP.
+At position 611 to 717, the domain is characterized as PH.
+At position 309 to 438, the domain is characterized as OTU.
+At position 457 to 476, the domain is characterized as UIM.
+At position 2 to 174, the domain is characterized as AMMECR1.
+At position 41 to 86, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 92 to 132, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 133 to 175, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 42 to 165, the domain is characterized as TBDR plug.
+At position 176 to 913, the domain is characterized as TBDR beta-barrel.
+At position 1 to 56, the domain is characterized as DEK-C.
+At position 119 to 195, the domain is characterized as SWIB/MDM2.
+At position 18 to 182, the domain is characterized as Radical SAM core.
+At position 257 to 330, the domain is characterized as RRM 1.
+At position 336 to 415, the domain is characterized as RRM 2.
+At position 21 to 281, the domain is characterized as Protein kinase.
+At position 323 to 395, the domain is characterized as NAF.
+At position 38 to 156, the domain is characterized as Ig-like V-type.
+At position 160 to 255, the domain is characterized as Link 1.
+At position 260 to 352, the domain is characterized as Link 2.
+At position 9 to 336, the domain is characterized as DhaK.
+At position 372 to 571, the domain is characterized as DhaL.
+At position 5 to 247, the domain is characterized as CN hydrolase.
+At position 1 to 49, the domain is characterized as Agenet-like 1.
+At position 65 to 117, the domain is characterized as Agenet-like 2.
+At position 221 to 282, the domain is characterized as KH 1.
+At position 284 to 353, the domain is characterized as KH 2.
+At position 27 to 279, the domain is characterized as Pyruvate carboxyltransferase.
+At position 325 to 564, the domain is characterized as ABC transporter 2.
+At position 1095 to 1258, the domain is characterized as JmjC.
+At position 4 to 148, the domain is characterized as MGS-like.
+At position 691 to 887, the domain is characterized as ATP-grasp 2.
+At position 963 to 1099, the domain is characterized as MGS-like.
+At position 496 to 777, the domain is characterized as Protein kinase.
+At position 778 to 861, the domain is characterized as AGC-kinase C-terminal.
+At position 38 to 202, the domain is characterized as SIS.
+At position 50 to 265, the domain is characterized as Radical SAM core.
+At position 30 to 96, the domain is characterized as BTB.
+At position 199 to 273, the domain is characterized as Toprim.
+At position 147 to 454, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 5 to 91, the domain is characterized as BMC.
+At position 4 to 243, the domain is characterized as CN hydrolase.
+At position 22 to 80, the domain is characterized as Chitin-binding type-2 1.
+At position 90 to 148, the domain is characterized as Chitin-binding type-2 2.
+At position 170 to 227, the domain is characterized as Chitin-binding type-2 3.
+At position 291 to 369, the domain is characterized as B5.
+At position 586 to 858, the domain is characterized as Protein kinase.
+At position 132 to 585, the domain is characterized as Urease.
+At position 227 to 301, the domain is characterized as POU-specific.
+At position 361 to 412, the domain is characterized as FBD.
+At position 193 to 308, the domain is characterized as SET.
+At position 1211 to 1273, the domain is characterized as FIP-RBD.
+At position 85 to 184, the domain is characterized as Toprim.
+At position 191 to 243, the domain is characterized as PQ-loop 2.
+At position 822 to 889, the domain is characterized as SH3 1.
+At position 982 to 1070, the domain is characterized as Fibronectin type-III 1.
+At position 1075 to 1171, the domain is characterized as Fibronectin type-III 2.
+At position 1420 to 1488, the domain is characterized as SH3 2.
+At position 1536 to 1603, the domain is characterized as SH3 3.
+At position 2 to 142, the domain is characterized as N-acetyltransferase.
+At position 207 to 237, the domain is characterized as EF-hand 3.
+At position 522 to 638, the domain is characterized as PI-PLC Y-box.
+At position 638 to 765, the domain is characterized as C2.
+At position 77 to 141, the domain is characterized as KH 1.
+At position 162 to 228, the domain is characterized as KH 2.
+At position 253 to 317, the domain is characterized as KH 3.
+At position 354 to 421, the domain is characterized as KH 4.
+At position 62 to 184, the domain is characterized as PX.
+At position 27 to 66, the domain is characterized as F-box.
+At position 334 to 383, the domain is characterized as bHLH.
+At position 35 to 146, the domain is characterized as Ig-like V-type 1.
+At position 153 to 241, the domain is characterized as Ig-like V-type 2.
+At position 55 to 124, the domain is characterized as H15.
+At position 19 to 108, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 246 to 427, the domain is characterized as FAD-binding PCMH-type.
+At position 110 to 163, the domain is characterized as bHLH.
+At position 20 to 220, the domain is characterized as Reticulon.
+At position 99 to 186, the domain is characterized as PB1.
+At position 420 to 534, the domain is characterized as Toprim.
+At position 402 to 465, the domain is characterized as SAM.
+At position 363 to 579, the domain is characterized as Histidine kinase.
+At position 165 to 241, the domain is characterized as Toprim.
+At position 125 to 307, the domain is characterized as PID.
+At position 478 to 569, the domain is characterized as SH2.
+At position 504 to 610, the domain is characterized as CBM20.
+At position 342 to 417, the domain is characterized as RRM 2.
+At position 111 to 238, the domain is characterized as OmpA-like.
+At position 947 to 1087, the domain is characterized as PINc.
+At position 176 to 269, the domain is characterized as 5'-3' exonuclease.
+At position 483 to 582, the domain is characterized as Peptidase S74.
+At position 48 to 130, the domain is characterized as GOLD.
+At position 53 to 125, the domain is characterized as Cadherin 1.
+At position 358 to 459, the domain is characterized as Cadherin 4.
+At position 174 to 357, the domain is characterized as MIF4G.
+At position 460 to 576, the domain is characterized as MI.
+At position 254 to 286, the domain is characterized as WW.
+At position 365 to 533, the domain is characterized as PID 1.
+At position 538 to 700, the domain is characterized as PID 2.
+At position 288 to 373, the domain is characterized as PDZ 1.
+At position 875 to 956, the domain is characterized as PDZ 2.
+At position 14 to 94, the domain is characterized as Expansin-like CBD.
+At position 6 to 61, the domain is characterized as Kazal-like.
+At position 24 to 122, the domain is characterized as Gnk2-homologous 1.
+At position 128 to 241, the domain is characterized as Gnk2-homologous 2.
+At position 522 to 593, the domain is characterized as KHA.
+At position 187 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 395 to 424, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 435 to 464, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 43 to 290, the domain is characterized as Laminin N-terminal.
+At position 291 to 346, the domain is characterized as Laminin EGF-like 1.
+At position 347 to 409, the domain is characterized as Laminin EGF-like 2.
+At position 410 to 459, the domain is characterized as Laminin EGF-like 3.
+At position 478 to 604, the domain is characterized as NTR.
+At position 26 to 364, the domain is characterized as Kinesin motor.
+At position 235 to 300, the domain is characterized as SH3.
+At position 81 to 200, the domain is characterized as RGS.
+At position 758 to 840, the domain is characterized as DIX.
+At position 204 to 310, the domain is characterized as HTH APSES-type.
+At position 174 to 209, the domain is characterized as EF-hand.
+At position 251 to 338, the domain is characterized as Ig-like 1.
+At position 24 to 114, the domain is characterized as Ig-like.
+At position 24 to 663, the domain is characterized as Vitellogenin.
+At position 1417 to 1593, the domain is characterized as VWFD.
+At position 160 to 325, the domain is characterized as OBG-type G.
+At position 315 to 546, the domain is characterized as START.
+At position 213 to 487, the domain is characterized as Protein kinase.
+At position 43 to 76, the domain is characterized as Collagen-like.
+At position 82 to 215, the domain is characterized as C1q.
+At position 1 to 61, the domain is characterized as Sm.
+At position 87 to 123, the domain is characterized as DFDF.
+At position 222 to 431, the domain is characterized as YjeF N-terminal.
+At position 6 to 66, the domain is characterized as MADS-box.
+At position 89 to 208, the domain is characterized as GST C-terminal.
+At position 216 to 365, the domain is characterized as JmjC.
+At position 150 to 273, the domain is characterized as MH1.
+At position 350 to 570, the domain is characterized as MH2.
+At position 99 to 178, the domain is characterized as PRC barrel.
+At position 31 to 139, the domain is characterized as DM13.
+At position 184 to 329, the domain is characterized as DOMON 1.
+At position 524 to 645, the domain is characterized as DOMON 2.
+At position 653 to 850, the domain is characterized as Cytochrome b561.
+At position 93 to 267, the domain is characterized as Prephenate dehydratase.
+At position 279 to 356, the domain is characterized as ACT.
+At position 3 to 67, the domain is characterized as SH3.
+At position 503 to 777, the domain is characterized as MYST-type HAT.
+At position 147 to 264, the domain is characterized as C2 1.
+At position 278 to 399, the domain is characterized as C2 2.
+At position 37 to 121, the domain is characterized as Saposin B-type.
+At position 99 to 157, the domain is characterized as J.
+At position 50 to 276, the domain is characterized as Radical SAM core.
+At position 676 to 751, the domain is characterized as RRM 1.
+At position 905 to 979, the domain is characterized as RRM 2.
+At position 1 to 247, the domain is characterized as F-BAR.
+At position 361 to 416, the domain is characterized as SH3.
+At position 8 to 140, the domain is characterized as NTF2.
+At position 418 to 494, the domain is characterized as RRM.
+At position 10 to 97, the domain is characterized as RRM 1.
+At position 113 to 190, the domain is characterized as RRM 2.
+At position 84 to 122, the domain is characterized as EGF-like.
+At position 375 to 617, the domain is characterized as ABC transporter.
+At position 476 to 664, the domain is characterized as Helicase ATP-binding.
+At position 905 to 1085, the domain is characterized as Helicase C-terminal.
+At position 21 to 327, the domain is characterized as PPM-type phosphatase.
+At position 204 to 388, the domain is characterized as Helicase ATP-binding.
+At position 201 to 274, the domain is characterized as RRM 1.
+At position 292 to 379, the domain is characterized as RRM 2.
+At position 431 to 504, the domain is characterized as RRM 3.
+At position 522 to 602, the domain is characterized as RRM 4.
+At position 10 to 84, the domain is characterized as H15 1.
+At position 145 to 220, the domain is characterized as H15 2.
+At position 100 to 141, the domain is characterized as UBA.
+At position 704 to 1009, the domain is characterized as Protein kinase.
+At position 1010 to 1089, the domain is characterized as AGC-kinase C-terminal.
+At position 18 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 209 to 398, the domain is characterized as GMPS ATP-PPase.
+At position 32 to 288, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 159 to 258, the domain is characterized as Fe2OG dioxygenase.
+At position 371 to 803, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1313 to 1631, the domain is characterized as PKS/mFAS DH.
+At position 1709 to 1788, the domain is characterized as Carrier.
+At position 216 to 361, the domain is characterized as TrmE-type G.
+At position 47 to 319, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 230, the domain is characterized as Lon N-terminal.
+At position 706 to 893, the domain is characterized as Lon proteolytic.
+At position 30 to 76, the domain is characterized as F-box.
+At position 51 to 142, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 16 to 206, the domain is characterized as Reticulon.
+At position 207 to 372, the domain is characterized as Peptidase M12B.
+At position 390 to 464, the domain is characterized as Disintegrin.
+At position 465 to 506, the domain is characterized as PLAC.
+At position 224 to 283, the domain is characterized as SH3.
+At position 517 to 552, the domain is characterized as EF-hand 3.
+At position 355 to 486, the domain is characterized as KARI C-terminal knotted 2.
+At position 794 to 1080, the domain is characterized as Protein kinase.
+At position 171 to 212, the domain is characterized as PAS 1.
+At position 313 to 341, the domain is characterized as PAS 2.
+At position 432 to 505, the domain is characterized as PAS 3.
+At position 574 to 797, the domain is characterized as Histidine kinase.
+At position 825 to 941, the domain is characterized as Response regulatory.
+At position 55 to 200, the domain is characterized as SCP.
+At position 87 to 198, the domain is characterized as PH.
+At position 288 to 477, the domain is characterized as Rho-GAP.
+At position 5 to 90, the domain is characterized as GIY-YIG.
+At position 7 to 32, the domain is characterized as IQ.
+At position 441 to 476, the domain is characterized as EF-hand 1.
+At position 526 to 561, the domain is characterized as EF-hand 2.
+At position 566 to 601, the domain is characterized as EF-hand 3.
+At position 14 to 109, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 116 to 217, the domain is characterized as FAD-binding FR-type.
+At position 100 to 334, the domain is characterized as Radical SAM core.
+At position 1337 to 1412, the domain is characterized as DEP.
+At position 31 to 113, the domain is characterized as Lipoyl-binding.
+At position 18 to 128, the domain is characterized as HIT.
+At position 405 to 462, the domain is characterized as LRRCT.
+At position 31 to 45, the domain is characterized as CRIB.
+At position 718 to 938, the domain is characterized as Histidine kinase.
+At position 960 to 1074, the domain is characterized as Response regulatory.
+At position 1098 to 1197, the domain is characterized as HPt.
+At position 199 to 509, the domain is characterized as USP.
+At position 34 to 150, the domain is characterized as RGS.
+At position 273 to 300, the domain is characterized as KOW 1.
+At position 425 to 452, the domain is characterized as KOW 2.
+At position 477 to 504, the domain is characterized as KOW 3.
+At position 601 to 628, the domain is characterized as KOW 4.
+At position 712 to 739, the domain is characterized as KOW 5.
+At position 988 to 1015, the domain is characterized as KOW 6.
+At position 6 to 90, the domain is characterized as Cytochrome b5 heme-binding.
+At position 213 to 275, the domain is characterized as t-SNARE coiled-coil homology.
+At position 1 to 299, the domain is characterized as SAM-dependent MTase C5-type.
+At position 45 to 108, the domain is characterized as HMA.
+At position 650 to 904, the domain is characterized as Protein kinase.
+At position 45 to 92, the domain is characterized as F-box.
+At position 114 to 297, the domain is characterized as FBA.
+At position 277 to 534, the domain is characterized as Protein kinase.
+At position 641 to 734, the domain is characterized as SH2.
+At position 7 to 120, the domain is characterized as NTF2.
+At position 27 to 303, the domain is characterized as tr-type G.
+At position 31 to 77, the domain is characterized as F-box.
+At position 292 to 343, the domain is characterized as FBD.
+At position 82 to 386, the domain is characterized as Peptidase A1.
+At position 339 to 389, the domain is characterized as FBD.
+At position 152 to 217, the domain is characterized as OVATE.
+At position 51 to 234, the domain is characterized as tr-type G.
+At position 133 to 240, the domain is characterized as Cadherin 1.
+At position 241 to 352, the domain is characterized as Cadherin 2.
+At position 353 to 470, the domain is characterized as Cadherin 3.
+At position 471 to 574, the domain is characterized as Cadherin 4.
+At position 575 to 682, the domain is characterized as Cadherin 5.
+At position 36 to 151, the domain is characterized as Ig-like V-type.
+At position 12 to 124, the domain is characterized as FAD-binding FR-type.
+At position 269 to 358, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 376 to 646, the domain is characterized as Phosphatase tensin-type.
+At position 20 to 69, the domain is characterized as LRRNT.
+At position 369 to 422, the domain is characterized as LRRCT.
+At position 422 to 511, the domain is characterized as Ig-like C2-type.
+At position 111 to 205, the domain is characterized as ATP-grasp.
+At position 27 to 84, the domain is characterized as bHLH.
+At position 112 to 182, the domain is characterized as PAS.
+At position 316 to 465, the domain is characterized as Cupin type-1 2.
+At position 116 to 442, the domain is characterized as NB-ARC.
+At position 675 to 780, the domain is characterized as PA.
+At position 28 to 76, the domain is characterized as RPE1 insert.
+At position 167 to 580, the domain is characterized as Protein kinase.
+At position 70 to 257, the domain is characterized as RNase H type-2.
+At position 45 to 200, the domain is characterized as VOC 1.
+At position 216 to 376, the domain is characterized as VOC 2.
+At position 135 to 242, the domain is characterized as Cadherin 1.
+At position 243 to 354, the domain is characterized as Cadherin 2.
+At position 355 to 471, the domain is characterized as Cadherin 3.
+At position 580 to 690, the domain is characterized as Cadherin 5.
+At position 77 to 358, the domain is characterized as Protein kinase.
+At position 401 to 436, the domain is characterized as EF-hand 1.
+At position 437 to 472, the domain is characterized as EF-hand 2.
+At position 473 to 500, the domain is characterized as EF-hand 3.
+At position 504 to 539, the domain is characterized as EF-hand 4.
+At position 546 to 621, the domain is characterized as PUA.
+At position 42 to 156, the domain is characterized as Expansin-like EG45.
+At position 166 to 245, the domain is characterized as Expansin-like CBD.
+At position 13 to 79, the domain is characterized as HMA.
+At position 215 to 372, the domain is characterized as TrmE-type G.
+At position 32 to 225, the domain is characterized as Lon N-terminal.
+At position 625 to 806, the domain is characterized as Lon proteolytic.
+At position 1 to 185, the domain is characterized as GMPS ATP-PPase.
+At position 912 to 944, the domain is characterized as LisH.
+At position 8 to 228, the domain is characterized as MIF4G.
+At position 303 to 583, the domain is characterized as ABC transmembrane type-1 1.
+At position 615 to 839, the domain is characterized as ABC transporter 1.
+At position 914 to 1198, the domain is characterized as ABC transmembrane type-1 2.
+At position 1235 to 1469, the domain is characterized as ABC transporter 2.
+At position 791 to 970, the domain is characterized as DOC.
+At position 22 to 261, the domain is characterized as ABC transporter.
+At position 7 to 93, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 249 to 434, the domain is characterized as FAD-binding PCMH-type.
+At position 83 to 117, the domain is characterized as EF-hand 2; degenerate.
+At position 503 to 651, the domain is characterized as N-acetyltransferase.
+At position 740 to 810, the domain is characterized as Bromo.
+At position 20 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 298 to 557, the domain is characterized as Clu.
+At position 105 to 244, the domain is characterized as SIS 1.
+At position 277 to 422, the domain is characterized as SIS 2.
+At position 11 to 228, the domain is characterized as ABC transporter.
+At position 161 to 330, the domain is characterized as OBG-type G.
+At position 157 to 352, the domain is characterized as CheB-type methylesterase.
+At position 26 to 189, the domain is characterized as N-acetyltransferase.
+At position 156 to 293, the domain is characterized as OTU.
+At position 196 to 250, the domain is characterized as CVC.
+At position 3 to 313, the domain is characterized as YjeF C-terminal.
+At position 360 to 623, the domain is characterized as Protein kinase.
+At position 303 to 356, the domain is characterized as MIR 1.
+At position 368 to 427, the domain is characterized as MIR 2.
+At position 439 to 495, the domain is characterized as MIR 3.
+At position 187 to 469, the domain is characterized as NPH3.
+At position 18 to 101, the domain is characterized as IGFBP N-terminal.
+At position 70 to 141, the domain is characterized as Kazal-like.
+At position 143 to 243, the domain is characterized as Ig-like C2-type.
+At position 380 to 427, the domain is characterized as GPS.
+At position 109 to 278, the domain is characterized as PA14.
+At position 75 to 196, the domain is characterized as HD.
+At position 157 to 222, the domain is characterized as HTH luxR-type.
+At position 210 to 480, the domain is characterized as Protein kinase.
+At position 519 to 776, the domain is characterized as Protein kinase.
+At position 56 to 337, the domain is characterized as tr-type G.
+At position 30 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 129 to 227, the domain is characterized as Fibronectin type-III 2.
+At position 230 to 331, the domain is characterized as Fibronectin type-III 3.
+At position 332 to 433, the domain is characterized as Fibronectin type-III 4.
+At position 253 to 281, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 179 to 260, the domain is characterized as RRM.
+At position 437 to 582, the domain is characterized as CID.
+At position 631 to 665, the domain is characterized as SAP.
+At position 129 to 437, the domain is characterized as PPM-type phosphatase.
+At position 68 to 310, the domain is characterized as Peptidase S1.
+At position 18 to 108, the domain is characterized as PDZ 1.
+At position 296 to 329, the domain is characterized as WW 1.
+At position 342 to 375, the domain is characterized as WW 2.
+At position 413 to 495, the domain is characterized as PDZ 2.
+At position 729 to 811, the domain is characterized as PDZ 4.
+At position 1022 to 1104, the domain is characterized as PDZ 6.
+At position 69 to 181, the domain is characterized as AB hydrolase-1.
+At position 660 to 891, the domain is characterized as NR LBD.
+At position 46 to 316, the domain is characterized as Pyruvate carboxyltransferase.
+At position 25 to 140, the domain is characterized as Response regulatory.
+At position 115 to 329, the domain is characterized as Radical SAM core.
+At position 41 to 126, the domain is characterized as Inhibitor I9.
+At position 130 to 634, the domain is characterized as Peptidase S8.
+At position 401 to 486, the domain is characterized as PA.
+At position 306 to 849, the domain is characterized as PLA2c.
+At position 34 to 74, the domain is characterized as F-box.
+At position 20 to 210, the domain is characterized as GH11.
+At position 150 to 463, the domain is characterized as IF rod.
+At position 40 to 143, the domain is characterized as Calponin-homology (CH).
+At position 436 to 746, the domain is characterized as Kinesin motor.
+At position 756 to 873, the domain is characterized as GAE.
+At position 97 to 349, the domain is characterized as Tyrosine-protein phosphatase.
+At position 344 to 599, the domain is characterized as Protein kinase.
+At position 600 to 670, the domain is characterized as AGC-kinase C-terminal.
+At position 403 to 588, the domain is characterized as Helicase ATP-binding.
+At position 866 to 1032, the domain is characterized as Helicase C-terminal.
+At position 525 to 619, the domain is characterized as Fibronectin type-III.
+At position 16 to 195, the domain is characterized as Macro.
+At position 1209 to 1303, the domain is characterized as SH2.
+At position 22 to 215, the domain is characterized as Lon N-terminal.
+At position 602 to 783, the domain is characterized as Lon proteolytic.
+At position 680 to 760, the domain is characterized as ERCC4.
+At position 8 to 186, the domain is characterized as Guanylate kinase-like.
+At position 187 to 299, the domain is characterized as Fe2OG dioxygenase.
+At position 154 to 373, the domain is characterized as Histidine kinase.
+At position 364 to 416, the domain is characterized as FBD.
+At position 191 to 383, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 561 to 619, the domain is characterized as RAP.
+At position 29 to 93, the domain is characterized as J.
+At position 247 to 327, the domain is characterized as BCNT-C.
+At position 32 to 289, the domain is characterized as Protein kinase.
+At position 78 to 155, the domain is characterized as RRM.
+At position 117 to 300, the domain is characterized as ATP-grasp.
+At position 52 to 130, the domain is characterized as RRM 1.
+At position 140 to 217, the domain is characterized as RRM 2.
+At position 233 to 310, the domain is characterized as RRM 3.
+At position 336 to 460, the domain is characterized as RRM 4.
+At position 648 to 725, the domain is characterized as PABC.
+At position 92 to 229, the domain is characterized as OmpA-like.
+At position 42 to 184, the domain is characterized as Clp R.
+At position 458 to 492, the domain is characterized as UVR.
+At position 62 to 244, the domain is characterized as tr-type G.
+At position 37 to 256, the domain is characterized as Radical SAM core.
+At position 116 to 195, the domain is characterized as Death.
+At position 2 to 368, the domain is characterized as SPX.
+At position 624 to 815, the domain is characterized as EXS.
+At position 1 to 77, the domain is characterized as GST N-terminal.
+At position 192 to 393, the domain is characterized as Rho-GAP.
+At position 31 to 79, the domain is characterized as EGF-like 1.
+At position 80 to 131, the domain is characterized as EGF-like 2; calcium-binding.
+At position 132 to 171, the domain is characterized as EGF-like 3; calcium-binding.
+At position 172 to 220, the domain is characterized as EGF-like 4; calcium-binding.
+At position 221 to 267, the domain is characterized as EGF-like 5; calcium-binding.
+At position 268 to 316, the domain is characterized as EGF-like 6; calcium-binding.
+At position 547 to 596, the domain is characterized as GPS.
+At position 54 to 378, the domain is characterized as Asparaginase/glutaminase.
+At position 165 to 227, the domain is characterized as t-SNARE coiled-coil homology.
+At position 614 to 748, the domain is characterized as BAH 1.
+At position 788 to 929, the domain is characterized as BAH 2.
+At position 969 to 1402, the domain is characterized as SAM-dependent MTase C5-type.
+At position 240 to 303, the domain is characterized as SAM.
+At position 351 to 620, the domain is characterized as Protein kinase.
+At position 455 to 504, the domain is characterized as bHLH.
+At position 865 to 995, the domain is characterized as Guanylate cyclase.
+At position 51 to 151, the domain is characterized as SRCR 1.
+At position 158 to 258, the domain is characterized as SRCR 2.
+At position 265 to 365, the domain is characterized as SRCR 3.
+At position 372 to 472, the domain is characterized as SRCR 4.
+At position 477 to 577, the domain is characterized as SRCR 5.
+At position 582 to 682, the domain is characterized as SRCR 6.
+At position 718 to 818, the domain is characterized as SRCR 7.
+At position 823 to 925, the domain is characterized as SRCR 8.
+At position 928 to 1028, the domain is characterized as SRCR 9.
+At position 65 to 741, the domain is characterized as Myosin motor.
+At position 745 to 765, the domain is characterized as IQ 1.
+At position 768 to 788, the domain is characterized as IQ 2.
+At position 791 to 811, the domain is characterized as IQ 3.
+At position 814 to 834, the domain is characterized as IQ 4.
+At position 837 to 857, the domain is characterized as IQ 5.
+At position 1017 to 1253, the domain is characterized as MyTH4 1.
+At position 1258 to 1602, the domain is characterized as FERM 1.
+At position 1603 to 1672, the domain is characterized as SH3.
+At position 1747 to 1896, the domain is characterized as MyTH4 2.
+At position 1902 to 2205, the domain is characterized as FERM 2.
+At position 271 to 356, the domain is characterized as PDZ 1.
+At position 749 to 835, the domain is characterized as PDZ 2.
+At position 679 to 712, the domain is characterized as WW.
+At position 1 to 340, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 4 to 128, the domain is characterized as PX.
+At position 166 to 225, the domain is characterized as SH3 1.
+At position 266 to 325, the domain is characterized as SH3 2.
+At position 447 to 506, the domain is characterized as SH3 3.
+At position 1063 to 1124, the domain is characterized as SH3 5.
+At position 185 to 374, the domain is characterized as Helicase ATP-binding.
+At position 385 to 545, the domain is characterized as Helicase C-terminal.
+At position 144 to 250, the domain is characterized as Rhodanese.
+At position 89 to 132, the domain is characterized as LysM 2.
+At position 141 to 265, the domain is characterized as Peptidase C51.
+At position 141 to 217, the domain is characterized as RRM.
+At position 119 to 195, the domain is characterized as RRM.
+At position 40 to 134, the domain is characterized as HTH arsR-type.
+At position 245 to 472, the domain is characterized as NR LBD.
+At position 2 to 248, the domain is characterized as F-BAR.
+At position 630 to 894, the domain is characterized as MHD.
+At position 124 to 537, the domain is characterized as Myotubularin phosphatase.
+At position 230 to 332, the domain is characterized as PpiC 1.
+At position 346 to 444, the domain is characterized as PpiC 2.
+At position 140 to 206, the domain is characterized as S1 motif.
+At position 308 to 374, the domain is characterized as KH.
+At position 19 to 97, the domain is characterized as Cytochrome b5 heme-binding.
+At position 671 to 867, the domain is characterized as ATP-grasp 2.
+At position 936 to 1068, the domain is characterized as MGS-like.
+At position 699 to 728, the domain is characterized as IQ.
+At position 25 to 63, the domain is characterized as Saposin A-type.
+At position 63 to 145, the domain is characterized as Saposin B-type 1.
+At position 194 to 271, the domain is characterized as Saposin B-type 2.
+At position 290 to 365, the domain is characterized as Saposin B-type 3.
+At position 404 to 526, the domain is characterized as RCK N-terminal.
+At position 274 to 388, the domain is characterized as PAZ.
+At position 557 to 865, the domain is characterized as Piwi.
+At position 199 to 399, the domain is characterized as HIN-200.
+At position 164 to 247, the domain is characterized as PPIase FKBP-type.
+At position 246 to 496, the domain is characterized as CN hydrolase.
+At position 624 to 901, the domain is characterized as Protein kinase.
+At position 500 to 604, the domain is characterized as RH2.
+At position 226 to 281, the domain is characterized as CBS 1.
+At position 281 to 335, the domain is characterized as CBS 2.
+At position 3 to 205, the domain is characterized as MIF4G.
+At position 113 to 312, the domain is characterized as MAGE.
+At position 114 to 183, the domain is characterized as SH3.
+At position 1 to 165, the domain is characterized as Thioredoxin 1.
+At position 178 to 322, the domain is characterized as Thioredoxin 2.
+At position 328 to 488, the domain is characterized as Thioredoxin 3.
+At position 469 to 596, the domain is characterized as Guanylate cyclase 1.
+At position 1071 to 1210, the domain is characterized as Guanylate cyclase 2.
+At position 14 to 78, the domain is characterized as HMA.
+At position 255 to 351, the domain is characterized as HTH La-type RNA-binding.
+At position 3 to 163, the domain is characterized as KaiA N-terminal.
+At position 173 to 281, the domain is characterized as KaiA C-terminal.
+At position 66 to 175, the domain is characterized as PET.
+At position 177 to 241, the domain is characterized as LIM zinc-binding 1.
+At position 242 to 302, the domain is characterized as LIM zinc-binding 2.
+At position 305 to 366, the domain is characterized as LIM zinc-binding 3.
+At position 677 to 867, the domain is characterized as ATP-grasp 2.
+At position 936 to 1078, the domain is characterized as MGS-like.
+At position 343 to 616, the domain is characterized as Protein kinase.
+At position 343 to 442, the domain is characterized as Rhodanese.
+At position 231 to 460, the domain is characterized as CN hydrolase.
+At position 47 to 236, the domain is characterized as BPL/LPL catalytic.
+At position 51 to 155, the domain is characterized as FAD-binding FR-type.
+At position 292 to 373, the domain is characterized as RCK C-terminal.
+At position 6 to 81, the domain is characterized as GIY-YIG.
+At position 103 to 235, the domain is characterized as PH.
+At position 102 to 137, the domain is characterized as EF-hand 1.
+At position 138 to 173, the domain is characterized as EF-hand 2.
+At position 402 to 437, the domain is characterized as EF-hand 3.
+At position 273 to 309, the domain is characterized as LRRNT 23.
+At position 1124 to 1160, the domain is characterized as EGF-like 6.
+At position 1163 to 1336, the domain is characterized as Laminin G-like.
+At position 1337 to 1371, the domain is characterized as EGF-like 7.
+At position 1374 to 1410, the domain is characterized as EGF-like 8.
+At position 1415 to 1451, the domain is characterized as EGF-like 9.
+At position 1456 to 1531, the domain is characterized as CTCK.
+At position 27 to 99, the domain is characterized as Sm.
+At position 255 to 364, the domain is characterized as DEUBAD.
+At position 56 to 116, the domain is characterized as Chromo.
+At position 131 to 338, the domain is characterized as tr-type G.
+At position 26 to 348, the domain is characterized as Protein kinase.
+At position 215 to 278, the domain is characterized as KH.
+At position 341 to 434, the domain is characterized as HD.
+At position 3 to 198, the domain is characterized as Lon N-terminal.
+At position 20 to 61, the domain is characterized as JmjN.
+At position 203 to 369, the domain is characterized as JmjC.
+At position 1 to 155, the domain is characterized as Macro.
+At position 705 to 797, the domain is characterized as FDX-ACB.
+At position 57 to 111, the domain is characterized as TCP.
+At position 64 to 262, the domain is characterized as OTU.
+At position 2 to 243, the domain is characterized as ABC transporter 1.
+At position 315 to 543, the domain is characterized as ABC transporter 2.
+At position 93 to 171, the domain is characterized as S4 RNA-binding.
+At position 89 to 160, the domain is characterized as POTRA.
+At position 102 to 182, the domain is characterized as RRM 1.
+At position 241 to 325, the domain is characterized as RRM 2.
+At position 761 to 807, the domain is characterized as G-patch.
+At position 13 to 71, the domain is characterized as CpcD-like.
+At position 22 to 142, the domain is characterized as Ricin B-type lectin.
+At position 163 to 211, the domain is characterized as Fibronectin type-II.
+At position 369 to 487, the domain is characterized as C-type lectin 2.
+At position 511 to 626, the domain is characterized as C-type lectin 3.
+At position 655 to 778, the domain is characterized as C-type lectin 4.
+At position 807 to 923, the domain is characterized as C-type lectin 5.
+At position 952 to 1080, the domain is characterized as C-type lectin 6.
+At position 1102 to 1213, the domain is characterized as C-type lectin 7.
+At position 1241 to 1356, the domain is characterized as C-type lectin 8.
+At position 164 to 393, the domain is characterized as Sigma-54 factor interaction.
+At position 88 to 103, the domain is characterized as EF-hand 2.
+At position 72 to 357, the domain is characterized as ABC transmembrane type-1 1.
+At position 391 to 634, the domain is characterized as ABC transporter 1.
+At position 713 to 1002, the domain is characterized as ABC transmembrane type-1 2.
+At position 1036 to 1274, the domain is characterized as ABC transporter 2.
+At position 19 to 58, the domain is characterized as EGF-like 1.
+At position 117 to 152, the domain is characterized as EGF-like 2.
+At position 154 to 190, the domain is characterized as EGF-like 3.
+At position 190 to 230, the domain is characterized as EGF-like 4.
+At position 232 to 269, the domain is characterized as EGF-like 5; calcium-binding.
+At position 271 to 308, the domain is characterized as EGF-like 6.
+At position 316 to 359, the domain is characterized as EGF-like 7.
+At position 369 to 406, the domain is characterized as EGF-like 8.
+At position 407 to 443, the domain is characterized as EGF-like 9.
+At position 446 to 479, the domain is characterized as EGF-like 10.
+At position 21 to 155, the domain is characterized as MPN.
+At position 227 to 365, the domain is characterized as PADR1 zinc-binding.
+At position 254 to 288, the domain is characterized as SAP.
+At position 381 to 473, the domain is characterized as BRCT.
+At position 504 to 604, the domain is characterized as WGR.
+At position 626 to 745, the domain is characterized as PARP alpha-helical.
+At position 752 to 977, the domain is characterized as PARP catalytic.
+At position 416 to 834, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1324 to 1637, the domain is characterized as PKS/mFAS DH.
+At position 1711 to 1788, the domain is characterized as Carrier.
+At position 63 to 388, the domain is characterized as A to I editase.
+At position 50 to 98, the domain is characterized as RPE1 insert.
+At position 36 to 96, the domain is characterized as MADS-box.
+At position 3 to 88, the domain is characterized as PTS EIIB type-3.
+At position 200 to 394, the domain is characterized as GMPS ATP-PPase.
+At position 56 to 409, the domain is characterized as GH26.
+At position 1 to 84, the domain is characterized as Glutaredoxin.
+At position 2 to 100, the domain is characterized as Ig-like.
+At position 25 to 343, the domain is characterized as Protein kinase.
+At position 71 to 329, the domain is characterized as Protein kinase.
+At position 376 to 411, the domain is characterized as EF-hand 1.
+At position 427 to 458, the domain is characterized as EF-hand 2.
+At position 459 to 494, the domain is characterized as EF-hand 3.
+At position 496 to 528, the domain is characterized as EF-hand 4.
+At position 180 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 239, the domain is characterized as IMD.
+At position 324 to 387, the domain is characterized as SH3.
+At position 173 to 289, the domain is characterized as TFIIS central.
+At position 255 to 338, the domain is characterized as RRM 1.
+At position 375 to 453, the domain is characterized as RRM 2.
+At position 494 to 580, the domain is characterized as RRM 3.
+At position 116 to 230, the domain is characterized as SET.
+At position 252 to 414, the domain is characterized as PCI.
+At position 28 to 297, the domain is characterized as Protein kinase.
+At position 106 to 441, the domain is characterized as SAC.
+At position 241 to 299, the domain is characterized as PUA.
+At position 17 to 137, the domain is characterized as VOC 1.
+At position 165 to 316, the domain is characterized as VOC 2.
+At position 68 to 146, the domain is characterized as Inhibitor I9.
+At position 166 to 454, the domain is characterized as Peptidase S8.
+At position 269 to 359, the domain is characterized as Ig-like 1.
+At position 435 to 531, the domain is characterized as Ig-like 2.
+At position 945 to 1029, the domain is characterized as Ig-like 3.
+At position 1073 to 1162, the domain is characterized as Ig-like 4.
+At position 1172 to 1262, the domain is characterized as Ig-like 5.
+At position 176 to 356, the domain is characterized as CNNM transmembrane.
+At position 375 to 436, the domain is characterized as CBS 1.
+At position 443 to 509, the domain is characterized as CBS 2.
+At position 11 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 242 to 492, the domain is characterized as CN hydrolase.
+At position 2 to 90, the domain is characterized as RRM 1.
+At position 330 to 408, the domain is characterized as RRM 2.
+At position 516 to 588, the domain is characterized as RRM 3.
+At position 651 to 734, the domain is characterized as RRM 4.
+At position 752 to 829, the domain is characterized as RRM 5.
+At position 9 to 110, the domain is characterized as EamA.
+At position 105 to 217, the domain is characterized as DUF1279.
+At position 23 to 294, the domain is characterized as PPM-type phosphatase.
+At position 65 to 110, the domain is characterized as F-box.
+At position 8 to 86, the domain is characterized as Cytochrome b5 heme-binding.
+At position 219 to 361, the domain is characterized as Fatty acid hydroxylase.
+At position 70 to 256, the domain is characterized as TR mART core.
+At position 13 to 203, the domain is characterized as Lon N-terminal.
+At position 600 to 791, the domain is characterized as Lon proteolytic.
+At position 184 to 257, the domain is characterized as PAS 1.
+At position 258 to 312, the domain is characterized as PAC 1.
+At position 462 to 535, the domain is characterized as PAS 2.
+At position 536 to 590, the domain is characterized as PAC 2.
+At position 663 to 952, the domain is characterized as Protein kinase.
+At position 1 to 201, the domain is characterized as Macro.
+At position 540 to 617, the domain is characterized as PABC.
+At position 224 to 415, the domain is characterized as Glutamine amidotransferase type-1.
+At position 43 to 205, the domain is characterized as PCI.
+At position 383 to 444, the domain is characterized as PWWP.
+At position 1 to 169, the domain is characterized as TCTP.
+At position 2 to 230, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 132, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 2 to 133, the domain is characterized as ADF-H.
+At position 472 to 531, the domain is characterized as SH3.
+At position 51 to 121, the domain is characterized as PAH 1.
+At position 136 to 206, the domain is characterized as PAH 2.
+At position 331 to 400, the domain is characterized as PAH 3.
+At position 489 to 711, the domain is characterized as Histidine kinase.
+At position 736 to 851, the domain is characterized as Response regulatory.
+At position 388 to 531, the domain is characterized as RCK N-terminal.
+At position 23 to 65, the domain is characterized as UBA.
+At position 243 to 308, the domain is characterized as SH3.
+At position 61 to 336, the domain is characterized as Pyruvate carboxyltransferase.
+At position 41 to 342, the domain is characterized as Protein kinase.
+At position 33 to 113, the domain is characterized as LITAF.
+At position 100 to 132, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 141 to 177, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 188 to 219, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 70 to 224, the domain is characterized as Obg.
+At position 225 to 390, the domain is characterized as OBG-type G.
+At position 42 to 353, the domain is characterized as PPM-type phosphatase.
+At position 11 to 184, the domain is characterized as PPIase cyclophilin-type.
+At position 34 to 80, the domain is characterized as F-box.
+At position 35 to 175, the domain is characterized as Nudix hydrolase.
+At position 7 to 108, the domain is characterized as LOB.
+At position 98 to 193, the domain is characterized as Plastocyanin-like 1.
+At position 258 to 359, the domain is characterized as Plastocyanin-like 2.
+At position 129 to 420, the domain is characterized as ABC transmembrane type-1 1.
+At position 460 to 684, the domain is characterized as ABC transporter 1.
+At position 756 to 1030, the domain is characterized as ABC transmembrane type-1 2.
+At position 1070 to 1334, the domain is characterized as ABC transporter 2.
+At position 241 to 498, the domain is characterized as ABC transporter 2.
+At position 1 to 55, the domain is characterized as HTH myb-type 1.
+At position 56 to 109, the domain is characterized as HTH myb-type 2.
+At position 3 to 251, the domain is characterized as ABC transporter.
+At position 189 to 267, the domain is characterized as RRM.
+At position 3 to 80, the domain is characterized as GST N-terminal.
+At position 82 to 204, the domain is characterized as GST C-terminal.
+At position 3 to 637, the domain is characterized as PFL.
+At position 645 to 765, the domain is characterized as Glycine radical.
+At position 144 to 265, the domain is characterized as Ig-like C2-type 2.
+At position 279 to 389, the domain is characterized as Ig-like C2-type 3.
+At position 408 to 525, the domain is characterized as Ig-like C2-type 4.
+At position 541 to 651, the domain is characterized as Ig-like C2-type 5.
+At position 656 to 794, the domain is characterized as Ig-like C2-type 6.
+At position 808 to 925, the domain is characterized as Ig-like C2-type 7.
+At position 13 to 145, the domain is characterized as uDENN.
+At position 162 to 298, the domain is characterized as cDENN.
+At position 300 to 378, the domain is characterized as dDENN.
+At position 467 to 691, the domain is characterized as ERCC4.
+At position 394 to 521, the domain is characterized as Guanylate cyclase 1.
+At position 1058 to 1198, the domain is characterized as Guanylate cyclase 2.
+At position 28 to 97, the domain is characterized as S1 motif 1.
+At position 115 to 179, the domain is characterized as S1 motif 2.
+At position 193 to 261, the domain is characterized as S1 motif 3.
+At position 1720 to 1797, the domain is characterized as Carrier.
+At position 16 to 406, the domain is characterized as PTS EIIC type-1.
+At position 1 to 453, the domain is characterized as PTS EIIC type-1.
+At position 473 to 555, the domain is characterized as PTS EIIB type-1.
+At position 596 to 700, the domain is characterized as PTS EIIA type-1.
+At position 30 to 109, the domain is characterized as Inhibitor I9.
+At position 113 to 621, the domain is characterized as Peptidase S8.
+At position 105 to 221, the domain is characterized as C-type lectin.
+At position 238 to 339, the domain is characterized as Fe2OG dioxygenase.
+At position 28 to 263, the domain is characterized as Alpha-carbonic anhydrase.
+At position 35 to 410, the domain is characterized as PTS EIIC type-2.
+At position 11 to 290, the domain is characterized as Radical SAM core.
+At position 32 to 259, the domain is characterized as ATP-grasp.
+At position 399 to 434, the domain is characterized as EF-hand 1.
+At position 435 to 467, the domain is characterized as EF-hand 2.
+At position 39 to 267, the domain is characterized as Radical SAM core.
+At position 68 to 187, the domain is characterized as Rhodanese.
+At position 244 to 387, the domain is characterized as Tyrosine-protein phosphatase.
+At position 526 to 798, the domain is characterized as Protein kinase.
+At position 14 to 119, the domain is characterized as SCP2.
+At position 82 to 350, the domain is characterized as Radical SAM core.
+At position 25 to 136, the domain is characterized as sHSP.
+At position 24 to 175, the domain is characterized as Saposin B-type.
+At position 232 to 393, the domain is characterized as TrmE-type G.
+At position 29 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 188 to 347, the domain is characterized as CRAL-TRIO.
+At position 171 to 278, the domain is characterized as FAD-binding FR-type.
+At position 27 to 71, the domain is characterized as CHCH.
+At position 34 to 145, the domain is characterized as Ig-like V-type.
+At position 153 to 234, the domain is characterized as Ig-like C2-type.
+At position 309 to 502, the domain is characterized as B30.2/SPRY.
+At position 297 to 572, the domain is characterized as Dynamin-type G.
+At position 68 to 333, the domain is characterized as ABC transporter.
+At position 421 to 631, the domain is characterized as ABC transmembrane type-2.
+At position 92 to 234, the domain is characterized as Clp R.
+At position 509 to 544, the domain is characterized as UVR.
+At position 315 to 551, the domain is characterized as NR LBD.
+At position 84 to 258, the domain is characterized as Helicase ATP-binding.
+At position 284 to 439, the domain is characterized as Helicase C-terminal.
+At position 207 to 405, the domain is characterized as Glutamine amidotransferase type-1.
+At position 194 to 245, the domain is characterized as bHLH.
+At position 26 to 114, the domain is characterized as PPIase FKBP-type.
+At position 160 to 336, the domain is characterized as Helicase ATP-binding.
+At position 350 to 519, the domain is characterized as Helicase C-terminal.
+At position 62 to 116, the domain is characterized as J.
+At position 140 to 200, the domain is characterized as v-SNARE coiled-coil homology.
+At position 17 to 95, the domain is characterized as Ubiquitin-like.
+At position 99 to 288, the domain is characterized as ABC transmembrane type-1.
+At position 74 to 262, the domain is characterized as RNase H type-2.
+At position 12 to 103, the domain is characterized as HIG1.
+At position 117 to 624, the domain is characterized as Peptidase S8.
+At position 386 to 481, the domain is characterized as PA.
+At position 470 to 523, the domain is characterized as HTH myb-type.
+At position 692 to 717, the domain is characterized as Myb-like.
+At position 250 to 324, the domain is characterized as PUA.
+At position 202 to 384, the domain is characterized as FAD-binding PCMH-type.
+At position 2 to 147, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 172 to 249, the domain is characterized as POU-specific.
+At position 20 to 66, the domain is characterized as EGF-like 1.
+At position 67 to 104, the domain is characterized as EGF-like 2.
+At position 205 to 247, the domain is characterized as EGF-like 3.
+At position 251 to 292, the domain is characterized as EGF-like 4.
+At position 291 to 335, the domain is characterized as EGF-like 5.
+At position 482 to 530, the domain is characterized as EGF-like 6.
+At position 531 to 568, the domain is characterized as EGF-like 7.
+At position 18 to 92, the domain is characterized as S1-like.
+At position 145 to 371, the domain is characterized as Radical SAM core.
+At position 374 to 436, the domain is characterized as TRAM.
+At position 33 to 141, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 75 to 129, the domain is characterized as TCP.
+At position 49 to 108, the domain is characterized as Collagen-like.
+At position 145 to 261, the domain is characterized as C-type lectin.
+At position 283 to 495, the domain is characterized as B30.2/SPRY.
+At position 13 to 99, the domain is characterized as ABM.
+At position 363 to 640, the domain is characterized as Radical SAM core.
+At position 57 to 260, the domain is characterized as Brix.
+At position 272 to 345, the domain is characterized as MIT.
+At position 77 to 112, the domain is characterized as EF-hand.
+At position 497 to 554, the domain is characterized as Chromo 1.
+At position 592 to 653, the domain is characterized as Chromo 2.
+At position 712 to 896, the domain is characterized as Helicase ATP-binding.
+At position 1028 to 1193, the domain is characterized as Helicase C-terminal.
+At position 744 to 793, the domain is characterized as KA1.
+At position 155 to 223, the domain is characterized as PAS.
+At position 520 to 781, the domain is characterized as Protein kinase.
+At position 784 to 912, the domain is characterized as KEN.
+At position 51 to 127, the domain is characterized as PDZ.
+At position 693 to 767, the domain is characterized as Carrier 1.
+At position 1724 to 1798, the domain is characterized as Carrier 2.
+At position 387 to 422, the domain is characterized as EF-hand 1.
+At position 424 to 459, the domain is characterized as EF-hand 2.
+At position 19 to 111, the domain is characterized as CFEM.
+At position 113 to 231, the domain is characterized as C-type lectin.
+At position 53 to 112, the domain is characterized as SH3.
+At position 148 to 332, the domain is characterized as DH.
+At position 363 to 470, the domain is characterized as PH.
+At position 42 to 138, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 231, the domain is characterized as Ig-like C2-type 2.
+At position 262 to 350, the domain is characterized as Ig-like C2-type 3.
+At position 355 to 442, the domain is characterized as Ig-like C2-type 4.
+At position 448 to 535, the domain is characterized as Ig-like C2-type 5.
+At position 539 to 626, the domain is characterized as Ig-like C2-type 6.
+At position 645 to 740, the domain is characterized as Fibronectin type-III 1.
+At position 745 to 838, the domain is characterized as Fibronectin type-III 2.
+At position 843 to 945, the domain is characterized as Fibronectin type-III 3.
+At position 949 to 1057, the domain is characterized as Fibronectin type-III 4.
+At position 1133 to 1222, the domain is characterized as Fibronectin type-III 5.
+At position 158 to 551, the domain is characterized as SAC.
+At position 38 to 150, the domain is characterized as TBDR plug.
+At position 161 to 739, the domain is characterized as TBDR beta-barrel.
+At position 3 to 162, the domain is characterized as N-acetyltransferase.
+At position 415 to 478, the domain is characterized as bZIP.
+At position 30 to 110, the domain is characterized as Ig-like 1.
+At position 111 to 193, the domain is characterized as Ig-like 2.
+At position 13 to 102, the domain is characterized as SUEL-type lectin.
+At position 24 to 59, the domain is characterized as EF-hand.
+At position 280 to 426, the domain is characterized as SIS 1.
+At position 125 to 488, the domain is characterized as Protein kinase.
+At position 18 to 450, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 979 to 1296, the domain is characterized as PKS/mFAS DH.
+At position 2353 to 2429, the domain is characterized as Carrier.
+At position 65 to 129, the domain is characterized as J.
+At position 325 to 379, the domain is characterized as SANT 1.
+At position 492 to 547, the domain is characterized as SANT 2.
+At position 120 to 289, the domain is characterized as tr-type G.
+At position 350 to 633, the domain is characterized as ABC transmembrane type-1.
+At position 666 to 902, the domain is characterized as ABC transporter.
+At position 106 to 135, the domain is characterized as IQ.
+At position 294 to 357, the domain is characterized as bZIP.
+At position 62 to 111, the domain is characterized as bHLH.
+At position 678 to 950, the domain is characterized as Histidine kinase.
+At position 1575 to 1695, the domain is characterized as Response regulatory.
+At position 51 to 160, the domain is characterized as THUMP.
+At position 9 to 233, the domain is characterized as ABC transporter.
+At position 131 to 225, the domain is characterized as Rhodanese.
+At position 1 to 197, the domain is characterized as RNase H type-2.
+At position 320 to 599, the domain is characterized as ABC transporter 1.
+At position 619 to 949, the domain is characterized as ABC transporter 2.
+At position 36 to 107, the domain is characterized as ACT.
+At position 1331 to 1417, the domain is characterized as DEP.
+At position 32 to 221, the domain is characterized as GH11.
+At position 190 to 272, the domain is characterized as RCK C-terminal 1.
+At position 274 to 355, the domain is characterized as RCK C-terminal 2.
+At position 56 to 90, the domain is characterized as EGF-like 1.
+At position 98 to 133, the domain is characterized as EGF-like 2.
+At position 163 to 193, the domain is characterized as EGF-like 3.
+At position 217 to 251, the domain is characterized as EGF-like 4.
+At position 304 to 341, the domain is characterized as EGF-like 5.
+At position 353 to 384, the domain is characterized as EGF-like 6.
+At position 12 to 80, the domain is characterized as KH type-2.
+At position 489 to 552, the domain is characterized as SAM 1.
+At position 558 to 622, the domain is characterized as SAM 2.
+At position 37 to 112, the domain is characterized as ACT 1.
+At position 130 to 212, the domain is characterized as ACT 2.
+At position 266 to 341, the domain is characterized as ACT 3.
+At position 344 to 423, the domain is characterized as ACT 4.
+At position 376 to 452, the domain is characterized as Carrier 1.
+At position 527 to 959, the domain is characterized as Ketosynthase family 3 (KS3) 1.
+At position 1114 to 1397, the domain is characterized as PKS/mFAS DH.
+At position 1407 to 1485, the domain is characterized as Carrier 2.
+At position 1528 to 1946, the domain is characterized as Ketosynthase family 3 (KS3) 2.
+At position 2134 to 2208, the domain is characterized as Carrier 3.
+At position 13 to 128, the domain is characterized as Thioredoxin.
+At position 261 to 353, the domain is characterized as Chromo 1.
+At position 378 to 456, the domain is characterized as Chromo 2.
+At position 496 to 666, the domain is characterized as Helicase ATP-binding.
+At position 795 to 946, the domain is characterized as Helicase C-terminal.
+At position 33 to 279, the domain is characterized as PPM-type phosphatase.
+At position 59 to 242, the domain is characterized as tr-type G.
+At position 306 to 383, the domain is characterized as B5.
+At position 17 to 690, the domain is characterized as Myosin motor.
+At position 693 to 722, the domain is characterized as IQ.
+At position 728 to 917, the domain is characterized as TH1.
+At position 1041 to 1098, the domain is characterized as SH3.
+At position 25 to 416, the domain is characterized as Helicase ATP-binding.
+At position 326 to 508, the domain is characterized as PCI.
+At position 932 to 1069, the domain is characterized as MGS-like.
+At position 57 to 92, the domain is characterized as EF-hand.
+At position 502 to 641, the domain is characterized as JmjC.
+At position 391 to 487, the domain is characterized as PH 2.
+At position 44 to 108, the domain is characterized as J.
+At position 26 to 128, the domain is characterized as Rhodanese.
+At position 18 to 235, the domain is characterized as Radical SAM core.
+At position 345 to 453, the domain is characterized as Rhodanese.
+At position 34 to 141, the domain is characterized as PI3K-ABD.
+At position 217 to 309, the domain is characterized as PI3K-RBD.
+At position 357 to 521, the domain is characterized as C2 PI3K-type.
+At position 541 to 723, the domain is characterized as PIK helical.
+At position 797 to 1080, the domain is characterized as PI3K/PI4K catalytic.
+At position 38 to 274, the domain is characterized as ABC transporter 1.
+At position 284 to 523, the domain is characterized as ABC transporter 2.
+At position 14 to 228, the domain is characterized as tr-type G.
+At position 67 to 260, the domain is characterized as HD.
+At position 421 to 645, the domain is characterized as ABC transporter 1.
+At position 49 to 224, the domain is characterized as BPL/LPL catalytic.
+At position 22 to 223, the domain is characterized as DPCK.
+At position 94 to 155, the domain is characterized as S4 RNA-binding.
+At position 534 to 609, the domain is characterized as Cytochrome b5 heme-binding.
+At position 663 to 775, the domain is characterized as FAD-binding FR-type.
+At position 119 to 237, the domain is characterized as N-acetyltransferase.
+At position 7 to 303, the domain is characterized as Helicase ATP-binding.
+At position 26 to 151, the domain is characterized as Cyclin N-terminal.
+At position 28 to 87, the domain is characterized as LIM zinc-binding 1.
+At position 88 to 150, the domain is characterized as LIM zinc-binding 2.
+At position 175 to 276, the domain is characterized as Fe2OG dioxygenase.
+At position 218 to 292, the domain is characterized as POU-specific.
+At position 329 to 414, the domain is characterized as PDZ.
+At position 69 to 195, the domain is characterized as Nudix hydrolase.
+At position 196 to 281, the domain is characterized as KH type-2.
+At position 132 to 370, the domain is characterized as Radical SAM core.
+At position 373 to 438, the domain is characterized as TRAM.
+At position 87 to 378, the domain is characterized as Protein kinase.
+At position 33 to 127, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 130 to 270, the domain is characterized as FAD-binding FR-type.
+At position 349 to 479, the domain is characterized as Ig-like.
+At position 82 to 366, the domain is characterized as FAE.
+At position 144 to 258, the domain is characterized as C-type lectin.
+At position 150 to 378, the domain is characterized as START.
+At position 205 to 284, the domain is characterized as UBX.
+At position 671 to 786, the domain is characterized as GAE.
+At position 22 to 110, the domain is characterized as Ig-like V-type.
+At position 12 to 141, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 78 to 248, the domain is characterized as FAD-binding PCMH-type.
+At position 429 to 478, the domain is characterized as bHLH.
+At position 153 to 324, the domain is characterized as VWFA.
+At position 32 to 115, the domain is characterized as GOLD.
+At position 336 to 458, the domain is characterized as RRM 4.
+At position 646 to 723, the domain is characterized as PABC.
+At position 252 to 582, the domain is characterized as Kinesin motor.
+At position 153 to 299, the domain is characterized as TRUD.
+At position 237 to 281, the domain is characterized as F-box.
+At position 140 to 389, the domain is characterized as AB hydrolase-1.
+At position 118 to 325, the domain is characterized as Histidine kinase.
+At position 174 to 266, the domain is characterized as RRM.
+At position 1 to 191, the domain is characterized as GH11.
+At position 146 to 340, the domain is characterized as ATP-grasp.
+At position 22 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 213 to 403, the domain is characterized as GMPS ATP-PPase.
+At position 24 to 231, the domain is characterized as AIG1-type G.
+At position 324 to 568, the domain is characterized as Clu.
+At position 34 to 270, the domain is characterized as ABC transporter.
+At position 284 to 340, the domain is characterized as CBS 1.
+At position 344 to 403, the domain is characterized as CBS 2.
+At position 154 to 377, the domain is characterized as Radical SAM core.
+At position 211 to 307, the domain is characterized as PH.
+At position 28 to 91, the domain is characterized as Chitin-binding type R&R 1.
+At position 572 to 640, the domain is characterized as Chitin-binding type R&R 2.
+At position 37 to 103, the domain is characterized as Importin N-terminal.
+At position 120 to 225, the domain is characterized as C-type lectin.
+At position 35 to 216, the domain is characterized as Eph LBD.
+At position 340 to 452, the domain is characterized as Fibronectin type-III 1.
+At position 456 to 554, the domain is characterized as Fibronectin type-III 2.
+At position 644 to 899, the domain is characterized as Protein kinase.
+At position 932 to 996, the domain is characterized as SAM.
+At position 89 to 216, the domain is characterized as TBDR plug.
+At position 224 to 1077, the domain is characterized as TBDR beta-barrel.
+At position 51 to 282, the domain is characterized as Radical SAM core.
+At position 55 to 86, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 87 to 116, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 79 to 408, the domain is characterized as Protein kinase.
+At position 38 to 170, the domain is characterized as Galectin.
+At position 104 to 276, the domain is characterized as Helicase ATP-binding.
+At position 307 to 453, the domain is characterized as Helicase C-terminal.
+At position 113 to 183, the domain is characterized as PAS.
+At position 42 to 154, the domain is characterized as AB hydrolase-1.
+At position 10 to 143, the domain is characterized as RNase III.
+At position 170 to 239, the domain is characterized as DRBM.
+At position 8 to 296, the domain is characterized as tr-type G.
+At position 109 to 525, the domain is characterized as PPM-type phosphatase.
+At position 51 to 169, the domain is characterized as HotDog ACOT-type 1.
+At position 225 to 339, the domain is characterized as HotDog ACOT-type 2.
+At position 152 to 437, the domain is characterized as Tyr recombinase Flp-type.
+At position 668 to 807, the domain is characterized as C2.
+At position 15 to 70, the domain is characterized as HTH cro/C1-type.
+At position 3 to 242, the domain is characterized as ABC transporter.
+At position 20 to 90, the domain is characterized as Sushi 1.
+At position 92 to 151, the domain is characterized as Sushi 2.
+At position 154 to 212, the domain is characterized as Sushi 3.
+At position 261 to 459, the domain is characterized as VWFA.
+At position 471 to 752, the domain is characterized as Peptidase S1.
+At position 12 to 267, the domain is characterized as ThyX.
+At position 108 to 130, the domain is characterized as OCA.
+At position 54 to 413, the domain is characterized as Peptidase A1.
+At position 153 to 284, the domain is characterized as Thioredoxin.
+At position 20 to 120, the domain is characterized as Rhodanese.
+At position 802 to 931, the domain is characterized as SH2.
+At position 161 to 217, the domain is characterized as BRX 1.
+At position 356 to 411, the domain is characterized as BRX 2.
+At position 26 to 158, the domain is characterized as ENTH.
+At position 91 to 219, the domain is characterized as GST C-terminal.
+At position 334 to 409, the domain is characterized as HSA.
+At position 576 to 638, the domain is characterized as Myb-like.
+At position 72 to 415, the domain is characterized as Kinesin motor.
+At position 203 to 460, the domain is characterized as Radical SAM core.
+At position 470 to 534, the domain is characterized as TRAM.
+At position 131 to 427, the domain is characterized as ABC transmembrane type-1.
+At position 463 to 697, the domain is characterized as ABC transporter.
+At position 181 to 300, the domain is characterized as C2 2.
+At position 339 to 474, the domain is characterized as C2 3.
+At position 1123 to 1251, the domain is characterized as C2 4.
+At position 1282 to 1410, the domain is characterized as C2 5.
+At position 1536 to 1654, the domain is characterized as C2 6.
+At position 1772 to 1920, the domain is characterized as C2 7.
+At position 211 to 404, the domain is characterized as GMPS ATP-PPase.
+At position 86 to 780, the domain is characterized as Myosin motor.
+At position 783 to 812, the domain is characterized as IQ.
+At position 10 to 350, the domain is characterized as Enoyl reductase (ER).
+At position 14 to 177, the domain is characterized as PPIase cyclophilin-type.
+At position 151 to 510, the domain is characterized as TTL.
+At position 14 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 24 to 73, the domain is characterized as FHA-like.
+At position 168 to 273, the domain is characterized as HIT.
+At position 266 to 317, the domain is characterized as TSP type-1.
+At position 23 to 195, the domain is characterized as EngB-type G.
+At position 1 to 273, the domain is characterized as Peptidase S1.
+At position 124 to 232, the domain is characterized as sHSP.
+At position 262 to 307, the domain is characterized as RPE1 insert.
+At position 2 to 221, the domain is characterized as Radical SAM core.
+At position 85 to 173, the domain is characterized as PB1.
+At position 110 to 157, the domain is characterized as LysM 1.
+At position 176 to 219, the domain is characterized as LysM 2.
+At position 233 to 456, the domain is characterized as Fibrinogen C-terminal.
+At position 849 to 1144, the domain is characterized as Protein kinase.
+At position 381 to 452, the domain is characterized as PAS 1.
+At position 469 to 508, the domain is characterized as PAC 1.
+At position 574 to 644, the domain is characterized as PAS 2.
+At position 650 to 691, the domain is characterized as PAC 2.
+At position 693 to 763, the domain is characterized as PAS 3.
+At position 14 to 262, the domain is characterized as Protein kinase.
+At position 25 to 104, the domain is characterized as DED.
+At position 230 to 469, the domain is characterized as CN hydrolase.
+At position 41 to 119, the domain is characterized as RRM.
+At position 23 to 99, the domain is characterized as MANSC.
+At position 345 to 436, the domain is characterized as PKD 1.
+At position 444 to 533, the domain is characterized as PKD 2.
+At position 539 to 629, the domain is characterized as PKD 3.
+At position 630 to 723, the domain is characterized as PKD 4.
+At position 729 to 820, the domain is characterized as PKD 5.
+At position 719 to 986, the domain is characterized as Protein kinase.
+At position 22 to 101, the domain is characterized as Ig-like C2-type 1.
+At position 95 to 184, the domain is characterized as Ig-like C2-type 2.
+At position 190 to 277, the domain is characterized as Ig-like C2-type 3.
+At position 1 to 238, the domain is characterized as Bin3-type SAM.
+At position 209 to 353, the domain is characterized as Cytochrome c.
+At position 292 to 405, the domain is characterized as CRC.
+At position 8 to 121, the domain is characterized as Response regulatory.
+At position 1 to 232, the domain is characterized as RMT2.
+At position 26 to 325, the domain is characterized as GH18.
+At position 111 to 299, the domain is characterized as Rab-GAP TBC.
+At position 127 to 376, the domain is characterized as Radical SAM core.
+At position 22 to 102, the domain is characterized as Ig-like C2-type 1.
+At position 119 to 188, the domain is characterized as Ig-like C2-type 2.
+At position 35 to 158, the domain is characterized as EamA.
+At position 15 to 50, the domain is characterized as EF-hand.
+At position 5 to 102, the domain is characterized as Ig-like.
+At position 41 to 143, the domain is characterized as Glutaredoxin.
+At position 225 to 273, the domain is characterized as F-box.
+At position 13 to 104, the domain is characterized as HIG1.
+At position 232 to 310, the domain is characterized as RRM.
+At position 355 to 420, the domain is characterized as R3H.
+At position 46 to 139, the domain is characterized as Ig-like C2-type 1.
+At position 249 to 335, the domain is characterized as Ig-like C2-type 3.
+At position 340 to 417, the domain is characterized as Ig-like C2-type 4.
+At position 423 to 510, the domain is characterized as Ig-like C2-type 5.
+At position 515 to 612, the domain is characterized as Ig-like C2-type 6.
+At position 619 to 718, the domain is characterized as Fibronectin type-III 1.
+At position 723 to 820, the domain is characterized as Fibronectin type-III 2.
+At position 825 to 918, the domain is characterized as Fibronectin type-III 3.
+At position 920 to 1015, the domain is characterized as Fibronectin type-III 4.
+At position 22 to 65, the domain is characterized as CHCH.
+At position 26 to 79, the domain is characterized as Kazal-like.
+At position 190 to 478, the domain is characterized as Protein kinase.
+At position 43 to 282, the domain is characterized as ABC transporter.
+At position 4 to 249, the domain is characterized as KaiC.
+At position 63 to 244, the domain is characterized as Rab-GAP TBC.
+At position 173 to 286, the domain is characterized as CUB 1.
+At position 288 to 347, the domain is characterized as Sushi 1.
+At position 349 to 459, the domain is characterized as CUB 2.
+At position 462 to 525, the domain is characterized as Sushi 2.
+At position 527 to 638, the domain is characterized as CUB 3.
+At position 642 to 701, the domain is characterized as Sushi 3.
+At position 703 to 766, the domain is characterized as Sushi 4.
+At position 769 to 830, the domain is characterized as Sushi 5.
+At position 51 to 120, the domain is characterized as HTH CENPB-type.
+At position 445 to 520, the domain is characterized as DRBM.
+At position 569 to 671, the domain is characterized as Ig-like C2-type.
+At position 221 to 490, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 21 to 133, the domain is characterized as 6-Cys 1.
+At position 241 to 375, the domain is characterized as 6-Cys 2.
+At position 273 to 541, the domain is characterized as Pterin-binding.
+At position 417 to 601, the domain is characterized as DH.
+At position 11 to 224, the domain is characterized as Glutamine amidotransferase type-2.
+At position 115 to 454, the domain is characterized as SAC.
+At position 122 to 198, the domain is characterized as RRM 1.
+At position 219 to 296, the domain is characterized as RRM 2.
+At position 349 to 426, the domain is characterized as RRM 3.
+At position 130 to 309, the domain is characterized as FAD-binding PCMH-type.
+At position 575 to 677, the domain is characterized as ASD1.
+At position 1092 to 1418, the domain is characterized as ASD2.
+At position 105 to 174, the domain is characterized as S4 RNA-binding.
+At position 7 to 99, the domain is characterized as HTH arsR-type.
+At position 161 to 249, the domain is characterized as BRCT.
+At position 358 to 554, the domain is characterized as UmuC.
+At position 99 to 287, the domain is characterized as Helicase ATP-binding.
+At position 647 to 825, the domain is characterized as Toprim.
+At position 175 to 400, the domain is characterized as Histidine kinase.
+At position 313 to 396, the domain is characterized as HTH OST-type.
+At position 422 to 497, the domain is characterized as RRM.
+At position 26 to 53, the domain is characterized as LDL-receptor class A 1; truncated.
+At position 64 to 222, the domain is characterized as MAM 1.
+At position 228 to 266, the domain is characterized as LDL-receptor class A 2.
+At position 269 to 425, the domain is characterized as MAM 2.
+At position 456 to 491, the domain is characterized as LDL-receptor class A 3.
+At position 491 to 644, the domain is characterized as MAM 3.
+At position 654 to 809, the domain is characterized as MAM 4.
+At position 811 to 969, the domain is characterized as MAM 5.
+At position 971 to 1138, the domain is characterized as MAM 6.
+At position 167 to 314, the domain is characterized as Thioredoxin.
+At position 15 to 300, the domain is characterized as Helicase ATP-binding.
+At position 11 to 81, the domain is characterized as H15.
+At position 121 to 351, the domain is characterized as Helicase ATP-binding.
+At position 390 to 584, the domain is characterized as Helicase C-terminal.
+At position 185 to 340, the domain is characterized as C1q.
+At position 116 to 151, the domain is characterized as EF-hand 3.
+At position 401 to 574, the domain is characterized as C2 DOCK-type.
+At position 1190 to 1596, the domain is characterized as DOCKER.
+At position 243 to 394, the domain is characterized as Exonuclease.
+At position 94 to 164, the domain is characterized as Chitin-binding type-2.
+At position 1 to 163, the domain is characterized as N-acetyltransferase.
+At position 878 to 944, the domain is characterized as SAM 1.
+At position 963 to 1027, the domain is characterized as SAM 2.
+At position 1051 to 1120, the domain is characterized as SAM 3.
+At position 18 to 127, the domain is characterized as RWD.
+At position 37 to 213, the domain is characterized as Helicase ATP-binding.
+At position 246 to 393, the domain is characterized as Helicase C-terminal.
+At position 14 to 147, the domain is characterized as DOD-type homing endonuclease.
+At position 125 to 309, the domain is characterized as PID.
+At position 18 to 208, the domain is characterized as Thioredoxin.
+At position 7 to 244, the domain is characterized as ABC transporter 1.
+At position 254 to 498, the domain is characterized as ABC transporter 2.
+At position 187 to 248, the domain is characterized as SH3.
+At position 254 to 346, the domain is characterized as SH2.
+At position 371 to 627, the domain is characterized as Protein kinase.
+At position 11 to 263, the domain is characterized as Pyruvate carboxyltransferase.
+At position 304 to 624, the domain is characterized as Protein kinase.
+At position 66 to 95, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 96 to 127, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 237 to 265, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 275 to 304, the domain is characterized as 4Fe-4S ferredoxin-type 9.
+At position 311 to 344, the domain is characterized as 4Fe-4S ferredoxin-type 10.
+At position 356 to 385, the domain is characterized as 4Fe-4S ferredoxin-type 11.
+At position 386 to 412, the domain is characterized as 4Fe-4S ferredoxin-type 12.
+At position 35 to 143, the domain is characterized as Ig-like V-type.
+At position 149 to 243, the domain is characterized as Link 1.
+At position 246 to 339, the domain is characterized as Link 2.
+At position 847 to 958, the domain is characterized as PH.
+At position 319 to 375, the domain is characterized as DEK-C.
+At position 1 to 71, the domain is characterized as U-box.
+At position 15 to 405, the domain is characterized as Glutamine amidotransferase type-2.
+At position 7 to 284, the domain is characterized as Helicase ATP-binding.
+At position 127 to 217, the domain is characterized as SH2.
+At position 242 to 493, the domain is characterized as Protein kinase.
+At position 21 to 299, the domain is characterized as ABC transmembrane type-1.
+At position 332 to 565, the domain is characterized as ABC transporter.
+At position 23 to 101, the domain is characterized as EMI.
+At position 181 to 215, the domain is characterized as EGF-like 1.
+At position 223 to 258, the domain is characterized as EGF-like 2.
+At position 266 to 301, the domain is characterized as EGF-like 3.
+At position 309 to 344, the domain is characterized as EGF-like 4.
+At position 398 to 433, the domain is characterized as EGF-like 5.
+At position 484 to 519, the domain is characterized as EGF-like 6.
+At position 575 to 605, the domain is characterized as EGF-like 7.
+At position 613 to 648, the domain is characterized as EGF-like 8.
+At position 656 to 691, the domain is characterized as EGF-like 9.
+At position 137 to 450, the domain is characterized as IF rod.
+At position 1 to 402, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 154 to 262, the domain is characterized as Cadherin 1.
+At position 487 to 595, the domain is characterized as Cadherin 4.
+At position 594 to 702, the domain is characterized as Cadherin 5.
+At position 328 to 534, the domain is characterized as MCM.
+At position 2 to 68, the domain is characterized as S4 RNA-binding.
+At position 50 to 113, the domain is characterized as J.
+At position 86 to 181, the domain is characterized as PH.
+At position 173 to 357, the domain is characterized as Rab-GAP TBC.
+At position 125 to 292, the domain is characterized as Helicase ATP-binding.
+At position 303 to 480, the domain is characterized as Helicase C-terminal.
+At position 6 to 89, the domain is characterized as RRM 1.
+At position 99 to 178, the domain is characterized as RRM 2.
+At position 5 to 289, the domain is characterized as Protein kinase.
+At position 32 to 247, the domain is characterized as BPL/LPL catalytic.
+At position 350 to 454, the domain is characterized as Rhodanese.
+At position 478 to 756, the domain is characterized as Protein kinase.
+At position 11 to 263, the domain is characterized as Protein kinase.
+At position 602 to 651, the domain is characterized as KA1.
+At position 65 to 82, the domain is characterized as RRM.
+At position 537 to 648, the domain is characterized as Fibronectin type-III.
+At position 311 to 588, the domain is characterized as ABC transporter 1.
+At position 70 to 271, the domain is characterized as TLC.
+At position 1 to 46, the domain is characterized as Cadherin 1.
+At position 47 to 161, the domain is characterized as Cadherin 2.
+At position 162 to 238, the domain is characterized as Cadherin 3.
+At position 93 to 165, the domain is characterized as J.
+At position 22 to 138, the domain is characterized as HSR.
+At position 580 to 661, the domain is characterized as SAND.
+At position 796 to 829, the domain is characterized as Bromo.
+At position 388 to 666, the domain is characterized as Protein kinase.
+At position 210 to 444, the domain is characterized as NR LBD.
+At position 5 to 123, the domain is characterized as MTTase N-terminal.
+At position 77 to 266, the domain is characterized as ABC transmembrane type-1.
+At position 255 to 292, the domain is characterized as PKD.
+At position 231 to 498, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 219 to 386, the domain is characterized as TrmE-type G.
+At position 14 to 116, the domain is characterized as AB hydrolase-1.
+At position 121 to 501, the domain is characterized as Protein kinase.
+At position 87 to 150, the domain is characterized as bZIP.
+At position 11 to 254, the domain is characterized as DOG1.
+At position 151 to 409, the domain is characterized as Protein kinase.
+At position 36 to 89, the domain is characterized as PSI.
+At position 1477 to 1770, the domain is characterized as Autotransporter.
+At position 1 to 148, the domain is characterized as Thioredoxin.
+At position 67 to 320, the domain is characterized as Pyruvate carboxyltransferase.
+At position 43 to 256, the domain is characterized as Radical SAM core.
+At position 64 to 181, the domain is characterized as Calponin-homology (CH).
+At position 1042 to 1128, the domain is characterized as PDZ.
+At position 1612 to 1678, the domain is characterized as LIM zinc-binding.
+At position 29 to 277, the domain is characterized as Peptidase S1.
+At position 159 to 391, the domain is characterized as Radical SAM core.
+At position 121 to 251, the domain is characterized as AB hydrolase-1.
+At position 192 to 244, the domain is characterized as HAMP.
+At position 291 to 512, the domain is characterized as Histidine kinase.
+At position 668 to 787, the domain is characterized as Response regulatory.
+At position 824 to 917, the domain is characterized as HPt.
+At position 55 to 165, the domain is characterized as Expansin-like EG45.
+At position 178 to 260, the domain is characterized as Expansin-like CBD.
+At position 406 to 823, the domain is characterized as FH2.
+At position 404 to 485, the domain is characterized as RCK C-terminal.
+At position 113 to 374, the domain is characterized as NR LBD.
+At position 239 to 465, the domain is characterized as Grh/CP2 DB.
+At position 159 to 253, the domain is characterized as Rhodanese.
+At position 15 to 152, the domain is characterized as N-acetyltransferase 1.
+At position 86 to 418, the domain is characterized as Peptidase A1.
+At position 169 to 270, the domain is characterized as PpiC 1.
+At position 280 to 379, the domain is characterized as PpiC 2.
+At position 17 to 344, the domain is characterized as tr-type G.
+At position 679 to 871, the domain is characterized as ATP-grasp 2.
+At position 938 to 1078, the domain is characterized as MGS-like.
+At position 179 to 244, the domain is characterized as SEP.
+At position 291 to 368, the domain is characterized as UBX.
+At position 155 to 444, the domain is characterized as GT92.
+At position 761 to 847, the domain is characterized as SUEL-type lectin.
+At position 11 to 219, the domain is characterized as CYTH.
+At position 228 to 506, the domain is characterized as CHAD.
+At position 115 to 370, the domain is characterized as ABC transporter 1.
+At position 808 to 1050, the domain is characterized as ABC transporter 2.
+At position 124 to 345, the domain is characterized as Radical SAM core.
+At position 9 to 238, the domain is characterized as PPM-type phosphatase.
+At position 116 to 248, the domain is characterized as Ricin B-type lectin 2.
+At position 220 to 286, the domain is characterized as J.
+At position 137 to 366, the domain is characterized as NR LBD.
+At position 126 to 435, the domain is characterized as NACHT.
+At position 789 to 906, the domain is characterized as FIIND (incomplete).
+At position 486 to 807, the domain is characterized as Reverse transcriptase.
+At position 101 to 208, the domain is characterized as S4 RNA-binding.
+At position 1 to 142, the domain is characterized as PTS EIIA type-2.
+At position 4 to 301, the domain is characterized as Protein kinase.
+At position 99 to 581, the domain is characterized as Peptidase S8.
+At position 31 to 71, the domain is characterized as P-type.
+At position 53 to 331, the domain is characterized as PPM-type phosphatase.
+At position 97 to 225, the domain is characterized as FAD-binding FR-type.
+At position 198 to 389, the domain is characterized as Peptidase M12B.
+At position 397 to 483, the domain is characterized as Disintegrin.
+At position 270 to 327, the domain is characterized as FF 1.
+At position 368 to 422, the domain is characterized as FF 2.
+At position 429 to 483, the domain is characterized as FF 3.
+At position 485 to 550, the domain is characterized as FF 4.
+At position 592 to 767, the domain is characterized as pG1 pseudoGTPase.
+At position 783 to 947, the domain is characterized as pG2 pseudoGTPase.
+At position 1249 to 1436, the domain is characterized as Rho-GAP.
+At position 602 to 703, the domain is characterized as tRNA-binding.
+At position 4 to 43, the domain is characterized as UBA-like.
+At position 188 to 207, the domain is characterized as UIM 1.
+At position 231 to 250, the domain is characterized as UIM 2.
+At position 386 to 464, the domain is characterized as UBX.
+At position 287 to 497, the domain is characterized as NEL.
+At position 872 to 1048, the domain is characterized as Exonuclease.
+At position 230 to 471, the domain is characterized as CN hydrolase.
+At position 125 to 305, the domain is characterized as CP-type G.
+At position 1 to 160, the domain is characterized as Macro.
+At position 634 to 705, the domain is characterized as S1 motif 7.
+At position 727 to 796, the domain is characterized as S1 motif 8.
+At position 844 to 909, the domain is characterized as S1 motif 9.
+At position 1034 to 1107, the domain is characterized as S1 motif 10.
+At position 1148 to 1222, the domain is characterized as S1 motif 11.
+At position 1230 to 1298, the domain is characterized as S1 motif 12.
+At position 1324 to 1396, the domain is characterized as S1 motif 13.
+At position 536 to 625, the domain is characterized as GED.
+At position 42 to 212, the domain is characterized as FAD-binding PCMH-type.
+At position 132 to 422, the domain is characterized as Peptidase S8.
+At position 49 to 87, the domain is characterized as LDL-receptor class A 1.
+At position 88 to 128, the domain is characterized as LDL-receptor class A 2.
+At position 129 to 169, the domain is characterized as LDL-receptor class A 3.
+At position 170 to 208, the domain is characterized as LDL-receptor class A 4.
+At position 209 to 249, the domain is characterized as LDL-receptor class A 5.
+At position 255 to 293, the domain is characterized as LDL-receptor class A 6.
+At position 294 to 332, the domain is characterized as LDL-receptor class A 7.
+At position 334 to 373, the domain is characterized as LDL-receptor class A 8.
+At position 374 to 413, the domain is characterized as EGF-like 1; calcium-binding.
+At position 414 to 453, the domain is characterized as EGF-like 2; calcium-binding.
+At position 722 to 770, the domain is characterized as EGF-like 3.
+At position 87 to 392, the domain is characterized as Peptidase A1.
+At position 126 to 208, the domain is characterized as S1 motif.
+At position 477 to 513, the domain is characterized as ATP-grasp.
+At position 1502 to 1619, the domain is characterized as SET.
+At position 1625 to 1641, the domain is characterized as Post-SET.
+At position 53 to 249, the domain is characterized as Peptidase M12A.
+At position 273 to 457, the domain is characterized as CP-type G.
+At position 150 to 221, the domain is characterized as Cache.
+At position 301 to 353, the domain is characterized as HAMP.
+At position 372 to 622, the domain is characterized as Methyl-accepting transducer.
+At position 31 to 55, the domain is characterized as LRRNT.
+At position 209 to 259, the domain is characterized as LRRCT 1.
+At position 268 to 304, the domain is characterized as LRRNT 2.
+At position 434 to 484, the domain is characterized as LRRCT 2.
+At position 493 to 529, the domain is characterized as LRRNT 3.
+At position 660 to 710, the domain is characterized as LRRCT 3.
+At position 714 to 750, the domain is characterized as LRRNT 4.
+At position 280 to 493, the domain is characterized as Peptidase M12B.
+At position 503 to 587, the domain is characterized as Disintegrin.
+At position 943 to 1003, the domain is characterized as TSP type-1 2.
+At position 1004 to 1057, the domain is characterized as TSP type-1 3.
+At position 1060 to 1115, the domain is characterized as TSP type-1 4.
+At position 1116 to 1165, the domain is characterized as TSP type-1 5.
+At position 1168 to 1227, the domain is characterized as TSP type-1 6.
+At position 1228 to 1277, the domain is characterized as TSP type-1 7.
+At position 1280 to 1339, the domain is characterized as TSP type-1 8.
+At position 1352 to 1409, the domain is characterized as TSP type-1 9.
+At position 1410 to 1469, the domain is characterized as TSP type-1 10.
+At position 1474 to 1524, the domain is characterized as TSP type-1 11.
+At position 1527 to 1585, the domain is characterized as TSP type-1 12.
+At position 1621 to 1675, the domain is characterized as TSP type-1 13.
+At position 1678 to 1736, the domain is characterized as TSP type-1 14.
+At position 1737 to 1793, the domain is characterized as TSP type-1 15.
+At position 1794 to 1866, the domain is characterized as TSP type-1 16.
+At position 1867 to 1924, the domain is characterized as TSP type-1 17.
+At position 1924 to 2123, the domain is characterized as GON.
+At position 34 to 286, the domain is characterized as Radical SAM core.
+At position 45 to 179, the domain is characterized as C2.
+At position 230 to 338, the domain is characterized as PH.
+At position 614 to 693, the domain is characterized as BRCT.
+At position 11 to 223, the domain is characterized as YjeF N-terminal.
+At position 9 to 83, the domain is characterized as RRM 1.
+At position 123 to 197, the domain is characterized as RRM 2.
+At position 31 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 53 to 72, the domain is characterized as Peptidase A1.
+At position 29 to 223, the domain is characterized as ABC transmembrane type-1.
+At position 37 to 94, the domain is characterized as SLH 1.
+At position 95 to 158, the domain is characterized as SLH 2.
+At position 161 to 224, the domain is characterized as SLH 3.
+At position 1 to 48, the domain is characterized as RsgI N-terminal anti-sigma.
+At position 80 to 391, the domain is characterized as IF rod.
+At position 36 to 169, the domain is characterized as Thioredoxin 1.
+At position 170 to 295, the domain is characterized as Thioredoxin 2.
+At position 304 to 429, the domain is characterized as Thioredoxin 3.
+At position 296 to 374, the domain is characterized as PDZ 1.
+At position 885 to 957, the domain is characterized as PDZ 2.
+At position 31 to 85, the domain is characterized as TCP.
+At position 480 to 572, the domain is characterized as PH 1.
+At position 585 to 677, the domain is characterized as PH 2.
+At position 674 to 809, the domain is characterized as Arf-GAP.
+At position 899 to 1001, the domain is characterized as PH 3.
+At position 1012 to 1110, the domain is characterized as PH 4.
+At position 1114 to 1295, the domain is characterized as Rho-GAP.
+At position 1324 to 1418, the domain is characterized as Ras-associating.
+At position 1428 to 1531, the domain is characterized as PH 5.
+At position 1 to 111, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 64, the domain is characterized as F-box.
+At position 41 to 129, the domain is characterized as PPIase FKBP-type.
+At position 23 to 247, the domain is characterized as Peptidase S1.
+At position 4 to 154, the domain is characterized as NAC.
+At position 115 to 474, the domain is characterized as PTS EIIC type-1.
+At position 117 to 189, the domain is characterized as HTH crp-type.
+At position 680 to 938, the domain is characterized as Protein kinase.
+At position 222 to 283, the domain is characterized as G protein gamma.
+At position 299 to 414, the domain is characterized as RGS.
+At position 12 to 125, the domain is characterized as Response regulatory.
+At position 492 to 710, the domain is characterized as ELMO.
+At position 287 to 365, the domain is characterized as PDZ 1.
+At position 867 to 948, the domain is characterized as PDZ 2.
+At position 532 to 719, the domain is characterized as SEC7.
+At position 6 to 148, the domain is characterized as RNase H type-1.
+At position 1107 to 1401, the domain is characterized as Protein kinase.
+At position 5 to 87, the domain is characterized as BMV.
+At position 29 to 148, the domain is characterized as VIT.
+At position 272 to 432, the domain is characterized as VWFA.
+At position 1 to 155, the domain is characterized as MGS-like.
+At position 142 to 308, the domain is characterized as Helicase ATP-binding.
+At position 377 to 544, the domain is characterized as Helicase C-terminal.
+At position 944 to 1004, the domain is characterized as Tudor.
+At position 233 to 266, the domain is characterized as WW 1.
+At position 279 to 312, the domain is characterized as WW 2.
+At position 384 to 470, the domain is characterized as PPIase FKBP-type.
+At position 291 to 515, the domain is characterized as ABC transmembrane type-1.
+At position 102 to 360, the domain is characterized as Protein kinase.
+At position 402 to 437, the domain is characterized as EF-hand 1.
+At position 438 to 473, the domain is characterized as EF-hand 2.
+At position 474 to 509, the domain is characterized as EF-hand 3.
+At position 510 to 544, the domain is characterized as EF-hand 4.
+At position 87 to 164, the domain is characterized as RRM.
+At position 745 to 838, the domain is characterized as PWI.
+At position 23 to 145, the domain is characterized as MsrB.
+At position 1 to 85, the domain is characterized as FAD-binding FR-type.
+At position 215 to 391, the domain is characterized as Helicase ATP-binding.
+At position 413 to 563, the domain is characterized as Helicase C-terminal.
+At position 50 to 104, the domain is characterized as Collagen-like.
+At position 111 to 221, the domain is characterized as Fibrinogen C-terminal.
+At position 84 to 228, the domain is characterized as Flavodoxin-like.
+At position 283 to 523, the domain is characterized as FAD-binding FR-type.
+At position 177 to 292, the domain is characterized as C2 1.
+At position 334 to 452, the domain is characterized as C2 2.
+At position 494 to 607, the domain is characterized as C2 3.
+At position 35 to 391, the domain is characterized as IF rod.
+At position 468 to 585, the domain is characterized as LTD.
+At position 196 to 503, the domain is characterized as Protein kinase.
+At position 243 to 459, the domain is characterized as FAD-binding FR-type.
+At position 20 to 126, the domain is characterized as Ig-like V-type.
+At position 56 to 750, the domain is characterized as Peptidase M13.
+At position 227 to 281, the domain is characterized as PpiC; truncated.
+At position 219 to 397, the domain is characterized as DOC.
+At position 512 to 857, the domain is characterized as HECT.
+At position 39 to 112, the domain is characterized as KH type-2.
+At position 1 to 81, the domain is characterized as Carrier.
+At position 102 to 346, the domain is characterized as Radical SAM core.
+At position 29 to 158, the domain is characterized as Bulb-type lectin.
+At position 292 to 328, the domain is characterized as EGF-like.
+At position 342 to 424, the domain is characterized as PAN.
+At position 534 to 817, the domain is characterized as Protein kinase.
+At position 62 to 304, the domain is characterized as Protein kinase.
+At position 23 to 121, the domain is characterized as Ig-like V-type.
+At position 122 to 202, the domain is characterized as Ig-like C2-type.
+At position 155 to 215, the domain is characterized as SH3.
+At position 4 to 206, the domain is characterized as RNase H type-2.
+At position 605 to 691, the domain is characterized as Thioredoxin.
+At position 203 to 400, the domain is characterized as GMPS ATP-PPase.
+At position 147 to 254, the domain is characterized as THUMP.
+At position 1438 to 2153, the domain is characterized as FAT.
+At position 2332 to 2647, the domain is characterized as PI3K/PI4K catalytic.
+At position 2665 to 2697, the domain is characterized as FATC.
+At position 259 to 531, the domain is characterized as AB hydrolase-1.
+At position 5 to 79, the domain is characterized as BTB.
+At position 200 to 466, the domain is characterized as NPH3.
+At position 161 to 402, the domain is characterized as NR LBD.
+At position 13 to 84, the domain is characterized as Tudor-knot.
+At position 145 to 316, the domain is characterized as MRG.
+At position 6 to 35, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 56 to 177, the domain is characterized as MI 1.
+At position 220 to 341, the domain is characterized as MI 2.
+At position 351 to 472, the domain is characterized as MI 3.
+At position 514 to 633, the domain is characterized as MI 4.
+At position 39 to 213, the domain is characterized as Plastocyanin-like 1.
+At position 214 to 378, the domain is characterized as Plastocyanin-like 2.
+At position 22 to 80, the domain is characterized as LIM zinc-binding 1.
+At position 81 to 129, the domain is characterized as LIM zinc-binding 2.
+At position 753 to 932, the domain is characterized as Rho-GAP.
+At position 135 to 486, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 247 to 521, the domain is characterized as Tyrosine-protein phosphatase.
+At position 565 to 647, the domain is characterized as S1 motif.
+At position 366 to 614, the domain is characterized as TLDc.
+At position 176 to 267, the domain is characterized as PDZ.
+At position 16 to 94, the domain is characterized as Rieske 1.
+At position 17 to 131, the domain is characterized as Rieske 2.
+At position 41 to 117, the domain is characterized as VWFC 1.
+At position 161 to 279, the domain is characterized as CHRD 1.
+At position 281 to 401, the domain is characterized as CHRD 2.
+At position 402 to 522, the domain is characterized as CHRD 3.
+At position 528 to 655, the domain is characterized as CHRD 4.
+At position 691 to 751, the domain is characterized as VWFC 2.
+At position 769 to 838, the domain is characterized as VWFC 3.
+At position 857 to 919, the domain is characterized as VWFC 4.
+At position 916 to 945, the domain is characterized as IQ 2.
+At position 68 to 190, the domain is characterized as Thioredoxin.
+At position 1 to 83, the domain is characterized as GH18.
+At position 48 to 165, the domain is characterized as FZ.
+At position 181 to 303, the domain is characterized as NTR.
+At position 97 to 158, the domain is characterized as PWWP.
+At position 2 to 1180, the domain is characterized as Zinc-hook.
+At position 522 to 633, the domain is characterized as SMC hinge.
+At position 767 to 951, the domain is characterized as Helicase ATP-binding.
+At position 986 to 1139, the domain is characterized as Helicase C-terminal.
+At position 325 to 377, the domain is characterized as Myb-like.
+At position 176 to 222, the domain is characterized as G-patch.
+At position 250 to 277, the domain is characterized as KOW 1.
+At position 447 to 474, the domain is characterized as KOW 2.
+At position 223 to 247, the domain is characterized as HhH.
+At position 45 to 126, the domain is characterized as GST N-terminal.
+At position 174 to 341, the domain is characterized as GST C-terminal.
+At position 71 to 243, the domain is characterized as Laminin G-like.
+At position 442 to 490, the domain is characterized as Collagen-like 1.
+At position 532 to 586, the domain is characterized as Collagen-like 2.
+At position 583 to 641, the domain is characterized as Collagen-like 3.
+At position 616 to 674, the domain is characterized as Collagen-like 4.
+At position 643 to 699, the domain is characterized as Collagen-like 5.
+At position 1393 to 1450, the domain is characterized as Collagen-like 6.
+At position 1429 to 1487, the domain is characterized as Collagen-like 7.
+At position 1483 to 1541, the domain is characterized as Collagen-like 8.
+At position 1577 to 1805, the domain is characterized as Fibrillar collagen NC1.
+At position 2 to 226, the domain is characterized as ABC transporter.
+At position 1 to 248, the domain is characterized as F-BAR.
+At position 609 to 872, the domain is characterized as MHD.
+At position 8 to 93, the domain is characterized as BMC.
+At position 299 to 369, the domain is characterized as Mop.
+At position 129 to 450, the domain is characterized as Peptidase S8.
+At position 460 to 597, the domain is characterized as P/Homo B.
+At position 153 to 223, the domain is characterized as POTRA.
+At position 142 to 214, the domain is characterized as HTH crp-type.
+At position 51 to 171, the domain is characterized as RGS.
+At position 31 to 307, the domain is characterized as CN hydrolase.
+At position 961 to 1036, the domain is characterized as Carrier 1.
+At position 2036 to 2111, the domain is characterized as Carrier 2.
+At position 128 to 195, the domain is characterized as KH 1.
+At position 280 to 344, the domain is characterized as KH 2.
+At position 862 to 925, the domain is characterized as SAM.
+At position 1 to 282, the domain is characterized as GH18.
+At position 280 to 559, the domain is characterized as Protein kinase.
+At position 86 to 138, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 82 to 360, the domain is characterized as Protein kinase.
+At position 155 to 376, the domain is characterized as Radical SAM core.
+At position 19 to 148, the domain is characterized as Plastocyanin-like.
+At position 36 to 194, the domain is characterized as Cupin type-1 1.
+At position 254 to 426, the domain is characterized as Cupin type-1 2.
+At position 35 to 178, the domain is characterized as SIS.
+At position 270 to 322, the domain is characterized as CBS 2.
+At position 174 to 206, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 226 to 257, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 99 to 219, the domain is characterized as MTTase N-terminal.
+At position 243 to 498, the domain is characterized as Radical SAM core.
+At position 500 to 575, the domain is characterized as TRAM.
+At position 402 to 491, the domain is characterized as EH.
+At position 47 to 279, the domain is characterized as Radical SAM core.
+At position 34 to 295, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 47 to 176, the domain is characterized as AB hydrolase-1.
+At position 35 to 106, the domain is characterized as KRAB.
+At position 43 to 214, the domain is characterized as Laminin G-like 1.
+At position 221 to 387, the domain is characterized as Laminin G-like 2.
+At position 76 to 302, the domain is characterized as ABC transmembrane type-1.
+At position 230 to 314, the domain is characterized as Death.
+At position 85 to 161, the domain is characterized as Biotinyl-binding.
+At position 302 to 582, the domain is characterized as Radical SAM core.
+At position 189 to 259, the domain is characterized as PAS 1.
+At position 339 to 409, the domain is characterized as PAS 2.
+At position 12 to 273, the domain is characterized as Protein kinase.
+At position 366 to 433, the domain is characterized as PASTA 1.
+At position 434 to 505, the domain is characterized as PASTA 2.
+At position 506 to 577, the domain is characterized as PASTA 3.
+At position 578 to 651, the domain is characterized as PASTA 4.
+At position 404 to 562, the domain is characterized as Exonuclease.
+At position 454 to 729, the domain is characterized as ZP.
+At position 9 to 276, the domain is characterized as ABC transporter 1.
+At position 288 to 536, the domain is characterized as ABC transporter 2.
+At position 64 to 289, the domain is characterized as OBG-type G.
+At position 289 to 365, the domain is characterized as TGS.
+At position 3 to 150, the domain is characterized as Clp R.
+At position 108 to 137, the domain is characterized as HhH.
+At position 8 to 75, the domain is characterized as MIT.
+At position 310 to 448, the domain is characterized as YDG.
+At position 528 to 578, the domain is characterized as Pre-SET.
+At position 581 to 723, the domain is characterized as SET.
+At position 739 to 755, the domain is characterized as Post-SET.
+At position 29 to 276, the domain is characterized as Protein kinase.
+At position 190 to 435, the domain is characterized as Peptidase S1.
+At position 4 to 49, the domain is characterized as SpoVT-AbrB.
+At position 809 to 880, the domain is characterized as KHA.
+At position 658 to 834, the domain is characterized as PCI.
+At position 82 to 328, the domain is characterized as PPM-type phosphatase.
+At position 44 to 168, the domain is characterized as PID.
+At position 76 to 136, the domain is characterized as SH3.
+At position 142 to 239, the domain is characterized as SH2.
+At position 260 to 513, the domain is characterized as Protein kinase.
+At position 146 to 394, the domain is characterized as Pterin-binding.
+At position 40 to 472, the domain is characterized as G-alpha.
+At position 650 to 679, the domain is characterized as IQ.
+At position 192 to 384, the domain is characterized as CheB-type methylesterase.
+At position 137 to 444, the domain is characterized as Peptidase A1.
+At position 363 to 435, the domain is characterized as ACT 1.
+At position 436 to 510, the domain is characterized as ACT 2.
+At position 148 to 175, the domain is characterized as PLD phosphodiesterase.
+At position 13 to 131, the domain is characterized as Pru.
+At position 239 to 346, the domain is characterized as DEUBAD.
+At position 41 to 280, the domain is characterized as ABC transporter.
+At position 38 to 322, the domain is characterized as Alpha-carbonic anhydrase.
+At position 158 to 267, the domain is characterized as FAD-binding FR-type.
+At position 719 to 836, the domain is characterized as PH.
+At position 1065 to 1275, the domain is characterized as Rho-GAP.
+At position 20 to 269, the domain is characterized as ABC transporter.
+At position 212 to 289, the domain is characterized as TFIIS N-terminal.
+At position 233 to 266, the domain is characterized as WW.
+At position 330 to 456, the domain is characterized as PID 1.
+At position 499 to 615, the domain is characterized as PID 2.
+At position 51 to 83, the domain is characterized as ShKT.
+At position 361 to 416, the domain is characterized as LRRNT.
+At position 505 to 554, the domain is characterized as LRRCT.
+At position 304 to 559, the domain is characterized as Glutamine amidotransferase type-1.
+At position 255 to 318, the domain is characterized as bZIP.
+At position 13 to 336, the domain is characterized as PTS EIIC type-2.
+At position 372 to 463, the domain is characterized as PTS EIIB type-2.
+At position 482 to 624, the domain is characterized as PTS EIIA type-2.
+At position 180 to 231, the domain is characterized as HAMP.
+At position 236 to 472, the domain is characterized as Methyl-accepting transducer.
+At position 687 to 704, the domain is characterized as WH2.
+At position 28 to 161, the domain is characterized as MPN.
+At position 269 to 459, the domain is characterized as GATase cobBQ-type.
+At position 134 to 374, the domain is characterized as Radical SAM core.
+At position 337 to 615, the domain is characterized as Protein kinase.
+At position 25 to 92, the domain is characterized as BTB.
+At position 127 to 236, the domain is characterized as BACK.
+At position 53 to 226, the domain is characterized as FAD-binding PCMH-type.
+At position 278 to 590, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 781 to 906, the domain is characterized as C2.
+At position 6 to 157, the domain is characterized as NAC.
+At position 123 to 320, the domain is characterized as Tyr recombinase.
+At position 38 to 257, the domain is characterized as Radical SAM core.
+At position 684 to 746, the domain is characterized as SH3.
+At position 3 to 151, the domain is characterized as NAC.
+At position 33 to 162, the domain is characterized as PX.
+At position 93 to 128, the domain is characterized as EF-hand 2.
+At position 129 to 164, the domain is characterized as EF-hand 3.
+At position 3 to 120, the domain is characterized as WH1.
+At position 195 to 247, the domain is characterized as KBD.
+At position 296 to 404, the domain is characterized as SPR.
+At position 7 to 117, the domain is characterized as PH.
+At position 149 to 254, the domain is characterized as IRS-type PTB.
+At position 9 to 431, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 571 to 888, the domain is characterized as Malonyl-CoA:ACP transacylase (MAT).
+At position 957 to 1254, the domain is characterized as PKS/mFAS DH.
+At position 1838 to 2141, the domain is characterized as Enoyl reductase (ER).
+At position 2165 to 2344, the domain is characterized as Ketoreductase (KR).
+At position 1 to 184, the domain is characterized as TCTP.
+At position 298 to 416, the domain is characterized as Nop.
+At position 1 to 57, the domain is characterized as CSD.
+At position 372 to 804, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1304 to 1612, the domain is characterized as PKS/mFAS DH.
+At position 1655 to 1729, the domain is characterized as Carrier 1.
+At position 1886 to 1964, the domain is characterized as Carrier 3.
+At position 63 to 287, the domain is characterized as OBG-type G.
+At position 287 to 363, the domain is characterized as TGS.
+At position 15 to 93, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 95 to 134, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 233 to 289, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 373 to 576, the domain is characterized as TR mART core.
+At position 139 to 320, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 49, the domain is characterized as BTB.
+At position 591 to 697, the domain is characterized as tRNA-binding.
+At position 29 to 444, the domain is characterized as GH18.
+At position 29 to 82, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 178 to 384, the domain is characterized as ATP-grasp.
+At position 19 to 126, the domain is characterized as Ig-like V-type 1; required for binding to polymeric IgA and IgM.
+At position 145 to 237, the domain is characterized as Ig-like V-type 2.
+At position 250 to 341, the domain is characterized as Ig-like V-type 3.
+At position 353 to 457, the domain is characterized as Ig-like V-type 4.
+At position 461 to 560, the domain is characterized as Ig-like V-type 5.
+At position 27 to 137, the domain is characterized as sHSP.
+At position 907 to 1070, the domain is characterized as JmjC.
+At position 2 to 36, the domain is characterized as ShKT.
+At position 390 to 663, the domain is characterized as Protein kinase.
+At position 86 to 181, the domain is characterized as Ig-like C2-type 1.
+At position 136 to 199, the domain is characterized as HTH crp-type.
+At position 88 to 340, the domain is characterized as GS catalytic.
+At position 104 to 388, the domain is characterized as ABC transmembrane type-1 1.
+At position 505 to 724, the domain is characterized as ABC transporter 1.
+At position 814 to 1093, the domain is characterized as ABC transmembrane type-1 2.
+At position 1137 to 1371, the domain is characterized as ABC transporter 2.
+At position 97 to 172, the domain is characterized as POTRA.
+At position 15 to 77, the domain is characterized as HTH iclR-type.
+At position 92 to 265, the domain is characterized as IclR-ED.
+At position 29 to 186, the domain is characterized as PPIase cyclophilin-type.
+At position 512 to 706, the domain is characterized as SEC7.
+At position 756 to 869, the domain is characterized as PH.
+At position 6 to 66, the domain is characterized as Chromo.
+At position 58 to 107, the domain is characterized as EGF-like 2; calcium-binding.
+At position 108 to 157, the domain is characterized as EGF-like 3; calcium-binding.
+At position 415 to 467, the domain is characterized as GPS.
+At position 115 to 277, the domain is characterized as Exonuclease.
+At position 593 to 822, the domain is characterized as Peptidase S1 2.
+At position 253 to 421, the domain is characterized as PCI.
+At position 59 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 118, the domain is characterized as Kringle.
+At position 120 to 214, the domain is characterized as WSC.
+At position 218 to 325, the domain is characterized as CUB.
+At position 25 to 241, the domain is characterized as tr-type G.
+At position 484 to 667, the domain is characterized as Helicase ATP-binding 1.
+At position 677 to 894, the domain is characterized as Helicase C-terminal.
+At position 975 to 1278, the domain is characterized as SEC63 1.
+At position 1331 to 1506, the domain is characterized as Helicase ATP-binding 2.
+At position 1 to 40, the domain is characterized as Gla.
+At position 42 to 102, the domain is characterized as CBS 1.
+At position 124 to 186, the domain is characterized as CBS 2.
+At position 197 to 259, the domain is characterized as CBS 3.
+At position 271 to 328, the domain is characterized as CBS 4.
+At position 1 to 174, the domain is characterized as Macro.
+At position 687 to 845, the domain is characterized as F5/8 type C.
+At position 70 to 210, the domain is characterized as HD.
+At position 18 to 272, the domain is characterized as ABC transporter 1.
+At position 317 to 567, the domain is characterized as ABC transporter 2.
+At position 98 to 298, the domain is characterized as VWFA.
+At position 541 to 792, the domain is characterized as STAS.
+At position 3 to 126, the domain is characterized as MATH.
+At position 199 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 1344 to 1419, the domain is characterized as DEP.
+At position 217 to 390, the domain is characterized as PCI.
+At position 64 to 99, the domain is characterized as EF-hand 2.
+At position 380 to 571, the domain is characterized as DH.
+At position 601 to 822, the domain is characterized as PH.
+At position 848 to 1117, the domain is characterized as Protein kinase.
+At position 51 to 163, the domain is characterized as PA.
+At position 411 to 461, the domain is characterized as EGF-like 1.
+At position 464 to 511, the domain is characterized as EGF-like 2.
+At position 512 to 554, the domain is characterized as EGF-like 3; calcium-binding.
+At position 66 to 199, the domain is characterized as GST C-terminal.
+At position 239 to 398, the domain is characterized as EF-1-gamma C-terminal.
+At position 300 to 774, the domain is characterized as USP.
+At position 576 to 617, the domain is characterized as UBA 1.
+At position 639 to 679, the domain is characterized as UBA 2.
+At position 3 to 47, the domain is characterized as CUE.
+At position 413 to 846, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1343 to 1653, the domain is characterized as PKS/mFAS DH.
+At position 1742 to 1819, the domain is characterized as Carrier.
+At position 446 to 524, the domain is characterized as GRAM.
+At position 1288 to 1513, the domain is characterized as ABC transporter 2.
+At position 321 to 519, the domain is characterized as Rho-GAP.
+At position 69 to 218, the domain is characterized as SCP.
+At position 456 to 573, the domain is characterized as Toprim.
+At position 41 to 92, the domain is characterized as F-box.
+At position 166 to 263, the domain is characterized as HTH araC/xylS-type.
+At position 71 to 330, the domain is characterized as Protein kinase.
+At position 199 to 397, the domain is characterized as GMPS ATP-PPase.
+At position 37 to 198, the domain is characterized as TLDc.
+At position 189 to 452, the domain is characterized as NR LBD.
+At position 131 to 185, the domain is characterized as HTH cro/C1-type.
+At position 199 to 281, the domain is characterized as RCK C-terminal 1.
+At position 453 to 725, the domain is characterized as Protein kinase.
+At position 515 to 734, the domain is characterized as FtsK.
+At position 49 to 101, the domain is characterized as FHA.
+At position 284 to 330, the domain is characterized as F-box.
+At position 614 to 746, the domain is characterized as B12-binding.
+At position 167 to 245, the domain is characterized as Thyroglobulin type-1.
+At position 286 to 397, the domain is characterized as PAZ.
+At position 561 to 853, the domain is characterized as Piwi.
+At position 406 to 461, the domain is characterized as Kazal-like.
+At position 48 to 369, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 7 to 202, the domain is characterized as Peptidase M12B.
+At position 13 to 58, the domain is characterized as Gla.
+At position 88 to 126, the domain is characterized as EGF-like 1.
+At position 128 to 171, the domain is characterized as EGF-like 2; calcium-binding.
+At position 172 to 213, the domain is characterized as EGF-like 3; calcium-binding.
+At position 214 to 254, the domain is characterized as EGF-like 4; calcium-binding.
+At position 270 to 446, the domain is characterized as Laminin G-like 1.
+At position 455 to 636, the domain is characterized as Laminin G-like 2.
+At position 40 to 217, the domain is characterized as EngB-type G.
+At position 198 to 356, the domain is characterized as Helicase ATP-binding.
+At position 357 to 525, the domain is characterized as Helicase C-terminal.
+At position 201 to 305, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 253, the domain is characterized as ABC transporter 1.
+At position 320 to 546, the domain is characterized as ABC transporter 2.
+At position 4 to 95, the domain is characterized as HIG1.
+At position 287 to 385, the domain is characterized as PDZ 1.
+At position 771 to 847, the domain is characterized as PDZ 2.
+At position 40 to 179, the domain is characterized as N-acetyltransferase 1.
+At position 187 to 344, the domain is characterized as N-acetyltransferase 2.
+At position 623 to 693, the domain is characterized as S1 motif.
+At position 411 to 459, the domain is characterized as Smr.
+At position 183 to 267, the domain is characterized as PDZ.
+At position 67 to 272, the domain is characterized as FAD-binding PCMH-type.
+At position 226 to 363, the domain is characterized as MPN.
+At position 1 to 267, the domain is characterized as SMP-LTD.
+At position 35 to 169, the domain is characterized as SIS 1.
+At position 201 to 331, the domain is characterized as SIS 2.
+At position 642 to 755, the domain is characterized as Calponin-homology (CH).
+At position 8 to 114, the domain is characterized as Calponin-homology (CH) 1.
+At position 123 to 230, the domain is characterized as Calponin-homology (CH) 2.
+At position 388 to 419, the domain is characterized as EF-hand 1.
+At position 487 to 549, the domain is characterized as EF-hand 2.
+At position 550 to 618, the domain is characterized as EF-hand 3.
+At position 170 to 271, the domain is characterized as Fe2OG dioxygenase.
+At position 208 to 259, the domain is characterized as FHA.
+At position 304 to 577, the domain is characterized as PPM-type phosphatase.
+At position 380 to 497, the domain is characterized as BRCT.
+At position 51 to 148, the domain is characterized as Ig-like.
+At position 150 to 245, the domain is characterized as Ig-like C2-type.
+At position 249 to 303, the domain is characterized as TSP type-1 1.
+At position 305 to 357, the domain is characterized as TSP type-1 2.
+At position 542 to 685, the domain is characterized as ZU5.
+At position 863 to 941, the domain is characterized as Death.
+At position 44 to 146, the domain is characterized as BTB.
+At position 49 to 168, the domain is characterized as Thioredoxin.
+At position 25 to 129, the domain is characterized as Thioredoxin.
+At position 54 to 191, the domain is characterized as MPN.
+At position 44 to 155, the domain is characterized as tRNA-binding.
+At position 734 to 827, the domain is characterized as FDX-ACB.
+At position 20 to 168, the domain is characterized as LRAT.
+At position 87 to 129, the domain is characterized as Agouti.
+At position 532 to 812, the domain is characterized as Protein kinase.
+At position 884 to 1014, the domain is characterized as Guanylate cyclase.
+At position 64 to 234, the domain is characterized as Helicase ATP-binding.
+At position 65 to 130, the domain is characterized as J.
+At position 8 to 244, the domain is characterized as Radical SAM core.
+At position 22 to 279, the domain is characterized as Protein kinase.
+At position 53 to 103, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 124 to 174, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 222 to 272, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 98 to 291, the domain is characterized as ATP-grasp.
+At position 262 to 343, the domain is characterized as Toprim.
+At position 145 to 435, the domain is characterized as USP.
+At position 241 to 306, the domain is characterized as LIM zinc-binding 1.
+At position 307 to 365, the domain is characterized as LIM zinc-binding 2.
+At position 458 to 629, the domain is characterized as tr-type G.
+At position 142 to 186, the domain is characterized as LysM.
+At position 341 to 628, the domain is characterized as Protein kinase.
+At position 816 to 891, the domain is characterized as ACT 2.
+At position 390 to 587, the domain is characterized as FtsK.
+At position 70 to 318, the domain is characterized as ABC transporter 1.
+At position 334 to 556, the domain is characterized as ABC transporter 2.
+At position 27 to 137, the domain is characterized as MTTase N-terminal.
+At position 154 to 387, the domain is characterized as Radical SAM core.
+At position 390 to 457, the domain is characterized as TRAM.
+At position 9 to 201, the domain is characterized as DhaL.
+At position 44 to 131, the domain is characterized as Myb-like.
+At position 1 to 96, the domain is characterized as Fibronectin type-III.
+At position 21 to 284, the domain is characterized as Protein kinase.
+At position 62 to 242, the domain is characterized as tr-type G.
+At position 18 to 162, the domain is characterized as N-acetyltransferase.
+At position 60 to 236, the domain is characterized as Helicase ATP-binding.
+At position 8 to 166, the domain is characterized as Thioredoxin.
+At position 441 to 505, the domain is characterized as SOCS box.
+At position 205 to 360, the domain is characterized as Flavodoxin-like.
+At position 463 to 713, the domain is characterized as Radical SAM core.
+At position 585 to 874, the domain is characterized as Protein kinase.
+At position 167 to 250, the domain is characterized as PPIase FKBP-type.
+At position 364 to 404, the domain is characterized as UBA 2.
+At position 58 to 268, the domain is characterized as ABC transmembrane type-1.
+At position 1094 to 1154, the domain is characterized as v-SNARE coiled-coil homology.
+At position 258 to 427, the domain is characterized as GATase cobBQ-type.
+At position 9 to 129, the domain is characterized as MTTase N-terminal.
+At position 477 to 649, the domain is characterized as tr-type G.
+At position 255 to 284, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 300 to 330, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 184 to 328, the domain is characterized as TIR.
+At position 221 to 438, the domain is characterized as Helicase ATP-binding.
+At position 490 to 648, the domain is characterized as Helicase C-terminal.
+At position 1 to 216, the domain is characterized as SMP-LTD.
+At position 8 to 295, the domain is characterized as Protein kinase.
+At position 490 to 662, the domain is characterized as tr-type G.
+At position 127 to 406, the domain is characterized as Peptidase S8.
+At position 619 to 685, the domain is characterized as LIM zinc-binding.
+At position 167 to 309, the domain is characterized as PPC.
+At position 1 to 103, the domain is characterized as HPt.
+At position 367 to 607, the domain is characterized as Histidine kinase.
+At position 609 to 745, the domain is characterized as CheW-like.
+At position 105 to 182, the domain is characterized as GST N-terminal.
+At position 266 to 377, the domain is characterized as GST C-terminal.
+At position 1 to 92, the domain is characterized as HD.
+At position 578 to 722, the domain is characterized as GGDEF.
+At position 858 to 937, the domain is characterized as Carrier.
+At position 52 to 88, the domain is characterized as VM.
+At position 324 to 628, the domain is characterized as Protein kinase.
+At position 19 to 107, the domain is characterized as PPIase FKBP-type.
+At position 19 to 238, the domain is characterized as tr-type G.
+At position 68 to 191, the domain is characterized as MATH.
+At position 1 to 302, the domain is characterized as PUM-HD.
+At position 166 to 398, the domain is characterized as Radical SAM core.
+At position 42 to 158, the domain is characterized as MRH 1.
+At position 167 to 315, the domain is characterized as MRH 2.
+At position 321 to 463, the domain is characterized as MRH 3.
+At position 468 to 613, the domain is characterized as MRH 4.
+At position 619 to 755, the domain is characterized as MRH 5.
+At position 758 to 917, the domain is characterized as MRH 6.
+At position 925 to 1072, the domain is characterized as MRH 7.
+At position 1075 to 1212, the domain is characterized as MRH 8.
+At position 1218 to 1356, the domain is characterized as MRH 9.
+At position 1360 to 1501, the domain is characterized as MRH 10.
+At position 1507 to 1641, the domain is characterized as MRH 11.
+At position 1643 to 1790, the domain is characterized as MRH 12.
+At position 1795 to 1982, the domain is characterized as MRH 13.
+At position 1891 to 1937, the domain is characterized as Fibronectin type-II.
+At position 1985 to 2120, the domain is characterized as MRH 14.
+At position 2128 to 2273, the domain is characterized as MRH 15.
+At position 599 to 700, the domain is characterized as tRNA-binding.
+At position 123 to 190, the domain is characterized as Mop 1.
+At position 195 to 261, the domain is characterized as Mop 2.
+At position 397 to 584, the domain is characterized as DH.
+At position 87 to 123, the domain is characterized as EGF-like 1.
+At position 125 to 166, the domain is characterized as EGF-like 2.
+At position 172 to 399, the domain is characterized as Peptidase S1.
+At position 74 to 212, the domain is characterized as GST C-terminal.
+At position 843 to 899, the domain is characterized as WHEP-TRS.
+At position 86 to 244, the domain is characterized as FCP1 homology.
+At position 119 to 301, the domain is characterized as tr-type G.
+At position 47 to 355, the domain is characterized as AB hydrolase-1.
+At position 24 to 54, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 65 to 97, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 18 to 151, the domain is characterized as Galectin 1.
+At position 186 to 316, the domain is characterized as Galectin 2.
+At position 12 to 163, the domain is characterized as MPN.
+At position 332 to 423, the domain is characterized as RRM 1.
+At position 440 to 522, the domain is characterized as RRM 2.
+At position 18 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 311 to 556, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 212 to 262, the domain is characterized as bHLH.
+At position 70 to 170, the domain is characterized as SRCR 1.
+At position 105 to 205, the domain is characterized as SRCR 2.
+At position 273 to 373, the domain is characterized as SRCR 3.
+At position 420 to 520, the domain is characterized as SRCR 4.
+At position 574 to 683, the domain is characterized as CUB 1.
+At position 711 to 820, the domain is characterized as CUB 2.
+At position 844 to 944, the domain is characterized as SRCR 5.
+At position 966 to 1075, the domain is characterized as CUB 3.
+At position 1084 to 1332, the domain is characterized as ZP.
+At position 10 to 251, the domain is characterized as ABC transporter.
+At position 205 to 400, the domain is characterized as GMPS ATP-PPase.
+At position 394 to 516, the domain is characterized as 6-Cys 1.
+At position 676 to 800, the domain is characterized as 6-Cys 2.
+At position 831 to 1096, the domain is characterized as 6-Cys 3.
+At position 1099 to 1231, the domain is characterized as 6-Cys 4.
+At position 1268 to 1428, the domain is characterized as 6-Cys 5.
+At position 1433 to 1565, the domain is characterized as 6-Cys 6.
+At position 1656 to 1804, the domain is characterized as 6-Cys 7.
+At position 1807 to 1984, the domain is characterized as 6-Cys 8.
+At position 2197 to 2354, the domain is characterized as 6-Cys 9.
+At position 2357 to 2481, the domain is characterized as 6-Cys 10.
+At position 35 to 103, the domain is characterized as Importin N-terminal.
+At position 109 to 186, the domain is characterized as RRM.
+At position 8 to 169, the domain is characterized as N-acetyltransferase.
+At position 34 to 149, the domain is characterized as GOLD.
+At position 33 to 152, the domain is characterized as Plastocyanin-like 1.
+At position 164 to 330, the domain is characterized as Plastocyanin-like 2.
+At position 374 to 553, the domain is characterized as Plastocyanin-like 3.
+At position 24 to 219, the domain is characterized as Pentraxin (PTX).
+At position 309 to 353, the domain is characterized as UBA.
+At position 81 to 109, the domain is characterized as ITAM.
+At position 213 to 366, the domain is characterized as TrmE-type G.
+At position 163 to 350, the domain is characterized as Glutamine amidotransferase type-1.
+At position 22 to 82, the domain is characterized as HTH tetR-type.
+At position 1 to 179, the domain is characterized as Macro.
+At position 658 to 849, the domain is characterized as ATP-grasp 2.
+At position 915 to 1054, the domain is characterized as MGS-like.
+At position 2 to 125, the domain is characterized as PINc.
+At position 97 to 265, the domain is characterized as Helicase ATP-binding.
+At position 276 to 453, the domain is characterized as Helicase C-terminal.
+At position 67 to 607, the domain is characterized as PLA2c.
+At position 322 to 357, the domain is characterized as EF-hand 1.
+At position 363 to 398, the domain is characterized as EF-hand 2.
+At position 158 to 379, the domain is characterized as TRUD.
+At position 2 to 145, the domain is characterized as RNase H type-1.
+At position 1149 to 1392, the domain is characterized as Rap-GAP.
+At position 369 to 564, the domain is characterized as Rho-GAP.
+At position 791 to 1154, the domain is characterized as Protein kinase.
+At position 179 to 239, the domain is characterized as SH3.
+At position 247 to 345, the domain is characterized as SH2.
+At position 370 to 623, the domain is characterized as Protein kinase.
+At position 154 to 211, the domain is characterized as CTLH.
+At position 227 to 301, the domain is characterized as U-box.
+At position 122 to 211, the domain is characterized as EH 1.
+At position 155 to 190, the domain is characterized as EF-hand 1.
+At position 472 to 561, the domain is characterized as EH 2.
+At position 505 to 540, the domain is characterized as EF-hand 2.
+At position 1365 to 1382, the domain is characterized as WH2.
+At position 140 to 168, the domain is characterized as KOW.
+At position 369 to 436, the domain is characterized as DRBM.
+At position 252 to 432, the domain is characterized as PBS-linker 1.
+At position 514 to 693, the domain is characterized as PBS-linker 2.
+At position 710 to 888, the domain is characterized as PBS-linker 3.
+At position 922 to 1080, the domain is characterized as PBS-linker 4.
+At position 46 to 192, the domain is characterized as VOC 1.
+At position 223 to 383, the domain is characterized as VOC 2.
+At position 445 to 949, the domain is characterized as USP.
+At position 24 to 148, the domain is characterized as Thioredoxin.
+At position 7 to 41, the domain is characterized as EF-hand 1.
+At position 15 to 103, the domain is characterized as Rhodanese.
+At position 165 to 244, the domain is characterized as SH3.
+At position 281 to 463, the domain is characterized as Rho-GAP.
+At position 214 to 378, the domain is characterized as PID.
+At position 391 to 477, the domain is characterized as PDZ 1.
+At position 482 to 556, the domain is characterized as PDZ 2.
+At position 483 to 532, the domain is characterized as bHLH.
+At position 2 to 125, the domain is characterized as RCK N-terminal.
+At position 137 to 218, the domain is characterized as RCK C-terminal.
+At position 230 to 274, the domain is characterized as PCI.
+At position 82 to 172, the domain is characterized as CTCK.
+At position 78 to 278, the domain is characterized as B30.2/SPRY.
+At position 101 to 196, the domain is characterized as Expansin-like EG45.
+At position 206 to 286, the domain is characterized as Expansin-like CBD.
+At position 280 to 327, the domain is characterized as GST C-terminal.
+At position 14 to 94, the domain is characterized as Sm.
+At position 1 to 68, the domain is characterized as Disintegrin.
+At position 35 to 64, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 5 to 773, the domain is characterized as Myosin motor.
+At position 1948 to 2003, the domain is characterized as DEK-C.
+At position 16 to 252, the domain is characterized as ABC transporter.
+At position 521 to 643, the domain is characterized as Ricin B-type lectin.
+At position 67 to 384, the domain is characterized as PPM-type phosphatase.
+At position 123 to 333, the domain is characterized as PPM-type phosphatase.
+At position 16 to 232, the domain is characterized as Radical SAM core.
+At position 172 to 234, the domain is characterized as t-SNARE coiled-coil homology.
+At position 358 to 513, the domain is characterized as Exonuclease.
+At position 192 to 508, the domain is characterized as Protein kinase.
+At position 224 to 667, the domain is characterized as Protein kinase.
+At position 28 to 117, the domain is characterized as Ig-like C1-type.
+At position 21 to 257, the domain is characterized as AB hydrolase-1.
+At position 128 to 409, the domain is characterized as Protein kinase.
+At position 643 to 741, the domain is characterized as tRNA-binding.
+At position 88 to 188, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 1 to 204, the domain is characterized as ThyX.
+At position 370 to 406, the domain is characterized as NAF.
+At position 5 to 257, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 18 to 118, the domain is characterized as Ig-like V-type.
+At position 51 to 221, the domain is characterized as VWFA 1.
+At position 295 to 332, the domain is characterized as EGF-like 1.
+At position 342 to 516, the domain is characterized as VWFA 2.
+At position 530 to 704, the domain is characterized as VWFA 3.
+At position 711 to 747, the domain is characterized as EGF-like 2.
+At position 54 to 91, the domain is characterized as EF-hand 1.
+At position 133 to 168, the domain is characterized as EF-hand 2.
+At position 168 to 200, the domain is characterized as EF-hand 3.
+At position 205 to 267, the domain is characterized as t-SNARE coiled-coil homology.
+At position 1933 to 1998, the domain is characterized as NAC-A/B.
+At position 2039 to 2078, the domain is characterized as UBA.
+At position 350 to 586, the domain is characterized as Histidine kinase.
+At position 609 to 726, the domain is characterized as Response regulatory.
+At position 69 to 398, the domain is characterized as Peptidase A1.
+At position 544 to 736, the domain is characterized as SEC7.
+At position 776 to 892, the domain is characterized as PH.
+At position 44 to 137, the domain is characterized as Inhibitor I9.
+At position 156 to 462, the domain is characterized as Peptidase S8.
+At position 218 to 450, the domain is characterized as Peptidase S1.
+At position 7 to 149, the domain is characterized as MABP.
+At position 213 to 263, the domain is characterized as UMA.
+At position 163 to 331, the domain is characterized as SUN.
+At position 216 to 279, the domain is characterized as PAS.
+At position 336 to 528, the domain is characterized as Histidine kinase.
+At position 29 to 171, the domain is characterized as GAF.
+At position 205 to 433, the domain is characterized as Sigma-54 factor interaction.
+At position 640 to 675, the domain is characterized as EGF-like 17; calcium-binding.
+At position 1306 to 1345, the domain is characterized as EGF-like 34.
+At position 7 to 109, the domain is characterized as Rieske.
+At position 72 to 191, the domain is characterized as CUB 1.
+At position 193 to 306, the domain is characterized as CUB 2.
+At position 309 to 421, the domain is characterized as CUB 3.
+At position 28 to 219, the domain is characterized as Radical SAM core.
+At position 605 to 779, the domain is characterized as PCI.
+At position 5 to 214, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 35 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 139 to 226, the domain is characterized as Ig-like C2-type 2.
+At position 240 to 328, the domain is characterized as Ig-like C2-type 3.
+At position 333 to 420, the domain is characterized as Ig-like C2-type 4.
+At position 425 to 507, the domain is characterized as Ig-like C2-type 5.
+At position 518 to 607, the domain is characterized as Ig-like C2-type 6.
+At position 615 to 712, the domain is characterized as Fibronectin type-III 1.
+At position 717 to 810, the domain is characterized as Fibronectin type-III 2.
+At position 814 to 916, the domain is characterized as Fibronectin type-III 3.
+At position 1016 to 1115, the domain is characterized as Fibronectin type-III 5.
+At position 34 to 83, the domain is characterized as Myosin N-terminal SH3-like.
+At position 87 to 781, the domain is characterized as Myosin motor.
+At position 525 to 759, the domain is characterized as NR LBD.
+At position 10 to 104, the domain is characterized as HTH arsR-type.
+At position 56 to 159, the domain is characterized as Glutaredoxin.
+At position 183 to 255, the domain is characterized as DRBM 2.
+At position 400 to 566, the domain is characterized as Helicase ATP-binding.
+At position 638 to 811, the domain is characterized as Helicase C-terminal.
+At position 31 to 227, the domain is characterized as DPCK.
+At position 526 to 757, the domain is characterized as NR LBD.
+At position 53 to 361, the domain is characterized as AB hydrolase-1.
+At position 79 to 181, the domain is characterized as Ricin B-type lectin.
+At position 104 to 389, the domain is characterized as Protein kinase.
+At position 75 to 246, the domain is characterized as Helicase ATP-binding.
+At position 32 to 525, the domain is characterized as Sema.
+At position 30 to 175, the domain is characterized as UBC core.
+At position 201 to 387, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 183, the domain is characterized as Macro.
+At position 329 to 388, the domain is characterized as Myb-like.
+At position 232 to 362, the domain is characterized as DOD-type homing endonuclease.
+At position 551 to 768, the domain is characterized as tr-type G.
+At position 45 to 146, the domain is characterized as SUZ.
+At position 102 to 297, the domain is characterized as ATP-grasp.
+At position 289 to 381, the domain is characterized as Ig-like C2-type 1.
+At position 389 to 474, the domain is characterized as Ig-like C2-type 2.
+At position 357 to 439, the domain is characterized as DIX.
+At position 88 to 179, the domain is characterized as K-box.
+At position 133 to 305, the domain is characterized as Helicase ATP-binding.
+At position 370 to 529, the domain is characterized as Helicase C-terminal.
+At position 11 to 95, the domain is characterized as Phosphagen kinase N-terminal 1.
+At position 123 to 362, the domain is characterized as Phosphagen kinase C-terminal 1.
+At position 365 to 447, the domain is characterized as Phosphagen kinase N-terminal 2.
+At position 475 to 714, the domain is characterized as Phosphagen kinase C-terminal 2.
+At position 37 to 154, the domain is characterized as Plastocyanin-like 1.
+At position 166 to 309, the domain is characterized as Plastocyanin-like 2.
+At position 374 to 495, the domain is characterized as Plastocyanin-like 3.
+At position 6 to 144, the domain is characterized as EamA 1.
+At position 162 to 294, the domain is characterized as EamA 2.
+At position 590 to 669, the domain is characterized as BRCT.
+At position 305 to 432, the domain is characterized as Guanylate cyclase 1.
+At position 871 to 1013, the domain is characterized as Guanylate cyclase 2.
+At position 34 to 142, the domain is characterized as Gnk2-homologous 1.
+At position 148 to 261, the domain is characterized as Gnk2-homologous 2.
+At position 98 to 271, the domain is characterized as CRAL-TRIO.
+At position 19 to 69, the domain is characterized as F-box.
+At position 78 to 132, the domain is characterized as TCP.
+At position 11 to 186, the domain is characterized as Era-type G.
+At position 314 to 596, the domain is characterized as ABC transmembrane type-1 1.
+At position 630 to 853, the domain is characterized as ABC transporter 1.
+At position 936 to 1218, the domain is characterized as ABC transmembrane type-1 2.
+At position 1257 to 1489, the domain is characterized as ABC transporter 2.
+At position 191 to 356, the domain is characterized as Helicase ATP-binding.
+At position 486 to 637, the domain is characterized as Helicase C-terminal.
+At position 839 to 891, the domain is characterized as SANT 1.
+At position 942 to 1006, the domain is characterized as SANT 2.
+At position 104 to 286, the domain is characterized as Tyr recombinase.
+At position 11 to 433, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 937 to 1216, the domain is characterized as PKS/mFAS DH.
+At position 2506 to 2583, the domain is characterized as Carrier.
+At position 114 to 151, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 17 to 304, the domain is characterized as Radical SAM core.
+At position 48 to 77, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 79 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 192 to 413, the domain is characterized as RMT2.
+At position 4 to 264, the domain is characterized as Protein kinase.
+At position 361 to 451, the domain is characterized as BRCT.
+At position 436 to 555, the domain is characterized as HD.
+At position 676 to 755, the domain is characterized as ACT 1.
+At position 784 to 852, the domain is characterized as ACT 2.
+At position 29 to 105, the domain is characterized as Inhibitor I9.
+At position 110 to 606, the domain is characterized as Peptidase S8.
+At position 365 to 459, the domain is characterized as PA.
+At position 30 to 64, the domain is characterized as Chitin-binding type-1.
+At position 21 to 186, the domain is characterized as Exonuclease.
+At position 66 to 291, the domain is characterized as OBG-type G.
+At position 291 to 367, the domain is characterized as TGS.
+At position 185 to 373, the domain is characterized as Histidine kinase.
+At position 25 to 202, the domain is characterized as Chitin-binding type-4.
+At position 439 to 480, the domain is characterized as Chitin-binding type-3.
+At position 318 to 374, the domain is characterized as MIR 1.
+At position 384 to 440, the domain is characterized as MIR 2.
+At position 445 to 501, the domain is characterized as MIR 3.
+At position 11 to 278, the domain is characterized as tr-type G.
+At position 233 to 403, the domain is characterized as SSD.
+At position 31 to 257, the domain is characterized as PARP catalytic.
+At position 250 to 321, the domain is characterized as RST.
+At position 1 to 70, the domain is characterized as U-box.
+At position 123 to 165, the domain is characterized as LRRCT.
+At position 125 to 222, the domain is characterized as Rhodanese.
+At position 186 to 519, the domain is characterized as NB-ARC.
+At position 92 to 170, the domain is characterized as HARP.
+At position 209 to 367, the domain is characterized as Helicase ATP-binding.
+At position 482 to 639, the domain is characterized as Helicase C-terminal.
+At position 378 to 462, the domain is characterized as SWIB/MDM2.
+At position 486 to 559, the domain is characterized as SUI1.
+At position 7 to 206, the domain is characterized as DhaL.
+At position 102 to 410, the domain is characterized as IF rod.
+At position 25 to 82, the domain is characterized as S4 RNA-binding.
+At position 171 to 200, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 203 to 232, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 17 to 155, the domain is characterized as SprT-like.
+At position 415 to 477, the domain is characterized as BRCT 1.
+At position 505 to 603, the domain is characterized as BRCT 2.
+At position 177 to 332, the domain is characterized as N-acetyltransferase.
+At position 421 to 491, the domain is characterized as Bromo.
+At position 69 to 764, the domain is characterized as Myosin motor.
+At position 767 to 789, the domain is characterized as IQ 1.
+At position 790 to 814, the domain is characterized as IQ 2.
+At position 815 to 837, the domain is characterized as IQ 3.
+At position 838 to 862, the domain is characterized as IQ 4.
+At position 863 to 887, the domain is characterized as IQ 5.
+At position 888 to 915, the domain is characterized as IQ 6.
+At position 1508 to 1784, the domain is characterized as Dilute.
+At position 302 to 549, the domain is characterized as Glutamine amidotransferase type-1.
+At position 340 to 584, the domain is characterized as START.
+At position 46 to 136, the domain is characterized as THUMP.
+At position 136 to 450, the domain is characterized as IF rod.
+At position 158 to 284, the domain is characterized as EamA 2.
+At position 9 to 209, the domain is characterized as YjeF N-terminal.
+At position 255 to 507, the domain is characterized as Histidine kinase.
+At position 509 to 644, the domain is characterized as CheW-like.
+At position 60 to 83, the domain is characterized as EF-hand 2.
+At position 133 to 162, the domain is characterized as EF-hand 4.
+At position 129 to 190, the domain is characterized as ANTAR.
+At position 106 to 296, the domain is characterized as Tyr recombinase.
+At position 525 to 717, the domain is characterized as Helicase ATP-binding.
+At position 757 to 949, the domain is characterized as Helicase C-terminal.
+At position 28 to 142, the domain is characterized as CMP/dCMP-type deaminase.
+At position 54 to 268, the domain is characterized as FAD-binding PCMH-type.
+At position 207 to 357, the domain is characterized as Plastocyanin-like 2.
+At position 1495 to 1822, the domain is characterized as F5/8 type A 3.
+At position 1495 to 1659, the domain is characterized as Plastocyanin-like 5.
+At position 1669 to 1822, the domain is characterized as Plastocyanin-like 6.
+At position 1822 to 1970, the domain is characterized as F5/8 type C 1.
+At position 1975 to 2127, the domain is characterized as F5/8 type C 2.
+At position 12 to 122, the domain is characterized as MTTase N-terminal.
+At position 142 to 385, the domain is characterized as Radical SAM core.
+At position 388 to 461, the domain is characterized as TRAM.
+At position 25 to 174, the domain is characterized as F5/8 type C.
+At position 1 to 57, the domain is characterized as Ubiquitin-like.
+At position 367 to 405, the domain is characterized as UBA.
+At position 103 to 152, the domain is characterized as GIY-YIG.
+At position 14 to 104, the domain is characterized as ABM.
+At position 8 to 426, the domain is characterized as PTS EIIC type-3.
+At position 450 to 578, the domain is characterized as Guanylate cyclase.
+At position 5 to 241, the domain is characterized as AB hydrolase-1.
+At position 46 to 103, the domain is characterized as Ig-like C2-type 1.
+At position 132 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 234 to 301, the domain is characterized as Ig-like C2-type 3.
+At position 329 to 382, the domain is characterized as Ig-like C2-type 4.
+At position 416 to 469, the domain is characterized as Ig-like C2-type 5.
+At position 308 to 483, the domain is characterized as PCI.
+At position 35 to 155, the domain is characterized as MTTase N-terminal.
+At position 185 to 417, the domain is characterized as Radical SAM core.
+At position 420 to 482, the domain is characterized as TRAM.
+At position 569 to 646, the domain is characterized as PABC.
+At position 4 to 189, the domain is characterized as CYTH.
+At position 32 to 62, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 469 to 559, the domain is characterized as EH.
+At position 281 to 586, the domain is characterized as UvrD-like helicase C-terminal.
+At position 31 to 69, the domain is characterized as LRRNT.
+At position 35 to 159, the domain is characterized as THUMP.
+At position 32 to 253, the domain is characterized as Peptidase S1.
+At position 49 to 162, the domain is characterized as Collagen-like.
+At position 222 to 321, the domain is characterized as C-type lectin.
+At position 41 to 89, the domain is characterized as Fibronectin type-II.
+At position 93 to 130, the domain is characterized as EGF-like 1.
+At position 132 to 172, the domain is characterized as Fibronectin type-I.
+At position 173 to 209, the domain is characterized as EGF-like 2.
+At position 216 to 294, the domain is characterized as Kringle.
+At position 359 to 602, the domain is characterized as Peptidase S1.
+At position 14 to 142, the domain is characterized as EamA 1.
+At position 191 to 317, the domain is characterized as EamA 2.
+At position 300 to 365, the domain is characterized as SAM.
+At position 962 to 1294, the domain is characterized as Protein kinase.
+At position 128 to 278, the domain is characterized as DAGKc.
+At position 18 to 68, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 72 to 122, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 305 to 357, the domain is characterized as Collagen-like.
+At position 393 to 493, the domain is characterized as SRCR.
+At position 39 to 157, the domain is characterized as TBDR plug.
+At position 162 to 697, the domain is characterized as TBDR beta-barrel.
+At position 10 to 103, the domain is characterized as MtN3/slv 1.
+At position 47 to 111, the domain is characterized as Myb-like.
+At position 238 to 405, the domain is characterized as Helicase ATP-binding.
+At position 484 to 663, the domain is characterized as Helicase C-terminal.
+At position 23 to 180, the domain is characterized as PPIase cyclophilin-type.
+At position 77 to 175, the domain is characterized as Fe2OG dioxygenase.
+At position 11 to 68, the domain is characterized as LIM zinc-binding 1.
+At position 69 to 129, the domain is characterized as LIM zinc-binding 2.
+At position 788 to 1006, the domain is characterized as Rho-GAP.
+At position 414 to 493, the domain is characterized as B5.
+At position 741 to 834, the domain is characterized as FDX-ACB.
+At position 1 to 129, the domain is characterized as Nudix hydrolase.
+At position 215 to 450, the domain is characterized as PABS.
+At position 167 to 414, the domain is characterized as Fibrinogen C-terminal.
+At position 55 to 108, the domain is characterized as Kazal-like.
+At position 114 to 212, the domain is characterized as SRCR.
+At position 213 to 257, the domain is characterized as LDL-receptor class A 1.
+At position 258 to 294, the domain is characterized as LDL-receptor class A 2.
+At position 340 to 574, the domain is characterized as Peptidase S1.
+At position 198 to 395, the domain is characterized as Helicase ATP-binding.
+At position 448 to 611, the domain is characterized as Helicase C-terminal.
+At position 563 to 714, the domain is characterized as STAS.
+At position 70 to 124, the domain is characterized as bHLH.
+At position 1209 to 1373, the domain is characterized as PNPLA.
+At position 634 to 908, the domain is characterized as Protein kinase.
+At position 27 to 70, the domain is characterized as CWF21.
+At position 1357 to 1645, the domain is characterized as Autotransporter.
+At position 204 to 438, the domain is characterized as START.
+At position 347 to 427, the domain is characterized as OCT.
+At position 68 to 312, the domain is characterized as Peptidase S1.
+At position 43 to 309, the domain is characterized as Protein kinase.
+At position 20 to 180, the domain is characterized as MRH.
+At position 212 to 353, the domain is characterized as DAGKc.
+At position 19 to 606, the domain is characterized as Peptidase M2.
+At position 613 to 804, the domain is characterized as Collectrin-like.
+At position 26 to 134, the domain is characterized as Glutaredoxin.
+At position 3 to 83, the domain is characterized as Toprim.
+At position 21 to 223, the domain is characterized as Pentraxin (PTX).
+At position 161 to 238, the domain is characterized as RRM 1.
+At position 262 to 338, the domain is characterized as RRM 2.
+At position 299 to 487, the domain is characterized as PCI.
+At position 36 to 166, the domain is characterized as VHS.
+At position 190 to 317, the domain is characterized as GAT.
+At position 474 to 595, the domain is characterized as GAE.
+At position 595 to 673, the domain is characterized as Carrier.
+At position 668 to 792, the domain is characterized as C2 2.
+At position 1102 to 1245, the domain is characterized as MHD1.
+At position 1354 to 1521, the domain is characterized as MHD2.
+At position 1535 to 1662, the domain is characterized as C2 3.
+At position 91 to 159, the domain is characterized as S4 RNA-binding.
+At position 10 to 188, the domain is characterized as Guanylate kinase-like.
+At position 389 to 671, the domain is characterized as Protein kinase.
+At position 615 to 696, the domain is characterized as S1 motif.
+At position 84 to 148, the domain is characterized as Z-binding 2.
+At position 21 to 207, the domain is characterized as Reticulon.
+At position 317 to 484, the domain is characterized as tr-type G.
+At position 51 to 276, the domain is characterized as Peptidase S1.
+At position 9 to 191, the domain is characterized as ABC transporter.
+At position 127 to 370, the domain is characterized as Radical SAM core.
+At position 162 to 314, the domain is characterized as Plastocyanin-like 2.
+At position 414 to 548, the domain is characterized as Plastocyanin-like 3.
+At position 26 to 73, the domain is characterized as F-box.
+At position 164 to 283, the domain is characterized as Fe2OG dioxygenase.
+At position 51 to 265, the domain is characterized as Radical SAM core.
+At position 10 to 249, the domain is characterized as ABC transporter.
+At position 48 to 274, the domain is characterized as Peptidase S1.
+At position 6 to 267, the domain is characterized as Pyruvate carboxyltransferase.
+At position 172 to 207, the domain is characterized as EF-hand 1.
+At position 227 to 262, the domain is characterized as EF-hand 2.
+At position 293 to 328, the domain is characterized as EF-hand 3.
+At position 362 to 397, the domain is characterized as EF-hand 4.
+At position 30 to 105, the domain is characterized as Sm.
+At position 1 to 27, the domain is characterized as H15.
+At position 270 to 333, the domain is characterized as PWWP 1.
+At position 960 to 1025, the domain is characterized as PWWP 2.
+At position 1096 to 1146, the domain is characterized as AWS.
+At position 1148 to 1265, the domain is characterized as SET.
+At position 1272 to 1288, the domain is characterized as Post-SET.
+At position 111 to 417, the domain is characterized as Peptidase S8.
+At position 312 to 388, the domain is characterized as ACT 1.
+At position 389 to 454, the domain is characterized as ACT 2.
+At position 98 to 166, the domain is characterized as DRBM.
+At position 258 to 584, the domain is characterized as A to I editase.
+At position 343 to 404, the domain is characterized as S4 RNA-binding.
+At position 4 to 80, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 18 to 273, the domain is characterized as SET.
+At position 28 to 81, the domain is characterized as bHLH.
+At position 220 to 320, the domain is characterized as Fibronectin type-III.
+At position 29 to 87, the domain is characterized as TCP.
+At position 18 to 100, the domain is characterized as SWIB/MDM2.
+At position 125 to 335, the domain is characterized as ATP-grasp.
+At position 188 to 288, the domain is characterized as Fe2OG dioxygenase.
+At position 6 to 117, the domain is characterized as Longin.
+At position 132 to 192, the domain is characterized as v-SNARE coiled-coil homology.
+At position 84 to 156, the domain is characterized as PUB.
+At position 57 to 144, the domain is characterized as ENT.
+At position 32 to 89, the domain is characterized as FHA.
+At position 169 to 204, the domain is characterized as EF-hand 1.
+At position 290 to 325, the domain is characterized as EF-hand 3.
+At position 359 to 394, the domain is characterized as EF-hand 4.
+At position 40 to 88, the domain is characterized as F-box.
+At position 122 to 206, the domain is characterized as LITAF.
+At position 44 to 89, the domain is characterized as Gla.
+At position 108 to 186, the domain is characterized as Kringle 1.
+At position 213 to 291, the domain is characterized as Kringle 2.
+At position 364 to 618, the domain is characterized as Peptidase S1.
+At position 79 to 217, the domain is characterized as Flavodoxin-like.
+At position 249 to 463, the domain is characterized as FAD-binding FR-type.
+At position 249 to 433, the domain is characterized as Helicase ATP-binding.
+At position 662 to 816, the domain is characterized as Helicase C-terminal.
+At position 1 to 359, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 282 to 588, the domain is characterized as UvrD-like helicase C-terminal.
+At position 151 to 329, the domain is characterized as Helicase ATP-binding.
+At position 340 to 504, the domain is characterized as Helicase C-terminal.
+At position 114 to 213, the domain is characterized as Ig-like 2.
+At position 222 to 318, the domain is characterized as Ig-like 3.
+At position 3 to 160, the domain is characterized as Obg.
+At position 355 to 444, the domain is characterized as OCT.
+At position 20 to 162, the domain is characterized as MPN.
+At position 3 to 165, the domain is characterized as FeoB-type G.
+At position 45 to 80, the domain is characterized as EF-hand 2.
+At position 118 to 152, the domain is characterized as EF-hand 4.
+At position 1 to 70, the domain is characterized as RRM 1.
+At position 182 to 255, the domain is characterized as RRM 2.
+At position 10 to 274, the domain is characterized as Protein kinase.
+At position 375 to 441, the domain is characterized as PASTA 1.
+At position 443 to 509, the domain is characterized as PASTA 2.
+At position 512 to 577, the domain is characterized as PASTA 3.
+At position 1 to 204, the domain is characterized as SMP-LTD.
+At position 7 to 154, the domain is characterized as MPN.
+At position 237 to 451, the domain is characterized as FAD-binding FR-type.
+At position 35 to 102, the domain is characterized as Histone-fold.
+At position 297 to 418, the domain is characterized as C2 1.
+At position 429 to 563, the domain is characterized as C2 2.
+At position 17 to 111, the domain is characterized as Rhodanese.
+At position 21 to 162, the domain is characterized as MPN.
+At position 159 to 204, the domain is characterized as UBA.
+At position 11 to 210, the domain is characterized as YjeF N-terminal.
+At position 132 to 171, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 247 to 515, the domain is characterized as CN hydrolase.
+At position 139 to 429, the domain is characterized as ABC transmembrane type-1.
+At position 465 to 701, the domain is characterized as ABC transporter.
+At position 82 to 256, the domain is characterized as Helicase ATP-binding.
+At position 282 to 431, the domain is characterized as Helicase C-terminal.
+At position 53 to 228, the domain is characterized as EngB-type G.
+At position 299 to 397, the domain is characterized as GTD-binding.
+At position 51 to 203, the domain is characterized as Tyrosine-protein phosphatase.
+At position 26 to 138, the domain is characterized as Ig-like V-type.
+At position 145 to 228, the domain is characterized as Ig-like C2-type 1.
+At position 250 to 334, the domain is characterized as Ig-like C2-type 2.
+At position 339 to 436, the domain is characterized as Ig-like C2-type 3.
+At position 18 to 261, the domain is characterized as tr-type G.
+At position 151 to 307, the domain is characterized as TRUD.
+At position 88 to 263, the domain is characterized as Helicase ATP-binding.
+At position 275 to 436, the domain is characterized as Helicase C-terminal.
+At position 154 to 272, the domain is characterized as OmpA-like.
+At position 595 to 676, the domain is characterized as BRCT.
+At position 508 to 649, the domain is characterized as Flavodoxin-like.
+At position 685 to 924, the domain is characterized as FAD-binding FR-type.
+At position 2 to 20, the domain is characterized as LCN-type CS-alpha/beta.
+At position 42 to 103, the domain is characterized as CBS 1.
+At position 123 to 186, the domain is characterized as CBS 2.
+At position 199 to 259, the domain is characterized as CBS 3.
+At position 268 to 328, the domain is characterized as CBS 4.
+At position 158 to 379, the domain is characterized as Radical SAM core.
+At position 12 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 56 to 83, the domain is characterized as Myb-like.
+At position 84 to 138, the domain is characterized as HTH myb-type.
+At position 602 to 739, the domain is characterized as B12-binding.
+At position 332 to 515, the domain is characterized as DUF1170.
+At position 21 to 192, the domain is characterized as EngB-type G.
+At position 101 to 332, the domain is characterized as Radical SAM core.
+At position 39 to 121, the domain is characterized as ACT 1.
+At position 136 to 213, the domain is characterized as ACT 2.
+At position 298 to 373, the domain is characterized as ACT 3.
+At position 376 to 459, the domain is characterized as ACT 4.
+At position 93 to 151, the domain is characterized as CBS 1.
+At position 152 to 211, the domain is characterized as CBS 2.
+At position 60 to 179, the domain is characterized as C-type lectin.
+At position 561 to 623, the domain is characterized as R3H.
+At position 690 to 737, the domain is characterized as G-patch.
+At position 608 to 886, the domain is characterized as Protein kinase.
+At position 28 to 145, the domain is characterized as C-type lectin.
+At position 26 to 80, the domain is characterized as TSP type-1 1.
+At position 304 to 361, the domain is characterized as TSP type-1 2.
+At position 362 to 421, the domain is characterized as TSP type-1 3.
+At position 423 to 481, the domain is characterized as TSP type-1 4.
+At position 484 to 539, the domain is characterized as TSP type-1 5.
+At position 754 to 804, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 900 to 995, the domain is characterized as Ig-like C2-type 1.
+At position 1033 to 1128, the domain is characterized as Ig-like C2-type 2.
+At position 1133 to 1218, the domain is characterized as Ig-like C2-type 3.
+At position 1231 to 1270, the domain is characterized as PLAC.
+At position 276 to 374, the domain is characterized as CS.
+At position 5 to 73, the domain is characterized as NAC-A/B.
+At position 383 to 526, the domain is characterized as RCK N-terminal.
+At position 217 to 295, the domain is characterized as RRM.
+At position 672 to 748, the domain is characterized as Carrier.
+At position 429 to 479, the domain is characterized as DHHC.
+At position 54 to 130, the domain is characterized as EMI.
+At position 203 to 505, the domain is characterized as Lon N-terminal.
+At position 964 to 1150, the domain is characterized as Lon proteolytic.
+At position 8 to 98, the domain is characterized as KRAB.
+At position 432 to 556, the domain is characterized as RNase III.
+At position 582 to 649, the domain is characterized as DRBM.
+At position 18 to 124, the domain is characterized as PH.
+At position 134 to 328, the domain is characterized as Rho-GAP.
+At position 375 to 432, the domain is characterized as CBS 1.
+At position 436 to 492, the domain is characterized as CBS 2.
+At position 227 to 688, the domain is characterized as Trm1 methyltransferase.
+At position 519 to 594, the domain is characterized as Carrier 1.
+At position 1544 to 1622, the domain is characterized as Carrier 2.
+At position 2061 to 2134, the domain is characterized as Carrier 3.
+At position 41 to 327, the domain is characterized as Protein kinase.
+At position 422 to 729, the domain is characterized as Peptidase S8.
+At position 268 to 331, the domain is characterized as bZIP.
+At position 253 to 303, the domain is characterized as DHHC.
+At position 96 to 238, the domain is characterized as Clp R.
+At position 645 to 735, the domain is characterized as bHLH.
+At position 4 to 90, the domain is characterized as GIY-YIG.
+At position 106 to 178, the domain is characterized as S4 RNA-binding.
+At position 31 to 185, the domain is characterized as F5/8 type C.
+At position 610 to 905, the domain is characterized as Protein kinase.
+At position 14 to 76, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 145 to 207, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 141 to 203, the domain is characterized as bZIP.
+At position 894 to 963, the domain is characterized as R3H.
+At position 257 to 338, the domain is characterized as Toprim.
+At position 135 to 296, the domain is characterized as CRAL-TRIO.
+At position 507 to 677, the domain is characterized as tr-type G.
+At position 1 to 159, the domain is characterized as TLDc.
+At position 1 to 483, the domain is characterized as SPX.
+At position 738 to 940, the domain is characterized as EXS.
+At position 5 to 378, the domain is characterized as DZF.
+At position 398 to 467, the domain is characterized as DRBM 1.
+At position 524 to 590, the domain is characterized as DRBM 2.
+At position 7 to 230, the domain is characterized as Radical SAM core.
+At position 54 to 89, the domain is characterized as EF-hand.
+At position 33 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 834 to 909, the domain is characterized as MBD.
+At position 971 to 1049, the domain is characterized as Pre-SET.
+At position 1052 to 1277, the domain is characterized as SET.
+At position 1286 to 1302, the domain is characterized as Post-SET.
+At position 1 to 93, the domain is characterized as BRCT 1.
+At position 644 to 734, the domain is characterized as BRCT 2.
+At position 755 to 837, the domain is characterized as BRCT 3.
+At position 252 to 329, the domain is characterized as POU-specific.
+At position 542 to 617, the domain is characterized as Cytochrome b5 heme-binding.
+At position 27 to 127, the domain is characterized as Ig-like 1.
+At position 134 to 232, the domain is characterized as Ig-like 2.
+At position 242 to 328, the domain is characterized as Ig-like 3.
+At position 340 to 436, the domain is characterized as Ig-like 4.
+At position 442 to 533, the domain is characterized as Ig-like 5.
+At position 540 to 627, the domain is characterized as Ig-like 6.
+At position 638 to 738, the domain is characterized as Fibronectin type-III.
+At position 739 to 914, the domain is characterized as MAM.
+At position 134 to 447, the domain is characterized as IF rod.
+At position 2 to 195, the domain is characterized as ABC transporter.
+At position 39 to 97, the domain is characterized as VWFC.
+At position 1266 to 1499, the domain is characterized as Fibrillar collagen NC1.
+At position 12 to 255, the domain is characterized as PABS.
+At position 441 to 711, the domain is characterized as Protein kinase.
+At position 249 to 444, the domain is characterized as GATase cobBQ-type.
+At position 84 to 315, the domain is characterized as AB hydrolase-1.
+At position 281 to 460, the domain is characterized as RHD.
+At position 659 to 747, the domain is characterized as BRCT.
+At position 134 to 343, the domain is characterized as ATP-grasp.
+At position 308 to 384, the domain is characterized as RRM 1.
+At position 394 to 467, the domain is characterized as RRM 2.
+At position 71 to 120, the domain is characterized as P-type 1.
+At position 936 to 984, the domain is characterized as P-type 2.
+At position 2 to 246, the domain is characterized as Deacetylase sirtuin-type.
+At position 564 to 651, the domain is characterized as Carrier.
+At position 114 to 149, the domain is characterized as Tify.
+At position 64 to 125, the domain is characterized as FHA.
+At position 1261 to 1364, the domain is characterized as PH.
+At position 457 to 637, the domain is characterized as N-acetyltransferase.
+At position 24 to 66, the domain is characterized as HNH.
+At position 21 to 410, the domain is characterized as Helicase ATP-binding.
+At position 425 to 578, the domain is characterized as Helicase C-terminal.
+At position 24 to 159, the domain is characterized as Jacalin-type lectin.
+At position 25 to 154, the domain is characterized as FZ.
+At position 2 to 136, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 429 to 533, the domain is characterized as Rhodanese.
+At position 156 to 346, the domain is characterized as CheB-type methylesterase.
+At position 31 to 267, the domain is characterized as BAR.
+At position 281 to 340, the domain is characterized as SH3.
+At position 108 to 143, the domain is characterized as EF-hand 1.
+At position 153 to 188, the domain is characterized as EF-hand 2.
+At position 365 to 498, the domain is characterized as DAGKc.
+At position 236 to 629, the domain is characterized as Protein kinase.
+At position 639 to 843, the domain is characterized as MRH.
+At position 134 to 201, the domain is characterized as SCA7.
+At position 34 to 261, the domain is characterized as ABC transporter.
+At position 67 to 173, the domain is characterized as Expansin-like EG45.
+At position 187 to 268, the domain is characterized as Expansin-like CBD.
+At position 70 to 144, the domain is characterized as Lipoyl-binding.
+At position 4 to 87, the domain is characterized as RRM 1.
+At position 183 to 268, the domain is characterized as RRM 2.
+At position 51 to 242, the domain is characterized as SMP-LBD.
+At position 245 to 362, the domain is characterized as C2.
+At position 48 to 172, the domain is characterized as sHSP.
+At position 13 to 154, the domain is characterized as RNase H type-1.
+At position 1 to 205, the domain is characterized as START.
+At position 80 to 395, the domain is characterized as IF rod.
+At position 147 to 248, the domain is characterized as BACK.
+At position 848 to 1043, the domain is characterized as DH.
+At position 1085 to 1187, the domain is characterized as PH.
+At position 4 to 472, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 503 to 785, the domain is characterized as UvrD-like helicase C-terminal.
+At position 611 to 886, the domain is characterized as DDHD.
+At position 17 to 99, the domain is characterized as GIY-YIG.
+At position 31 to 270, the domain is characterized as Laminin N-terminal.
+At position 271 to 334, the domain is characterized as Laminin EGF-like 1.
+At position 335 to 397, the domain is characterized as Laminin EGF-like 2.
+At position 398 to 457, the domain is characterized as Laminin EGF-like 3.
+At position 458 to 509, the domain is characterized as Laminin EGF-like 4.
+At position 510 to 540, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 549 to 767, the domain is characterized as Laminin IV type B.
+At position 773 to 820, the domain is characterized as Laminin EGF-like 6.
+At position 821 to 866, the domain is characterized as Laminin EGF-like 7.
+At position 867 to 916, the domain is characterized as Laminin EGF-like 8.
+At position 917 to 975, the domain is characterized as Laminin EGF-like 9.
+At position 976 to 1027, the domain is characterized as Laminin EGF-like 10.
+At position 1028 to 1083, the domain is characterized as Laminin EGF-like 11.
+At position 1084 to 1131, the domain is characterized as Laminin EGF-like 12.
+At position 1132 to 1178, the domain is characterized as Laminin EGF-like 13.
+At position 133 to 338, the domain is characterized as ATP-grasp.
+At position 110 to 304, the domain is characterized as SEC7.
+At position 447 to 571, the domain is characterized as PH.
+At position 229 to 277, the domain is characterized as Fibronectin type-II 1.
+At position 287 to 335, the domain is characterized as Fibronectin type-II 2.
+At position 345 to 393, the domain is characterized as Fibronectin type-II 3.
+At position 24 to 99, the domain is characterized as Kringle.
+At position 9 to 85, the domain is characterized as Cytochrome b5 heme-binding.
+At position 79 to 334, the domain is characterized as Protein kinase.
+At position 532 to 655, the domain is characterized as STAS.
+At position 78 to 325, the domain is characterized as ATP-grasp.
+At position 18 to 96, the domain is characterized as GIY-YIG.
+At position 24 to 335, the domain is characterized as USP.
+At position 416 to 549, the domain is characterized as RanBD1.
+At position 142 to 205, the domain is characterized as CBS 1.
+At position 206 to 262, the domain is characterized as CBS 2.
+At position 11 to 346, the domain is characterized as Kinesin motor.
+At position 207 to 270, the domain is characterized as bZIP.
+At position 105 to 142, the domain is characterized as LRRNT.
+At position 218 to 293, the domain is characterized as MIT.
+At position 189 to 295, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 169 to 284, the domain is characterized as SET.
+At position 1 to 42, the domain is characterized as Kazal-like.
+At position 135 to 201, the domain is characterized as Z-binding 1.
+At position 243 to 307, the domain is characterized as Z-binding 2.
+At position 453 to 521, the domain is characterized as DRBM 1.
+At position 564 to 632, the domain is characterized as DRBM 2.
+At position 672 to 740, the domain is characterized as DRBM 3.
+At position 832 to 1167, the domain is characterized as A to I editase.
+At position 24 to 83, the domain is characterized as HTH tetR-type.
+At position 252 to 316, the domain is characterized as EamA.
+At position 95 to 312, the domain is characterized as Radical SAM core.
+At position 18 to 126, the domain is characterized as PET.
+At position 128 to 193, the domain is characterized as LIM zinc-binding 1.
+At position 193 to 253, the domain is characterized as LIM zinc-binding 2.
+At position 253 to 317, the domain is characterized as LIM zinc-binding 3.
+At position 1 to 59, the domain is characterized as HTH araC/xylS-type.
+At position 7 to 82, the domain is characterized as Ubiquitin-like.
+At position 155 to 309, the domain is characterized as Nudix hydrolase.
+At position 2 to 118, the domain is characterized as PINc.
+At position 227 to 254, the domain is characterized as PLD phosphodiesterase 1.
+At position 408 to 435, the domain is characterized as PLD phosphodiesterase 2.
+At position 241 to 334, the domain is characterized as PDZ.
+At position 14 to 184, the domain is characterized as Era-type G.
+At position 215 to 292, the domain is characterized as KH type-2.
+At position 85 to 161, the domain is characterized as RRM.
+At position 69 to 422, the domain is characterized as IF rod.
+At position 455 to 572, the domain is characterized as LTD.
+At position 1301 to 1611, the domain is characterized as PKS/mFAS DH.
+At position 1700 to 1777, the domain is characterized as Carrier.
+At position 34 to 113, the domain is characterized as Death.
+At position 162 to 296, the domain is characterized as TIR.
+At position 645 to 821, the domain is characterized as PCI.
+At position 521 to 575, the domain is characterized as LRRCT.
+At position 412 to 438, the domain is characterized as PLD phosphodiesterase 2.
+At position 6 to 61, the domain is characterized as SANT.
+At position 276 to 589, the domain is characterized as Protein kinase.
+At position 30 to 110, the domain is characterized as GS beta-grasp.
+At position 117 to 367, the domain is characterized as GS catalytic.
+At position 288 to 347, the domain is characterized as LIM zinc-binding.
+At position 23 to 214, the domain is characterized as RNase H type-2.
+At position 167 to 361, the domain is characterized as Helicase ATP-binding.
+At position 396 to 588, the domain is characterized as Helicase C-terminal.
+At position 252 to 498, the domain is characterized as ABC transporter 2.
+At position 205 to 449, the domain is characterized as PABS.
+At position 349 to 555, the domain is characterized as MCM.
+At position 5 to 67, the domain is characterized as S4 RNA-binding.
+At position 23 to 166, the domain is characterized as VHS.
+At position 271 to 290, the domain is characterized as UIM 1.
+At position 313 to 332, the domain is characterized as UIM 2.
+At position 380 to 495, the domain is characterized as C2.
+At position 521 to 624, the domain is characterized as PH.
+At position 931 to 1111, the domain is characterized as MHD1.
+At position 22 to 74, the domain is characterized as Tudor-knot.
+At position 179 to 451, the domain is characterized as MYST-type HAT.
+At position 19 to 76, the domain is characterized as 4Fe-4S Wbl-type.
+At position 25 to 73, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 685 to 972, the domain is characterized as Protein kinase.
+At position 133 to 311, the domain is characterized as Helicase ATP-binding.
+At position 830 to 1101, the domain is characterized as PI3K/PI4K catalytic.
+At position 77 to 266, the domain is characterized as Thioredoxin.
+At position 136 to 198, the domain is characterized as t-SNARE coiled-coil homology.
+At position 93 to 121, the domain is characterized as IQ 1.
+At position 122 to 144, the domain is characterized as IQ 2.
+At position 8 to 289, the domain is characterized as tr-type G.
+At position 93 to 290, the domain is characterized as ABC transmembrane type-1.
+At position 39 to 400, the domain is characterized as GBD/FH3.
+At position 2 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 11 to 265, the domain is characterized as Protein kinase.
+At position 656 to 705, the domain is characterized as KA1.
+At position 110 to 244, the domain is characterized as C1q.
+At position 153 to 222, the domain is characterized as DRBM.
+At position 7 to 280, the domain is characterized as DegV.
+At position 370 to 801, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1293 to 1600, the domain is characterized as PKS/mFAS DH.
+At position 1653 to 1730, the domain is characterized as Carrier.
+At position 51 to 485, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1019 to 1344, the domain is characterized as PKS/mFAS DH.
+At position 2490 to 2568, the domain is characterized as Carrier.
+At position 131 to 312, the domain is characterized as CP-type G.
+At position 79 to 320, the domain is characterized as ABC transporter.
+At position 3 to 73, the domain is characterized as PAS 1.
+At position 77 to 116, the domain is characterized as PAC 1.
+At position 140 to 214, the domain is characterized as PAS 2.
+At position 218 to 255, the domain is characterized as PAC 2.
+At position 265 to 335, the domain is characterized as PAS 3.
+At position 402 to 606, the domain is characterized as Histidine kinase.
+At position 89 to 153, the domain is characterized as SEP.
+At position 8 to 124, the domain is characterized as SET.
+At position 655 to 736, the domain is characterized as S1 motif.
+At position 534 to 644, the domain is characterized as SMC hinge.
+At position 63 to 253, the domain is characterized as KARI N-terminal Rossmann.
+At position 254 to 401, the domain is characterized as KARI C-terminal knotted.
+At position 85 to 119, the domain is characterized as SAP.
+At position 90 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 125 to 240, the domain is characterized as Integrase catalytic.
+At position 465 to 657, the domain is characterized as DH.
+At position 692 to 855, the domain is characterized as PH.
+At position 930 to 1239, the domain is characterized as CNH.
+At position 125 to 168, the domain is characterized as EGF-like 2.
+At position 241 to 473, the domain is characterized as Peptidase S1.
+At position 80 to 175, the domain is characterized as Fibronectin type-III 1.
+At position 179 to 267, the domain is characterized as Ig-like C2-type 1.
+At position 276 to 371, the domain is characterized as Fibronectin type-III 2.
+At position 389 to 479, the domain is characterized as Ig-like C2-type 2.
+At position 58 to 154, the domain is characterized as Plastocyanin-like.
+At position 450 to 500, the domain is characterized as DHHC.
+At position 478 to 548, the domain is characterized as SUI1.
+At position 2 to 154, the domain is characterized as PPIase cyclophilin-type.
+At position 2507 to 2584, the domain is characterized as Carrier.
+At position 48 to 304, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 20 to 91, the domain is characterized as GRAM.
+At position 164 to 543, the domain is characterized as Myotubularin phosphatase.
+At position 30 to 209, the domain is characterized as SIS.
+At position 2 to 110, the domain is characterized as MTTase N-terminal.
+At position 130 to 355, the domain is characterized as Radical SAM core.
+At position 37 to 467, the domain is characterized as uDENN FNIP1/2-type.
+At position 475 to 1083, the domain is characterized as cDENN FNIP1/2-type.
+At position 1093 to 1148, the domain is characterized as dDENN FNIP1/2-type.
+At position 25 to 183, the domain is characterized as Tyrosine-protein phosphatase.
+At position 110 to 258, the domain is characterized as PPC.
+At position 281 to 563, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 222, the domain is characterized as ABC transporter.
+At position 222 to 383, the domain is characterized as TrmE-type G.
+At position 14 to 249, the domain is characterized as BAR.
+At position 255 to 445, the domain is characterized as Rho-GAP.
+At position 343 to 386, the domain is characterized as LysM.
+At position 124 to 241, the domain is characterized as EamA.
+At position 1 to 162, the domain is characterized as Obg.
+At position 163 to 335, the domain is characterized as OBG-type G.
+At position 90 to 207, the domain is characterized as C-type lectin.
+At position 1 to 83, the domain is characterized as ELM2.
+At position 84 to 135, the domain is characterized as SANT 1.
+At position 285 to 336, the domain is characterized as SANT 2.
+At position 263 to 312, the domain is characterized as GYF.
+At position 1266 to 1383, the domain is characterized as SET.
+At position 37 to 151, the domain is characterized as Calponin-homology (CH).
+At position 240 to 437, the domain is characterized as DH.
+At position 470 to 598, the domain is characterized as PH.
+At position 688 to 750, the domain is characterized as SH3 1.
+At position 831 to 925, the domain is characterized as SH2.
+At position 926 to 991, the domain is characterized as SH3 2.
+At position 110 to 425, the domain is characterized as Peptidase A1.
+At position 1 to 158, the domain is characterized as Thioredoxin.
+At position 1 to 105, the domain is characterized as Reverse transcriptase.
+At position 30 to 89, the domain is characterized as LIM zinc-binding 1.
+At position 94 to 153, the domain is characterized as LIM zinc-binding 2.
+At position 19 to 272, the domain is characterized as Protein kinase.
+At position 459 to 739, the domain is characterized as Protein kinase.
+At position 137 to 377, the domain is characterized as GT92.
+At position 58 to 252, the domain is characterized as TNase-like.
+At position 3 to 147, the domain is characterized as Flavodoxin-like.
+At position 226 to 465, the domain is characterized as FAD-binding FR-type.
+At position 278 to 314, the domain is characterized as DFDF.
+At position 307 to 462, the domain is characterized as MATH.
+At position 6 to 154, the domain is characterized as Nudix hydrolase.
+At position 24 to 100, the domain is characterized as REM-1 1.
+At position 114 to 194, the domain is characterized as REM-1 2.
+At position 200 to 280, the domain is characterized as REM-1 3.
+At position 298 to 468, the domain is characterized as C2.
+At position 650 to 909, the domain is characterized as Protein kinase.
+At position 910 to 977, the domain is characterized as AGC-kinase C-terminal.
+At position 21 to 161, the domain is characterized as PLAT.
+At position 164 to 859, the domain is characterized as Lipoxygenase.
+At position 683 to 718, the domain is characterized as Anaphylatoxin-like.
+At position 1506 to 1649, the domain is characterized as NTR.
+At position 196 to 246, the domain is characterized as F-box.
+At position 109 to 161, the domain is characterized as FHA.
+At position 271 to 511, the domain is characterized as MHD.
+At position 742 to 771, the domain is characterized as IQ 1.
+At position 765 to 794, the domain is characterized as IQ 2.
+At position 1214 to 1312, the domain is characterized as PH 1.
+At position 1394 to 1499, the domain is characterized as PH 2.
+At position 1549 to 1697, the domain is characterized as MyTH4.
+At position 1702 to 2046, the domain is characterized as FERM.
+At position 121 to 341, the domain is characterized as Fibrinogen C-terminal.
+At position 88 to 483, the domain is characterized as FH2.
+At position 20 to 137, the domain is characterized as CUB 1.
+At position 138 to 181, the domain is characterized as EGF-like; calcium-binding.
+At position 184 to 296, the domain is characterized as CUB 2.
+At position 298 to 363, the domain is characterized as Sushi 1.
+At position 364 to 431, the domain is characterized as Sushi 2.
+At position 444 to 683, the domain is characterized as Peptidase S1.
+At position 391 to 809, the domain is characterized as PIPK.
+At position 64 to 292, the domain is characterized as Radical SAM core.
+At position 73 to 141, the domain is characterized as POTRA.
+At position 4 to 143, the domain is characterized as PTS EIIA type-2.
+At position 10 to 81, the domain is characterized as PAS 1.
+At position 134 to 207, the domain is characterized as PAS 2.
+At position 208 to 260, the domain is characterized as PAC.
+At position 402 to 532, the domain is characterized as GGDEF.
+At position 541 to 795, the domain is characterized as EAL.
+At position 238 to 312, the domain is characterized as PUA.
+At position 228 to 299, the domain is characterized as HARP 1.
+At position 331 to 402, the domain is characterized as HARP 2.
+At position 448 to 603, the domain is characterized as Helicase ATP-binding.
+At position 719 to 872, the domain is characterized as Helicase C-terminal.
+At position 203 to 241, the domain is characterized as LRRCT.
+At position 16 to 279, the domain is characterized as Deacetylase sirtuin-type.
+At position 196 to 301, the domain is characterized as Ig-like V-type.
+At position 302 to 399, the domain is characterized as Ig-like C1-type.
+At position 201 to 252, the domain is characterized as bHLH.
+At position 5 to 287, the domain is characterized as DegV.
+At position 268 to 369, the domain is characterized as Fibronectin type-III 1.
+At position 373 to 465, the domain is characterized as Fibronectin type-III 2.
+At position 469 to 562, the domain is characterized as Fibronectin type-III 3.
+At position 566 to 660, the domain is characterized as Fibronectin type-III 4.
+At position 664 to 757, the domain is characterized as Fibronectin type-III 5.
+At position 761 to 851, the domain is characterized as Fibronectin type-III 6.
+At position 861 to 950, the domain is characterized as Fibronectin type-III 7.
+At position 951 to 1045, the domain is characterized as Fibronectin type-III 8.
+At position 405 to 478, the domain is characterized as Disintegrin.
+At position 29 to 161, the domain is characterized as CBM6 1.
+At position 211 to 345, the domain is characterized as CBM6 2.
+At position 490 to 638, the domain is characterized as PA14.
+At position 662 to 793, the domain is characterized as CBM6 3.
+At position 642 to 818, the domain is characterized as PCI.
+At position 39 to 123, the domain is characterized as Rhodanese.
+At position 218 to 427, the domain is characterized as Peptidase M12B.
+At position 428 to 515, the domain is characterized as Disintegrin.
+At position 516 to 571, the domain is characterized as TSP type-1 1.
+At position 839 to 895, the domain is characterized as TSP type-1 2.
+At position 896 to 949, the domain is characterized as TSP type-1 3.
+At position 490 to 775, the domain is characterized as Protein kinase.
+At position 173 to 310, the domain is characterized as GGDEF.
+At position 110 to 161, the domain is characterized as bHLH.
+At position 707 to 760, the domain is characterized as Myb-like.
+At position 46 to 109, the domain is characterized as R3H.
+At position 212 to 298, the domain is characterized as Ig-like C1-type.
+At position 30 to 201, the domain is characterized as EngB-type G.
+At position 20 to 74, the domain is characterized as HTH cro/C1-type.
+At position 135 to 290, the domain is characterized as RNase NYN.
+At position 22 to 276, the domain is characterized as Protein kinase.
+At position 87 to 240, the domain is characterized as Ferritin-like diiron.
+At position 63 to 280, the domain is characterized as GH16.
+At position 84 to 175, the domain is characterized as GIY-YIG.
+At position 61 to 341, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 17 to 128, the domain is characterized as STAS.
+At position 324 to 498, the domain is characterized as Helicase ATP-binding.
+At position 528 to 707, the domain is characterized as Helicase C-terminal.
+At position 23 to 167, the domain is characterized as TNase-like 1.
+At position 195 to 333, the domain is characterized as TNase-like 2.
+At position 346 to 505, the domain is characterized as TNase-like 3.
+At position 535 to 674, the domain is characterized as TNase-like 4.
+At position 749 to 807, the domain is characterized as Tudor.
+At position 63 to 138, the domain is characterized as HTH CENPB-type.
+At position 5 to 131, the domain is characterized as VOC 1.
+At position 154 to 278, the domain is characterized as VOC 2.
+At position 5 to 280, the domain is characterized as DegV.
+At position 538 to 825, the domain is characterized as Protein kinase.
+At position 488 to 610, the domain is characterized as Ricin B-type lectin.
+At position 36 to 155, the domain is characterized as MARVEL.
+At position 186 to 415, the domain is characterized as Sigma-54 factor interaction.
+At position 482 to 887, the domain is characterized as USP.
+At position 939 to 1110, the domain is characterized as Exonuclease.
+At position 154 to 343, the domain is characterized as CheB-type methylesterase.
+At position 176 to 223, the domain is characterized as LRRCT.
+At position 229 to 327, the domain is characterized as Ig-like.
+At position 676 to 727, the domain is characterized as GPS.
+At position 295 to 414, the domain is characterized as VOC 1.
+At position 440 to 590, the domain is characterized as VOC 2.
+At position 31 to 169, the domain is characterized as C-type lectin.
+At position 241 to 281, the domain is characterized as EGF-like 1.
+At position 284 to 324, the domain is characterized as EGF-like 2.
+At position 325 to 363, the domain is characterized as EGF-like 3; calcium-binding.
+At position 365 to 405, the domain is characterized as EGF-like 4.
+At position 404 to 440, the domain is characterized as EGF-like 5.
+At position 441 to 481, the domain is characterized as EGF-like 6; calcium-binding.
+At position 9 to 121, the domain is characterized as HotDog ACOT-type.
+At position 33 to 116, the domain is characterized as Ig-like C2-type.
+At position 177 to 205, the domain is characterized as ITAM.
+At position 236 to 404, the domain is characterized as TLDc.
+At position 194 to 387, the domain is characterized as Helicase ATP-binding.
+At position 439 to 576, the domain is characterized as Helicase C-terminal.
+At position 229 to 299, the domain is characterized as HARP 1.
+At position 325 to 396, the domain is characterized as HARP 2.
+At position 442 to 597, the domain is characterized as Helicase ATP-binding.
+At position 708 to 864, the domain is characterized as Helicase C-terminal.
+At position 11 to 217, the domain is characterized as YjeF N-terminal.
+At position 77 to 239, the domain is characterized as CP-type G.
+At position 30 to 202, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 310, the domain is characterized as Protein kinase.
+At position 59 to 421, the domain is characterized as Peptidase S8.
+At position 456 to 622, the domain is characterized as P/Homo B.
+At position 15 to 118, the domain is characterized as PINc.
+At position 1 to 443, the domain is characterized as Biotin carboxylation.
+At position 18 to 109, the domain is characterized as PB1.
+At position 166 to 419, the domain is characterized as Protein kinase.
+At position 229 to 325, the domain is characterized as Fibronectin type-III 1.
+At position 531 to 630, the domain is characterized as Fibronectin type-III 2.
+At position 642 to 740, the domain is characterized as Fibronectin type-III 3.
+At position 1072 to 1334, the domain is characterized as Tyrosine-protein phosphatase.
+At position 593 to 771, the domain is characterized as Lon proteolytic.
+At position 18 to 101, the domain is characterized as Saposin B-type.
+At position 223 to 553, the domain is characterized as Kinesin motor.
+At position 86 to 168, the domain is characterized as PDZ 1.
+At position 210 to 293, the domain is characterized as PDZ 2.
+At position 862 to 934, the domain is characterized as PDZ 3.
+At position 267 to 471, the domain is characterized as Peptidase M12B.
+At position 480 to 560, the domain is characterized as Disintegrin.
+At position 561 to 617, the domain is characterized as TSP type-1 1.
+At position 855 to 913, the domain is characterized as TSP type-1 2.
+At position 915 to 975, the domain is characterized as TSP type-1 3.
+At position 976 to 1030, the domain is characterized as TSP type-1 4.
+At position 1060 to 1098, the domain is characterized as PLAC.
+At position 27 to 94, the domain is characterized as Importin N-terminal.
+At position 253 to 582, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 4 to 60, the domain is characterized as L27.
+At position 153 to 240, the domain is characterized as PDZ 1.
+At position 248 to 335, the domain is characterized as PDZ 2.
+At position 393 to 474, the domain is characterized as PDZ 3.
+At position 507 to 577, the domain is characterized as SH3.
+At position 610 to 786, the domain is characterized as Guanylate kinase-like.
+At position 86 to 97, the domain is characterized as EGF-like.
+At position 276 to 417, the domain is characterized as RanBD1.
+At position 11 to 358, the domain is characterized as Kinesin motor.
+At position 460 to 523, the domain is characterized as FHA.
+At position 61 to 103, the domain is characterized as CHCH.
+At position 157 to 412, the domain is characterized as Peptidase S1.
+At position 59 to 89, the domain is characterized as EF-hand 2.
+At position 162 to 191, the domain is characterized as EF-hand 5.
+At position 1 to 420, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 920 to 1235, the domain is characterized as PKS/mFAS DH.
+At position 2297 to 2375, the domain is characterized as Carrier.
+At position 245 to 494, the domain is characterized as CN hydrolase.
+At position 1 to 84, the domain is characterized as Carrier.
+At position 1 to 144, the domain is characterized as SPX.
+At position 9 to 67, the domain is characterized as TRAM.
+At position 517 to 632, the domain is characterized as Fibronectin type-III 1.
+At position 636 to 726, the domain is characterized as Fibronectin type-III 2.
+At position 756 to 861, the domain is characterized as Fibronectin type-III 3.
+At position 870 to 967, the domain is characterized as Fibronectin type-III 4.
+At position 1037 to 1308, the domain is characterized as Protein kinase.
+At position 175 to 245, the domain is characterized as EB1 C-terminal.
+At position 365 to 639, the domain is characterized as Protein kinase.
+At position 2 to 77, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 77 to 116, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 23 to 105, the domain is characterized as Chorismate mutase.
+At position 54 to 288, the domain is characterized as Radical SAM core.
+At position 241 to 432, the domain is characterized as B30.2/SPRY.
+At position 248 to 427, the domain is characterized as CRAL-TRIO.
+At position 18 to 219, the domain is characterized as Radical SAM core.
+At position 56 to 93, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 186 to 260, the domain is characterized as POU-specific.
+At position 472 to 563, the domain is characterized as RRM 1.
+At position 580 to 662, the domain is characterized as RRM 2.
+At position 45 to 110, the domain is characterized as SAM.
+At position 164 to 316, the domain is characterized as HD.
+At position 139 to 194, the domain is characterized as BRX 1.
+At position 289 to 344, the domain is characterized as BRX 2.
+At position 556 to 733, the domain is characterized as tr-type G.
+At position 346 to 382, the domain is characterized as CBM1.
+At position 2 to 59, the domain is characterized as PQ-loop.
+At position 63 to 271, the domain is characterized as TLDc.
+At position 883 to 1158, the domain is characterized as Protein kinase.
+At position 415 to 442, the domain is characterized as PLD phosphodiesterase 2.
+At position 356 to 464, the domain is characterized as PX.
+At position 1 to 226, the domain is characterized as PABS.
+At position 222 to 374, the domain is characterized as TrmE-type G.
+At position 133 to 248, the domain is characterized as C-type lectin.
+At position 198 to 466, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 44 to 243, the domain is characterized as TLC.
+At position 8 to 92, the domain is characterized as MtN3/slv 1.
+At position 131 to 213, the domain is characterized as MtN3/slv 2.
+At position 14 to 210, the domain is characterized as Cytochrome b561.
+At position 159 to 355, the domain is characterized as Peptidase M12B.
+At position 255 to 530, the domain is characterized as ABC transmembrane type-1 1.
+At position 564 to 791, the domain is characterized as ABC transporter 1.
+At position 852 to 1139, the domain is characterized as ABC transmembrane type-1 2.
+At position 1174 to 1407, the domain is characterized as ABC transporter 2.
+At position 601 to 702, the domain is characterized as BRCT.
+At position 65 to 372, the domain is characterized as GH18.
+At position 518 to 591, the domain is characterized as Biotinyl-binding.
+At position 32 to 114, the domain is characterized as PAS.
+At position 118 to 161, the domain is characterized as PAC.
+At position 195 to 241, the domain is characterized as F-box.
+At position 18 to 98, the domain is characterized as GS beta-grasp.
+At position 105 to 355, the domain is characterized as GS catalytic.
+At position 607 to 850, the domain is characterized as MIF4G.
+At position 11 to 91, the domain is characterized as GIY-YIG.
+At position 195 to 230, the domain is characterized as UVR.
+At position 144 to 238, the domain is characterized as Rhodanese.
+At position 259 to 318, the domain is characterized as Ubiquitin-like.
+At position 286 to 488, the domain is characterized as Pentraxin (PTX).
+At position 139 to 211, the domain is characterized as RBD.
+At position 442 to 702, the domain is characterized as Protein kinase.
+At position 84 to 777, the domain is characterized as Myosin motor.
+At position 90 to 160, the domain is characterized as BTB.
+At position 34 to 69, the domain is characterized as EF-hand 1.
+At position 56 to 204, the domain is characterized as Flavodoxin-like.
+At position 324 to 567, the domain is characterized as Radical SAM core.
+At position 612 to 677, the domain is characterized as KHA.
+At position 22 to 149, the domain is characterized as Bulb-type lectin.
+At position 293 to 346, the domain is characterized as EGF-like; atypical.
+At position 354 to 433, the domain is characterized as PAN.
+At position 523 to 797, the domain is characterized as Protein kinase.
+At position 60 to 349, the domain is characterized as Protein kinase.
+At position 19 to 238, the domain is characterized as ABC transporter.
+At position 339 to 496, the domain is characterized as SSD.
+At position 1 to 65, the domain is characterized as SAM.
+At position 232 to 396, the domain is characterized as TrmE-type G.
+At position 30 to 118, the domain is characterized as Plastocyanin-like.
+At position 487 to 674, the domain is characterized as Rab-GAP TBC.
+At position 858 to 893, the domain is characterized as EF-hand.
+At position 262 to 459, the domain is characterized as GATase cobBQ-type.
+At position 39 to 159, the domain is characterized as Thioredoxin.
+At position 524 to 559, the domain is characterized as EF-hand 2.
+At position 756 to 791, the domain is characterized as EF-hand 4.
+At position 792 to 827, the domain is characterized as EF-hand 5.
+At position 864 to 899, the domain is characterized as EF-hand 6.
+At position 112 to 176, the domain is characterized as J.
+At position 427 to 560, the domain is characterized as SHD.
+At position 568 to 878, the domain is characterized as MHD.
+At position 86 to 208, the domain is characterized as FAD-binding FR-type.
+At position 40 to 117, the domain is characterized as GST N-terminal.
+At position 119 to 241, the domain is characterized as GST C-terminal.
+At position 1862 to 1925, the domain is characterized as SAM.
+At position 1017 to 1237, the domain is characterized as Alpha-type protein kinase.
+At position 476 to 644, the domain is characterized as Integrase catalytic.
+At position 35 to 208, the domain is characterized as Laminin G-like 1.
+At position 215 to 381, the domain is characterized as Laminin G-like 2.
+At position 91 to 161, the domain is characterized as MEIS N-terminal.
+At position 53 to 98, the domain is characterized as LysM 1.
+At position 113 to 160, the domain is characterized as LysM 2.
+At position 179 to 227, the domain is characterized as LysM 3.
+At position 330 to 612, the domain is characterized as Protein kinase.
+At position 2 to 225, the domain is characterized as Glutamine amidotransferase type-2.
+At position 297 to 436, the domain is characterized as SIS 1.
+At position 469 to 614, the domain is characterized as SIS 2.
+At position 131 to 387, the domain is characterized as Olfactomedin-like.
+At position 1 to 33, the domain is characterized as Peptidase M12B.
+At position 27 to 57, the domain is characterized as LRRNT.
+At position 260 to 311, the domain is characterized as LRRCT.
+At position 61 to 200, the domain is characterized as MPN.
+At position 26 to 147, the domain is characterized as FZ.
+At position 286 to 332, the domain is characterized as RPE1 insert.
+At position 27 to 100, the domain is characterized as CSD.
+At position 124 to 290, the domain is characterized as Laminin G-like 1.
+At position 444 to 481, the domain is characterized as EGF-like 1.
+At position 695 to 863, the domain is characterized as Laminin G-like 2.
+At position 859 to 896, the domain is characterized as EGF-like 2.
+At position 62 to 173, the domain is characterized as AB hydrolase-1.
+At position 3 to 124, the domain is characterized as MAGE.
+At position 126 to 297, the domain is characterized as Helicase ATP-binding.
+At position 307 to 467, the domain is characterized as Helicase C-terminal.
+At position 61 to 161, the domain is characterized as Rieske.
+At position 1238 to 1507, the domain is characterized as Protein kinase.
+At position 365 to 431, the domain is characterized as PASTA 1.
+At position 432 to 500, the domain is characterized as PASTA 2.
+At position 501 to 565, the domain is characterized as PASTA 3.
+At position 570 to 638, the domain is characterized as PASTA 4.
+At position 63 to 114, the domain is characterized as AWS.
+At position 116 to 233, the domain is characterized as SET.
+At position 239 to 255, the domain is characterized as Post-SET.
+At position 197 to 900, the domain is characterized as USP.
+At position 25 to 110, the domain is characterized as PDZ.
+At position 928 to 1030, the domain is characterized as ASD1.
+At position 1669 to 1957, the domain is characterized as ASD2.
+At position 27 to 76, the domain is characterized as bHLH.
+At position 106 to 166, the domain is characterized as LIM zinc-binding 2.
+At position 26 to 130, the domain is characterized as Phytocyanin.
+At position 355 to 451, the domain is characterized as Rhodanese.
+At position 58 to 212, the domain is characterized as UBC core.
+At position 11 to 190, the domain is characterized as Guanylate kinase-like.
+At position 119 to 339, the domain is characterized as Radical SAM core.
+At position 655 to 857, the domain is characterized as FtsK 1.
+At position 1001 to 1188, the domain is characterized as FtsK 2.
+At position 280 to 359, the domain is characterized as PB1.
+At position 287 to 362, the domain is characterized as B5.
+At position 399 to 469, the domain is characterized as ACT.
+At position 3 to 161, the domain is characterized as DHFR.
+At position 13 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 210 to 414, the domain is characterized as GMPS ATP-PPase.
+At position 235 to 401, the domain is characterized as CYTH.
+At position 171 to 229, the domain is characterized as FHA.
+At position 287 to 376, the domain is characterized as Ig-like.
+At position 415 to 510, the domain is characterized as Fibronectin type-III.
+At position 192 to 279, the domain is characterized as TonB C-terminal.
+At position 11 to 73, the domain is characterized as HTH deoR-type.
+At position 112 to 172, the domain is characterized as KH.
+At position 238 to 331, the domain is characterized as HD.
+At position 24 to 360, the domain is characterized as TROVE.
+At position 244 to 274, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 292 to 321, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 581 to 610, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 611 to 640, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 300 to 468, the domain is characterized as tr-type G.
+At position 633 to 712, the domain is characterized as BRCT.
+At position 46 to 242, the domain is characterized as tr-type G.
+At position 92 to 423, the domain is characterized as Asparaginase/glutaminase.
+At position 1 to 31, the domain is characterized as CARD.
+At position 46 to 50, the domain is characterized as NB-ARC.
+At position 42 to 259, the domain is characterized as Rab-GAP TBC.
+At position 337 to 549, the domain is characterized as TLDc.
+At position 103 to 292, the domain is characterized as ABC transmembrane type-1.
+At position 187 to 401, the domain is characterized as Galectin.
+At position 106 to 361, the domain is characterized as Protein kinase.
+At position 40 to 152, the domain is characterized as GOLD.
+At position 1 to 436, the domain is characterized as SMP-LTD.
+At position 411 to 845, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1338 to 1648, the domain is characterized as PKS/mFAS DH.
+At position 1732 to 1806, the domain is characterized as Carrier.
+At position 18 to 122, the domain is characterized as Ig-like V-type.
+At position 46 to 150, the domain is characterized as Cadherin 1.
+At position 151 to 259, the domain is characterized as Cadherin 2.
+At position 260 to 374, the domain is characterized as Cadherin 3.
+At position 375 to 479, the domain is characterized as Cadherin 4.
+At position 479 to 592, the domain is characterized as Cadherin 5.
+At position 17 to 218, the domain is characterized as PNPLA.
+At position 63 to 320, the domain is characterized as Protein kinase.
+At position 54 to 239, the domain is characterized as GH11.
+At position 248 to 340, the domain is characterized as CBM2.
+At position 1 to 136, the domain is characterized as N-acetyltransferase.
+At position 402 to 571, the domain is characterized as tr-type G.
+At position 4 to 46, the domain is characterized as SpoVT-AbrB 1.
+At position 728 to 1021, the domain is characterized as Protein kinase.
+At position 50 to 132, the domain is characterized as SCAN box.
+At position 86 to 192, the domain is characterized as HTH APSES-type.
+At position 41 to 170, the domain is characterized as N-terminal Ras-GEF.
+At position 214 to 461, the domain is characterized as Ras-GEF.
+At position 145 to 354, the domain is characterized as ATP-grasp.
+At position 171 to 479, the domain is characterized as USP.
+At position 71 to 384, the domain is characterized as Peptidase A1.
+At position 8 to 275, the domain is characterized as tr-type G.
+At position 169 to 415, the domain is characterized as Fibrinogen C-terminal.
+At position 350 to 457, the domain is characterized as Rhodanese.
+At position 416 to 517, the domain is characterized as CBM2.
+At position 33 to 148, the domain is characterized as AA1-like.
+At position 24 to 107, the domain is characterized as Lipoyl-binding.
+At position 3 to 194, the domain is characterized as Prephenate dehydratase.
+At position 208 to 285, the domain is characterized as ACT.
+At position 147 to 459, the domain is characterized as Reverse transcriptase.
+At position 6 to 48, the domain is characterized as CHCH.
+At position 254 to 273, the domain is characterized as UIM 1.
+At position 292 to 311, the domain is characterized as UIM 2.
+At position 226 to 305, the domain is characterized as KRAB.
+At position 37 to 102, the domain is characterized as SAM.
+At position 155 to 307, the domain is characterized as HD.
+At position 55 to 312, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 262 to 437, the domain is characterized as Helicase ATP-binding.
+At position 119 to 197, the domain is characterized as RRM 2.
+At position 55 to 340, the domain is characterized as Protein kinase.
+At position 132 to 385, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 21 to 76, the domain is characterized as Kazal-like.
+At position 32 to 146, the domain is characterized as CUB 1.
+At position 37 to 461, the domain is characterized as Sema.
+At position 463 to 515, the domain is characterized as PSI 1.
+At position 609 to 671, the domain is characterized as PSI 2.
+At position 776 to 822, the domain is characterized as PSI 3.
+At position 823 to 914, the domain is characterized as IPT/TIG 1.
+At position 915 to 1001, the domain is characterized as IPT/TIG 2.
+At position 1003 to 1134, the domain is characterized as IPT/TIG 3.
+At position 1154 to 1221, the domain is characterized as IPT/TIG 4.
+At position 11 to 123, the domain is characterized as FAD-binding FR-type.
+At position 204 to 379, the domain is characterized as EngA-type G 2.
+At position 544 to 622, the domain is characterized as IPT/TIG.
+At position 1054 to 1083, the domain is characterized as IQ 1.
+At position 1107 to 1136, the domain is characterized as IQ 2.
+At position 35 to 129, the domain is characterized as SH2.
+At position 164 to 259, the domain is characterized as PH.
+At position 2 to 130, the domain is characterized as RCK N-terminal 1.
+At position 142 to 226, the domain is characterized as RCK C-terminal 1.
+At position 233 to 353, the domain is characterized as RCK N-terminal 2.
+At position 367 to 452, the domain is characterized as RCK C-terminal 2.
+At position 262 to 571, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 386 to 476, the domain is characterized as IPT/TIG.
+At position 599 to 854, the domain is characterized as Protein kinase.
+At position 19 to 136, the domain is characterized as Response regulatory.
+At position 162 to 356, the domain is characterized as CheB-type methylesterase.
+At position 120 to 292, the domain is characterized as Helicase ATP-binding.
+At position 361 to 515, the domain is characterized as Helicase C-terminal.
+At position 761 to 843, the domain is characterized as DIX.
+At position 25 to 130, the domain is characterized as WAC.
+At position 603 to 667, the domain is characterized as DDT.
+At position 1383 to 1453, the domain is characterized as Bromo.
+At position 234 to 419, the domain is characterized as FAD-binding PCMH-type.
+At position 639 to 815, the domain is characterized as PCI.
+At position 27 to 226, the domain is characterized as RNase H type-2.
+At position 1023 to 1296, the domain is characterized as Autotransporter.
+At position 124 to 230, the domain is characterized as HTH APSES-type.
+At position 600 to 1008, the domain is characterized as FH2.
+At position 1026 to 1057, the domain is characterized as DAD.
+At position 473 to 534, the domain is characterized as MIR 1.
+At position 545 to 602, the domain is characterized as MIR 2.
+At position 608 to 664, the domain is characterized as MIR 3.
+At position 604 to 686, the domain is characterized as BRCT.
+At position 120 to 206, the domain is characterized as PPIase FKBP-type.
+At position 25 to 143, the domain is characterized as Rhodanese.
+At position 176 to 317, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 327, the domain is characterized as 5'-3' exonuclease.
+At position 328 to 520, the domain is characterized as 3'-5' exonuclease.
+At position 282 to 350, the domain is characterized as SH3b.
+At position 240 to 456, the domain is characterized as Histidine kinase.
+At position 1 to 174, the domain is characterized as N-acetyltransferase.
+At position 5 to 245, the domain is characterized as Radical SAM core.
+At position 36 to 174, the domain is characterized as Thioredoxin.
+At position 1239 to 1403, the domain is characterized as PNPLA.
+At position 7 to 112, the domain is characterized as Calponin-homology (CH).
+At position 60 to 138, the domain is characterized as RRM.
+At position 124 to 313, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 52, the domain is characterized as F-box.
+At position 155 to 444, the domain is characterized as Lon N-terminal.
+At position 895 to 1082, the domain is characterized as Lon proteolytic.
+At position 5 to 37, the domain is characterized as LisH.
+At position 51 to 210, the domain is characterized as Helicase ATP-binding.
+At position 261 to 440, the domain is characterized as PCI.
+At position 362 to 413, the domain is characterized as bHLH.
+At position 10 to 195, the domain is characterized as Ku.
+At position 409 to 495, the domain is characterized as PPIase FKBP-type.
+At position 6 to 241, the domain is characterized as PABS.
+At position 33 to 214, the domain is characterized as FAD-binding PCMH-type.
+At position 51 to 336, the domain is characterized as FIIND.
+At position 336 to 426, the domain is characterized as CARD.
+At position 87 to 220, the domain is characterized as Rhodanese.
+At position 13 to 139, the domain is characterized as C-type lectin.
+At position 728 to 815, the domain is characterized as PDZ 1.
+At position 862 to 950, the domain is characterized as PDZ 2.
+At position 1004 to 1093, the domain is characterized as PDZ 3.
+At position 1100 to 1194, the domain is characterized as PDZ 4.
+At position 603 to 796, the domain is characterized as Helicase ATP-binding.
+At position 934 to 1087, the domain is characterized as Helicase C-terminal.
+At position 1 to 196, the domain is characterized as SMP-LTD.
+At position 12 to 150, the domain is characterized as MPN.
+At position 29 to 286, the domain is characterized as Protein kinase.
+At position 39 to 154, the domain is characterized as sHSP.
+At position 39 to 129, the domain is characterized as Link.
+At position 51 to 276, the domain is characterized as Cache.
+At position 373 to 609, the domain is characterized as Methyl-accepting transducer.
+At position 16 to 94, the domain is characterized as RRM.
+At position 86 to 176, the domain is characterized as Inhibitor I9.
+At position 186 to 467, the domain is characterized as Peptidase S8.
+At position 293 to 430, the domain is characterized as Helicase C-terminal.
+At position 447 to 721, the domain is characterized as Protein kinase.
+At position 68 to 410, the domain is characterized as Calpain catalytic.
+At position 638 to 672, the domain is characterized as EF-hand 1.
+At position 681 to 714, the domain is characterized as EF-hand 2.
+At position 711 to 746, the domain is characterized as EF-hand 3.
+At position 776 to 810, the domain is characterized as EF-hand 4.
+At position 543 to 720, the domain is characterized as W2.
+At position 246 to 451, the domain is characterized as Histidine kinase.
+At position 7 to 123, the domain is characterized as MATH.
+At position 147 to 206, the domain is characterized as BTB.
+At position 314 to 594, the domain is characterized as Protein kinase.
+At position 1 to 197, the domain is characterized as GH11.
+At position 49 to 110, the domain is characterized as Chitin-binding type R&R.
+At position 264 to 482, the domain is characterized as Radical SAM core.
+At position 1 to 101, the domain is characterized as PX.
+At position 202 to 261, the domain is characterized as SH3 2.
+At position 571 to 653, the domain is characterized as BRCT.
+At position 47 to 305, the domain is characterized as Protein kinase.
+At position 348 to 383, the domain is characterized as EF-hand 1.
+At position 384 to 419, the domain is characterized as EF-hand 2.
+At position 420 to 455, the domain is characterized as EF-hand 3.
+At position 458 to 489, the domain is characterized as EF-hand 4.
+At position 8 to 109, the domain is characterized as LOB.
+At position 37 to 128, the domain is characterized as UPAR/Ly6.
+At position 25 to 117, the domain is characterized as Ig-like C2-type.
+At position 125 to 230, the domain is characterized as Fibronectin type-III 1.
+At position 233 to 332, the domain is characterized as Fibronectin type-III 2.
+At position 334 to 430, the domain is characterized as Fibronectin type-III 3.
+At position 431 to 528, the domain is characterized as Fibronectin type-III 4.
+At position 530 to 623, the domain is characterized as Fibronectin type-III 5.
+At position 126 to 385, the domain is characterized as Protein kinase.
+At position 388 to 448, the domain is characterized as SH3.
+At position 958 to 998, the domain is characterized as UBA.
+At position 248 to 563, the domain is characterized as NR LBD.
+At position 24 to 243, the domain is characterized as tr-type G.
+At position 13 to 302, the domain is characterized as Protein kinase.
+At position 33 to 152, the domain is characterized as FZ.
+At position 10 to 211, the domain is characterized as YjeF N-terminal.
+At position 221 to 488, the domain is characterized as YjeF C-terminal.
+At position 3 to 311, the domain is characterized as SAM-dependent MTase C5-type.
+At position 635 to 716, the domain is characterized as RWP-RK.
+At position 862 to 945, the domain is characterized as PB1.
+At position 109 to 171, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 356 to 418, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 624 to 659, the domain is characterized as EF-hand 1.
+At position 660 to 695, the domain is characterized as EF-hand 2.
+At position 44 to 322, the domain is characterized as tr-type G.
+At position 98 to 372, the domain is characterized as MYST-type HAT.
+At position 6 to 104, the domain is characterized as CARD 1.
+At position 106 to 200, the domain is characterized as CARD 2.
+At position 273 to 600, the domain is characterized as NACHT.
+At position 506 to 819, the domain is characterized as CNH.
+At position 26 to 97, the domain is characterized as PAS 1.
+At position 98 to 153, the domain is characterized as PAC 1.
+At position 249 to 320, the domain is characterized as PAS 2.
+At position 320 to 376, the domain is characterized as PAC 2.
+At position 433 to 599, the domain is characterized as Helicase C-terminal.
+At position 3 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 103 to 214, the domain is characterized as DOMON.
+At position 122 to 395, the domain is characterized as Septin-type G.
+At position 170 to 578, the domain is characterized as Protein kinase.
+At position 55 to 366, the domain is characterized as IF rod.
+At position 106 to 206, the domain is characterized as Fibronectin type-III.
+At position 231 to 375, the domain is characterized as FCP1 homology.
+At position 12 to 106, the domain is characterized as HTH hxlR-type.
+At position 25 to 319, the domain is characterized as Protein kinase.
+At position 71 to 220, the domain is characterized as GAF 1.
+At position 252 to 429, the domain is characterized as GAF 2.
+At position 401 to 826, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1339 to 1651, the domain is characterized as PKS/mFAS DH.
+At position 1723 to 1797, the domain is characterized as Carrier.
+At position 196 to 240, the domain is characterized as DSL.
+At position 241 to 274, the domain is characterized as EGF-like 1.
+At position 275 to 305, the domain is characterized as EGF-like 2; atypical.
+At position 307 to 345, the domain is characterized as EGF-like 3.
+At position 347 to 383, the domain is characterized as EGF-like 4.
+At position 385 to 421, the domain is characterized as EGF-like 5; calcium-binding.
+At position 423 to 459, the domain is characterized as EGF-like 6; calcium-binding.
+At position 461 to 496, the domain is characterized as EGF-like 7; calcium-binding.
+At position 498 to 534, the domain is characterized as EGF-like 8.
+At position 536 to 572, the domain is characterized as EGF-like 9.
+At position 574 to 634, the domain is characterized as EGF-like 10; atypical.
+At position 636 to 672, the domain is characterized as EGF-like 11; calcium-binding.
+At position 674 to 710, the domain is characterized as EGF-like 12; calcium-binding.
+At position 712 to 748, the domain is characterized as EGF-like 13.
+At position 751 to 787, the domain is characterized as EGF-like 14.
+At position 789 to 825, the domain is characterized as EGF-like 15; calcium-binding.
+At position 827 to 863, the domain is characterized as EGF-like 16; calcium-binding.
+At position 870 to 944, the domain is characterized as VWFC.
+At position 159 to 332, the domain is characterized as OBG-type G.
+At position 14 to 76, the domain is characterized as t-SNARE coiled-coil homology.
+At position 14 to 76, the domain is characterized as TRAM.
+At position 26 to 129, the domain is characterized as Gnk2-homologous 1.
+At position 135 to 244, the domain is characterized as Gnk2-homologous 2.
+At position 53 to 141, the domain is characterized as BTB.
+At position 64 to 182, the domain is characterized as PINc.
+At position 29 to 319, the domain is characterized as Protein kinase.
+At position 484 to 671, the domain is characterized as DH.
+At position 11 to 75, the domain is characterized as Carrier.
+At position 353 to 439, the domain is characterized as KH-like.
+At position 65 to 164, the domain is characterized as AB hydrolase-1.
+At position 41 to 102, the domain is characterized as Ig-like C2-type 1.
+At position 127 to 195, the domain is characterized as Ig-like C2-type 2.
+At position 232 to 299, the domain is characterized as Ig-like C2-type 3.
+At position 327 to 381, the domain is characterized as Ig-like C2-type 4.
+At position 415 to 468, the domain is characterized as Ig-like C2-type 5.
+At position 297 to 594, the domain is characterized as ABC transmembrane type-1 1.
+At position 668 to 908, the domain is characterized as ABC transporter 1.
+At position 990 to 1270, the domain is characterized as ABC transmembrane type-1 2.
+At position 1308 to 1542, the domain is characterized as ABC transporter 2.
+At position 379 to 524, the domain is characterized as N-acetyltransferase.
+At position 360 to 683, the domain is characterized as Transferrin-like 2.
+At position 22 to 120, the domain is characterized as Phytocyanin.
+At position 26 to 91, the domain is characterized as J.
+At position 17 to 180, the domain is characterized as FAD-binding PCMH-type.
+At position 165 to 276, the domain is characterized as STAS.
+At position 41 to 110, the domain is characterized as Chitin-binding type R&R.
+At position 698 to 873, the domain is characterized as Integrase catalytic.
+At position 1376 to 1514, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1648 to 1790, the domain is characterized as RNase H Ty1/copia-type.
+At position 191 to 244, the domain is characterized as AWS.
+At position 246 to 363, the domain is characterized as SET.
+At position 370 to 386, the domain is characterized as Post-SET.
+At position 45 to 182, the domain is characterized as 6-Cys 1.
+At position 294 to 426, the domain is characterized as 6-Cys 2.
+At position 24 to 102, the domain is characterized as LCN-type CS-alpha/beta.
+At position 618 to 727, the domain is characterized as PH.
+At position 139 to 207, the domain is characterized as DRBM 2.
+At position 273 to 341, the domain is characterized as DRBM 3.
+At position 24 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 225 to 314, the domain is characterized as Ig-like C2-type 2.
+At position 323 to 408, the domain is characterized as Ig-like C2-type 3.
+At position 29 to 78, the domain is characterized as Clip.
+At position 144 to 389, the domain is characterized as Peptidase S1.
+At position 661 to 980, the domain is characterized as Autotransporter.
+At position 181 to 221, the domain is characterized as UBA.
+At position 633 to 696, the domain is characterized as J.
+At position 11 to 79, the domain is characterized as HTH merR-type.
+At position 69 to 101, the domain is characterized as LisH.
+At position 23 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 210, the domain is characterized as Ig-like C2-type 2.
+At position 301 to 399, the domain is characterized as Ig-like C2-type 4.
+At position 404 to 489, the domain is characterized as Ig-like C2-type 5.
+At position 495 to 578, the domain is characterized as Ig-like C2-type 6.
+At position 570 to 672, the domain is characterized as Ig-like C2-type 7.
+At position 788 to 1058, the domain is characterized as Protein kinase; inactive.
+At position 20 to 120, the domain is characterized as Ig-like 1.
+At position 126 to 221, the domain is characterized as Ig-like 2.
+At position 235 to 324, the domain is characterized as Ig-like 3.
+At position 331 to 426, the domain is characterized as Ig-like 4.
+At position 431 to 576, the domain is characterized as Ig-like 5.
+At position 581 to 685, the domain is characterized as Ig-like 6.
+At position 782 to 866, the domain is characterized as Ig-like 7.
+At position 872 to 965, the domain is characterized as Ig-like 8.
+At position 976 to 1066, the domain is characterized as Fibronectin type-III.
+At position 52 to 166, the domain is characterized as EamA 1.
+At position 178 to 306, the domain is characterized as EamA 2.
+At position 697 to 757, the domain is characterized as RAP.
+At position 350 to 685, the domain is characterized as F5/8 type A 2.
+At position 823 to 1143, the domain is characterized as F5/8 type A 3.
+At position 1000 to 1143, the domain is characterized as Plastocyanin-like 6.
+At position 24 to 105, the domain is characterized as GST N-terminal.
+At position 153 to 309, the domain is characterized as GST C-terminal.
+At position 19 to 108, the domain is characterized as CFEM.
+At position 5 to 87, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 16 to 137, the domain is characterized as CUB 1.
+At position 364 to 432, the domain is characterized as Sushi 2.
+At position 445 to 684, the domain is characterized as Peptidase S1.
+At position 591 to 689, the domain is characterized as tRNA-binding.
+At position 69 to 111, the domain is characterized as Collagen-like.
+At position 112 to 252, the domain is characterized as C1q.
+At position 10 to 132, the domain is characterized as C-type lectin.
+At position 81 to 468, the domain is characterized as Peptidase A1.
+At position 350 to 475, the domain is characterized as DBINO.
+At position 598 to 769, the domain is characterized as Helicase ATP-binding.
+At position 1210 to 1360, the domain is characterized as Helicase C-terminal.
+At position 21 to 473, the domain is characterized as Biotin carboxylation.
+At position 143 to 340, the domain is characterized as ATP-grasp.
+At position 559 to 826, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1099 to 1174, the domain is characterized as Biotinyl-binding.
+At position 6 to 197, the domain is characterized as GATase cobBQ-type.
+At position 98 to 252, the domain is characterized as NIDO.
+At position 260 to 314, the domain is characterized as VWFC.
+At position 320 to 500, the domain is characterized as VWFD 1.
+At position 597 to 650, the domain is characterized as TIL 1.
+At position 711 to 886, the domain is characterized as VWFD 2.
+At position 984 to 1036, the domain is characterized as TIL 2.
+At position 1098 to 1278, the domain is characterized as VWFD 3.
+At position 1372 to 1425, the domain is characterized as TIL 3.
+At position 1485 to 1666, the domain is characterized as VWFD 4.
+At position 1805 to 2059, the domain is characterized as ZP.
+At position 49 to 281, the domain is characterized as Radical SAM core.
+At position 122 to 185, the domain is characterized as bZIP.
+At position 26 to 135, the domain is characterized as Ig-like C2-type 1.
+At position 139 to 229, the domain is characterized as Ig-like C2-type 2.
+At position 234 to 326, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 416, the domain is characterized as Ig-like C2-type 4.
+At position 431 to 524, the domain is characterized as Fibronectin type-III 1.
+At position 530 to 620, the domain is characterized as Fibronectin type-III 2.
+At position 625 to 718, the domain is characterized as Fibronectin type-III 3.
+At position 728 to 821, the domain is characterized as Fibronectin type-III 4.
+At position 846 to 942, the domain is characterized as Fibronectin type-III 5.
+At position 947 to 1044, the domain is characterized as Fibronectin type-III 6.
+At position 609 to 638, the domain is characterized as IQ.
+At position 212 to 296, the domain is characterized as KRAB.
+At position 28 to 159, the domain is characterized as MPN.
+At position 182 to 308, the domain is characterized as Rhodanese.
+At position 519 to 879, the domain is characterized as USP.
+At position 15 to 713, the domain is characterized as Myosin motor.
+At position 716 to 745, the domain is characterized as IQ.
+At position 830 to 1023, the domain is characterized as TH1.
+At position 16 to 66, the domain is characterized as F-box.
+At position 20 to 54, the domain is characterized as WW 1.
+At position 124 to 154, the domain is characterized as WW 2.
+At position 421 to 498, the domain is characterized as BAG.
+At position 1437 to 1454, the domain is characterized as WH2.
+At position 114 to 347, the domain is characterized as Radical SAM core.
+At position 56 to 160, the domain is characterized as Cadherin 1.
+At position 385 to 489, the domain is characterized as Cadherin 4.
+At position 489 to 603, the domain is characterized as Cadherin 5.
+At position 147 to 315, the domain is characterized as JmjC.
+At position 985 to 1030, the domain is characterized as F-box.
+At position 31 to 699, the domain is characterized as PFL.
+At position 706 to 829, the domain is characterized as Glycine radical.
+At position 522 to 579, the domain is characterized as Chromo 1.
+At position 615 to 676, the domain is characterized as Chromo 2.
+At position 731 to 915, the domain is characterized as Helicase ATP-binding.
+At position 1047 to 1196, the domain is characterized as Helicase C-terminal.
+At position 26 to 115, the domain is characterized as PI3K-ABD.
+At position 194 to 285, the domain is characterized as PI3K-RBD.
+At position 327 to 496, the domain is characterized as C2 PI3K-type.
+At position 524 to 701, the domain is characterized as PIK helical.
+At position 772 to 1053, the domain is characterized as PI3K/PI4K catalytic.
+At position 370 to 417, the domain is characterized as FBD.
+At position 804 to 1035, the domain is characterized as ABC transporter 1.
+At position 1807 to 2039, the domain is characterized as ABC transporter 2.
+At position 18 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 49 to 111, the domain is characterized as KH 1.
+At position 124 to 189, the domain is characterized as KH 2.
+At position 316 to 379, the domain is characterized as KH 3.
+At position 2 to 183, the domain is characterized as KARI N-terminal Rossmann.
+At position 32 to 120, the domain is characterized as PPIase FKBP-type 1.
+At position 149 to 235, the domain is characterized as PPIase FKBP-type 2.
+At position 34 to 122, the domain is characterized as Link.
+At position 788 to 978, the domain is characterized as TH1.
+At position 1076 to 1137, the domain is characterized as SH3.
+At position 34 to 175, the domain is characterized as Thioredoxin.
+At position 117 to 252, the domain is characterized as BFN.
+At position 284 to 318, the domain is characterized as UVR.
+At position 4 to 57, the domain is characterized as Myosin N-terminal SH3-like.
+At position 70 to 774, the domain is characterized as Myosin motor.
+At position 778 to 798, the domain is characterized as IQ 1.
+At position 800 to 824, the domain is characterized as IQ 2.
+At position 825 to 847, the domain is characterized as IQ 3.
+At position 848 to 872, the domain is characterized as IQ 4.
+At position 873 to 895, the domain is characterized as IQ 5.
+At position 896 to 925, the domain is characterized as IQ 6.
+At position 1205 to 1480, the domain is characterized as Dilute.
+At position 1764 to 1862, the domain is characterized as Calx-beta 1.
+At position 1875 to 1985, the domain is characterized as Calx-beta 2.
+At position 2000 to 2106, the domain is characterized as Calx-beta 3.
+At position 20 to 139, the domain is characterized as Bulb-type lectin.
+At position 273 to 309, the domain is characterized as EGF-like.
+At position 328 to 410, the domain is characterized as PAN.
+At position 489 to 774, the domain is characterized as Protein kinase.
+At position 26 to 97, the domain is characterized as H15.
+At position 19 to 137, the domain is characterized as MARVEL.
+At position 47 to 152, the domain is characterized as Fibronectin type-III 1.
+At position 152 to 258, the domain is characterized as Fibronectin type-III 2.
+At position 259 to 359, the domain is characterized as Fibronectin type-III 3.
+At position 360 to 465, the domain is characterized as Fibronectin type-III 4.
+At position 469 to 565, the domain is characterized as Fibronectin type-III 5.
+At position 59 to 219, the domain is characterized as NAC.
+At position 120 to 187, the domain is characterized as PAS 1.
+At position 258 to 324, the domain is characterized as PAS 2.
+At position 333 to 376, the domain is characterized as PAC.
+At position 143 to 432, the domain is characterized as ABC transmembrane type-1.
+At position 57 to 166, the domain is characterized as HIT.
+At position 687 to 955, the domain is characterized as Autotransporter.
+At position 134 to 230, the domain is characterized as Ig-like V-type 2.
+At position 521 to 540, the domain is characterized as WH2.
+At position 214 to 508, the domain is characterized as NPH3.
+At position 27 to 90, the domain is characterized as S5 DRBM.
+At position 443 to 592, the domain is characterized as Thioredoxin.
+At position 126 to 216, the domain is characterized as Ig-like 2.
+At position 229 to 316, the domain is characterized as Ig-like 3.
+At position 321 to 405, the domain is characterized as Ig-like 4.
+At position 415 to 509, the domain is characterized as Fibronectin type-III 1.
+At position 511 to 607, the domain is characterized as Fibronectin type-III 2.
+At position 612 to 711, the domain is characterized as Fibronectin type-III 3.
+At position 718 to 811, the domain is characterized as Fibronectin type-III 4.
+At position 816 to 911, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 143, the domain is characterized as PTS EIIA type-2.
+At position 29 to 125, the domain is characterized as GOLD.
+At position 1068 to 1158, the domain is characterized as IPT/TIG 1.
+At position 1160 to 1247, the domain is characterized as IPT/TIG 2.
+At position 1250 to 1359, the domain is characterized as IPT/TIG 3.
+At position 214 to 528, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 96 to 328, the domain is characterized as Radical SAM core.
+At position 351 to 434, the domain is characterized as KH-like.
+At position 20 to 202, the domain is characterized as Eph LBD.
+At position 621 to 884, the domain is characterized as Protein kinase.
+At position 913 to 977, the domain is characterized as SAM.
+At position 23 to 326, the domain is characterized as Protein kinase.
+At position 30 to 161, the domain is characterized as Ephrin RBD.
+At position 18 to 267, the domain is characterized as ABC transporter.
+At position 23 to 104, the domain is characterized as Chorismate mutase.
+At position 162 to 232, the domain is characterized as PAS.
+At position 1494 to 1548, the domain is characterized as AWS.
+At position 1550 to 1667, the domain is characterized as SET.
+At position 1674 to 1690, the domain is characterized as Post-SET.
+At position 2389 to 2422, the domain is characterized as WW.
+At position 170 to 271, the domain is characterized as PpiC 1.
+At position 281 to 380, the domain is characterized as PpiC 2.
+At position 121 to 388, the domain is characterized as NR LBD.
+At position 26 to 172, the domain is characterized as FAS1 1.
+At position 187 to 327, the domain is characterized as FAS1 2.
+At position 1 to 110, the domain is characterized as Toprim.
+At position 29 to 108, the domain is characterized as Inhibitor I9.
+At position 112 to 621, the domain is characterized as Peptidase S8.
+At position 383 to 478, the domain is characterized as PA.
+At position 119 to 157, the domain is characterized as F-box.
+At position 328 to 374, the domain is characterized as F-box.
+At position 45 to 223, the domain is characterized as Helicase ATP-binding.
+At position 233 to 485, the domain is characterized as Helicase C-terminal.
+At position 37 to 103, the domain is characterized as HMA 1.
+At position 111 to 177, the domain is characterized as HMA 2.
+At position 186 to 252, the domain is characterized as HMA 3.
+At position 5 to 207, the domain is characterized as RNase H type-2.
+At position 115 to 308, the domain is characterized as Peptidase M12A.
+At position 303 to 343, the domain is characterized as EGF-like.
+At position 350 to 458, the domain is characterized as CUB.
+At position 576 to 627, the domain is characterized as TSP type-1.
+At position 4 to 109, the domain is characterized as FAD-binding FR-type.
+At position 233 to 321, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 355 to 445, the domain is characterized as IPT/TIG.
+At position 302 to 921, the domain is characterized as USP.
+At position 371 to 423, the domain is characterized as SOCS box.
+At position 192 to 255, the domain is characterized as CBS 1.
+At position 267 to 327, the domain is characterized as CBS 2.
+At position 40 to 128, the domain is characterized as PPIase FKBP-type.
+At position 327 to 362, the domain is characterized as DMA.
+At position 1086 to 1291, the domain is characterized as JmjC.
+At position 15 to 128, the domain is characterized as AB hydrolase-1.
+At position 3 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 14 to 76, the domain is characterized as HTH iclR-type.
+At position 89 to 253, the domain is characterized as IclR-ED.
+At position 352 to 489, the domain is characterized as NYN.
+At position 781 to 860, the domain is characterized as RRM.
+At position 865 to 939, the domain is characterized as HTH OST-type 1.
+At position 993 to 1069, the domain is characterized as HTH OST-type 2.
+At position 1089 to 1163, the domain is characterized as HTH OST-type 3.
+At position 1165 to 1241, the domain is characterized as HTH OST-type 4.
+At position 1249 to 1324, the domain is characterized as HTH OST-type 5.
+At position 1325 to 1400, the domain is characterized as HTH OST-type 6.
+At position 1401 to 1475, the domain is characterized as HTH OST-type 7.
+At position 1476 to 1550, the domain is characterized as HTH OST-type 8.
+At position 20 to 315, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 2 to 155, the domain is characterized as PPIase cyclophilin-type.
+At position 159 to 432, the domain is characterized as ABC transporter 1.
+At position 510 to 722, the domain is characterized as ABC transmembrane type-2 1.
+At position 1163 to 1379, the domain is characterized as ABC transmembrane type-2 2.
+At position 250 to 497, the domain is characterized as ABC transporter 2.
+At position 121 to 159, the domain is characterized as LRRCT.
+At position 9 to 259, the domain is characterized as UmuC.
+At position 16 to 145, the domain is characterized as PLAT.
+At position 148 to 839, the domain is characterized as Lipoxygenase.
+At position 416 to 486, the domain is characterized as PAS.
+At position 39 to 317, the domain is characterized as Pyruvate carboxyltransferase.
+At position 29 to 96, the domain is characterized as DRBM 1.
+At position 150 to 218, the domain is characterized as DRBM 2.
+At position 278 to 346, the domain is characterized as DRBM 3.
+At position 75 to 169, the domain is characterized as CS.
+At position 170 to 230, the domain is characterized as SGS.
+At position 381 to 471, the domain is characterized as IPT/TIG.
+At position 17 to 154, the domain is characterized as MPN.
+At position 107 to 281, the domain is characterized as Tyr recombinase.
+At position 29 to 137, the domain is characterized as CUB 1.
+At position 140 to 176, the domain is characterized as LDL-receptor class A 1.
+At position 308 to 355, the domain is characterized as LDL-receptor class A 2.
+At position 356 to 398, the domain is characterized as LDL-receptor class A 3.
+At position 399 to 435, the domain is characterized as LDL-receptor class A 4.
+At position 12 to 251, the domain is characterized as ABC transporter.
+At position 18 to 379, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 71 to 314, the domain is characterized as PPM-type phosphatase.
+At position 37 to 207, the domain is characterized as CP-type G.
+At position 148 to 216, the domain is characterized as MBD.
+At position 59 to 237, the domain is characterized as Helicase ATP-binding.
+At position 248 to 478, the domain is characterized as Helicase C-terminal.
+At position 283 to 329, the domain is characterized as NAF.
+At position 420 to 581, the domain is characterized as Helicase ATP-binding.
+At position 600 to 765, the domain is characterized as Helicase C-terminal.
+At position 134 to 213, the domain is characterized as Ig-like C2-type.
+At position 49 to 95, the domain is characterized as TRM112.
+At position 128 to 330, the domain is characterized as GST C-terminal.
+At position 47 to 182, the domain is characterized as Thioredoxin.
+At position 1 to 110, the domain is characterized as C2 1.
+At position 277 to 399, the domain is characterized as C2 2.
+At position 440 to 563, the domain is characterized as C2 3.
+At position 607 to 734, the domain is characterized as C2 4.
+At position 1647 to 1741, the domain is characterized as Peptidase C50.
+At position 231 to 329, the domain is characterized as HTH araC/xylS-type.
+At position 92 to 221, the domain is characterized as GST C-terminal.
+At position 179 to 273, the domain is characterized as PDZ.
+At position 121 to 153, the domain is characterized as EF-hand 4.
+At position 343 to 404, the domain is characterized as PWWP.
+At position 327 to 347, the domain is characterized as ELK.
+At position 3 to 70, the domain is characterized as Sm.
+At position 60 to 151, the domain is characterized as UPAR/Ly6.
+At position 74 to 407, the domain is characterized as Asparaginase/glutaminase.
+At position 8 to 205, the domain is characterized as YjeF N-terminal.
+At position 213 to 464, the domain is characterized as YjeF C-terminal.
+At position 45 to 176, the domain is characterized as FAS1.
+At position 255 to 349, the domain is characterized as PA.
+At position 28 to 70, the domain is characterized as LRRNT.
+At position 176 to 226, the domain is characterized as LRRCT.
+At position 231 to 329, the domain is characterized as Ig-like.
+At position 687 to 738, the domain is characterized as GPS.
+At position 80 to 418, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 73 to 243, the domain is characterized as YDG.
+At position 319 to 441, the domain is characterized as Pre-SET.
+At position 455 to 920, the domain is characterized as SET.
+At position 941 to 957, the domain is characterized as Post-SET.
+At position 221 to 351, the domain is characterized as OmpA-like.
+At position 10 to 88, the domain is characterized as ACT.
+At position 43 to 225, the domain is characterized as BPL/LPL catalytic.
+At position 250 to 313, the domain is characterized as bZIP.
+At position 53 to 161, the domain is characterized as sHSP.
+At position 532 to 1369, the domain is characterized as USP.
+At position 555 to 727, the domain is characterized as tr-type G.
+At position 6 to 168, the domain is characterized as Flavodoxin-like.
+At position 222 to 475, the domain is characterized as FAD-binding FR-type.
+At position 52 to 130, the domain is characterized as GIY-YIG.
+At position 240 to 275, the domain is characterized as UVR.
+At position 206 to 391, the domain is characterized as Glutamine amidotransferase type-1.
+At position 100 to 351, the domain is characterized as Radical SAM core.
+At position 86 to 125, the domain is characterized as EGF-like 1.
+At position 126 to 178, the domain is characterized as EGF-like 2; calcium-binding.
+At position 179 to 218, the domain is characterized as EGF-like 3; calcium-binding.
+At position 224 to 266, the domain is characterized as EGF-like 4.
+At position 531 to 745, the domain is characterized as TSP C-terminal.
+At position 216 to 276, the domain is characterized as HTH myb-type.
+At position 21 to 212, the domain is characterized as RNase H type-2.
+At position 209 to 319, the domain is characterized as Fe2OG dioxygenase.
+At position 69 to 104, the domain is characterized as EF-hand 1.
+At position 29 to 135, the domain is characterized as Glutaredoxin.
+At position 97 to 413, the domain is characterized as IF rod.
+At position 88 to 148, the domain is characterized as Tudor.
+At position 122 to 433, the domain is characterized as IF rod.
+At position 449 to 537, the domain is characterized as EH.
+At position 481 to 516, the domain is characterized as EF-hand.
+At position 222 to 403, the domain is characterized as SSD.
+At position 5 to 77, the domain is characterized as Sm.
+At position 16 to 185, the domain is characterized as FAD-binding PCMH-type.
+At position 82 to 402, the domain is characterized as G-alpha.
+At position 696 to 789, the domain is characterized as FDX-ACB.
+At position 310 to 556, the domain is characterized as FAD-binding FR-type.
+At position 362 to 580, the domain is characterized as Histidine kinase.
+At position 161 to 211, the domain is characterized as DHHC.
+At position 26 to 230, the domain is characterized as uDENN.
+At position 251 to 390, the domain is characterized as cDENN.
+At position 392 to 496, the domain is characterized as dDENN.
+At position 1109 to 1184, the domain is characterized as Death.
+At position 31 to 382, the domain is characterized as FERM.
+At position 20 to 132, the domain is characterized as Ig-like V-type.
+At position 109 to 220, the domain is characterized as sHSP.
+At position 90 to 212, the domain is characterized as FAD-binding FR-type.
+At position 9 to 225, the domain is characterized as Radical SAM core.
+At position 164 to 441, the domain is characterized as CP-type G.
+At position 34 to 821, the domain is characterized as Protein kinase.
+At position 822 to 865, the domain is characterized as AGC-kinase C-terminal.
+At position 51 to 152, the domain is characterized as SRCR 1.
+At position 159 to 259, the domain is characterized as SRCR 2.
+At position 266 to 366, the domain is characterized as SRCR 3.
+At position 373 to 473, the domain is characterized as SRCR 4.
+At position 478 to 578, the domain is characterized as SRCR 5.
+At position 719 to 819, the domain is characterized as SRCR 7.
+At position 824 to 926, the domain is characterized as SRCR 8.
+At position 929 to 1029, the domain is characterized as SRCR 9.
+At position 526 to 698, the domain is characterized as tr-type G.
+At position 51 to 127, the domain is characterized as S1 motif.
+At position 135 to 196, the domain is characterized as KH.
+At position 146 to 186, the domain is characterized as LDL-receptor class A 4.
+At position 196 to 234, the domain is characterized as LDL-receptor class A 5.
+At position 235 to 273, the domain is characterized as LDL-receptor class A 6.
+At position 275 to 314, the domain is characterized as LDL-receptor class A 7.
+At position 315 to 354, the domain is characterized as EGF-like 1.
+At position 355 to 394, the domain is characterized as EGF-like 2; calcium-binding.
+At position 663 to 713, the domain is characterized as EGF-like 3.
+At position 530 to 559, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 70 to 240, the domain is characterized as Helicase ATP-binding.
+At position 251 to 412, the domain is characterized as Helicase C-terminal.
+At position 295 to 373, the domain is characterized as PUA.
+At position 99 to 386, the domain is characterized as tr-type G.
+At position 418 to 590, the domain is characterized as tr-type G.
+At position 311 to 446, the domain is characterized as Fido.
+At position 13 to 209, the domain is characterized as Lon N-terminal.
+At position 4 to 148, the domain is characterized as Flavodoxin-like.
+At position 283 to 534, the domain is characterized as Protein kinase.
+At position 83 to 197, the domain is characterized as SET.
+At position 191 to 466, the domain is characterized as Protein kinase.
+At position 31 to 275, the domain is characterized as Peptidase S1.
+At position 282 to 359, the domain is characterized as BCNT-C.
+At position 338 to 544, the domain is characterized as MCM.
+At position 151 to 223, the domain is characterized as PA.
+At position 9 to 144, the domain is characterized as MPN.
+At position 859 to 1156, the domain is characterized as ABC transmembrane type-1 2.
+At position 29 to 73, the domain is characterized as WAP 1.
+At position 74 to 123, the domain is characterized as WAP 2.
+At position 627 to 673, the domain is characterized as Kazal-like 1.
+At position 698 to 752, the domain is characterized as Kazal-like 2.
+At position 704 to 750, the domain is characterized as Kazal-like 2; degenerate.
+At position 753 to 789, the domain is characterized as Kazal-like 3.
+At position 111 to 364, the domain is characterized as Protein kinase.
+At position 3 to 109, the domain is characterized as SSB.
+At position 150 to 303, the domain is characterized as N-acetyltransferase.
+At position 61 to 442, the domain is characterized as Protein kinase.
+At position 27 to 169, the domain is characterized as Jacalin-type lectin 1.
+At position 172 to 314, the domain is characterized as Jacalin-type lectin 2.
+At position 317 to 462, the domain is characterized as Jacalin-type lectin 3.
+At position 468 to 611, the domain is characterized as Jacalin-type lectin 4.
+At position 25 to 139, the domain is characterized as CUB 1.
+At position 145 to 263, the domain is characterized as CUB 2.
+At position 273 to 422, the domain is characterized as F5/8 type C 1.
+At position 429 to 581, the domain is characterized as F5/8 type C 2.
+At position 642 to 811, the domain is characterized as MAM.
+At position 13 to 297, the domain is characterized as tr-type G.
+At position 46 to 228, the domain is characterized as FAD-binding PCMH-type.
+At position 86 to 319, the domain is characterized as Helicase ATP-binding.
+At position 355 to 499, the domain is characterized as Helicase C-terminal.
+At position 492 to 810, the domain is characterized as Protein kinase.
+At position 190 to 388, the domain is characterized as HIN-200.
+At position 254 to 409, the domain is characterized as JmjC.
+At position 5 to 155, the domain is characterized as N-acetyltransferase 1.
+At position 160 to 309, the domain is characterized as N-acetyltransferase 2.
+At position 459 to 686, the domain is characterized as ABC transmembrane type-2.
+At position 72 to 107, the domain is characterized as EF-hand 3.
+At position 108 to 134, the domain is characterized as EF-hand 4.
+At position 17 to 203, the domain is characterized as tr-type G.
+At position 40 to 68, the domain is characterized as LRRNT.
+At position 228 to 284, the domain is characterized as LRRCT.
+At position 289 to 379, the domain is characterized as Ig-like C2-type.
+At position 32 to 330, the domain is characterized as ABC transmembrane type-1.
+At position 364 to 598, the domain is characterized as ABC transporter.
+At position 46 to 299, the domain is characterized as ABC transporter 1.
+At position 343 to 586, the domain is characterized as ABC transporter 2.
+At position 244 to 321, the domain is characterized as TFIIS N-terminal.
+At position 32 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 235 to 317, the domain is characterized as Ig-like C2-type 3.
+At position 517 to 606, the domain is characterized as Fibronectin type-III 3.
+At position 608 to 692, the domain is characterized as Fibronectin type-III 4.
+At position 961 to 1216, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1248 to 1507, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 112 to 183, the domain is characterized as PAS.
+At position 283 to 542, the domain is characterized as Deacetylase sirtuin-type.
+At position 722 to 1015, the domain is characterized as Peptidase S8.
+At position 5 to 176, the domain is characterized as PITH.
+At position 33 to 92, the domain is characterized as TIL.
+At position 2 to 162, the domain is characterized as Clp R.
+At position 236 to 357, the domain is characterized as C2 2.
+At position 400 to 531, the domain is characterized as C2 3.
+At position 944 to 1069, the domain is characterized as C2 4.
+At position 1115 to 1242, the domain is characterized as C2 5.
+At position 1464 to 1593, the domain is characterized as C2 6.
+At position 1714 to 1865, the domain is characterized as C2 7.
+At position 3 to 281, the domain is characterized as DegV.
+At position 160 to 226, the domain is characterized as DRBM.
+At position 5 to 95, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 142 to 171, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 216 to 364, the domain is characterized as N-acetyltransferase.
+At position 20 to 115, the domain is characterized as Ig-like.
+At position 1 to 67, the domain is characterized as LCN-type CS-alpha/beta.
+At position 82 to 147, the domain is characterized as NAC-A/B.
+At position 26 to 68, the domain is characterized as Fibronectin type-III 1.
+At position 100 to 161, the domain is characterized as Fibronectin type-III 2.
+At position 162 to 263, the domain is characterized as Fibronectin type-III 3.
+At position 141 to 455, the domain is characterized as IF rod.
+At position 880 to 956, the domain is characterized as Carrier.
+At position 4 to 17, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 108 to 191, the domain is characterized as MEIS N-terminal.
+At position 18 to 67, the domain is characterized as Myosin N-terminal SH3-like.
+At position 72 to 741, the domain is characterized as Myosin motor.
+At position 744 to 773, the domain is characterized as IQ 1.
+At position 767 to 796, the domain is characterized as IQ 2.
+At position 792 to 821, the domain is characterized as IQ 3.
+At position 813 to 842, the domain is characterized as IQ 4.
+At position 836 to 865, the domain is characterized as IQ 5.
+At position 859 to 888, the domain is characterized as IQ 6.
+At position 1161 to 1444, the domain is characterized as Dilute.
+At position 250 to 290, the domain is characterized as UBA.
+At position 617 to 677, the domain is characterized as Tudor.
+At position 141 to 263, the domain is characterized as Cyclin N-terminal.
+At position 92 to 120, the domain is characterized as IQ 1.
+At position 121 to 143, the domain is characterized as IQ 2.
+At position 144 to 169, the domain is characterized as IQ 3.
+At position 298 to 413, the domain is characterized as RGS.
+At position 176 to 335, the domain is characterized as C2 1.
+At position 663 to 784, the domain is characterized as MHD1.
+At position 888 to 996, the domain is characterized as MHD2.
+At position 1010 to 1136, the domain is characterized as C2 2.
+At position 259 to 405, the domain is characterized as MATH.
+At position 2 to 225, the domain is characterized as Peptidase S1.
+At position 348 to 437, the domain is characterized as PDZ.
+At position 59 to 105, the domain is characterized as F-box.
+At position 49 to 89, the domain is characterized as UBA.
+At position 137 to 209, the domain is characterized as HTH crp-type.
+At position 29 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 113 to 238, the domain is characterized as EamA 1.
+At position 266 to 390, the domain is characterized as EamA 2.
+At position 104 to 264, the domain is characterized as PINIT.
+At position 237 to 296, the domain is characterized as SH3.
+At position 129 to 213, the domain is characterized as PNT.
+At position 138 to 368, the domain is characterized as Radical SAM core.
+At position 309 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 407 to 492, the domain is characterized as Ig-like C2-type 5.
+At position 500 to 599, the domain is characterized as Fibronectin type-III 1.
+At position 601 to 696, the domain is characterized as Fibronectin type-III 2.
+At position 31 to 235, the domain is characterized as Lon N-terminal.
+At position 626 to 806, the domain is characterized as Lon proteolytic.
+At position 101 to 276, the domain is characterized as Helicase ATP-binding.
+At position 291 to 456, the domain is characterized as Helicase C-terminal.
+At position 1 to 142, the domain is characterized as Clp R.
+At position 40 to 187, the domain is characterized as GAF.
+At position 226 to 454, the domain is characterized as Sigma-54 factor interaction.
+At position 336 to 580, the domain is characterized as Clu.
+At position 644 to 705, the domain is characterized as CBS 1.
+At position 944 to 994, the domain is characterized as CBS 2.
+At position 107 to 485, the domain is characterized as PRONE.
+At position 44 to 230, the domain is characterized as GH11.
+At position 243 to 335, the domain is characterized as CBM2.
+At position 112 to 359, the domain is characterized as Lon N-terminal.
+At position 748 to 938, the domain is characterized as Lon proteolytic.
+At position 31 to 230, the domain is characterized as BPL/LPL catalytic.
+At position 32 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 429 to 549, the domain is characterized as Ig-like C2-type 5.
+At position 556 to 655, the domain is characterized as Ig-like C2-type 6.
+At position 32 to 144, the domain is characterized as EamA 1.
+At position 237 to 346, the domain is characterized as EamA 2.
+At position 80 to 175, the domain is characterized as SH2.
+At position 162 to 211, the domain is characterized as SOCS box.
+At position 112 to 338, the domain is characterized as ABC transporter.
+At position 496 to 562, the domain is characterized as Dockerin.
+At position 104 to 207, the domain is characterized as PH.
+At position 267 to 328, the domain is characterized as SH3.
+At position 42 to 316, the domain is characterized as PPM-type phosphatase.
+At position 724 to 819, the domain is characterized as BRCT 1.
+At position 840 to 941, the domain is characterized as BRCT 2.
+At position 34 to 72, the domain is characterized as EGF-like.
+At position 231 to 264, the domain is characterized as WW 1.
+At position 339 to 372, the domain is characterized as WW 2.
+At position 399 to 432, the domain is characterized as WW 3.
+At position 488 to 821, the domain is characterized as HECT.
+At position 210 to 263, the domain is characterized as CVC.
+At position 458 to 600, the domain is characterized as Thioredoxin.
+At position 58 to 223, the domain is characterized as Helicase ATP-binding.
+At position 351 to 513, the domain is characterized as Helicase C-terminal.
+At position 704 to 897, the domain is characterized as Macro.
+At position 7 to 240, the domain is characterized as Radical SAM core.
+At position 110 to 149, the domain is characterized as LRRCT.
+At position 7 to 52, the domain is characterized as F-box.
+At position 1085 to 1253, the domain is characterized as DH.
+At position 1265 to 1372, the domain is characterized as PH.
+At position 596 to 657, the domain is characterized as SH3.
+At position 3 to 70, the domain is characterized as HMA.
+At position 159 to 313, the domain is characterized as N-acetyltransferase.
+At position 40 to 106, the domain is characterized as Importin N-terminal.
+At position 1729 to 1764, the domain is characterized as EF-hand.
+At position 21 to 140, the domain is characterized as Cadherin 1.
+At position 141 to 250, the domain is characterized as Cadherin 2.
+At position 251 to 371, the domain is characterized as Cadherin 3.
+At position 370 to 478, the domain is characterized as Cadherin 4.
+At position 162 to 323, the domain is characterized as CRAL-TRIO.
+At position 441 to 563, the domain is characterized as HD.
+At position 680 to 760, the domain is characterized as ACT 1.
+At position 788 to 857, the domain is characterized as ACT 2.
+At position 217 to 252, the domain is characterized as EF-hand 2.
+At position 427 to 561, the domain is characterized as DAGKc.
+At position 141 to 216, the domain is characterized as Histone-fold.
+At position 5 to 239, the domain is characterized as SET.
+At position 163 to 249, the domain is characterized as PPIase FKBP-type.
+At position 17 to 85, the domain is characterized as HTH gntR-type.
+At position 521 to 591, the domain is characterized as KHA.
+At position 201 to 270, the domain is characterized as Rieske.
+At position 197 to 332, the domain is characterized as Fatty acid hydroxylase.
+At position 44 to 73, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 139 to 166, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 2 to 400, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 29 to 94, the domain is characterized as J.
+At position 324 to 416, the domain is characterized as PH.
+At position 439 to 560, the domain is characterized as Arf-GAP.
+At position 1067 to 1129, the domain is characterized as SH3.
+At position 5 to 51, the domain is characterized as RPE1 insert.
+At position 170 to 250, the domain is characterized as RRM Nup35-type.
+At position 27 to 140, the domain is characterized as Ig-like V-type 1.
+At position 148 to 234, the domain is characterized as Ig-like V-type 2.
+At position 285 to 479, the domain is characterized as B30.2/SPRY.
+At position 20 to 72, the domain is characterized as HTH myb-type 1.
+At position 73 to 127, the domain is characterized as HTH myb-type 2.
+At position 20 to 307, the domain is characterized as Radical SAM core.
+At position 84 to 115, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 168 to 277, the domain is characterized as CHRD 1.
+At position 279 to 402, the domain is characterized as CHRD 2.
+At position 403 to 524, the domain is characterized as CHRD 3.
+At position 530 to 650, the domain is characterized as CHRD 4.
+At position 703 to 763, the domain is characterized as VWFC 2.
+At position 784 to 850, the domain is characterized as VWFC 3.
+At position 872 to 932, the domain is characterized as VWFC 4.
+At position 9 to 187, the domain is characterized as Guanylate kinase-like.
+At position 95 to 401, the domain is characterized as Peptidase A1.
+At position 861 to 1157, the domain is characterized as ABC transmembrane type-1 2.
+At position 1214 to 1447, the domain is characterized as ABC transporter 2.
+At position 281 to 348, the domain is characterized as KH 2.
+At position 235 to 288, the domain is characterized as SOCS box.
+At position 1 to 359, the domain is characterized as SPX.
+At position 618 to 813, the domain is characterized as EXS.
+At position 32 to 61, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 231 to 377, the domain is characterized as Helicase C-terminal.
+At position 203 to 424, the domain is characterized as Helicase ATP-binding.
+At position 473 to 618, the domain is characterized as Helicase C-terminal.
+At position 9 to 71, the domain is characterized as S4 RNA-binding.
+At position 21 to 162, the domain is characterized as Thioredoxin 1.
+At position 162 to 294, the domain is characterized as Thioredoxin 2.
+At position 498 to 629, the domain is characterized as Thioredoxin 3.
+At position 43 to 128, the domain is characterized as YbbR-like 1.
+At position 138 to 220, the domain is characterized as YbbR-like 2.
+At position 11 to 77, the domain is characterized as BTB.
+At position 156 to 414, the domain is characterized as NPH3.
+At position 48 to 175, the domain is characterized as ALOG.
+At position 11 to 83, the domain is characterized as S1-like.
+At position 57 to 311, the domain is characterized as Peptidase S6.
+At position 1034 to 1300, the domain is characterized as Autotransporter.
+At position 434 to 463, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 106 to 368, the domain is characterized as GS catalytic.
+At position 1 to 261, the domain is characterized as F-BAR.
+At position 599 to 667, the domain is characterized as SH3.
+At position 88 to 166, the domain is characterized as GRAM.
+At position 214 to 369, the domain is characterized as TrmE-type G.
+At position 292 to 327, the domain is characterized as EF-hand 2.
+At position 100 to 178, the domain is characterized as RRM 1.
+At position 233 to 310, the domain is characterized as RRM 2.
+At position 523 to 599, the domain is characterized as RRM 3.
+At position 144 to 321, the domain is characterized as TNase-like.
+At position 20 to 85, the domain is characterized as Sushi 1.
+At position 86 to 147, the domain is characterized as Sushi 2.
+At position 148 to 206, the domain is characterized as Sushi 3.
+At position 209 to 267, the domain is characterized as Sushi 4.
+At position 268 to 332, the domain is characterized as Sushi 5.
+At position 333 to 394, the domain is characterized as Sushi 6.
+At position 395 to 453, the domain is characterized as Sushi 7.
+At position 456 to 514, the domain is characterized as Sushi 8.
+At position 515 to 578, the domain is characterized as Sushi 9.
+At position 108 to 166, the domain is characterized as Collagen-like 1.
+At position 173 to 232, the domain is characterized as Collagen-like 2.
+At position 240 to 298, the domain is characterized as Collagen-like 3.
+At position 313 to 372, the domain is characterized as Collagen-like 4.
+At position 404 to 452, the domain is characterized as Collagen-like 5.
+At position 455 to 514, the domain is characterized as Collagen-like 6.
+At position 22 to 153, the domain is characterized as VHS.
+At position 175 to 194, the domain is characterized as UIM.
+At position 255 to 315, the domain is characterized as SH3.
+At position 215 to 303, the domain is characterized as GAT.
+At position 30 to 96, the domain is characterized as S1 motif 1.
+At position 114 to 180, the domain is characterized as S1 motif 2.
+At position 201 to 269, the domain is characterized as S1 motif 3.
+At position 286 to 356, the domain is characterized as S1 motif 4.
+At position 373 to 443, the domain is characterized as S1 motif 5.
+At position 454 to 529, the domain is characterized as S1 motif 6.
+At position 2 to 79, the domain is characterized as Core-binding (CB).
+At position 95 to 271, the domain is characterized as Tyr recombinase.
+At position 268 to 308, the domain is characterized as SOCS box.
+At position 29 to 140, the domain is characterized as SSB.
+At position 9 to 122, the domain is characterized as C-type lectin.
+At position 64 to 279, the domain is characterized as Radical SAM core.
+At position 45 to 111, the domain is characterized as Disintegrin.
+At position 57 to 73, the domain is characterized as Peptidase A1.
+At position 82 to 322, the domain is characterized as Lon N-terminal.
+At position 9 to 172, the domain is characterized as Exonuclease.
+At position 16 to 214, the domain is characterized as ABC transporter.
+At position 22 to 402, the domain is characterized as Lon N-terminal.
+At position 989 to 1230, the domain is characterized as Lon proteolytic.
+At position 4 to 141, the domain is characterized as SprT-like.
+At position 162 to 416, the domain is characterized as ABC transporter 1.
+At position 852 to 1095, the domain is characterized as ABC transporter 2.
+At position 63 to 435, the domain is characterized as AB hydrolase-1.
+At position 96 to 235, the domain is characterized as N-acetyltransferase.
+At position 3 to 214, the domain is characterized as Glutamine amidotransferase type-1.
+At position 58 to 172, the domain is characterized as HD.
+At position 196 to 278, the domain is characterized as RCK C-terminal 1.
+At position 286 to 370, the domain is characterized as RCK C-terminal 2.
+At position 645 to 880, the domain is characterized as Helicase ATP-binding.
+At position 1213 to 1379, the domain is characterized as Helicase C-terminal.
+At position 68 to 183, the domain is characterized as Expansin-like EG45.
+At position 193 to 273, the domain is characterized as Expansin-like CBD.
+At position 23 to 107, the domain is characterized as DEP.
+At position 49 to 273, the domain is characterized as Radical SAM core.
+At position 136 to 164, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 10 to 159, the domain is characterized as NAC.
+At position 13 to 354, the domain is characterized as Kinesin motor.
+At position 81 to 192, the domain is characterized as Rieske.
+At position 212 to 382, the domain is characterized as Hflx-type G.
+At position 2 to 238, the domain is characterized as Glutamine amidotransferase type-2.
+At position 239 to 313, the domain is characterized as U-box.
+At position 160 to 344, the domain is characterized as FAD-binding PCMH-type.
+At position 106 to 282, the domain is characterized as CRAL-TRIO.
+At position 51 to 97, the domain is characterized as Gla.
+At position 1 to 457, the domain is characterized as Biotin carboxylation.
+At position 125 to 321, the domain is characterized as ATP-grasp.
+At position 534 to 802, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1071 to 1146, the domain is characterized as Biotinyl-binding.
+At position 253 to 501, the domain is characterized as ABC transporter 2.
+At position 2 to 112, the domain is characterized as PINc.
+At position 358 to 513, the domain is characterized as Helicase C-terminal.
+At position 1906 to 1935, the domain is characterized as IQ.
+At position 253 to 302, the domain is characterized as bHLH.
+At position 170 to 273, the domain is characterized as PpiC 1.
+At position 271 to 381, the domain is characterized as PpiC 2.
+At position 2 to 186, the domain is characterized as RNase H type-2.
+At position 523 to 542, the domain is characterized as WH2.
+At position 1445 to 1669, the domain is characterized as Collagen IV NC1.
+At position 396 to 493, the domain is characterized as Zinc-hook.
+At position 32 to 358, the domain is characterized as PORR.
+At position 1 to 146, the domain is characterized as Integrase catalytic.
+At position 134 to 234, the domain is characterized as Fibronectin type-III.
+At position 303 to 557, the domain is characterized as Protein kinase.
+At position 740 to 826, the domain is characterized as SUEL-type lectin.
+At position 173 to 530, the domain is characterized as Protein kinase.
+At position 111 to 329, the domain is characterized as DOG1.
+At position 26 to 194, the domain is characterized as RabBD.
+At position 677 to 763, the domain is characterized as PDZ.
+At position 814 to 937, the domain is characterized as C2 1.
+At position 1376 to 1494, the domain is characterized as C2 2.
+At position 9 to 94, the domain is characterized as BMC.
+At position 19 to 103, the domain is characterized as Ig-like C2-type.
+At position 105 to 199, the domain is characterized as Ig-like V-type.
+At position 745 to 827, the domain is characterized as DIX.
+At position 208 to 334, the domain is characterized as Cyclin N-terminal.
+At position 28 to 250, the domain is characterized as AB hydrolase-1.
+At position 118 to 307, the domain is characterized as NodB homology.
+At position 1 to 51, the domain is characterized as RRM.
+At position 234 to 462, the domain is characterized as ATP-grasp.
+At position 1031 to 1209, the domain is characterized as C2.
+At position 18 to 167, the domain is characterized as FAS1 1.
+At position 169 to 296, the domain is characterized as FAS1 2.
+At position 179 to 336, the domain is characterized as Tyrosine-protein phosphatase.
+At position 153 to 228, the domain is characterized as Ubiquitin-like.
+At position 146 to 236, the domain is characterized as RRM.
+At position 4 to 86, the domain is characterized as Cytochrome b5 heme-binding.
+At position 661 to 750, the domain is characterized as BRCT.
+At position 949 to 1257, the domain is characterized as PKS/mFAS DH.
+At position 2411 to 2489, the domain is characterized as Carrier.
+At position 66 to 260, the domain is characterized as FtsK 1.
+At position 350 to 546, the domain is characterized as FtsK 2.
+At position 463 to 618, the domain is characterized as Protein kinase.
+At position 237 to 311, the domain is characterized as U-box.
+At position 250 to 299, the domain is characterized as bZIP.
+At position 33 to 207, the domain is characterized as Helicase ATP-binding.
+At position 218 to 382, the domain is characterized as Helicase C-terminal.
+At position 546 to 853, the domain is characterized as Protein kinase.
+At position 264 to 448, the domain is characterized as Helicase ATP-binding.
+At position 485 to 642, the domain is characterized as Helicase C-terminal.
+At position 938 to 1245, the domain is characterized as PKS/mFAS DH.
+At position 2378 to 2456, the domain is characterized as Carrier.
+At position 4 to 56, the domain is characterized as bHLH.
+At position 203 to 236, the domain is characterized as WW.
+At position 604 to 684, the domain is characterized as BRCT.
+At position 201 to 346, the domain is characterized as YEATS.
+At position 199 to 462, the domain is characterized as NR LBD.
+At position 314 to 388, the domain is characterized as POU-specific.
+At position 111 to 413, the domain is characterized as Peptidase S8.
+At position 407 to 537, the domain is characterized as P/Homo B.
+At position 543 to 608, the domain is characterized as SAM.
+At position 253 to 481, the domain is characterized as Ras-GAP.
+At position 33 to 108, the domain is characterized as C-type lectin.
+At position 16 to 382, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 68 to 373, the domain is characterized as Peptidase A1.
+At position 74 to 248, the domain is characterized as Thioredoxin.
+At position 107 to 135, the domain is characterized as IQ.
+At position 232 to 267, the domain is characterized as UVR.
+At position 1014 to 1198, the domain is characterized as Laminin G-like 4.
+At position 181 to 359, the domain is characterized as Rho-GAP.
+At position 2 to 238, the domain is characterized as PABS.
+At position 69 to 364, the domain is characterized as Protein kinase.
+At position 1 to 206, the domain is characterized as RNase H type-2.
+At position 99 to 242, the domain is characterized as RDD.
+At position 198 to 392, the domain is characterized as CheB-type methylesterase.
+At position 1 to 203, the domain is characterized as SEC7.
+At position 333 to 475, the domain is characterized as PH.
+At position 84 to 388, the domain is characterized as Peptidase A1.
+At position 600 to 686, the domain is characterized as BRCT.
+At position 10 to 245, the domain is characterized as ABC transporter.
+At position 37 to 89, the domain is characterized as HTH myb-type 1.
+At position 90 to 144, the domain is characterized as HTH myb-type 2.
+At position 195 to 280, the domain is characterized as KH type-2.
+At position 6 to 256, the domain is characterized as Protein kinase.
+At position 9 to 121, the domain is characterized as CMP/dCMP-type deaminase.
+At position 377 to 446, the domain is characterized as TRAM.
+At position 318 to 466, the domain is characterized as PI-PLC X-box.
+At position 599 to 715, the domain is characterized as PI-PLC Y-box.
+At position 38 to 149, the domain is characterized as PH.
+At position 159 to 194, the domain is characterized as EF-hand 1.
+At position 195 to 230, the domain is characterized as EF-hand 2.
+At position 313 to 458, the domain is characterized as PI-PLC X-box.
+At position 506 to 621, the domain is characterized as PI-PLC Y-box.
+At position 621 to 750, the domain is characterized as C2.
+At position 240 to 420, the domain is characterized as PCI.
+At position 32 to 273, the domain is characterized as Peptidase S1.
+At position 34 to 110, the domain is characterized as ACT 1.
+At position 115 to 196, the domain is characterized as ACT 2.
+At position 248 to 324, the domain is characterized as ACT 3.
+At position 326 to 405, the domain is characterized as ACT 4.
+At position 33 to 214, the domain is characterized as Plastocyanin-like 1.
+At position 215 to 379, the domain is characterized as Plastocyanin-like 2.
+At position 1 to 128, the domain is characterized as CMP/dCMP-type deaminase.
+At position 134 to 393, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 425 to 688, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 374 to 435, the domain is characterized as TRAM.
+At position 39 to 294, the domain is characterized as ABC transporter.
+At position 389 to 646, the domain is characterized as ABC transmembrane type-2.
+At position 35 to 183, the domain is characterized as CBM-cenC 1.
+At position 197 to 359, the domain is characterized as CBM-cenC 2.
+At position 365 to 710, the domain is characterized as GH10.
+At position 113 to 191, the domain is characterized as RRM 1.
+At position 207 to 285, the domain is characterized as RRM 2.
+At position 13 to 74, the domain is characterized as LIM zinc-binding 1.
+At position 76 to 133, the domain is characterized as LIM zinc-binding 2.
+At position 138 to 195, the domain is characterized as LIM zinc-binding 3.
+At position 196 to 255, the domain is characterized as LIM zinc-binding 4.
+At position 256 to 315, the domain is characterized as LIM zinc-binding 5.
+At position 230 to 386, the domain is characterized as JmjC.
+At position 684 to 804, the domain is characterized as PH.
+At position 901 to 1093, the domain is characterized as Rho-GAP.
+At position 688 to 780, the domain is characterized as FDX-ACB.
+At position 235 to 305, the domain is characterized as EB1 C-terminal.
+At position 131 to 372, the domain is characterized as Radical SAM core.
+At position 72 to 268, the domain is characterized as DH.
+At position 254 to 387, the domain is characterized as GGDEF.
+At position 396 to 644, the domain is characterized as EAL.
+At position 112 to 279, the domain is characterized as Helicase ATP-binding.
+At position 290 to 459, the domain is characterized as Helicase C-terminal.
+At position 30 to 327, the domain is characterized as F5/8 type A 1.
+At position 203 to 327, the domain is characterized as Plastocyanin-like 2.
+At position 348 to 686, the domain is characterized as F5/8 type A 2.
+At position 535 to 686, the domain is characterized as Plastocyanin-like 4.
+At position 1569 to 1890, the domain is characterized as F5/8 type A 3.
+At position 1569 to 1738, the domain is characterized as Plastocyanin-like 5.
+At position 1748 to 1890, the domain is characterized as Plastocyanin-like 6.
+At position 1894 to 2048, the domain is characterized as F5/8 type C 1.
+At position 2053 to 2208, the domain is characterized as F5/8 type C 2.
+At position 2 to 94, the domain is characterized as Acylphosphatase-like.
+At position 546 to 712, the domain is characterized as C2 DOCK-type.
+At position 1620 to 2056, the domain is characterized as DOCKER.
+At position 6 to 92, the domain is characterized as BMC.
+At position 139 to 392, the domain is characterized as PPM-type phosphatase.
+At position 172 to 269, the domain is characterized as HTH araC/xylS-type.
+At position 53 to 143, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 18 to 135, the domain is characterized as Ig-like C2-type 1.
+At position 140 to 258, the domain is characterized as Ig-like C2-type 2.
+At position 272 to 382, the domain is characterized as Ig-like C2-type 3.
+At position 402 to 523, the domain is characterized as Ig-like C2-type 4.
+At position 674 to 796, the domain is characterized as Ig-like C2-type 6.
+At position 806 to 930, the domain is characterized as Ig-like C2-type 7.
+At position 947 to 1063, the domain is characterized as Ig-like C2-type 8.
+At position 150 to 259, the domain is characterized as CUB 1.
+At position 265 to 301, the domain is characterized as LDL-receptor class A 1.
+At position 307 to 420, the domain is characterized as CUB 2.
+At position 426 to 460, the domain is characterized as LDL-receptor class A 2.
+At position 466 to 584, the domain is characterized as FZ.
+At position 382 to 468, the domain is characterized as OCT.
+At position 135 to 354, the domain is characterized as Radical SAM core.
+At position 7 to 297, the domain is characterized as Protein kinase.
+At position 12 to 79, the domain is characterized as S4 RNA-binding.
+At position 215 to 289, the domain is characterized as RRM.
+At position 115 to 150, the domain is characterized as EF-hand 4.
+At position 254 to 364, the domain is characterized as C2.
+At position 173 to 301, the domain is characterized as GGDEF.
+At position 279 to 462, the domain is characterized as Helicase ATP-binding.
+At position 497 to 643, the domain is characterized as Helicase C-terminal.
+At position 143 to 261, the domain is characterized as C-type lectin.
+At position 127 to 213, the domain is characterized as APO 1.
+At position 294 to 380, the domain is characterized as APO 2.
+At position 11 to 379, the domain is characterized as DZF.
+At position 402 to 471, the domain is characterized as DRBM 1.
+At position 527 to 593, the domain is characterized as DRBM 2.
+At position 81 to 328, the domain is characterized as ATP-grasp.
+At position 12 to 46, the domain is characterized as WAP.
+At position 128 to 440, the domain is characterized as IF rod.
+At position 184 to 415, the domain is characterized as Radical SAM core.
+At position 417 to 487, the domain is characterized as TRAM.
+At position 81 to 366, the domain is characterized as Protein kinase.
+At position 499 to 672, the domain is characterized as tr-type G.
+At position 77 to 129, the domain is characterized as bHLH.
+At position 1250 to 1518, the domain is characterized as NR LBD.
+At position 68 to 218, the domain is characterized as FAD-binding FR-type.
+At position 10 to 226, the domain is characterized as ABC transporter.
+At position 45 to 115, the domain is characterized as BIG2.
+At position 55 to 167, the domain is characterized as DOMON.
+At position 174 to 369, the domain is characterized as Cytochrome b561.
+At position 618 to 770, the domain is characterized as Collagen-like.
+At position 206 to 296, the domain is characterized as Ig-like C1-type.
+At position 235 to 449, the domain is characterized as FAD-binding FR-type.
+At position 68 to 286, the domain is characterized as Methyl-accepting transducer.
+At position 6 to 52, the domain is characterized as Peptidase M12B.
+At position 53 to 80, the domain is characterized as Disintegrin.
+At position 129 to 314, the domain is characterized as tr-type G.
+At position 43 to 62, the domain is characterized as UIM 1.
+At position 92 to 111, the domain is characterized as UIM 2.
+At position 155 to 174, the domain is characterized as UIM 3.
+At position 199 to 269, the domain is characterized as LIM zinc-binding.
+At position 26 to 235, the domain is characterized as Saposin B-type.
+At position 39 to 278, the domain is characterized as ABC transporter.
+At position 115 to 211, the domain is characterized as Rieske.
+At position 145 to 235, the domain is characterized as Rhodanese.
+At position 284 to 563, the domain is characterized as Protein kinase.
+At position 11 to 174, the domain is characterized as Exonuclease.
+At position 637 to 803, the domain is characterized as Integrase catalytic.
+At position 108 to 136, the domain is characterized as IQ 1.
+At position 137 to 154, the domain is characterized as IQ 2.
+At position 132 to 419, the domain is characterized as ABC transmembrane type-1.
+At position 454 to 691, the domain is characterized as ABC transporter.
+At position 68 to 157, the domain is characterized as GIY-YIG.
+At position 89 to 421, the domain is characterized as USP.
+At position 460 to 554, the domain is characterized as DUSP 1.
+At position 569 to 691, the domain is characterized as DUSP 2.
+At position 711 to 824, the domain is characterized as DUSP 3.
+At position 929 to 1009, the domain is characterized as Ubiquitin-like.
+At position 479 to 593, the domain is characterized as Toprim.
+At position 227 to 500, the domain is characterized as USP.
+At position 154 to 167, the domain is characterized as DUF1725.
+At position 56 to 118, the domain is characterized as Tudor 1.
+At position 440 to 628, the domain is characterized as Helicase ATP-binding.
+At position 809 to 909, the domain is characterized as Tudor 2.
+At position 1073 to 1159, the domain is characterized as CS.
+At position 19 to 70, the domain is characterized as F-box.
+At position 263 to 283, the domain is characterized as IQ.
+At position 7 to 55, the domain is characterized as WAP.
+At position 73 to 472, the domain is characterized as GH18.
+At position 29 to 60, the domain is characterized as LRRNT.
+At position 493 to 568, the domain is characterized as Biotinyl-binding.
+At position 252 to 493, the domain is characterized as ABC transporter 2.
+At position 434 to 492, the domain is characterized as COS.
+At position 603 to 701, the domain is characterized as Fibronectin type-III.
+At position 1 to 91, the domain is characterized as GST N-terminal.
+At position 97 to 221, the domain is characterized as GST C-terminal.
+At position 409 to 613, the domain is characterized as Thioredoxin.
+At position 1 to 120, the domain is characterized as Glutamine amidotransferase type-1; truncated.
+At position 121 to 310, the domain is characterized as GMPS ATP-PPase.
+At position 401 to 611, the domain is characterized as Rab-GAP TBC.
+At position 229 to 279, the domain is characterized as bHLH.
+At position 559 to 726, the domain is characterized as W2.
+At position 381 to 413, the domain is characterized as EGF-like 2.
+At position 536 to 588, the domain is characterized as TB 1.
+At position 609 to 649, the domain is characterized as EGF-like 3; calcium-binding.
+At position 659 to 711, the domain is characterized as TB 2.
+At position 835 to 877, the domain is characterized as EGF-like 4.
+At position 878 to 920, the domain is characterized as EGF-like 5; calcium-binding.
+At position 921 to 960, the domain is characterized as EGF-like 6; calcium-binding.
+At position 961 to 1000, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1001 to 1041, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1042 to 1083, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1084 to 1125, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1126 to 1166, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1167 to 1208, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1209 to 1250, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1725 to 1765, the domain is characterized as EGF-like 19; calcium-binding.
+At position 1766 to 1810, the domain is characterized as EGF-like 20; calcium-binding.
+At position 29 to 151, the domain is characterized as FAS1 1.
+At position 154 to 285, the domain is characterized as FAS1 2.
+At position 27 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 605 to 814, the domain is characterized as FtsK.
+At position 647 to 738, the domain is characterized as Fe2OG dioxygenase.
+At position 74 to 161, the domain is characterized as PB1.
+At position 130 to 458, the domain is characterized as Protein kinase.
+At position 125 to 149, the domain is characterized as KOW.
+At position 164 to 419, the domain is characterized as SMP-LTD.
+At position 105 to 416, the domain is characterized as IF rod.
+At position 155 to 227, the domain is characterized as RBD.
+At position 497 to 757, the domain is characterized as Protein kinase.
+At position 9 to 170, the domain is characterized as EngA-type G 1.
+At position 185 to 362, the domain is characterized as EngA-type G 2.
+At position 363 to 448, the domain is characterized as KH-like.
+At position 1 to 5, the domain is characterized as Laminin EGF-like 1.
+At position 6 to 53, the domain is characterized as Laminin EGF-like 2.
+At position 54 to 100, the domain is characterized as Laminin EGF-like 3.
+At position 1 to 94, the domain is characterized as YcgL.
+At position 23 to 132, the domain is characterized as Cadherin 1.
+At position 136 to 236, the domain is characterized as Cadherin 2.
+At position 237 to 344, the domain is characterized as Cadherin 3.
+At position 346 to 466, the domain is characterized as Cadherin 4.
+At position 462 to 566, the domain is characterized as Cadherin 5.
+At position 567 to 695, the domain is characterized as Cadherin 6.
+At position 4 to 48, the domain is characterized as RPE1 insert.
+At position 51 to 220, the domain is characterized as Era-type G.
+At position 248 to 325, the domain is characterized as KH type-2.
+At position 47 to 278, the domain is characterized as Radical SAM core.
+At position 541 to 818, the domain is characterized as Protein kinase.
+At position 893 to 1023, the domain is characterized as Guanylate cyclase.
+At position 228 to 266, the domain is characterized as LRRCT.
+At position 6 to 148, the domain is characterized as Jacalin-type lectin 1.
+At position 157 to 300, the domain is characterized as Jacalin-type lectin 2.
+At position 310 to 453, the domain is characterized as Jacalin-type lectin 3.
+At position 8 to 63, the domain is characterized as HTH lacI-type.
+At position 24 to 93, the domain is characterized as KH type-2.
+At position 151 to 255, the domain is characterized as PB1.
+At position 2061 to 2121, the domain is characterized as FYR N-terminal.
+At position 2122 to 2209, the domain is characterized as FYR C-terminal.
+At position 2291 to 2407, the domain is characterized as SET.
+At position 2415 to 2431, the domain is characterized as Post-SET.
+At position 1 to 43, the domain is characterized as Rab-GAP TBC; truncated.
+At position 323 to 370, the domain is characterized as GRAM 1.
+At position 374 to 470, the domain is characterized as PH.
+At position 464 to 495, the domain is characterized as GRAM 2.
+At position 834 to 900, the domain is characterized as GRAM 3.
+At position 222 to 474, the domain is characterized as ABC transporter 1.
+At position 918 to 1160, the domain is characterized as ABC transporter 2.
+At position 5 to 276, the domain is characterized as CN hydrolase.
+At position 8 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 240 to 425, the domain is characterized as FAD-binding PCMH-type.
+At position 399 to 460, the domain is characterized as PWWP.
+At position 243 to 346, the domain is characterized as Cadherin 3.
+At position 347 to 450, the domain is characterized as Cadherin 4.
+At position 451 to 560, the domain is characterized as Cadherin 5.
+At position 575 to 675, the domain is characterized as Cadherin 6.
+At position 253 to 348, the domain is characterized as Ig-like C2-type.
+At position 357 to 398, the domain is characterized as EGF-like.
+At position 7 to 124, the domain is characterized as MTTase N-terminal.
+At position 149 to 379, the domain is characterized as Radical SAM core.
+At position 74 to 197, the domain is characterized as RWD.
+At position 494 to 1027, the domain is characterized as Protein kinase.
+At position 1 to 65, the domain is characterized as HTH dtxR-type.
+At position 48 to 126, the domain is characterized as RRM 1.
+At position 136 to 213, the domain is characterized as RRM 2.
+At position 229 to 306, the domain is characterized as RRM 3.
+At position 332 to 462, the domain is characterized as RRM 4.
+At position 647 to 724, the domain is characterized as PABC.
+At position 180 to 232, the domain is characterized as KH.
+At position 250 to 338, the domain is characterized as PKD.
+At position 32 to 147, the domain is characterized as SCP.
+At position 101 to 227, the domain is characterized as Nudix hydrolase.
+At position 331 to 499, the domain is characterized as Helicase ATP-binding.
+At position 675 to 846, the domain is characterized as Helicase C-terminal.
+At position 151 to 253, the domain is characterized as Glutaredoxin 1.
+At position 287 to 389, the domain is characterized as Glutaredoxin 2.
+At position 394 to 491, the domain is characterized as Glutaredoxin 3.
+At position 760 to 842, the domain is characterized as DIX.
+At position 293 to 327, the domain is characterized as SAP.
+At position 109 to 302, the domain is characterized as ATP-grasp.
+At position 117 to 355, the domain is characterized as Radical SAM core.
+At position 22 to 182, the domain is characterized as RabBD.
+At position 605 to 691, the domain is characterized as PDZ.
+At position 742 to 865, the domain is characterized as C2 1.
+At position 1538 to 1656, the domain is characterized as C2 2.
+At position 99 to 268, the domain is characterized as PCI.
+At position 77 to 163, the domain is characterized as ZAD.
+At position 636 to 715, the domain is characterized as Cytochrome c.
+At position 2 to 213, the domain is characterized as RNase H type-2.
+At position 40 to 94, the domain is characterized as LysM.
+At position 346 to 409, the domain is characterized as S4 RNA-binding.
+At position 163 to 416, the domain is characterized as Protein kinase.
+At position 696 to 780, the domain is characterized as POLO box 1.
+At position 826 to 904, the domain is characterized as POLO box 2.
+At position 6 to 70, the domain is characterized as NAC-A/B.
+At position 286 to 460, the domain is characterized as Helicase ATP-binding.
+At position 490 to 634, the domain is characterized as Helicase C-terminal.
+At position 13 to 148, the domain is characterized as SprT-like.
+At position 83 to 398, the domain is characterized as Peptidase A1.
+At position 89 to 155, the domain is characterized as bZIP.
+At position 3 to 87, the domain is characterized as Acylphosphatase-like.
+At position 193 to 373, the domain is characterized as YrdC-like.
+At position 8 to 394, the domain is characterized as BRO1.
+At position 1192 to 1452, the domain is characterized as Tyrosine-protein phosphatase.
+At position 4 to 94, the domain is characterized as Chorismate mutase.
+At position 66 to 320, the domain is characterized as Protein kinase.
+At position 119 to 167, the domain is characterized as WAP.
+At position 547 to 827, the domain is characterized as Protein kinase.
+At position 10 to 236, the domain is characterized as Radical SAM core.
+At position 72 to 330, the domain is characterized as Protein kinase.
+At position 409 to 444, the domain is characterized as EF-hand 2.
+At position 445 to 480, the domain is characterized as EF-hand 3.
+At position 484 to 514, the domain is characterized as EF-hand 4.
+At position 1 to 219, the domain is characterized as PABS.
+At position 108 to 266, the domain is characterized as FCP1 homology.
+At position 188 to 280, the domain is characterized as GTD-binding.
+At position 98 to 168, the domain is characterized as J.
+At position 200 to 503, the domain is characterized as SEC63.
+At position 37 to 108, the domain is characterized as KRAB 1.
+At position 433 to 447, the domain is characterized as KRAB 2.
+At position 379 to 501, the domain is characterized as C2 1.
+At position 537 to 670, the domain is characterized as C2 2.
+At position 155 to 576, the domain is characterized as Myotubularin phosphatase.
+At position 1321 to 1631, the domain is characterized as PKS/mFAS DH.
+At position 1719 to 1796, the domain is characterized as Carrier.
+At position 22 to 251, the domain is characterized as ABC transmembrane type-2.
+At position 275 to 473, the domain is characterized as B30.2/SPRY.
+At position 38 to 137, the domain is characterized as Cadherin 1.
+At position 138 to 249, the domain is characterized as Cadherin 2.
+At position 250 to 356, the domain is characterized as Cadherin 3.
+At position 362 to 475, the domain is characterized as Cadherin 4.
+At position 476 to 579, the domain is characterized as Cadherin 5.
+At position 571 to 690, the domain is characterized as Cadherin 6.
+At position 376 to 445, the domain is characterized as PAS.
+At position 265 to 421, the domain is characterized as Cupin type-1.
+At position 47 to 610, the domain is characterized as Lipoxygenase.
+At position 361 to 562, the domain is characterized as MIF4G.
+At position 54 to 120, the domain is characterized as CBS 1.
+At position 214 to 275, the domain is characterized as CBS 2.
+At position 292 to 350, the domain is characterized as CBS 3.
+At position 374 to 433, the domain is characterized as CBS 4.
+At position 8 to 60, the domain is characterized as L27 1.
+At position 84 to 142, the domain is characterized as L27 2.
+At position 185 to 240, the domain is characterized as PDZ.
+At position 249 to 317, the domain is characterized as SH3.
+At position 374 to 561, the domain is characterized as Guanylate kinase-like.
+At position 147 to 251, the domain is characterized as HTH LytTR-type.
+At position 31 to 210, the domain is characterized as Radical SAM core.
+At position 254 to 584, the domain is characterized as Kinesin motor.
+At position 41 to 120, the domain is characterized as GIY-YIG.
+At position 230 to 265, the domain is characterized as UVR.
+At position 376 to 756, the domain is characterized as PIPK.
+At position 25 to 76, the domain is characterized as HTH myb-type 1.
+At position 77 to 131, the domain is characterized as HTH myb-type 2.
+At position 74 to 255, the domain is characterized as ABC transmembrane type-1.
+At position 34 to 156, the domain is characterized as Calponin-homology (CH).
+At position 197 to 270, the domain is characterized as GAR.
+At position 859 to 1111, the domain is characterized as ABC transporter 2.
+At position 1184 to 1398, the domain is characterized as ABC transmembrane type-2 2.
+At position 1 to 37, the domain is characterized as GH18.
+At position 256 to 316, the domain is characterized as PDZ.
+At position 218 to 237, the domain is characterized as UIM 1.
+At position 243 to 262, the domain is characterized as UIM 2.
+At position 100 to 135, the domain is characterized as Tify.
+At position 39 to 241, the domain is characterized as GH11.
+At position 300 to 335, the domain is characterized as CBM1.
+At position 52 to 74, the domain is characterized as Follistatin-like 1.
+At position 85 to 109, the domain is characterized as Follistatin-like 2.
+At position 117 to 139, the domain is characterized as Follistatin-like 3.
+At position 184 to 206, the domain is characterized as Follistatin-like 4.
+At position 215 to 234, the domain is characterized as Follistatin-like 5.
+At position 299 to 322, the domain is characterized as Follistatin-like 6.
+At position 36 to 49, the domain is characterized as CRIB.
+At position 80 to 115, the domain is characterized as ShKT.
+At position 198 to 347, the domain is characterized as MH1.
+At position 657 to 880, the domain is characterized as MH2.
+At position 18 to 470, the domain is characterized as Biotin carboxylation.
+At position 140 to 337, the domain is characterized as ATP-grasp.
+At position 557 to 824, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1094 to 1169, the domain is characterized as Biotinyl-binding.
+At position 38 to 173, the domain is characterized as C-type lectin.
+At position 77 to 388, the domain is characterized as IF rod.
+At position 18 to 219, the domain is characterized as Cytochrome b561.
+At position 34 to 150, the domain is characterized as GOLD.
+At position 234 to 409, the domain is characterized as Rho-GAP.
+At position 485 to 763, the domain is characterized as Protein kinase.
+At position 127 to 336, the domain is characterized as ATP-grasp.
+At position 228 to 554, the domain is characterized as G-alpha.
+At position 233 to 376, the domain is characterized as VPS9.
+At position 68 to 183, the domain is characterized as I-type lysozyme.
+At position 71 to 131, the domain is characterized as CBS 1.
+At position 136 to 193, the domain is characterized as CBS 2.
+At position 59 to 318, the domain is characterized as Protein kinase 1.
+At position 319 to 388, the domain is characterized as AGC-kinase C-terminal.
+At position 415 to 672, the domain is characterized as Protein kinase 2.
+At position 508 to 794, the domain is characterized as UvrD-like helicase C-terminal.
+At position 105 to 306, the domain is characterized as ATP-grasp.
+At position 402 to 485, the domain is characterized as Ig-like C2-type 3.
+At position 502 to 587, the domain is characterized as Ig-like C2-type 4.
+At position 611 to 699, the domain is characterized as Ig-like C2-type 5.
+At position 709 to 809, the domain is characterized as Ig-like C2-type 6.
+At position 1120 to 1208, the domain is characterized as Ig-like C2-type 7.
+At position 1260 to 1348, the domain is characterized as Ig-like C2-type 8.
+At position 1356 to 1449, the domain is characterized as Fibronectin type-III.
+At position 1486 to 1741, the domain is characterized as Protein kinase.
+At position 1831 to 1920, the domain is characterized as Ig-like C2-type 9.
+At position 1 to 73, the domain is characterized as HTH merR-type.
+At position 8 to 244, the domain is characterized as ABC transporter.
+At position 14 to 108, the domain is characterized as RH1.
+At position 121 to 197, the domain is characterized as RH2.
+At position 40 to 152, the domain is characterized as TBDR plug.
+At position 157 to 606, the domain is characterized as TBDR beta-barrel.
+At position 24 to 259, the domain is characterized as AB hydrolase-1.
+At position 30 to 245, the domain is characterized as Radical SAM core.
+At position 37 to 195, the domain is characterized as SIS.
+At position 56 to 102, the domain is characterized as Gla.
+At position 147 to 255, the domain is characterized as BTB.
+At position 1 to 35, the domain is characterized as LCN-type CS-alpha/beta.
+At position 1 to 90, the domain is characterized as Protein kinase.
+At position 301 to 465, the domain is characterized as SSD.
+At position 207 to 537, the domain is characterized as NACHT.
+At position 124 to 264, the domain is characterized as SIS.
+At position 4 to 191, the domain is characterized as RNase H type-2.
+At position 364 to 793, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1276 to 1582, the domain is characterized as PKS/mFAS DH.
+At position 1617 to 1694, the domain is characterized as Carrier 1.
+At position 1729 to 1806, the domain is characterized as Carrier 2.
+At position 145 to 339, the domain is characterized as ATP-grasp.
+At position 37 to 194, the domain is characterized as PPIase cyclophilin-type.
+At position 1039 to 1148, the domain is characterized as SEA.
+At position 51 to 133, the domain is characterized as Saposin B-type.
+At position 421 to 577, the domain is characterized as Exonuclease.
+At position 232 to 433, the domain is characterized as Helicase C-terminal.
+At position 53 to 153, the domain is characterized as SRCR 1.
+At position 192 to 292, the domain is characterized as SRCR 2.
+At position 323 to 423, the domain is characterized as SRCR 3.
+At position 454 to 551, the domain is characterized as SRCR 4.
+At position 582 to 682, the domain is characterized as SRCR 5.
+At position 713 to 813, the domain is characterized as SRCR 6.
+At position 821 to 921, the domain is characterized as SRCR 7.
+At position 951 to 1061, the domain is characterized as CUB 1.
+At position 1067 to 1170, the domain is characterized as SRCR 8.
+At position 1192 to 1301, the domain is characterized as CUB 2.
+At position 1310 to 1558, the domain is characterized as ZP.
+At position 106 to 135, the domain is characterized as EF-hand 2.
+At position 172 to 207, the domain is characterized as EF-hand 4.
+At position 591 to 659, the domain is characterized as CBS 1.
+At position 688 to 744, the domain is characterized as CBS 2.
+At position 1 to 115, the domain is characterized as HIT.
+At position 32 to 516, the domain is characterized as Sema.
+At position 581 to 669, the domain is characterized as Ig-like C2-type.
+At position 471 to 553, the domain is characterized as PDZ 2.
+At position 642 to 720, the domain is characterized as PDZ 3.
+At position 840 to 922, the domain is characterized as PDZ 4.
+At position 997 to 1093, the domain is characterized as PDZ 5.
+At position 1151 to 1233, the domain is characterized as PDZ 6.
+At position 47 to 162, the domain is characterized as MTTase N-terminal.
+At position 180 to 413, the domain is characterized as Radical SAM core.
+At position 513 to 573, the domain is characterized as Tudor 1.
+At position 706 to 763, the domain is characterized as Tudor 2.
+At position 401 to 509, the domain is characterized as Fe2OG dioxygenase.
+At position 204 to 400, the domain is characterized as Peptidase M12B.
+At position 12 to 103, the domain is characterized as ATP-cone.
+At position 65 to 107, the domain is characterized as EGF-like 2; calcium-binding.
+At position 108 to 149, the domain is characterized as EGF-like 3; calcium-binding.
+At position 292 to 323, the domain is characterized as EGF-like 4.
+At position 334 to 589, the domain is characterized as ZP.
+At position 426 to 741, the domain is characterized as NB-ARC.
+At position 737 to 849, the domain is characterized as CRC.
+At position 552 to 585, the domain is characterized as KOW.
+At position 33 to 95, the domain is characterized as Chitin-binding type-2.
+At position 86 to 267, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 266, the domain is characterized as Protein kinase.
+At position 218 to 271, the domain is characterized as HAMP.
+At position 276 to 512, the domain is characterized as Methyl-accepting transducer.
+At position 109 to 352, the domain is characterized as NR LBD.
+At position 3 to 94, the domain is characterized as Chorein N-terminal.
+At position 44 to 273, the domain is characterized as FAD-binding PCMH-type.
+At position 6 to 49, the domain is characterized as SpoVT-AbrB 1.
+At position 65 to 263, the domain is characterized as Peptidase M12A.
+At position 496 to 646, the domain is characterized as F5/8 type C.
+At position 264 to 300, the domain is characterized as LRRNT 2.
+At position 430 to 480, the domain is characterized as LRRCT 2.
+At position 497 to 533, the domain is characterized as LRRNT 3.
+At position 664 to 714, the domain is characterized as LRRCT 3.
+At position 718 to 754, the domain is characterized as LRRNT 4.
+At position 859 to 909, the domain is characterized as LRRCT 4.
+At position 918 to 955, the domain is characterized as EGF-like 1.
+At position 998 to 1034, the domain is characterized as EGF-like 3; calcium-binding.
+At position 1036 to 1074, the domain is characterized as EGF-like 4.
+At position 1076 to 1112, the domain is characterized as EGF-like 5; calcium-binding.
+At position 1121 to 1157, the domain is characterized as EGF-like 6.
+At position 1160 to 1333, the domain is characterized as Laminin G-like.
+At position 1332 to 1368, the domain is characterized as EGF-like 7.
+At position 1453 to 1528, the domain is characterized as CTCK.
+At position 22 to 209, the domain is characterized as Albumin 1.
+At position 51 to 154, the domain is characterized as FAD-binding FR-type.
+At position 174 to 432, the domain is characterized as Protein kinase.
+At position 42 to 236, the domain is characterized as PBC.
+At position 5 to 77, the domain is characterized as ACT.
+At position 227 to 273, the domain is characterized as G-patch.
+At position 7 to 262, the domain is characterized as Chorismate mutase.
+At position 190 to 240, the domain is characterized as bHLH.
+At position 15 to 125, the domain is characterized as Thioredoxin 1.
+At position 338 to 467, the domain is characterized as Thioredoxin 2.
+At position 6 to 115, the domain is characterized as Toprim.
+At position 42 to 107, the domain is characterized as NAC-A/B.
+At position 66 to 189, the domain is characterized as Plastocyanin-like 1.
+At position 198 to 356, the domain is characterized as Plastocyanin-like 2.
+At position 416 to 551, the domain is characterized as Plastocyanin-like 3.
+At position 704 to 1070, the domain is characterized as HECT.
+At position 43 to 161, the domain is characterized as MTTase N-terminal.
+At position 184 to 414, the domain is characterized as Radical SAM core.
+At position 70 to 390, the domain is characterized as G-alpha.
+At position 325 to 458, the domain is characterized as GGDEF.
+At position 80 to 134, the domain is characterized as HTH cro/C1-type.
+At position 10 to 85, the domain is characterized as S1-like.
+At position 243 to 316, the domain is characterized as RRM 1.
+At position 322 to 401, the domain is characterized as RRM 2.
+At position 113 to 270, the domain is characterized as Integrase catalytic.
+At position 486 to 625, the domain is characterized as Flavodoxin-like.
+At position 663 to 896, the domain is characterized as FAD-binding FR-type.
+At position 412 to 467, the domain is characterized as SOCS box.
+At position 154 to 311, the domain is characterized as Cupin type-1 1.
+At position 370 to 533, the domain is characterized as Cupin type-1 2.
+At position 226 to 497, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 316 to 599, the domain is characterized as ABC transporter 1.
+At position 619 to 948, the domain is characterized as ABC transporter 2.
+At position 473 to 680, the domain is characterized as MCM.
+At position 27 to 103, the domain is characterized as Inhibitor I9.
+At position 107 to 617, the domain is characterized as Peptidase S8.
+At position 367 to 459, the domain is characterized as PA.
+At position 787 to 980, the domain is characterized as TH1.
+At position 1092 to 1153, the domain is characterized as SH3.
+At position 282 to 488, the domain is characterized as Rab-GAP TBC.
+At position 272 to 389, the domain is characterized as PX.
+At position 84 to 378, the domain is characterized as AB hydrolase-1.
+At position 39 to 263, the domain is characterized as Radical SAM core.
+At position 1 to 66, the domain is characterized as J.
+At position 85 to 413, the domain is characterized as Protein kinase.
+At position 403 to 438, the domain is characterized as EF-hand 3.
+At position 330 to 459, the domain is characterized as Peptidase C51.
+At position 321 to 410, the domain is characterized as EH 1.
+At position 354 to 389, the domain is characterized as EF-hand 1.
+At position 661 to 750, the domain is characterized as EH 2.
+At position 32 to 84, the domain is characterized as Rhodanese.
+At position 31 to 289, the domain is characterized as Protein kinase.
+At position 938 to 1055, the domain is characterized as SET.
+At position 1064 to 1080, the domain is characterized as Post-SET.
+At position 70 to 366, the domain is characterized as AB hydrolase-1.
+At position 96 to 150, the domain is characterized as J.
+At position 493 to 686, the domain is characterized as SEC7.
+At position 726 to 841, the domain is characterized as PH.
+At position 9 to 92, the domain is characterized as RRM 1.
+At position 293 to 406, the domain is characterized as PAZ.
+At position 578 to 868, the domain is characterized as Piwi.
+At position 241 to 427, the domain is characterized as GATase cobBQ-type.
+At position 298 to 373, the domain is characterized as S1 motif 1.
+At position 380 to 455, the domain is characterized as S1 motif 2.
+At position 476 to 544, the domain is characterized as S1 motif 3.
+At position 561 to 630, the domain is characterized as S1 motif 4.
+At position 234 to 297, the domain is characterized as bZIP.
+At position 332 to 431, the domain is characterized as Rhodanese.
+At position 125 to 193, the domain is characterized as KH.
+At position 661 to 858, the domain is characterized as FtsK 1.
+At position 993 to 1177, the domain is characterized as FtsK 2.
+At position 32 to 74, the domain is characterized as Histone-fold.
+At position 37 to 235, the domain is characterized as Rab-GAP TBC.
+At position 26 to 355, the domain is characterized as Protein kinase.
+At position 71 to 169, the domain is characterized as Mis18.
+At position 21 to 126, the domain is characterized as Ig-like V-type 1; required for binding to polymeric IgA and IgM.
+At position 240 to 341, the domain is characterized as Ig-like V-type 3.
+At position 67 to 171, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 111 to 357, the domain is characterized as GS catalytic.
+At position 626 to 693, the domain is characterized as S1 motif.
+At position 8 to 122, the domain is characterized as PINc.
+At position 37 to 95, the domain is characterized as Chromo.
+At position 33 to 269, the domain is characterized as ABC transporter 1.
+At position 279 to 523, the domain is characterized as ABC transporter 2.
+At position 133 to 383, the domain is characterized as Protein kinase.
+At position 13 to 71, the domain is characterized as Tudor-knot.
+At position 168 to 517, the domain is characterized as MRG.
+At position 252 to 449, the domain is characterized as PCI.
+At position 1 to 76, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 497 to 563, the domain is characterized as FHA.
+At position 1542 to 1640, the domain is characterized as PH.
+At position 93 to 181, the domain is characterized as Ig-like C1-type.
+At position 14 to 89, the domain is characterized as ACT.
+At position 24 to 134, the domain is characterized as Ig-like V-type 1.
+At position 138 to 244, the domain is characterized as Ig-like V-type 2.
+At position 250 to 355, the domain is characterized as Ig-like C2-type.
+At position 143 to 172, the domain is characterized as IQ.
+At position 418 to 498, the domain is characterized as IPT/TIG.
+At position 957 to 984, the domain is characterized as IQ.
+At position 1 to 52, the domain is characterized as TRAM.
+At position 159 to 282, the domain is characterized as Fe2OG dioxygenase.
+At position 194 to 368, the domain is characterized as Exonuclease.
+At position 8 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 620 to 810, the domain is characterized as FtsK.
+At position 1 to 101, the domain is characterized as PTS EIIB type-2.
+At position 33 to 98, the domain is characterized as BTB.
+At position 1 to 110, the domain is characterized as IF rod.
+At position 12 to 179, the domain is characterized as TIR.
+At position 315 to 407, the domain is characterized as SH2.
+At position 135 to 236, the domain is characterized as BACK.
+At position 91 to 266, the domain is characterized as Helicase ATP-binding.
+At position 294 to 439, the domain is characterized as Helicase C-terminal.
+At position 38 to 151, the domain is characterized as tRNA-binding.
+At position 398 to 474, the domain is characterized as B5.
+At position 694 to 787, the domain is characterized as FDX-ACB.
+At position 85 to 147, the domain is characterized as Z-binding 2.
+At position 256 to 376, the domain is characterized as Sox C-terminal.
+At position 10 to 135, the domain is characterized as RNase III.
+At position 42 to 241, the domain is characterized as Cupin type-1 1.
+At position 302 to 451, the domain is characterized as Cupin type-1 2.
+At position 207 to 394, the domain is characterized as Helicase ATP-binding.
+At position 416 to 570, the domain is characterized as Helicase C-terminal.
+At position 60 to 118, the domain is characterized as HTH myb-type 1.
+At position 119 to 170, the domain is characterized as HTH myb-type 2.
+At position 172 to 223, the domain is characterized as Myb-like.
+At position 30 to 302, the domain is characterized as CN hydrolase.
+At position 47 to 284, the domain is characterized as AB hydrolase-1.
+At position 200 to 275, the domain is characterized as SPOR.
+At position 9 to 147, the domain is characterized as MPN.
+At position 83 to 325, the domain is characterized as ABC transporter.
+At position 948 to 1383, the domain is characterized as CBP/p300-type HAT.
+At position 18 to 106, the domain is characterized as N-acetyltransferase.
+At position 40 to 216, the domain is characterized as Helicase ATP-binding.
+At position 240 to 387, the domain is characterized as Helicase C-terminal.
+At position 182 to 210, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 211 to 241, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 36 to 106, the domain is characterized as HMA.
+At position 141 to 234, the domain is characterized as PpiC.
+At position 196 to 439, the domain is characterized as NR LBD.
+At position 295 to 573, the domain is characterized as Protein kinase.
+At position 49 to 85, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 278 to 506, the domain is characterized as Lon N-terminal.
+At position 505 to 614, the domain is characterized as CULT.
+At position 74 to 103, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 41 to 161, the domain is characterized as C-type lectin.
+At position 51 to 157, the domain is characterized as Fe2OG dioxygenase.
+At position 144 to 454, the domain is characterized as NB-ARC.
+At position 101 to 129, the domain is characterized as EGF-like.
+At position 132 to 248, the domain is characterized as CUB.
+At position 703 to 748, the domain is characterized as PSI 1.
+At position 755 to 794, the domain is characterized as PSI 2.
+At position 795 to 919, the domain is characterized as C-type lectin.
+At position 932 to 983, the domain is characterized as PSI 3.
+At position 986 to 1061, the domain is characterized as PSI 4.
+At position 1063 to 1108, the domain is characterized as Laminin EGF-like 1.
+At position 1109 to 1157, the domain is characterized as Laminin EGF-like 2.
+At position 578 to 672, the domain is characterized as PH 1.
+At position 687 to 796, the domain is characterized as PH 2.
+At position 832 to 986, the domain is characterized as MyTH4.
+At position 997 to 1333, the domain is characterized as FERM.
+At position 55 to 228, the domain is characterized as Laminin G-like.
+At position 1 to 237, the domain is characterized as Peptidase S1.
+At position 6 to 294, the domain is characterized as SET.
+At position 26 to 171, the domain is characterized as Tyrosine-protein phosphatase.
+At position 78 to 111, the domain is characterized as WW 1.
+At position 123 to 156, the domain is characterized as WW 2.
+At position 224 to 282, the domain is characterized as FF 1.
+At position 295 to 349, the domain is characterized as FF 2.
+At position 353 to 422, the domain is characterized as FF 3.
+At position 442 to 502, the domain is characterized as FF 4.
+At position 507 to 562, the domain is characterized as FF 5.
+At position 578 to 632, the domain is characterized as FF 6.
+At position 676 to 705, the domain is characterized as IQ.
+At position 296 to 436, the domain is characterized as N-acetyltransferase.
+At position 210 to 270, the domain is characterized as HTH myb-type.
+At position 35 to 295, the domain is characterized as Alpha-carbonic anhydrase.
+At position 6 to 85, the domain is characterized as PDZ.
+At position 604 to 710, the domain is characterized as tRNA-binding.
+At position 291 to 527, the domain is characterized as NR LBD.
+At position 40 to 69, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 49 to 287, the domain is characterized as Ras-GEF.
+At position 457 to 569, the domain is characterized as PH.
+At position 557 to 826, the domain is characterized as Protein kinase.
+At position 898 to 1028, the domain is characterized as Guanylate cyclase.
+At position 2 to 78, the domain is characterized as S1-like.
+At position 35 to 165, the domain is characterized as Cadherin 1.
+At position 166 to 275, the domain is characterized as Cadherin 2.
+At position 276 to 396, the domain is characterized as Cadherin 3.
+At position 397 to 500, the domain is characterized as Cadherin 4.
+At position 382 to 623, the domain is characterized as NR LBD.
+At position 12 to 332, the domain is characterized as Hcy-binding.
+At position 363 to 624, the domain is characterized as Pterin-binding.
+At position 655 to 749, the domain is characterized as B12-binding N-terminal.
+At position 752 to 888, the domain is characterized as B12-binding.
+At position 904 to 1234, the domain is characterized as AdoMet activation.
+At position 445 to 523, the domain is characterized as GRAM.
+At position 219 to 278, the domain is characterized as Chromo.
+At position 410 to 474, the domain is characterized as Pre-SET.
+At position 477 to 603, the domain is characterized as SET.
+At position 619 to 635, the domain is characterized as Post-SET.
+At position 1410 to 1955, the domain is characterized as FAT.
+At position 2060 to 2363, the domain is characterized as PI3K/PI4K catalytic.
+At position 2347 to 2379, the domain is characterized as FATC.
+At position 50 to 285, the domain is characterized as Thioredoxin.
+At position 550 to 720, the domain is characterized as tr-type G.
+At position 127 to 422, the domain is characterized as NR LBD.
+At position 13 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 171 to 260, the domain is characterized as BRCT 1.
+At position 266 to 354, the domain is characterized as BRCT 2.
+At position 452 to 641, the domain is characterized as DH.
+At position 675 to 794, the domain is characterized as PH.
+At position 249 to 547, the domain is characterized as YjeF C-terminal.
+At position 42 to 222, the domain is characterized as PCI.
+At position 159 to 267, the domain is characterized as Fe2OG dioxygenase.
+At position 969 to 1000, the domain is characterized as Bromo.
+At position 138 to 180, the domain is characterized as F-box.
+At position 7 to 143, the domain is characterized as HTH marR-type.
+At position 101 to 259, the domain is characterized as CP-type G.
+At position 220 to 416, the domain is characterized as Pentraxin (PTX).
+At position 10 to 200, the domain is characterized as RNase H type-2.
+At position 29 to 96, the domain is characterized as HMA.
+At position 261 to 354, the domain is characterized as CobW C-terminal.
+At position 455 to 513, the domain is characterized as Tudor 1.
+At position 641 to 696, the domain is characterized as Tudor 2.
+At position 1062 to 1122, the domain is characterized as Tudor 3.
+At position 1355 to 1414, the domain is characterized as Tudor 4.
+At position 1662 to 1718, the domain is characterized as Tudor 5.
+At position 1839 to 1898, the domain is characterized as Tudor 6.
+At position 2023 to 2082, the domain is characterized as Tudor 7.
+At position 2211 to 2269, the domain is characterized as Tudor 8.
+At position 2392 to 2451, the domain is characterized as Tudor 9.
+At position 272 to 332, the domain is characterized as CBS 1.
+At position 354 to 412, the domain is characterized as CBS 2.
+At position 427 to 489, the domain is characterized as CBS 3.
+At position 501 to 559, the domain is characterized as CBS 4.
+At position 151 to 292, the domain is characterized as Jacalin-type lectin 2.
+At position 26 to 136, the domain is characterized as Ig-like V-type 1.
+At position 141 to 251, the domain is characterized as Ig-like V-type 2.
+At position 268 to 343, the domain is characterized as Ig-like C2-type 1.
+At position 357 to 436, the domain is characterized as Ig-like C2-type 2.
+At position 443 to 534, the domain is characterized as Ig-like C2-type 3.
+At position 30 to 126, the domain is characterized as Cytochrome c.
+At position 32 to 109, the domain is characterized as RRM 1.
+At position 123 to 198, the domain is characterized as RRM 2.
+At position 7 to 126, the domain is characterized as Arf-GAP.
+At position 129 to 230, the domain is characterized as PH 1.
+At position 252 to 356, the domain is characterized as PH 2.
+At position 117 to 401, the domain is characterized as Protein kinase.
+At position 78 to 368, the domain is characterized as Radical SAM core.
+At position 392 to 547, the domain is characterized as N-acetyltransferase.
+At position 90 to 159, the domain is characterized as S4 RNA-binding.
+At position 11 to 227, the domain is characterized as ABC transporter.
+At position 36 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 8 to 130, the domain is characterized as RCK N-terminal.
+At position 139 to 222, the domain is characterized as RCK C-terminal.
+At position 494 to 574, the domain is characterized as Ras-associating.
+At position 1173 to 1439, the domain is characterized as PPM-type phosphatase.
+At position 1483 to 1620, the domain is characterized as Guanylate cyclase.
+At position 3 to 122, the domain is characterized as MTTase N-terminal.
+At position 148 to 392, the domain is characterized as Radical SAM core.
+At position 395 to 452, the domain is characterized as TRAM.
+At position 125 to 295, the domain is characterized as Helicase ATP-binding.
+At position 306 to 474, the domain is characterized as Helicase C-terminal.
+At position 9 to 260, the domain is characterized as ABC transporter.
+At position 61 to 301, the domain is characterized as ABC transporter.
+At position 386 to 641, the domain is characterized as ABC transmembrane type-2.
+At position 133 to 159, the domain is characterized as PLD phosphodiesterase 1.
+At position 352 to 379, the domain is characterized as PLD phosphodiesterase 2.
+At position 2 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 32 to 137, the domain is characterized as sHSP.
+At position 1 to 124, the domain is characterized as ApaG.
+At position 3 to 121, the domain is characterized as N-terminal Ras-GEF.
+At position 149 to 382, the domain is characterized as Ras-GEF.
+At position 418 to 453, the domain is characterized as EF-hand 1.
+At position 455 to 482, the domain is characterized as EF-hand 2.
+At position 7 to 47, the domain is characterized as HTH cro/C1-type.
+At position 231 to 404, the domain is characterized as EngA-type G 2.
+At position 405 to 489, the domain is characterized as KH-like.
+At position 175 to 349, the domain is characterized as Helicase ATP-binding.
+At position 506 to 663, the domain is characterized as Helicase C-terminal.
+At position 261 to 396, the domain is characterized as Plus3.
+At position 189 to 477, the domain is characterized as Protein kinase.
+At position 9 to 213, the domain is characterized as YjeF N-terminal.
+At position 217 to 499, the domain is characterized as YjeF C-terminal.
+At position 65 to 181, the domain is characterized as C2 1.
+At position 225 to 356, the domain is characterized as C2 2.
+At position 810 to 937, the domain is characterized as C2 3.
+At position 969 to 1099, the domain is characterized as C2 4.
+At position 1338 to 1457, the domain is characterized as C2 5.
+At position 1578 to 1729, the domain is characterized as C2 6.
+At position 29 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 1213 to 1269, the domain is characterized as DEK-C.
+At position 1 to 40, the domain is characterized as Core-binding (CB).
+At position 58 to 231, the domain is characterized as Tyr recombinase.
+At position 508 to 808, the domain is characterized as Protein kinase.
+At position 878 to 1008, the domain is characterized as Guanylate cyclase.
+At position 377 to 515, the domain is characterized as Thioredoxin.
+At position 100 to 327, the domain is characterized as Radical SAM core.
+At position 35 to 112, the domain is characterized as Inhibitor I9.
+At position 117 to 579, the domain is characterized as Peptidase S8.
+At position 355 to 437, the domain is characterized as PA.
+At position 17 to 221, the domain is characterized as Peptidase M12B.
+At position 40 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 81 to 673, the domain is characterized as Protein kinase.
+At position 21 to 101, the domain is characterized as GS beta-grasp.
+At position 108 to 370, the domain is characterized as GS catalytic.
+At position 805 to 984, the domain is characterized as DH.
+At position 996 to 1104, the domain is characterized as PH.
+At position 20 to 139, the domain is characterized as C-type lectin.
+At position 245 to 367, the domain is characterized as SET.
+At position 64 to 212, the domain is characterized as Cupin type-1.
+At position 55 to 182, the domain is characterized as N-acetyltransferase.
+At position 199 to 276, the domain is characterized as KH type-2.
+At position 22 to 105, the domain is characterized as ACT 1.
+At position 111 to 194, the domain is characterized as ACT 2.
+At position 243 to 322, the domain is characterized as ACT 3.
+At position 570 to 653, the domain is characterized as Death.
+At position 99 to 327, the domain is characterized as Radical SAM core.
+At position 45 to 342, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 42 to 117, the domain is characterized as Lipoyl-binding.
+At position 38 to 306, the domain is characterized as Protein kinase.
+At position 21 to 118, the domain is characterized as Fibronectin type-III 1.
+At position 119 to 228, the domain is characterized as Fibronectin type-III 2.
+At position 10 to 89, the domain is characterized as GIY-YIG.
+At position 387 to 459, the domain is characterized as TRAM.
+At position 114 to 238, the domain is characterized as RCK N-terminal.
+At position 37 to 72, the domain is characterized as EF-hand.
+At position 82 to 173, the domain is characterized as K-box.
+At position 300 to 461, the domain is characterized as Helicase ATP-binding.
+At position 15 to 143, the domain is characterized as Cyclin N-terminal.
+At position 24 to 327, the domain is characterized as Peptidase S8.
+At position 112 to 368, the domain is characterized as ABC transporter 1.
+At position 789 to 1032, the domain is characterized as ABC transporter 2.
+At position 100 to 315, the domain is characterized as Fibrinogen C-terminal.
+At position 399 to 516, the domain is characterized as NlpC/P60.
+At position 297 to 521, the domain is characterized as ABC transmembrane type-1.
+At position 29 to 150, the domain is characterized as Bulb-type lectin.
+At position 292 to 331, the domain is characterized as EGF-like.
+At position 350 to 431, the domain is characterized as PAN.
+At position 525 to 814, the domain is characterized as Protein kinase.
+At position 309 to 469, the domain is characterized as PNPLA.
+At position 128 to 307, the domain is characterized as JmjC.
+At position 4 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 200 to 217, the domain is characterized as R.
+At position 64 to 112, the domain is characterized as F-box.
+At position 126 to 442, the domain is characterized as IF rod.
+At position 1346 to 1577, the domain is characterized as ABC transporter 1.
+At position 2254 to 2489, the domain is characterized as ABC transporter 2.
+At position 13 to 204, the domain is characterized as RNase H type-2.
+At position 334 to 477, the domain is characterized as Jacalin-type lectin 3.
+At position 490 to 633, the domain is characterized as Jacalin-type lectin 4.
+At position 31 to 117, the domain is characterized as Acylphosphatase-like.
+At position 196 to 371, the domain is characterized as Helicase ATP-binding.
+At position 399 to 544, the domain is characterized as Helicase C-terminal.
+At position 98 to 155, the domain is characterized as S4 RNA-binding.
+At position 64 to 138, the domain is characterized as U-box.
+At position 682 to 757, the domain is characterized as Smr.
+At position 182 to 225, the domain is characterized as CAP-Gly.
+At position 1 to 281, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 25 to 465, the domain is characterized as Hexokinase.
+At position 9 to 95, the domain is characterized as Acylphosphatase-like.
+At position 15 to 71, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 909 to 1003, the domain is characterized as PH 1.
+At position 1017 to 1124, the domain is characterized as PH 2.
+At position 1159 to 1378, the domain is characterized as MyTH4.
+At position 1389 to 1712, the domain is characterized as FERM.
+At position 145 to 267, the domain is characterized as Cyclin N-terminal.
+At position 45 to 109, the domain is characterized as SH3.
+At position 137 to 405, the domain is characterized as Protein kinase.
+At position 216 to 265, the domain is characterized as LRRCT 1.
+At position 331 to 373, the domain is characterized as LRRNT.
+At position 54 to 109, the domain is characterized as F-box.
+At position 66 to 88, the domain is characterized as Follistatin-like.
+At position 84 to 146, the domain is characterized as Kazal-like.
+At position 256 to 291, the domain is characterized as EF-hand.
+At position 21 to 203, the domain is characterized as Eph LBD.
+At position 622 to 885, the domain is characterized as Protein kinase.
+At position 914 to 978, the domain is characterized as SAM.
+At position 144 to 405, the domain is characterized as Protein kinase.
+At position 26 to 60, the domain is characterized as EF-hand.
+At position 114 to 257, the domain is characterized as PI-PLC X-box.
+At position 333 to 449, the domain is characterized as PI-PLC Y-box.
+At position 449 to 579, the domain is characterized as C2.
+At position 133 to 199, the domain is characterized as Chitin-binding type R&R.
+At position 237 to 495, the domain is characterized as Protein kinase.
+At position 597 to 707, the domain is characterized as SH2.
+At position 129 to 263, the domain is characterized as Fatty acid hydroxylase.
+At position 11 to 110, the domain is characterized as HTH hxlR-type.
+At position 25 to 177, the domain is characterized as C2 PI3K-type.
+At position 274 to 449, the domain is characterized as PIK helical.
+At position 532 to 799, the domain is characterized as PI3K/PI4K catalytic.
+At position 224 to 267, the domain is characterized as CUE.
+At position 322 to 361, the domain is characterized as UBA.
+At position 241 to 490, the domain is characterized as CN hydrolase.
+At position 226 to 300, the domain is characterized as U-box.
+At position 46 to 121, the domain is characterized as Cytochrome b5 heme-binding.
+At position 129 to 228, the domain is characterized as Fibronectin type-III 2.
+At position 231 to 331, the domain is characterized as Fibronectin type-III 3.
+At position 333 to 434, the domain is characterized as Fibronectin type-III 4.
+At position 263 to 311, the domain is characterized as FBD.
+At position 39 to 79, the domain is characterized as Chaplin 1.
+At position 119 to 159, the domain is characterized as Chaplin 2.
+At position 101 to 347, the domain is characterized as PPM-type phosphatase.
+At position 181 to 254, the domain is characterized as N-acetyltransferase.
+At position 513 to 547, the domain is characterized as TSP type-1.
+At position 128 to 418, the domain is characterized as NR LBD.
+At position 43 to 81, the domain is characterized as Collagen-like.
+At position 85 to 215, the domain is characterized as C1q.
+At position 24 to 506, the domain is characterized as Sema.
+At position 508 to 558, the domain is characterized as PSI 1.
+At position 654 to 701, the domain is characterized as PSI 2.
+At position 802 to 855, the domain is characterized as PSI 3.
+At position 857 to 951, the domain is characterized as IPT/TIG 1.
+At position 953 to 1036, the domain is characterized as IPT/TIG 2.
+At position 1039 to 1138, the domain is characterized as IPT/TIG 3.
+At position 1141 to 1229, the domain is characterized as IPT/TIG 4.
+At position 6 to 189, the domain is characterized as ABC transporter.
+At position 4 to 250, the domain is characterized as F-BAR.
+At position 580 to 848, the domain is characterized as MHD.
+At position 124 to 288, the domain is characterized as PINIT.
+At position 81 to 213, the domain is characterized as Toprim.
+At position 14 to 200, the domain is characterized as tr-type G.
+At position 460 to 582, the domain is characterized as HD.
+At position 701 to 779, the domain is characterized as ACT 1.
+At position 809 to 878, the domain is characterized as ACT 2.
+At position 542 to 705, the domain is characterized as Helicase ATP-binding.
+At position 727 to 902, the domain is characterized as Helicase C-terminal.
+At position 1 to 148, the domain is characterized as PPIase cyclophilin-type.
+At position 203 to 266, the domain is characterized as KH.
+At position 434 to 702, the domain is characterized as Protein kinase.
+At position 55 to 217, the domain is characterized as SIS.
+At position 36 to 121, the domain is characterized as Inhibitor I9.
+At position 496 to 515, the domain is characterized as UIM.
+At position 316 to 467, the domain is characterized as PI-PLC X-box.
+At position 540 to 656, the domain is characterized as PI-PLC Y-box.
+At position 656 to 786, the domain is characterized as C2.
+At position 5 to 123, the domain is characterized as Calponin-homology (CH).
+At position 44 to 349, the domain is characterized as Protein kinase.
+At position 1 to 159, the domain is characterized as PCI.
+At position 49 to 548, the domain is characterized as Sema.
+At position 893 to 977, the domain is characterized as IPT/TIG 1.
+At position 983 to 1065, the domain is characterized as IPT/TIG 2.
+At position 1071 to 1145, the domain is characterized as IPT/TIG 3.
+At position 244 to 444, the domain is characterized as Helicase ATP-binding.
+At position 477 to 645, the domain is characterized as Helicase C-terminal.
+At position 495 to 656, the domain is characterized as SSD.
+At position 39 to 177, the domain is characterized as Nudix hydrolase.
+At position 181 to 273, the domain is characterized as ARID.
+At position 356 to 464, the domain is characterized as REKLES.
+At position 11 to 177, the domain is characterized as Ku.
+At position 147 to 287, the domain is characterized as PPC.
+At position 32 to 92, the domain is characterized as 4Fe-4S.
+At position 133 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 206 to 237, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 239 to 269, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 157 to 232, the domain is characterized as H15 1.
+At position 255 to 330, the domain is characterized as H15 2.
+At position 337 to 413, the domain is characterized as H15 3.
+At position 539 to 600, the domain is characterized as SAM.
+At position 26 to 89, the domain is characterized as SAM.
+At position 143 to 296, the domain is characterized as HD.
+At position 196 to 261, the domain is characterized as KH 1.
+At position 277 to 344, the domain is characterized as KH 2.
+At position 409 to 474, the domain is characterized as KH 3.
+At position 491 to 557, the domain is characterized as KH 4.
+At position 1 to 107, the domain is characterized as PX.
+At position 30 to 86, the domain is characterized as Tudor-knot.
+At position 168 to 446, the domain is characterized as MYST-type HAT.
+At position 35 to 275, the domain is characterized as Radical SAM core.
+At position 440 to 514, the domain is characterized as PAS.
+At position 20 to 114, the domain is characterized as Ig-like V-type.
+At position 135 to 176, the domain is characterized as EGF-like; calcium-binding.
+At position 247 to 292, the domain is characterized as Collagen-like 1.
+At position 302 to 335, the domain is characterized as Collagen-like 2.
+At position 375 to 444, the domain is characterized as TRAM.
+At position 24 to 150, the domain is characterized as VIT.
+At position 283 to 469, the domain is characterized as VWFA.
+At position 430 to 602, the domain is characterized as tr-type G.
+At position 185 to 715, the domain is characterized as USP.
+At position 717 to 810, the domain is characterized as DUSP 1.
+At position 818 to 921, the domain is characterized as DUSP 2.
+At position 43 to 327, the domain is characterized as FERM.
+At position 610 to 693, the domain is characterized as BRCT.
+At position 176 to 299, the domain is characterized as Fatty acid hydroxylase.
+At position 20 to 111, the domain is characterized as Ig-like C1-type.
+At position 237 to 272, the domain is characterized as EF-hand 1.
+At position 289 to 324, the domain is characterized as EF-hand 2.
+At position 1 to 438, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 452 to 700, the domain is characterized as UvrD-like helicase C-terminal.
+At position 27 to 90, the domain is characterized as SLH 1.
+At position 92 to 155, the domain is characterized as SLH 2.
+At position 156 to 204, the domain is characterized as SLH 3.
+At position 47 to 272, the domain is characterized as Peptidase S1.
+At position 87 to 163, the domain is characterized as Biotinyl-binding.
+At position 1 to 149, the domain is characterized as N-acetyltransferase.
+At position 426 to 750, the domain is characterized as PDEase.
+At position 21 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 219, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 304, the domain is characterized as Ig-like C2-type 3.
+At position 309 to 391, the domain is characterized as Ig-like C2-type 4.
+At position 395 to 497, the domain is characterized as Ig-like C2-type 5.
+At position 1 to 156, the domain is characterized as Macro.
+At position 13 to 108, the domain is characterized as Chorein N-terminal.
+At position 497 to 560, the domain is characterized as bZIP.
+At position 1419 to 1703, the domain is characterized as Autotransporter.
+At position 31 to 76, the domain is characterized as F-box.
+At position 454 to 549, the domain is characterized as Fibronectin type-III 1.
+At position 553 to 648, the domain is characterized as Fibronectin type-III 2.
+At position 650 to 741, the domain is characterized as Fibronectin type-III 3.
+At position 745 to 842, the domain is characterized as Fibronectin type-III 4.
+At position 914 to 1007, the domain is characterized as Fibronectin type-III 5.
+At position 1017 to 1103, the domain is characterized as Fibronectin type-III 6.
+At position 1104 to 1199, the domain is characterized as Fibronectin type-III 7.
+At position 1202 to 1299, the domain is characterized as Fibronectin type-III 8.
+At position 25 to 55, the domain is characterized as LRRNT.
+At position 88 to 372, the domain is characterized as ABC transmembrane type-1.
+At position 430 to 697, the domain is characterized as ABC transporter.
+At position 340 to 406, the domain is characterized as SAM.
+At position 32 to 352, the domain is characterized as GH10.
+At position 18 to 297, the domain is characterized as PH 1.
+At position 111 to 194, the domain is characterized as PDZ.
+At position 321 to 432, the domain is characterized as PH 2.
+At position 481 to 537, the domain is characterized as SU.
+At position 97 to 154, the domain is characterized as CBS 1.
+At position 155 to 211, the domain is characterized as CBS 2.
+At position 213 to 353, the domain is characterized as TrmE-type G.
+At position 782 to 869, the domain is characterized as LRRCT.
+At position 1507 to 1566, the domain is characterized as MucBP 1.
+At position 1572 to 1631, the domain is characterized as MucBP 2.
+At position 1641 to 1702, the domain is characterized as MucBP 3.
+At position 63 to 113, the domain is characterized as F-box.
+At position 777 to 1036, the domain is characterized as Protein kinase.
+At position 1037 to 1088, the domain is characterized as AGC-kinase C-terminal.
+At position 41 to 70, the domain is characterized as IQ.
+At position 794 to 1142, the domain is characterized as HECT.
+At position 43 to 129, the domain is characterized as PNT.
+At position 26 to 151, the domain is characterized as Cyclin N-terminal 1.
+At position 158 to 241, the domain is characterized as Cyclin N-terminal 2.
+At position 36 to 254, the domain is characterized as L-type lectin-like.
+At position 253 to 330, the domain is characterized as POU-specific.
+At position 5 to 141, the domain is characterized as RNase H type-1.
+At position 17 to 100, the domain is characterized as Doublecortin 1.
+At position 139 to 221, the domain is characterized as Doublecortin 2.
+At position 105 to 302, the domain is characterized as ATP-grasp.
+At position 365 to 400, the domain is characterized as UVR.
+At position 126 to 570, the domain is characterized as Kinesin motor.
+At position 1 to 150, the domain is characterized as UBC core.
+At position 11 to 97, the domain is characterized as FAR1.
+At position 212 to 308, the domain is characterized as MULE.
+At position 1171 to 1288, the domain is characterized as SET.
+At position 1297 to 1313, the domain is characterized as Post-SET.
+At position 232 to 278, the domain is characterized as EGF-like 1.
+At position 279 to 325, the domain is characterized as EGF-like 2; calcium-binding.
+At position 410 to 693, the domain is characterized as Protein kinase.
+At position 20 to 258, the domain is characterized as ABC transporter.
+At position 199 to 527, the domain is characterized as Protein kinase.
+At position 56 to 163, the domain is characterized as Rieske.
+At position 164 to 217, the domain is characterized as HAMP.
+At position 236 to 476, the domain is characterized as Methyl-accepting transducer.
+At position 231 to 280, the domain is characterized as HAMP.
+At position 289 to 359, the domain is characterized as PAS.
+At position 424 to 654, the domain is characterized as Histidine kinase.
+At position 237 to 284, the domain is characterized as GRAM 1.
+At position 285 to 384, the domain is characterized as PH.
+At position 714 to 817, the domain is characterized as GRAM 2.
+At position 33 to 149, the domain is characterized as Plastocyanin-like 1.
+At position 159 to 307, the domain is characterized as Plastocyanin-like 2.
+At position 411 to 552, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 118, the domain is characterized as Nudix hydrolase.
+At position 217 to 322, the domain is characterized as HD.
+At position 18 to 280, the domain is characterized as Protein kinase.
+At position 442 to 508, the domain is characterized as PASTA 2.
+At position 509 to 576, the domain is characterized as PASTA 3.
+At position 577 to 641, the domain is characterized as PASTA 4.
+At position 128 to 259, the domain is characterized as HD.
+At position 20 to 145, the domain is characterized as CMP/dCMP-type deaminase.
+At position 163 to 209, the domain is characterized as F-box.
+At position 121 to 164, the domain is characterized as Collagen-like 1.
+At position 192 to 247, the domain is characterized as Collagen-like 2.
+At position 249 to 308, the domain is characterized as Collagen-like 3.
+At position 311 to 370, the domain is characterized as Collagen-like 4.
+At position 373 to 425, the domain is characterized as Collagen-like 5.
+At position 529 to 588, the domain is characterized as Collagen-like 7.
+At position 589 to 648, the domain is characterized as Collagen-like 8.
+At position 18 to 256, the domain is characterized as ABC transporter.
+At position 1050 to 1276, the domain is characterized as Histidine kinase.
+At position 1519 to 1633, the domain is characterized as Response regulatory.
+At position 306 to 325, the domain is characterized as UIM 2.
+At position 31 to 93, the domain is characterized as LIM zinc-binding 1.
+At position 94 to 154, the domain is characterized as LIM zinc-binding 2.
+At position 174 to 274, the domain is characterized as PDZ.
+At position 401 to 686, the domain is characterized as Protein kinase.
+At position 159 to 355, the domain is characterized as OBG-type G.
+At position 504 to 618, the domain is characterized as PH 1.
+At position 831 to 902, the domain is characterized as RBD.
+At position 911 to 997, the domain is characterized as PDZ.
+At position 1120 to 1314, the domain is characterized as DH.
+At position 276 to 533, the domain is characterized as GP-PDE.
+At position 50 to 349, the domain is characterized as Rab-GAP TBC.
+At position 15 to 228, the domain is characterized as HORMA.
+At position 351 to 449, the domain is characterized as SWIRM.
+At position 171 to 206, the domain is characterized as EF-hand 3.
+At position 207 to 242, the domain is characterized as EF-hand 4.
+At position 9 to 150, the domain is characterized as RNase H type-1.
+At position 259 to 442, the domain is characterized as GAF.
+At position 661 to 732, the domain is characterized as PAS 1.
+At position 795 to 866, the domain is characterized as PAS 2.
+At position 943 to 1161, the domain is characterized as Histidine kinase.
+At position 443 to 517, the domain is characterized as GW 1.
+At position 519 to 593, the domain is characterized as GW 2.
+At position 612 to 686, the domain is characterized as GW 3.
+At position 688 to 762, the domain is characterized as GW 4.
+At position 784 to 859, the domain is characterized as GW 5.
+At position 861 to 936, the domain is characterized as GW 6.
+At position 943 to 1017, the domain is characterized as GW 7.
+At position 194 to 292, the domain is characterized as HTH araC/xylS-type.
+At position 102 to 181, the domain is characterized as Kringle 1.
+At position 274 to 352, the domain is characterized as Kringle 3.
+At position 375 to 454, the domain is characterized as Kringle 4.
+At position 480 to 560, the domain is characterized as Kringle 5.
+At position 582 to 810, the domain is characterized as Peptidase S1.
+At position 35 to 191, the domain is characterized as Ferritin-like diiron.
+At position 16 to 135, the domain is characterized as RWD.
+At position 107 to 322, the domain is characterized as Radical SAM core.
+At position 1 to 115, the domain is characterized as MSP.
+At position 477 to 612, the domain is characterized as Jacalin-type lectin.
+At position 166 to 409, the domain is characterized as Protein kinase.
+At position 253 to 430, the domain is characterized as GATase cobBQ-type.
+At position 87 to 277, the domain is characterized as CBM11.
+At position 17 to 254, the domain is characterized as ABC transporter.
+At position 313 to 377, the domain is characterized as Mop.
+At position 152 to 218, the domain is characterized as S5 DRBM.
+At position 622 to 658, the domain is characterized as UVR.
+At position 46 to 127, the domain is characterized as SCAN box.
+At position 237 to 308, the domain is characterized as KRAB.
+At position 50 to 100, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 121 to 171, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 213 to 263, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 346 to 585, the domain is characterized as Hflx-type G.
+At position 69 to 313, the domain is characterized as Peptidase S1.
+At position 167 to 360, the domain is characterized as Ras-GAP.
+At position 411 to 507, the domain is characterized as PH.
+At position 34 to 348, the domain is characterized as G-alpha.
+At position 16 to 108, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 114 to 213, the domain is characterized as FAD-binding FR-type.
+At position 114 to 157, the domain is characterized as LysM.
+At position 781 to 942, the domain is characterized as TLDc.
+At position 44 to 79, the domain is characterized as ShKT.
+At position 25 to 92, the domain is characterized as Histone-fold.
+At position 80 to 251, the domain is characterized as Tyrosine-protein phosphatase.
+At position 164 to 298, the domain is characterized as TRUD.
+At position 18 to 47, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 65 to 95, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 138 to 411, the domain is characterized as ABC transporter 1.
+At position 805 to 1050, the domain is characterized as ABC transporter 2.
+At position 1122 to 1336, the domain is characterized as ABC transmembrane type-2 2.
+At position 531 to 610, the domain is characterized as UBX.
+At position 34 to 378, the domain is characterized as Protein kinase.
+At position 202 to 375, the domain is characterized as EngA-type G 2.
+At position 376 to 458, the domain is characterized as KH-like.
+At position 45 to 205, the domain is characterized as PX.
+At position 215 to 343, the domain is characterized as PH.
+At position 472 to 499, the domain is characterized as PLD phosphodiesterase 1.
+At position 847 to 874, the domain is characterized as PLD phosphodiesterase 2.
+At position 116 to 207, the domain is characterized as SH2.
+At position 130 to 300, the domain is characterized as Helicase ATP-binding.
+At position 311 to 478, the domain is characterized as Helicase C-terminal.
+At position 18 to 90, the domain is characterized as RRM 1.
+At position 95 to 166, the domain is characterized as RRM 2.
+At position 206 to 281, the domain is characterized as RRM 3.
+At position 441 to 537, the domain is characterized as SPOC.
+At position 3 to 82, the domain is characterized as Sm.
+At position 8 to 271, the domain is characterized as Protein kinase.
+At position 598 to 779, the domain is characterized as Guanylate kinase-like.
+At position 1634 to 1748, the domain is characterized as ZU5.
+At position 92 to 508, the domain is characterized as GBD/FH3.
+At position 845 to 1257, the domain is characterized as FH2.
+At position 69 to 160, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 202 to 232, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 53 to 90, the domain is characterized as EF-hand 1.
+At position 132 to 167, the domain is characterized as EF-hand 2.
+At position 167 to 199, the domain is characterized as EF-hand 3.
+At position 274 to 702, the domain is characterized as GBD/FH3.
+At position 955 to 1136, the domain is characterized as FH1.
+At position 1141 to 1564, the domain is characterized as FH2.
+At position 1581 to 1613, the domain is characterized as DAD.
+At position 22 to 252, the domain is characterized as ABC transporter.
+At position 21 to 289, the domain is characterized as tr-type G.
+At position 155 to 348, the domain is characterized as CheB-type methylesterase.
+At position 102 to 386, the domain is characterized as Protein kinase.
+At position 222 to 301, the domain is characterized as Chorismate mutase.
+At position 175 to 244, the domain is characterized as PUB.
+At position 332 to 408, the domain is characterized as UBX.
+At position 505 to 792, the domain is characterized as NB-ARC.
+At position 1211 to 1278, the domain is characterized as HMA.
+At position 36 to 187, the domain is characterized as DAGKc.
+At position 15 to 98, the domain is characterized as BRCT.
+At position 112 to 169, the domain is characterized as Myb-like.
+At position 28 to 240, the domain is characterized as Ch-type lysozyme.
+At position 148 to 186, the domain is characterized as LRRCT.
+At position 19 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 341 to 576, the domain is characterized as ABC transporter.
+At position 213 to 305, the domain is characterized as ARID.
+At position 425 to 522, the domain is characterized as REKLES.
+At position 38 to 107, the domain is characterized as DRBM 1.
+At position 128 to 195, the domain is characterized as DRBM 2.
+At position 304 to 378, the domain is characterized as U-box.
+At position 201 to 343, the domain is characterized as AXH.
+At position 514 to 733, the domain is characterized as FtsK.
+At position 453 to 514, the domain is characterized as SH3 3.
+At position 835 to 894, the domain is characterized as SH3 4.
+At position 355 to 467, the domain is characterized as PLAT.
+At position 582 to 642, the domain is characterized as KH.
+At position 659 to 726, the domain is characterized as S1 motif.
+At position 92 to 162, the domain is characterized as C-type lectin.
+At position 5 to 110, the domain is characterized as SSB 1.
+At position 129 to 232, the domain is characterized as SSB 2.
+At position 26 to 343, the domain is characterized as Calpain catalytic.
+At position 499 to 617, the domain is characterized as C2.
+At position 64 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 110 to 139, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 489 to 764, the domain is characterized as Protein kinase.
+At position 855 to 890, the domain is characterized as EF-hand 1.
+At position 891 to 926, the domain is characterized as EF-hand 2.
+At position 936 to 971, the domain is characterized as EF-hand 3.
+At position 1078 to 1218, the domain is characterized as Ferric oxidoreductase.
+At position 1253 to 1358, the domain is characterized as FAD-binding FR-type.
+At position 47 to 306, the domain is characterized as Radical SAM core.
+At position 103 to 285, the domain is characterized as Helicase ATP-binding.
+At position 316 to 472, the domain is characterized as Helicase C-terminal.
+At position 45 to 73, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 74 to 102, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 222 to 378, the domain is characterized as TrmE-type G.
+At position 3 to 477, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 505 to 788, the domain is characterized as UvrD-like helicase C-terminal.
+At position 17 to 247, the domain is characterized as Radical SAM core.
+At position 33 to 133, the domain is characterized as Fibronectin type-III 1.
+At position 138 to 234, the domain is characterized as Fibronectin type-III 2.
+At position 239 to 338, the domain is characterized as Fibronectin type-III 3.
+At position 101 to 120, the domain is characterized as HhH.
+At position 482 to 737, the domain is characterized as Protein kinase.
+At position 82 to 153, the domain is characterized as Chitin-binding type R&R.
+At position 74 to 306, the domain is characterized as Fibrinogen C-terminal.
+At position 261 to 373, the domain is characterized as Rhodanese.
+At position 260 to 770, the domain is characterized as PPM-type phosphatase.
+At position 629 to 759, the domain is characterized as DBINO.
+At position 883 to 1055, the domain is characterized as Helicase ATP-binding.
+At position 1457 to 1607, the domain is characterized as Helicase C-terminal.
+At position 188 to 367, the domain is characterized as MARVEL.
+At position 440 to 551, the domain is characterized as OCEL.
+At position 209 to 294, the domain is characterized as KH.
+At position 220 to 326, the domain is characterized as AB hydrolase-1.
+At position 4 to 192, the domain is characterized as Glutamine amidotransferase type-1.
+At position 193 to 381, the domain is characterized as GMPS ATP-PPase.
+At position 363 to 533, the domain is characterized as ZP.
+At position 121 to 317, the domain is characterized as ATP-grasp.
+At position 164 to 250, the domain is characterized as PNT.
+At position 185 to 401, the domain is characterized as Rap-GAP.
+At position 483 to 792, the domain is characterized as CNH.
+At position 12 to 174, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 141, the domain is characterized as Response regulatory.
+At position 166 to 256, the domain is characterized as 5'-3' exonuclease.
+At position 262 to 322, the domain is characterized as KH.
+At position 388 to 481, the domain is characterized as HD.
+At position 25 to 145, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 301, the domain is characterized as Plastocyanin-like 2.
+At position 345 to 524, the domain is characterized as Plastocyanin-like 3.
+At position 20 to 88, the domain is characterized as LCN-type CS-alpha/beta.
+At position 462 to 629, the domain is characterized as tr-type G.
+At position 135 to 412, the domain is characterized as RHD.
+At position 810 to 892, the domain is characterized as BRCT.
+At position 374 to 656, the domain is characterized as Protein kinase.
+At position 75 to 263, the domain is characterized as Flavodoxin-like.
+At position 33 to 121, the domain is characterized as Plastocyanin-like.
+At position 103 to 173, the domain is characterized as Myb-like.
+At position 228 to 412, the domain is characterized as Helicase ATP-binding.
+At position 441 to 592, the domain is characterized as Helicase C-terminal.
+At position 120 to 477, the domain is characterized as PTS EIIC type-1.
+At position 15 to 95, the domain is characterized as PB1.
+At position 201 to 462, the domain is characterized as Protein kinase.
+At position 946 to 1157, the domain is characterized as JmjC.
+At position 7 to 155, the domain is characterized as MPN.
+At position 171 to 298, the domain is characterized as GAT.
+At position 506 to 627, the domain is characterized as GAE.
+At position 4 to 82, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 127 to 157, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 178 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 7 to 253, the domain is characterized as Glutamine amidotransferase type-1.
+At position 47 to 303, the domain is characterized as GB1/RHD3-type G.
+At position 3 to 87, the domain is characterized as BMC.
+At position 258 to 398, the domain is characterized as Ferric oxidoreductase.
+At position 399 to 522, the domain is characterized as FAD-binding FR-type.
+At position 587 to 646, the domain is characterized as KH.
+At position 658 to 730, the domain is characterized as S1 motif.
+At position 138 to 173, the domain is characterized as EF-hand 3.
+At position 189 to 383, the domain is characterized as CheB-type methylesterase.
+At position 310 to 407, the domain is characterized as RRM 1.
+At position 429 to 510, the domain is characterized as RRM 2.
+At position 196 to 554, the domain is characterized as GRAS.
+At position 11 to 72, the domain is characterized as Sm.
+At position 37 to 298, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 39 to 321, the domain is characterized as ABC transmembrane type-1.
+At position 362 to 599, the domain is characterized as ABC transporter.
+At position 258 to 419, the domain is characterized as Helicase C-terminal.
+At position 1 to 97, the domain is characterized as SSB.
+At position 28 to 242, the domain is characterized as tr-type G.
+At position 44 to 304, the domain is characterized as Deacetylase sirtuin-type.
+At position 116 to 249, the domain is characterized as PX.
+At position 40 to 173, the domain is characterized as PX.
+At position 166 to 253, the domain is characterized as GIY-YIG.
+At position 246 to 420, the domain is characterized as DUF724.
+At position 29 to 115, the domain is characterized as KRAB.
+At position 203 to 332, the domain is characterized as Galectin 2.
+At position 137 to 380, the domain is characterized as Radical SAM core.
+At position 383 to 455, the domain is characterized as TRAM.
+At position 225 to 291, the domain is characterized as J.
+At position 48 to 215, the domain is characterized as NAC.
+At position 25 to 137, the domain is characterized as sHSP.
+At position 1 to 39, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 40 to 82, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 129 to 169, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 136 to 178, the domain is characterized as EGF-like.
+At position 291 to 317, the domain is characterized as EGF-like 2; calcium-binding; truncated.
+At position 640 to 741, the domain is characterized as Zinc-hook.
+At position 104 to 172, the domain is characterized as S4 RNA-binding.
+At position 122 to 334, the domain is characterized as Radical SAM core.
+At position 220 to 328, the domain is characterized as EamA 2.
+At position 2 to 79, the domain is characterized as Cytochrome b5 heme-binding.
+At position 101 to 478, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 239 to 373, the domain is characterized as Ferric oxidoreductase.
+At position 374 to 492, the domain is characterized as FAD-binding FR-type.
+At position 32 to 69, the domain is characterized as EGF-like 1.
+At position 81 to 119, the domain is characterized as EGF-like 2.
+At position 133 to 172, the domain is characterized as EGF-like 3; calcium-binding.
+At position 173 to 210, the domain is characterized as EGF-like 4; calcium-binding.
+At position 222 to 260, the domain is characterized as EGF-like 5; calcium-binding.
+At position 272 to 307, the domain is characterized as EGF-like 6; calcium-binding.
+At position 319 to 354, the domain is characterized as EGF-like 7; calcium-binding.
+At position 593 to 642, the domain is characterized as GPS.
+At position 496 to 694, the domain is characterized as N-terminal Ras-GEF.
+At position 726 to 1003, the domain is characterized as Ras-GEF.
+At position 35 to 157, the domain is characterized as MARVEL.
+At position 1 to 72, the domain is characterized as KRAB.
+At position 17 to 262, the domain is characterized as BAR.
+At position 276 to 469, the domain is characterized as Rho-GAP.
+At position 43 to 121, the domain is characterized as KH type-2.
+At position 210 to 394, the domain is characterized as Helicase ATP-binding.
+At position 435 to 584, the domain is characterized as Helicase C-terminal.
+At position 182 to 365, the domain is characterized as CheB-type methylesterase.
+At position 310 to 400, the domain is characterized as HPr.
+At position 46 to 171, the domain is characterized as C-type lectin.
+At position 326 to 444, the domain is characterized as PX.
+At position 19 to 69, the domain is characterized as Kazal-like 1.
+At position 72 to 122, the domain is characterized as Kazal-like 2.
+At position 131 to 181, the domain is characterized as Kazal-like 3.
+At position 184 to 234, the domain is characterized as Kazal-like 4.
+At position 240 to 289, the domain is characterized as Kazal-like 5.
+At position 297 to 347, the domain is characterized as Kazal-like 6.
+At position 158 to 285, the domain is characterized as EamA 2.
+At position 276 to 437, the domain is characterized as EF-1-gamma C-terminal.
+At position 399 to 471, the domain is characterized as B5.
+At position 696 to 788, the domain is characterized as FDX-ACB.
+At position 212 to 290, the domain is characterized as UBX.
+At position 44 to 229, the domain is characterized as GH11.
+At position 242 to 333, the domain is characterized as CBM2 1.
+At position 356 to 532, the domain is characterized as NodB homology.
+At position 553 to 644, the domain is characterized as CBM2 2.
+At position 242 to 277, the domain is characterized as EF-hand 2.
+At position 361 to 519, the domain is characterized as Ferric oxidoreductase.
+At position 558 to 681, the domain is characterized as FAD-binding FR-type.
+At position 5 to 87, the domain is characterized as Ubiquitin-like.
+At position 161 to 285, the domain is characterized as OTU.
+At position 506 to 612, the domain is characterized as CBM20.
+At position 30 to 139, the domain is characterized as Ig-like.
+At position 21 to 253, the domain is characterized as Phosphagen kinase C-terminal.
+At position 539 to 677, the domain is characterized as Flavodoxin-like.
+At position 730 to 970, the domain is characterized as FAD-binding FR-type.
+At position 1 to 172, the domain is characterized as Macro.
+At position 69 to 763, the domain is characterized as Myosin motor.
+At position 766 to 788, the domain is characterized as IQ 1.
+At position 789 to 813, the domain is characterized as IQ 2.
+At position 814 to 836, the domain is characterized as IQ 3.
+At position 837 to 861, the domain is characterized as IQ 4.
+At position 862 to 884, the domain is characterized as IQ 5.
+At position 885 to 913, the domain is characterized as IQ 6.
+At position 1532 to 1808, the domain is characterized as Dilute.
+At position 36 to 62, the domain is characterized as IQ 1.
+At position 63 to 87, the domain is characterized as IQ 2.
+At position 7 to 370, the domain is characterized as Enoyl reductase (ER).
+At position 486 to 602, the domain is characterized as PI-PLC Y-box.
+At position 602 to 731, the domain is characterized as C2.
+At position 246 to 362, the domain is characterized as Sox C-terminal.
+At position 231 to 321, the domain is characterized as Ig-like C1-type.
+At position 43 to 325, the domain is characterized as GH10.
+At position 8 to 85, the domain is characterized as TFIIS N-terminal.
+At position 66 to 105, the domain is characterized as BTB.
+At position 1 to 19, the domain is characterized as UBA 1.
+At position 30 to 76, the domain is characterized as UBA 2.
+At position 95 to 135, the domain is characterized as UBA 3.
+At position 118 to 312, the domain is characterized as ATP-grasp.
+At position 124 to 219, the domain is characterized as Rhodanese.
+At position 23 to 181, the domain is characterized as Cupin type-1 1.
+At position 241 to 409, the domain is characterized as Cupin type-1 2.
+At position 146 to 404, the domain is characterized as Protein kinase.
+At position 1 to 108, the domain is characterized as FHA-like.
+At position 118 to 282, the domain is characterized as Collagen-like 1.
+At position 293 to 307, the domain is characterized as Collagen-like 2.
+At position 155 to 192, the domain is characterized as LDL-receptor class A.
+At position 205 to 438, the domain is characterized as Peptidase S1 1.
+At position 506 to 738, the domain is characterized as Peptidase S1 2.
+At position 834 to 1064, the domain is characterized as Peptidase S1 3.
+At position 215 to 494, the domain is characterized as Protein kinase.
+At position 125 to 265, the domain is characterized as PA14.
+At position 55 to 347, the domain is characterized as Protein kinase.
+At position 7 to 35, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 175 to 206, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 208 to 237, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 113 to 342, the domain is characterized as Radical SAM core.
+At position 512 to 789, the domain is characterized as Protein kinase.
+At position 335 to 534, the domain is characterized as Protein kinase.
+At position 142 to 506, the domain is characterized as Protein kinase.
+At position 1 to 234, the domain is characterized as PTS EIIC type-4.
+At position 5 to 107, the domain is characterized as PH.
+At position 148 to 405, the domain is characterized as Protein kinase.
+At position 406 to 479, the domain is characterized as AGC-kinase C-terminal.
+At position 370 to 433, the domain is characterized as TRAM.
+At position 17 to 148, the domain is characterized as VOC 1.
+At position 179 to 339, the domain is characterized as VOC 2.
+At position 15 to 136, the domain is characterized as Nudix hydrolase.
+At position 491 to 609, the domain is characterized as Fibronectin type-III 1.
+At position 610 to 708, the domain is characterized as Fibronectin type-III 2.
+At position 735 to 828, the domain is characterized as Fibronectin type-III 3.
+At position 834 to 927, the domain is characterized as Fibronectin type-III 4.
+At position 999 to 1274, the domain is characterized as Protein kinase.
+At position 135 to 295, the domain is characterized as CRAL-TRIO.
+At position 184 to 327, the domain is characterized as KARI C-terminal knotted.
+At position 34 to 126, the domain is characterized as PpiC.
+At position 2 to 124, the domain is characterized as CMP/dCMP-type deaminase.
+At position 7 to 242, the domain is characterized as ABC transporter 1.
+At position 256 to 500, the domain is characterized as ABC transporter 2.
+At position 29 to 87, the domain is characterized as Sushi 1.
+At position 88 to 145, the domain is characterized as Sushi 2.
+At position 24 to 156, the domain is characterized as EXPERA.
+At position 65 to 173, the domain is characterized as Expansin-like EG45.
+At position 186 to 269, the domain is characterized as Expansin-like CBD.
+At position 260 to 296, the domain is characterized as EGF-like 7; calcium-binding.
+At position 298 to 336, the domain is characterized as EGF-like 8; calcium-binding.
+At position 338 to 374, the domain is characterized as EGF-like 9; calcium-binding.
+At position 375 to 413, the domain is characterized as EGF-like 10.
+At position 415 to 454, the domain is characterized as EGF-like 11; calcium-binding.
+At position 456 to 492, the domain is characterized as EGF-like 12; calcium-binding.
+At position 494 to 530, the domain is characterized as EGF-like 13; calcium-binding.
+At position 532 to 568, the domain is characterized as EGF-like 14; calcium-binding.
+At position 570 to 605, the domain is characterized as EGF-like 15; calcium-binding.
+At position 607 to 643, the domain is characterized as EGF-like 16; calcium-binding.
+At position 645 to 680, the domain is characterized as EGF-like 17; calcium-binding.
+At position 682 to 718, the domain is characterized as EGF-like 18; calcium-binding.
+At position 720 to 755, the domain is characterized as EGF-like 19.
+At position 757 to 793, the domain is characterized as EGF-like 20; calcium-binding.
+At position 795 to 831, the domain is characterized as EGF-like 21; calcium-binding.
+At position 833 to 871, the domain is characterized as EGF-like 22.
+At position 873 to 909, the domain is characterized as EGF-like 23; calcium-binding.
+At position 911 to 947, the domain is characterized as EGF-like 24; calcium-binding.
+At position 949 to 985, the domain is characterized as EGF-like 25; calcium-binding.
+At position 987 to 1023, the domain is characterized as EGF-like 26; calcium-binding.
+At position 1025 to 1061, the domain is characterized as EGF-like 27; calcium-binding.
+At position 1063 to 1099, the domain is characterized as EGF-like 28.
+At position 1101 to 1147, the domain is characterized as EGF-like 29.
+At position 1149 to 1185, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1187 to 1223, the domain is characterized as EGF-like 31; calcium-binding.
+At position 1225 to 1262, the domain is characterized as EGF-like 32; calcium-binding.
+At position 1264 to 1302, the domain is characterized as EGF-like 33.
+At position 1304 to 1343, the domain is characterized as EGF-like 34.
+At position 1374 to 1412, the domain is characterized as EGF-like 35.
+At position 27 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 13 to 157, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 31 to 279, the domain is characterized as Protein kinase.
+At position 130 to 397, the domain is characterized as Peptidase S8.
+At position 49 to 142, the domain is characterized as Stress-response A/B barrel 1.
+At position 158 to 252, the domain is characterized as Stress-response A/B barrel 2.
+At position 34 to 125, the domain is characterized as MaoC-like.
+At position 186 to 247, the domain is characterized as LIM zinc-binding 1.
+At position 248 to 305, the domain is characterized as LIM zinc-binding 2.
+At position 306 to 375, the domain is characterized as LIM zinc-binding 3.
+At position 26 to 126, the domain is characterized as Fibronectin type-III.
+At position 245 to 507, the domain is characterized as Olfactomedin-like.
+At position 65 to 174, the domain is characterized as C-type lectin.
+At position 287 to 479, the domain is characterized as Helicase ATP-binding 1.
+At position 513 to 723, the domain is characterized as Helicase C-terminal 1.
+At position 787 to 1093, the domain is characterized as SEC63 1.
+At position 1144 to 1319, the domain is characterized as Helicase ATP-binding 2.
+At position 1351 to 1546, the domain is characterized as Helicase C-terminal 2.
+At position 1618 to 1934, the domain is characterized as SEC63 2.
+At position 508 to 756, the domain is characterized as NR LBD.
+At position 2 to 89, the domain is characterized as CS.
+At position 21 to 100, the domain is characterized as Ig-like C2-type 1.
+At position 202 to 297, the domain is characterized as Ig-like C2-type 3.
+At position 400 to 499, the domain is characterized as Ig-like C2-type 5.
+At position 579 to 908, the domain is characterized as Protein kinase.
+At position 220 to 302, the domain is characterized as Cytochrome c 2.
+At position 25 to 131, the domain is characterized as Ig-like V-type 1; required for binding to polymeric IgA and IgM.
+At position 138 to 232, the domain is characterized as Ig-like V-type 2.
+At position 233 to 340, the domain is characterized as Ig-like V-type 3.
+At position 352 to 455, the domain is characterized as Ig-like V-type 4.
+At position 461 to 557, the domain is characterized as Ig-like V-type 5.
+At position 43 to 136, the domain is characterized as PDZ.
+At position 161 to 269, the domain is characterized as PX.
+At position 273 to 362, the domain is characterized as Ras-associating.
+At position 106 to 165, the domain is characterized as CBS 1.
+At position 169 to 225, the domain is characterized as CBS 2.
+At position 723 to 961, the domain is characterized as NR LBD.
+At position 370 to 500, the domain is characterized as CMP/dCMP-type deaminase.
+At position 21 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 114 to 211, the domain is characterized as Ig-like C2-type 2.
+At position 216 to 302, the domain is characterized as Ig-like C2-type 3.
+At position 311 to 398, the domain is characterized as Ig-like C2-type 4.
+At position 400 to 481, the domain is characterized as Ig-like C2-type 5.
+At position 570 to 658, the domain is characterized as Ig-like C2-type 6.
+At position 659 to 753, the domain is characterized as Ig-like C2-type 7.
+At position 758 to 850, the domain is characterized as Ig-like C2-type 8.
+At position 854 to 938, the domain is characterized as Ig-like C2-type 9.
+At position 946 to 1041, the domain is characterized as Ig-like C2-type 10.
+At position 1046 to 1131, the domain is characterized as Ig-like C2-type 11.
+At position 1142 to 1223, the domain is characterized as Ig-like C2-type 12.
+At position 181 to 288, the domain is characterized as Fe2OG dioxygenase.
+At position 264 to 327, the domain is characterized as PWWP.
+At position 402 to 461, the domain is characterized as FYR N-terminal.
+At position 465 to 548, the domain is characterized as FYR C-terminal.
+At position 861 to 979, the domain is characterized as SET.
+At position 985 to 1001, the domain is characterized as Post-SET.
+At position 260 to 310, the domain is characterized as LRRCT.
+At position 249 to 430, the domain is characterized as PCI.
+At position 1 to 148, the domain is characterized as N-acetyltransferase.
+At position 21 to 96, the domain is characterized as Ubiquitin-like.
+At position 601 to 710, the domain is characterized as Peptidase S72.
+At position 550 to 723, the domain is characterized as tr-type G.
+At position 151 to 309, the domain is characterized as TRUD.
+At position 570 to 632, the domain is characterized as FIP-RBD.
+At position 208 to 392, the domain is characterized as Helicase ATP-binding.
+At position 403 to 563, the domain is characterized as Helicase C-terminal.
+At position 31 to 148, the domain is characterized as C-type lectin.
+At position 81 to 262, the domain is characterized as NodB homology.
+At position 9 to 695, the domain is characterized as Myosin motor.
+At position 699 to 719, the domain is characterized as IQ 1.
+At position 721 to 741, the domain is characterized as IQ 2.
+At position 812 to 1005, the domain is characterized as TH1.
+At position 15 to 96, the domain is characterized as HTH IS408-type.
+At position 138 to 319, the domain is characterized as Integrase catalytic.
+At position 6 to 67, the domain is characterized as S4 RNA-binding.
+At position 6 to 137, the domain is characterized as Toprim.
+At position 202 to 394, the domain is characterized as CheB-type methylesterase.
+At position 166 to 251, the domain is characterized as Ig-like.
+At position 100 to 200, the domain is characterized as FAD-binding FR-type.
+At position 159 to 347, the domain is characterized as CheB-type methylesterase.
+At position 129 to 210, the domain is characterized as Ig-like C2-type 2.
+At position 21 to 367, the domain is characterized as GH10.
+At position 35 to 114, the domain is characterized as RRM 1.
+At position 140 to 231, the domain is characterized as RRM 2.
+At position 61 to 105, the domain is characterized as LysM.
+At position 583 to 672, the domain is characterized as BRCT.
+At position 179 to 438, the domain is characterized as Pterin-binding.
+At position 48 to 120, the domain is characterized as ACT.
+At position 688 to 772, the domain is characterized as ACT 1.
+At position 1 to 98, the domain is characterized as Plastocyanin-like.
+At position 557 to 598, the domain is characterized as JmjN.
+At position 621 to 713, the domain is characterized as ARID.
+At position 884 to 1048, the domain is characterized as JmjC.
+At position 98 to 373, the domain is characterized as tr-type G.
+At position 108 to 167, the domain is characterized as Chromo 1.
+At position 378 to 442, the domain is characterized as Chromo 2; shadow subtype.
+At position 54 to 356, the domain is characterized as ABC transmembrane type-1 1.
+At position 708 to 996, the domain is characterized as ABC transmembrane type-1 2.
+At position 60 to 176, the domain is characterized as CMP/dCMP-type deaminase.
+At position 177 to 249, the domain is characterized as DRBM 2.
+At position 395 to 561, the domain is characterized as Helicase ATP-binding.
+At position 633 to 806, the domain is characterized as Helicase C-terminal.
+At position 1609 to 1659, the domain is characterized as GRIP.
+At position 349 to 404, the domain is characterized as EGF-like.
+At position 18 to 213, the domain is characterized as RNase H type-2.
+At position 515 to 567, the domain is characterized as HTH psq-type.
+At position 90 to 146, the domain is characterized as HTH myb-type.
+At position 74 to 543, the domain is characterized as Sema.
+At position 10 to 193, the domain is characterized as Josephin.
+At position 244 to 263, the domain is characterized as UIM.
+At position 349 to 413, the domain is characterized as S4 RNA-binding.
+At position 60 to 131, the domain is characterized as KRAB.
+At position 9 to 176, the domain is characterized as Era-type G.
+At position 199 to 285, the domain is characterized as KH type-2.
+At position 137 to 212, the domain is characterized as PDZ.
+At position 29 to 134, the domain is characterized as UPAR/Ly6.
+At position 144 to 239, the domain is characterized as Fibronectin type-III 2.
+At position 339 to 377, the domain is characterized as EGF-like 1.
+At position 382 to 560, the domain is characterized as Laminin G-like 1.
+At position 561 to 598, the domain is characterized as EGF-like 2.
+At position 605 to 784, the domain is characterized as Laminin G-like 2.
+At position 780 to 816, the domain is characterized as EGF-like 3.
+At position 823 to 1002, the domain is characterized as Laminin G-like 3.
+At position 72 to 248, the domain is characterized as FAD-binding PCMH-type.
+At position 69 to 241, the domain is characterized as FAD-binding PCMH-type.
+At position 601 to 690, the domain is characterized as BRCT.
+At position 16 to 88, the domain is characterized as Myb-like.
+At position 1057 to 1135, the domain is characterized as Carrier 2.
+At position 415 to 520, the domain is characterized as B5.
+At position 743 to 836, the domain is characterized as FDX-ACB.
+At position 42 to 84, the domain is characterized as CHCH.
+At position 53 to 188, the domain is characterized as N-acetyltransferase.
+At position 37 to 227, the domain is characterized as GH11.
+At position 146 to 188, the domain is characterized as CCT.
+At position 88 to 241, the domain is characterized as Ferritin-like diiron.
+At position 66 to 328, the domain is characterized as Ras-GEF.
+At position 910 to 1058, the domain is characterized as PI-PLC X-box.
+At position 1279 to 1385, the domain is characterized as PI-PLC Y-box.
+At position 1391 to 1517, the domain is characterized as C2.
+At position 1570 to 1665, the domain is characterized as Ras-associating 1.
+At position 1738 to 1857, the domain is characterized as Ras-associating 2.
+At position 87 to 283, the domain is characterized as tr-type G.
+At position 29 to 266, the domain is characterized as Alpha-carbonic anhydrase.
+At position 20 to 112, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 122 to 221, the domain is characterized as FAD-binding FR-type.
+At position 1 to 184, the domain is characterized as YrdC-like.
+At position 123 to 440, the domain is characterized as Peptidase A1.
+At position 100 to 155, the domain is characterized as bHLH.
+At position 174 to 210, the domain is characterized as Orange.
+At position 43 to 164, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 199 to 320, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 167 to 374, the domain is characterized as ATP-grasp.
+At position 81 to 257, the domain is characterized as Helicase ATP-binding.
+At position 271 to 440, the domain is characterized as Helicase C-terminal.
+At position 615 to 661, the domain is characterized as Kazal-like 1.
+At position 686 to 741, the domain is characterized as Kazal-like 2.
+At position 742 to 778, the domain is characterized as Kazal-like 3.
+At position 624 to 713, the domain is characterized as BRCT.
+At position 513 to 675, the domain is characterized as HNH Cas9-type.
+At position 29 to 316, the domain is characterized as Protein kinase.
+At position 9 to 237, the domain is characterized as Sigma-54 factor interaction.
+At position 73 to 154, the domain is characterized as Ig-like C2-type.
+At position 287 to 347, the domain is characterized as KH.
+At position 20 to 99, the domain is characterized as GIY-YIG.
+At position 99 to 380, the domain is characterized as Protein kinase.
+At position 12 to 402, the domain is characterized as Glutamine amidotransferase type-2.
+At position 97 to 183, the domain is characterized as ELM2.
+At position 184 to 235, the domain is characterized as SANT 1.
+At position 375 to 426, the domain is characterized as SANT 2.
+At position 112 to 191, the domain is characterized as PDZ 1.
+At position 196 to 271, the domain is characterized as PDZ 2.
+At position 227 to 305, the domain is characterized as RRM.
+At position 24 to 216, the domain is characterized as RNase H type-2.
+At position 521 to 919, the domain is characterized as USP.
+At position 977 to 1151, the domain is characterized as Exonuclease.
+At position 3 to 80, the domain is characterized as DED 1.
+At position 101 to 177, the domain is characterized as DED 2.
+At position 134 to 167, the domain is characterized as EF-hand 4.
+At position 18 to 130, the domain is characterized as Thioredoxin.
+At position 513 to 588, the domain is characterized as Cytochrome b5 heme-binding.
+At position 630 to 742, the domain is characterized as FAD-binding FR-type.
+At position 7 to 227, the domain is characterized as Radical SAM core.
+At position 213 to 276, the domain is characterized as PAS.
+At position 333 to 528, the domain is characterized as Histidine kinase.
+At position 58 to 168, the domain is characterized as Cadherin 1.
+At position 169 to 280, the domain is characterized as Cadherin 2.
+At position 281 to 387, the domain is characterized as Cadherin 3.
+At position 396 to 506, the domain is characterized as Cadherin 4.
+At position 507 to 612, the domain is characterized as Cadherin 5.
+At position 613 to 715, the domain is characterized as Cadherin 6.
+At position 718 to 844, the domain is characterized as Cadherin 7.
+At position 95 to 147, the domain is characterized as bHLH.
+At position 31 to 59, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 10 to 156, the domain is characterized as MGS-like.
+At position 1 to 141, the domain is characterized as Tyrosine-protein phosphatase.
+At position 371 to 543, the domain is characterized as DUF724.
+At position 1 to 385, the domain is characterized as BRO1.
+At position 207 to 358, the domain is characterized as DIPSY.
+At position 154 to 267, the domain is characterized as Rhodanese 2.
+At position 109 to 417, the domain is characterized as IF rod.
+At position 76 to 232, the domain is characterized as PI-PLC X-box.
+At position 9 to 190, the domain is characterized as tr-type G.
+At position 50 to 221, the domain is characterized as VWFA 1.
+At position 342 to 518, the domain is characterized as VWFA 2.
+At position 532 to 702, the domain is characterized as VWFA 3.
+At position 713 to 748, the domain is characterized as EGF-like 2.
+At position 495 to 618, the domain is characterized as HD.
+At position 736 to 818, the domain is characterized as ACT 1.
+At position 849 to 929, the domain is characterized as ACT 2.
+At position 59 to 126, the domain is characterized as Histone-fold.
+At position 670 to 790, the domain is characterized as TFIIS central.
+At position 80 to 162, the domain is characterized as SAND.
+At position 370 to 515, the domain is characterized as VPS9.
+At position 157 to 368, the domain is characterized as ATP-grasp.
+At position 4 to 259, the domain is characterized as ABC transporter 1.
+At position 327 to 541, the domain is characterized as ABC transporter 2.
+At position 8 to 128, the domain is characterized as MTTase N-terminal.
+At position 385 to 447, the domain is characterized as TRAM.
+At position 5 to 475, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 508 to 804, the domain is characterized as UvrD-like helicase C-terminal.
+At position 41 to 144, the domain is characterized as Rieske.
+At position 47 to 123, the domain is characterized as EMI.
+At position 852 to 913, the domain is characterized as Collagen-like.
+At position 922 to 1073, the domain is characterized as C1q.
+At position 94 to 237, the domain is characterized as N-acetyltransferase.
+At position 11 to 436, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 954 to 1278, the domain is characterized as PKS/mFAS DH.
+At position 2442 to 2519, the domain is characterized as Carrier.
+At position 212 to 402, the domain is characterized as Peptidase M12B.
+At position 638 to 667, the domain is characterized as EGF-like.
+At position 303 to 374, the domain is characterized as RBD 1.
+At position 376 to 446, the domain is characterized as RBD 2.
+At position 500 to 522, the domain is characterized as GoLoco.
+At position 86 to 242, the domain is characterized as DAGKc.
+At position 42 to 72, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 88 to 117, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 71, the domain is characterized as NAC-A/B.
+At position 118 to 157, the domain is characterized as UBA.
+At position 19 to 55, the domain is characterized as Oxidoreductase-like.
+At position 75 to 177, the domain is characterized as FAD-binding FR-type.
+At position 97 to 373, the domain is characterized as Protein kinase.
+At position 329 to 364, the domain is characterized as EF-hand 1.
+At position 365 to 387, the domain is characterized as EF-hand 2.
+At position 220 to 279, the domain is characterized as CBS 1.
+At position 286 to 345, the domain is characterized as CBS 2.
+At position 65 to 257, the domain is characterized as NodB homology.
+At position 165 to 383, the domain is characterized as Radical SAM core.
+At position 3 to 184, the domain is characterized as DHFR.
+At position 39 to 89, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 405 to 620, the domain is characterized as SEC7.
+At position 844 to 1074, the domain is characterized as PH.
+At position 94 to 113, the domain is characterized as UIM.
+At position 156 to 651, the domain is characterized as USP.
+At position 2 to 72, the domain is characterized as PPIase FKBP-type.
+At position 36 to 114, the domain is characterized as BIG2.
+At position 299 to 349, the domain is characterized as DHHC.
+At position 25 to 256, the domain is characterized as Protein kinase.
+At position 792 to 942, the domain is characterized as RNase NYN.
+At position 1304 to 1450, the domain is characterized as RNase H type-1.
+At position 1609 to 1774, the domain is characterized as Integrase catalytic.
+At position 220 to 566, the domain is characterized as TTL.
+At position 14 to 22, the domain is characterized as Peptidase M12B.
+At position 86 to 267, the domain is characterized as Brix.
+At position 709 to 790, the domain is characterized as ACT 1.
+At position 11 to 245, the domain is characterized as PABS.
+At position 209 to 490, the domain is characterized as MHD.
+At position 588 to 667, the domain is characterized as BRCT.
+At position 26 to 129, the domain is characterized as HIT.
+At position 44 to 160, the domain is characterized as tRNA-binding.
+At position 742 to 835, the domain is characterized as FDX-ACB.
+At position 19 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 12 to 498, the domain is characterized as Hexokinase.
+At position 28 to 278, the domain is characterized as AB hydrolase-1.
+At position 527 to 756, the domain is characterized as Tyrosine-protein phosphatase.
+At position 752 to 877, the domain is characterized as BAH 1.
+At position 969 to 1097, the domain is characterized as BAH 2.
+At position 1136 to 1595, the domain is characterized as SAM-dependent MTase C5-type.
+At position 1 to 72, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 302 to 507, the domain is characterized as MCM.
+At position 59 to 166, the domain is characterized as THUMP.
+At position 6 to 60, the domain is characterized as bHLH.
+At position 40 to 168, the domain is characterized as Thioredoxin.
+At position 555 to 636, the domain is characterized as BTB 1.
+At position 758 to 826, the domain is characterized as BTB 2.
+At position 175 to 295, the domain is characterized as AB hydrolase-1.
+At position 47 to 225, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 390 to 895, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 904 to 962, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 186 to 244, the domain is characterized as CBS 2.
+At position 57 to 251, the domain is characterized as Lon N-terminal.
+At position 640 to 821, the domain is characterized as Lon proteolytic.
+At position 2 to 183, the domain is characterized as UmuC.
+At position 141 to 206, the domain is characterized as SEP.
+At position 252 to 329, the domain is characterized as UBX.
+At position 36 to 264, the domain is characterized as Alpha-carbonic anhydrase.
+At position 41 to 154, the domain is characterized as Expansin-like EG45.
+At position 4 to 149, the domain is characterized as Toprim.
+At position 484 to 519, the domain is characterized as EF-hand 1.
+At position 567 to 602, the domain is characterized as EF-hand 2.
+At position 607 to 642, the domain is characterized as EF-hand 3.
+At position 19 to 133, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 144 to 250, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 7 to 92, the domain is characterized as BMC.
+At position 47 to 272, the domain is characterized as SET.
+At position 10 to 187, the domain is characterized as Guanylate kinase-like.
+At position 413 to 534, the domain is characterized as Ricin B-type lectin.
+At position 751 to 840, the domain is characterized as SUEL-type lectin.
+At position 34 to 299, the domain is characterized as Protein kinase.
+At position 108 to 200, the domain is characterized as Cytochrome c 1.
+At position 207 to 292, the domain is characterized as Cytochrome c 2.
+At position 8 to 276, the domain is characterized as Protein kinase.
+At position 215 to 318, the domain is characterized as PH.
+At position 549 to 635, the domain is characterized as GED.
+At position 15 to 359, the domain is characterized as Kinesin motor.
+At position 111 to 139, the domain is characterized as HhH.
+At position 222 to 254, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 303 to 332, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 286 to 345, the domain is characterized as OVATE.
+At position 53 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 5 to 88, the domain is characterized as RRM 1.
+At position 231 to 314, the domain is characterized as RRM 2.
+At position 251 to 1040, the domain is characterized as Peptidase M13.
+At position 5 to 163, the domain is characterized as Thioredoxin.
+At position 142 to 231, the domain is characterized as CS.
+At position 249 to 338, the domain is characterized as SGS.
+At position 32 to 113, the domain is characterized as Collagen-like.
+At position 116 to 246, the domain is characterized as C1q.
+At position 22 to 190, the domain is characterized as EngB-type G.
+At position 827 to 917, the domain is characterized as BRCT 1.
+At position 984 to 1088, the domain is characterized as BRCT 2.
+At position 92 to 199, the domain is characterized as Guanylate cyclase.
+At position 22 to 68, the domain is characterized as WAP.
+At position 61 to 127, the domain is characterized as CBS 1.
+At position 136 to 194, the domain is characterized as CBS 2.
+At position 292 to 641, the domain is characterized as Protein kinase.
+At position 39 to 112, the domain is characterized as EamA.
+At position 12 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 14 to 71, the domain is characterized as HTH lysR-type.
+At position 5 to 297, the domain is characterized as Protein kinase.
+At position 129 to 413, the domain is characterized as Peptidase S8.
+At position 248 to 415, the domain is characterized as Helicase C-terminal.
+At position 498 to 670, the domain is characterized as tr-type G.
+At position 423 to 606, the domain is characterized as VWFD.
+At position 1177 to 1216, the domain is characterized as EGF-like 1.
+At position 1294 to 1326, the domain is characterized as EGF-like 2.
+At position 1358 to 1390, the domain is characterized as EGF-like 3.
+At position 1422 to 1454, the domain is characterized as EGF-like 4.
+At position 1455 to 1486, the domain is characterized as EGF-like 5.
+At position 1518 to 1550, the domain is characterized as EGF-like 6.
+At position 1551 to 1582, the domain is characterized as EGF-like 7.
+At position 72 to 174, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 14 to 88, the domain is characterized as KRAB.
+At position 448 to 639, the domain is characterized as Helicase C-terminal.
+At position 41 to 132, the domain is characterized as Ig-like V-type.
+At position 184 to 212, the domain is characterized as ITAM.
+At position 99 to 407, the domain is characterized as IF rod.
+At position 491 to 641, the domain is characterized as Helicase C-terminal.
+At position 44 to 314, the domain is characterized as Protein kinase.
+At position 11 to 202, the domain is characterized as Lon N-terminal.
+At position 603 to 785, the domain is characterized as Lon proteolytic.
+At position 465 to 636, the domain is characterized as tr-type G.
+At position 114 to 207, the domain is characterized as PRC barrel.
+At position 6 to 40, the domain is characterized as EF-hand 1.
+At position 89 to 138, the domain is characterized as bHLH.
+At position 97 to 407, the domain is characterized as IF rod.
+At position 24 to 631, the domain is characterized as PLA2c.
+At position 69 to 206, the domain is characterized as 6-Cys 1.
+At position 215 to 379, the domain is characterized as 6-Cys 2.
+At position 596 to 681, the domain is characterized as BRCT.
+At position 42 to 179, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 368 to 446, the domain is characterized as ACT-like 1.
+At position 468 to 539, the domain is characterized as ACT-like 2.
+At position 201 to 230, the domain is characterized as IQ.
+At position 239 to 425, the domain is characterized as DH.
+At position 466 to 584, the domain is characterized as PH 2.
+At position 631 to 745, the domain is characterized as N-terminal Ras-GEF.
+At position 1009 to 1241, the domain is characterized as Ras-GEF.
+At position 193 to 254, the domain is characterized as Thyroglobulin type-1.
+At position 383 to 446, the domain is characterized as TRAM.
+At position 41 to 98, the domain is characterized as HTH lysR-type.
+At position 2 to 37, the domain is characterized as ShKT.
+At position 197 to 270, the domain is characterized as RRM 1.
+At position 282 to 355, the domain is characterized as RRM 2.
+At position 356 to 455, the domain is characterized as UBX.
+At position 139 to 413, the domain is characterized as ABC transporter 1.
+At position 491 to 703, the domain is characterized as ABC transmembrane type-2 1.
+At position 800 to 1045, the domain is characterized as ABC transporter 2.
+At position 1117 to 1331, the domain is characterized as ABC transmembrane type-2 2.
+At position 161 to 255, the domain is characterized as PPIase FKBP-type.
+At position 1 to 157, the domain is characterized as Brix.
+At position 212 to 364, the domain is characterized as Laminin G-like 1.
+At position 398 to 547, the domain is characterized as Laminin G-like 2.
+At position 549 to 586, the domain is characterized as EGF-like 1.
+At position 587 to 792, the domain is characterized as Fibrinogen C-terminal.
+At position 793 to 957, the domain is characterized as Laminin G-like 3.
+At position 958 to 997, the domain is characterized as EGF-like 2.
+At position 1046 to 1202, the domain is characterized as Laminin G-like 4.
+At position 3 to 118, the domain is characterized as PH.
+At position 123 to 136, the domain is characterized as CRIB.
+At position 360 to 639, the domain is characterized as Protein kinase.
+At position 11 to 179, the domain is characterized as Ku.
+At position 380 to 813, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1289 to 1599, the domain is characterized as PKS/mFAS DH.
+At position 1635 to 1712, the domain is characterized as Carrier.
+At position 171 to 484, the domain is characterized as SAC.
+At position 145 to 362, the domain is characterized as NR LBD.
+At position 170 to 236, the domain is characterized as HTH luxR-type.
+At position 277 to 415, the domain is characterized as SIS 1.
+At position 438 to 580, the domain is characterized as SIS 2.
+At position 9 to 30, the domain is characterized as C-type lectin.
+At position 229 to 491, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 153 to 311, the domain is characterized as FCP1 homology.
+At position 1 to 369, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 3 to 87, the domain is characterized as GST N-terminal.
+At position 41 to 169, the domain is characterized as Thioredoxin.
+At position 200 to 392, the domain is characterized as Helicase ATP-binding.
+At position 403 to 564, the domain is characterized as Helicase C-terminal.
+At position 135 to 311, the domain is characterized as Integrase catalytic.
+At position 130 to 305, the domain is characterized as Helicase ATP-binding.
+At position 333 to 478, the domain is characterized as Helicase C-terminal.
+At position 4 to 449, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 479 to 745, the domain is characterized as UvrD-like helicase C-terminal.
+At position 53 to 108, the domain is characterized as AWS.
+At position 452 to 484, the domain is characterized as WW.
+At position 151 to 265, the domain is characterized as C-type lectin.
+At position 249 to 276, the domain is characterized as PLD phosphodiesterase 1.
+At position 427 to 454, the domain is characterized as PLD phosphodiesterase 2.
+At position 167 to 260, the domain is characterized as 5'-3' exonuclease.
+At position 27 to 257, the domain is characterized as ABC transporter.
+At position 168 to 463, the domain is characterized as ABC transmembrane type-1.
+At position 497 to 733, the domain is characterized as ABC transporter.
+At position 406 to 576, the domain is characterized as tr-type G.
+At position 30 to 62, the domain is characterized as bZIP.
+At position 337 to 369, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 371 to 400, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 564 to 644, the domain is characterized as Carrier.
+At position 245 to 565, the domain is characterized as Kinesin motor.
+At position 139 to 237, the domain is characterized as Fibronectin type-III 1.
+At position 242 to 335, the domain is characterized as Fibronectin type-III 2.
+At position 336 to 430, the domain is characterized as Fibronectin type-III 3.
+At position 438 to 530, the domain is characterized as Fibronectin type-III 4.
+At position 536 to 635, the domain is characterized as Fibronectin type-III 5.
+At position 57 to 107, the domain is characterized as F-box.
+At position 537 to 841, the domain is characterized as Autotransporter.
+At position 130 to 406, the domain is characterized as Peptidase S8.
+At position 117 to 197, the domain is characterized as PDZ.
+At position 28 to 297, the domain is characterized as Septin-type G.
+At position 39 to 713, the domain is characterized as Myosin motor.
+At position 717 to 737, the domain is characterized as IQ 1.
+At position 738 to 763, the domain is characterized as IQ 2.
+At position 771 to 961, the domain is characterized as TH1.
+At position 1064 to 1123, the domain is characterized as SH3.
+At position 4 to 130, the domain is characterized as RNase III.
+At position 154 to 222, the domain is characterized as DRBM.
+At position 79 to 159, the domain is characterized as S1 motif.
+At position 270 to 449, the domain is characterized as PI-PLC X-box.
+At position 24 to 329, the domain is characterized as Transferrin-like 1.
+At position 114 to 263, the domain is characterized as Thioredoxin.
+At position 16 to 71, the domain is characterized as HTH cro/C1-type.
+At position 79 to 387, the domain is characterized as SAM-dependent MTase C5-type.
+At position 478 to 646, the domain is characterized as tr-type G.
+At position 305 to 340, the domain is characterized as EF-hand 1.
+At position 345 to 380, the domain is characterized as EF-hand 2.
+At position 8 to 75, the domain is characterized as CSD.
+At position 74 to 202, the domain is characterized as Thioredoxin.
+At position 31 to 133, the domain is characterized as Phytocyanin.
+At position 951 to 980, the domain is characterized as IQ 2.
+At position 279 to 474, the domain is characterized as MRH.
+At position 465 to 594, the domain is characterized as Ricin B-type lectin.
+At position 353 to 522, the domain is characterized as tr-type G.
+At position 158 to 350, the domain is characterized as CheB-type methylesterase.
+At position 288 to 614, the domain is characterized as FERM.
+At position 402 to 507, the domain is characterized as PH.
+At position 387 to 484, the domain is characterized as Zinc-hook.
+At position 395 to 661, the domain is characterized as Protein kinase.
+At position 217 to 269, the domain is characterized as HAMP.
+At position 277 to 471, the domain is characterized as Histidine kinase.
+At position 6 to 220, the domain is characterized as tr-type G.
+At position 9 to 217, the domain is characterized as YjeF N-terminal.
+At position 220 to 495, the domain is characterized as YjeF C-terminal.
+At position 29 to 151, the domain is characterized as RNase III.
+At position 179 to 249, the domain is characterized as DRBM.
+At position 11 to 124, the domain is characterized as NTF2.
+At position 211 to 410, the domain is characterized as Peptidase M12B.
+At position 418 to 504, the domain is characterized as Disintegrin.
+At position 47 to 60, the domain is characterized as LRRNT.
+At position 74 to 171, the domain is characterized as PH.
+At position 78 to 128, the domain is characterized as Myosin N-terminal SH3-like.
+At position 132 to 867, the domain is characterized as Myosin motor.
+At position 870 to 899, the domain is characterized as IQ.
+At position 2 to 198, the domain is characterized as ABC transporter.
+At position 569 to 692, the domain is characterized as DUSP 2.
+At position 712 to 825, the domain is characterized as DUSP 3.
+At position 930 to 1010, the domain is characterized as Ubiquitin-like.
+At position 598 to 680, the domain is characterized as BRCT.
+At position 77 to 343, the domain is characterized as Protein kinase.
+At position 344 to 414, the domain is characterized as AGC-kinase C-terminal.
+At position 1082 to 1201, the domain is characterized as PH.
+At position 1227 to 1499, the domain is characterized as CNH.
+At position 1571 to 1584, the domain is characterized as CRIB.
+At position 6 to 256, the domain is characterized as ABC transporter.
+At position 85 to 250, the domain is characterized as Helicase ATP-binding.
+At position 275 to 455, the domain is characterized as Helicase C-terminal.
+At position 383 to 561, the domain is characterized as ELMO.
+At position 238 to 330, the domain is characterized as ARID.
+At position 444 to 541, the domain is characterized as REKLES.
+At position 34 to 106, the domain is characterized as BTB.
+At position 55 to 314, the domain is characterized as Protein kinase.
+At position 119 to 413, the domain is characterized as ABC transmembrane type-1.
+At position 493 to 733, the domain is characterized as ABC transporter.
+At position 35 to 222, the domain is characterized as B30.2/SPRY.
+At position 253 to 285, the domain is characterized as LisH.
+At position 291 to 348, the domain is characterized as CTLH.
+At position 107 to 360, the domain is characterized as SET.
+At position 34 to 312, the domain is characterized as ABC transmembrane type-1.
+At position 216 to 332, the domain is characterized as SCP.
+At position 74 to 215, the domain is characterized as Cupin type-1 1.
+At position 249 to 393, the domain is characterized as Cupin type-1 2.
+At position 124 to 374, the domain is characterized as Protein kinase.
+At position 75 to 183, the domain is characterized as THUMP.
+At position 408 to 547, the domain is characterized as N-acetyltransferase.
+At position 1 to 32, the domain is characterized as GH18.
+At position 302 to 426, the domain is characterized as C2 2.
+At position 460 to 582, the domain is characterized as C2 3.
+At position 617 to 745, the domain is characterized as C2 4.
+At position 128 to 223, the domain is characterized as Ig-like C2-type 1.
+At position 228 to 306, the domain is characterized as Ig-like C2-type 2.
+At position 138 to 332, the domain is characterized as ATP-grasp.
+At position 76 to 148, the domain is characterized as Inhibitor I9.
+At position 154 to 460, the domain is characterized as Peptidase S8.
+At position 775 to 869, the domain is characterized as Fibronectin type-III 1.
+At position 969 to 1067, the domain is characterized as Fibronectin type-III 2.
+At position 1077 to 1179, the domain is characterized as Fibronectin type-III 3.
+At position 1246 to 1528, the domain is characterized as Protein kinase.
+At position 20 to 116, the domain is characterized as Mis18.
+At position 237 to 404, the domain is characterized as tr-type G.
+At position 538 to 608, the domain is characterized as J.
+At position 305 to 592, the domain is characterized as Protein kinase.
+At position 29 to 145, the domain is characterized as Plastocyanin-like 1.
+At position 157 to 308, the domain is characterized as Plastocyanin-like 2.
+At position 418 to 553, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 55, the domain is characterized as Kazal-like.
+At position 186 to 230, the domain is characterized as DSL.
+At position 231 to 264, the domain is characterized as EGF-like 1.
+At position 265 to 295, the domain is characterized as EGF-like 2; atypical.
+At position 297 to 335, the domain is characterized as EGF-like 3.
+At position 337 to 373, the domain is characterized as EGF-like 4.
+At position 375 to 411, the domain is characterized as EGF-like 5; calcium-binding.
+At position 413 to 449, the domain is characterized as EGF-like 6; calcium-binding.
+At position 451 to 486, the domain is characterized as EGF-like 7; calcium-binding.
+At position 488 to 524, the domain is characterized as EGF-like 8; calcium-binding.
+At position 526 to 562, the domain is characterized as EGF-like 9.
+At position 575 to 630, the domain is characterized as EGF-like 10.
+At position 632 to 668, the domain is characterized as EGF-like 11; calcium-binding.
+At position 670 to 706, the domain is characterized as EGF-like 12; calcium-binding.
+At position 708 to 744, the domain is characterized as EGF-like 13.
+At position 747 to 783, the domain is characterized as EGF-like 14.
+At position 785 to 821, the domain is characterized as EGF-like 15; calcium-binding.
+At position 823 to 859, the domain is characterized as EGF-like 16; calcium-binding.
+At position 917 to 959, the domain is characterized as EGF-like 17.
+At position 156 to 349, the domain is characterized as CheB-type methylesterase.
+At position 31 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 729 to 779, the domain is characterized as LRRCT.
+At position 832 to 975, the domain is characterized as TIR.
+At position 28 to 439, the domain is characterized as GH18.
+At position 137 to 575, the domain is characterized as Urease.
+At position 977 to 1036, the domain is characterized as SH3.
+At position 2271 to 2306, the domain is characterized as EF-hand 1.
+At position 2314 to 2349, the domain is characterized as EF-hand 2.
+At position 2352 to 2386, the domain is characterized as EF-hand 3.
+At position 214 to 326, the domain is characterized as Fe2OG dioxygenase.
+At position 40 to 113, the domain is characterized as RRM.
+At position 24 to 232, the domain is characterized as HD Cas3-type.
+At position 345 to 663, the domain is characterized as Peptidase S8.
+At position 101 to 185, the domain is characterized as Rhodanese.
+At position 49 to 232, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 148, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 183 to 304, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 432 to 767, the domain is characterized as Kinesin motor.
+At position 467 to 630, the domain is characterized as VPS9.
+At position 437 to 483, the domain is characterized as PAP-associated.
+At position 80 to 218, the domain is characterized as Flavodoxin-like.
+At position 251 to 465, the domain is characterized as FAD-binding FR-type.
+At position 20 to 212, the domain is characterized as Ch-type lysozyme.
+At position 1003 to 1082, the domain is characterized as Carrier.
+At position 35 to 278, the domain is characterized as ABC transporter.
+At position 4 to 236, the domain is characterized as GP-PDE.
+At position 109 to 446, the domain is characterized as Protein kinase.
+At position 128 to 217, the domain is characterized as EH 1.
+At position 161 to 196, the domain is characterized as EF-hand 1.
+At position 480 to 569, the domain is characterized as EH 2.
+At position 513 to 548, the domain is characterized as EF-hand 2.
+At position 1415 to 1432, the domain is characterized as WH2.
+At position 224 to 432, the domain is characterized as Ku.
+At position 116 to 219, the domain is characterized as Glutaredoxin.
+At position 88 to 280, the domain is characterized as ABC transmembrane type-1.
+At position 297 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 91 to 168, the domain is characterized as MIT.
+At position 438 to 578, the domain is characterized as Thioredoxin.
+At position 215 to 390, the domain is characterized as CRAL-TRIO.
+At position 155 to 396, the domain is characterized as Radical SAM core.
+At position 399 to 471, the domain is characterized as TRAM.
+At position 262 to 429, the domain is characterized as Helicase ATP-binding.
+At position 459 to 716, the domain is characterized as Helicase C-terminal.
+At position 235 to 407, the domain is characterized as EngA-type G 2.
+At position 408 to 492, the domain is characterized as KH-like.
+At position 469 to 482, the domain is characterized as CRIB.
+At position 947 to 1199, the domain is characterized as Protein kinase.
+At position 209 to 393, the domain is characterized as Albumin 2.
+At position 394 to 474, the domain is characterized as Albumin 3.
+At position 12 to 291, the domain is characterized as Protein kinase.
+At position 250 to 296, the domain is characterized as F-box.
+At position 2 to 119, the domain is characterized as Arf-GAP.
+At position 34 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 296 to 535, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 60 to 177, the domain is characterized as SEA.
+At position 200 to 430, the domain is characterized as Peptidase S1.
+At position 47 to 194, the domain is characterized as Histone-fold.
+At position 106 to 287, the domain is characterized as Helicase ATP-binding.
+At position 426 to 597, the domain is characterized as Helicase C-terminal.
+At position 623 to 713, the domain is characterized as Dicer dsRNA-binding fold.
+At position 862 to 990, the domain is characterized as PAZ.
+At position 1061 to 1172, the domain is characterized as RNase III 1.
+At position 1223 to 1374, the domain is characterized as RNase III 2.
+At position 1408 to 1476, the domain is characterized as DRBM.
+At position 68 to 151, the domain is characterized as Saposin B-type.
+At position 21 to 129, the domain is characterized as Calponin-homology (CH).
+At position 450 to 574, the domain is characterized as Ricin B-type lectin.
+At position 9 to 189, the domain is characterized as YrdC-like.
+At position 147 to 160, the domain is characterized as CRIB.
+At position 386 to 637, the domain is characterized as Protein kinase.
+At position 7 to 43, the domain is characterized as EF-hand 1.
+At position 88 to 121, the domain is characterized as EF-hand 3.
+At position 122 to 155, the domain is characterized as EF-hand 4.
+At position 56 to 317, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 422 to 518, the domain is characterized as Fibronectin type-III.
+At position 103 to 154, the domain is characterized as IF rod.
+At position 252 to 280, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 281 to 310, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 209 to 236, the domain is characterized as PLD phosphodiesterase 1.
+At position 423 to 449, the domain is characterized as PLD phosphodiesterase 2.
+At position 343 to 505, the domain is characterized as Helicase C-terminal.
+At position 5 to 149, the domain is characterized as Clp R.
+At position 141 to 377, the domain is characterized as Radical SAM core.
+At position 261 to 524, the domain is characterized as F-BAR.
+At position 730 to 942, the domain is characterized as Rho-GAP.
+At position 169 to 311, the domain is characterized as GAF.
+At position 347 to 576, the domain is characterized as Sigma-54 factor interaction.
+At position 531 to 706, the domain is characterized as Helicase ATP-binding.
+At position 871 to 1032, the domain is characterized as Helicase C-terminal.
+At position 201 to 425, the domain is characterized as CN hydrolase.
+At position 101 to 144, the domain is characterized as KH.
+At position 108 to 492, the domain is characterized as PTS EIIC type-1.
+At position 533 to 637, the domain is characterized as PTS EIIA type-1.
+At position 201 to 283, the domain is characterized as PDZ.
+At position 17 to 152, the domain is characterized as SprT-like.
+At position 185 to 247, the domain is characterized as LRRCT.
+At position 292 to 379, the domain is characterized as Fibronectin type-III.
+At position 418 to 464, the domain is characterized as F-box.
+At position 130 to 411, the domain is characterized as Protein kinase.
+At position 112 to 168, the domain is characterized as J.
+At position 14 to 185, the domain is characterized as FAD-binding PCMH-type.
+At position 35 to 99, the domain is characterized as HMA 1.
+At position 125 to 189, the domain is characterized as HMA 2.
+At position 7 to 102, the domain is characterized as Ig-like.
+At position 125 to 293, the domain is characterized as tr-type G.
+At position 53 to 139, the domain is characterized as Doublecortin 1.
+At position 180 to 263, the domain is characterized as Doublecortin 2.
+At position 344 to 958, the domain is characterized as USP.
+At position 712 to 731, the domain is characterized as UIM 1.
+At position 813 to 832, the domain is characterized as UIM 2.
+At position 835 to 854, the domain is characterized as UIM 3.
+At position 12 to 70, the domain is characterized as Collagen-like 1.
+At position 69 to 126, the domain is characterized as Collagen-like 2.
+At position 337 to 387, the domain is characterized as Collagen-like 3.
+At position 390 to 448, the domain is characterized as Collagen-like 4.
+At position 438 to 493, the domain is characterized as Collagen-like 5.
+At position 525 to 582, the domain is characterized as Collagen-like 6.
+At position 636 to 694, the domain is characterized as Collagen-like 7.
+At position 822 to 873, the domain is characterized as Collagen-like 8.
+At position 969 to 1026, the domain is characterized as Collagen-like 9.
+At position 5 to 117, the domain is characterized as PH.
+At position 3 to 149, the domain is characterized as MPN.
+At position 9 to 131, the domain is characterized as Arf-GAP.
+At position 130 to 200, the domain is characterized as BTB.
+At position 245 to 310, the domain is characterized as BACK.
+At position 594 to 672, the domain is characterized as BRCT.
+At position 158 to 353, the domain is characterized as CheB-type methylesterase.
+At position 100 to 323, the domain is characterized as Radical SAM core.
+At position 82 to 175, the domain is characterized as Toprim.
+At position 94 to 153, the domain is characterized as Myb-like.
+At position 617 to 1049, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1776 to 1851, the domain is characterized as Carrier 2.
+At position 415 to 523, the domain is characterized as Ig-like C2-type 4.
+At position 115 to 295, the domain is characterized as FAD-binding PCMH-type.
+At position 77 to 195, the domain is characterized as MTTase N-terminal.
+At position 218 to 448, the domain is characterized as Radical SAM core.
+At position 450 to 513, the domain is characterized as TRAM.
+At position 454 to 728, the domain is characterized as Protein kinase.
+At position 137 to 346, the domain is characterized as ATP-grasp.
+At position 454 to 707, the domain is characterized as ABC transporter.
+At position 902 to 1154, the domain is characterized as ABC transmembrane type-2.
+At position 134 to 386, the domain is characterized as AB hydrolase-1.
+At position 39 to 385, the domain is characterized as GH18.
+At position 1098 to 1170, the domain is characterized as RRM.
+At position 41 to 346, the domain is characterized as AB hydrolase-1.
+At position 148 to 353, the domain is characterized as ATP-grasp.
+At position 55 to 130, the domain is characterized as Rho RNA-BD.
+At position 5 to 142, the domain is characterized as SprT-like.
+At position 570 to 786, the domain is characterized as ABC transporter 1.
+At position 812 to 1129, the domain is characterized as ABC transporter 2.
+At position 942 to 1003, the domain is characterized as Chromo.
+At position 51 to 176, the domain is characterized as EamA 1.
+At position 274 to 327, the domain is characterized as EamA 2.
+At position 25 to 60, the domain is characterized as Chitin-binding type-1.
+At position 26 to 121, the domain is characterized as EthD.
+At position 48 to 91, the domain is characterized as EGF-like 1.
+At position 107 to 154, the domain is characterized as EGF-like 2.
+At position 180 to 226, the domain is characterized as EGF-like 3.
+At position 252 to 298, the domain is characterized as EGF-like 4.
+At position 1449 to 1691, the domain is characterized as Peptidase S1.
+At position 221 to 371, the domain is characterized as Collagen-like.
+At position 19 to 57, the domain is characterized as LRRNT.
+At position 331 to 383, the domain is characterized as LRRCT.
+At position 38 to 131, the domain is characterized as CTCK.
+At position 45 to 287, the domain is characterized as ATP-grasp.
+At position 38 to 90, the domain is characterized as HTH myb-type 1.
+At position 91 to 145, the domain is characterized as HTH myb-type 2.
+At position 32 to 178, the domain is characterized as UBC core.
+At position 77 to 145, the domain is characterized as Biotinyl-binding.
+At position 23 to 115, the domain is characterized as CARD.
+At position 49 to 228, the domain is characterized as sHSP.
+At position 1377 to 1450, the domain is characterized as J.
+At position 7 to 420, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 352 to 449, the domain is characterized as PFU.
+At position 465 to 715, the domain is characterized as PUL.
+At position 202 to 369, the domain is characterized as PCI.
+At position 99 to 169, the domain is characterized as S1 motif 1.
+At position 187 to 251, the domain is characterized as S1 motif 2.
+At position 264 to 332, the domain is characterized as S1 motif 3.
+At position 31 to 304, the domain is characterized as Pyruvate carboxyltransferase.
+At position 26 to 53, the domain is characterized as LRRNT.
+At position 182 to 234, the domain is characterized as LRRCT.
+At position 236 to 324, the domain is characterized as Ig-like C2-type 1.
+At position 332 to 418, the domain is characterized as Ig-like C2-type 2.
+At position 423 to 510, the domain is characterized as Ig-like C2-type 3.
+At position 515 to 600, the domain is characterized as Ig-like C2-type 4.
+At position 1392 to 1450, the domain is characterized as VWFC.
+At position 172 to 239, the domain is characterized as KH 1.
+At position 324 to 392, the domain is characterized as KH 2.
+At position 805 to 868, the domain is characterized as SAM.
+At position 58 to 264, the domain is characterized as ABC transmembrane type-1.
+At position 34 to 181, the domain is characterized as N-acetyltransferase.
+At position 159 to 336, the domain is characterized as PCI.
+At position 214 to 271, the domain is characterized as LRRCT.
+At position 56 to 261, the domain is characterized as ABC transmembrane type-1 1.
+At position 331 to 525, the domain is characterized as ABC transmembrane type-1 2.
+At position 115 to 249, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 32 to 247, the domain is characterized as ABC transporter.
+At position 25 to 86, the domain is characterized as Pre-SET.
+At position 89 to 213, the domain is characterized as SET.
+At position 221 to 237, the domain is characterized as Post-SET.
+At position 41 to 135, the domain is characterized as Fibronectin type-III 1.
+At position 145 to 249, the domain is characterized as Fibronectin type-III 2.
+At position 250 to 311, the domain is characterized as Fibronectin type-III 3.
+At position 1 to 204, the domain is characterized as PPIase cyclophilin-type.
+At position 4 to 265, the domain is characterized as ATP-grasp.
+At position 73 to 360, the domain is characterized as Protein kinase.
+At position 616 to 701, the domain is characterized as BRCT.
+At position 50 to 240, the domain is characterized as Cupin type-1 1.
+At position 330 to 479, the domain is characterized as Cupin type-1 2.
+At position 593 to 622, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 23 to 102, the domain is characterized as GS beta-grasp.
+At position 109 to 369, the domain is characterized as GS catalytic.
+At position 124 to 220, the domain is characterized as Fibronectin type-III 1.
+At position 227 to 327, the domain is characterized as Fibronectin type-III 2.
+At position 329 to 431, the domain is characterized as Fibronectin type-III 3.
+At position 436 to 535, the domain is characterized as Fibronectin type-III 4.
+At position 537 to 631, the domain is characterized as Fibronectin type-III 5.
+At position 635 to 735, the domain is characterized as Fibronectin type-III 6.
+At position 736 to 836, the domain is characterized as Fibronectin type-III 7.
+At position 16 to 86, the domain is characterized as Chromo 1.
+At position 111 to 176, the domain is characterized as Chromo 2.
+At position 217 to 387, the domain is characterized as Helicase ATP-binding.
+At position 518 to 669, the domain is characterized as Helicase C-terminal.
+At position 2 to 127, the domain is characterized as Nudix hydrolase.
+At position 16 to 186, the domain is characterized as FAD-binding PCMH-type.
+At position 226 to 273, the domain is characterized as RPE1 insert.
+At position 99 to 199, the domain is characterized as HTH araC/xylS-type.
+At position 337 to 375, the domain is characterized as LRRCT.
+At position 414 to 597, the domain is characterized as Guanylate kinase-like.
+At position 228 to 250, the domain is characterized as FBD.
+At position 32 to 129, the domain is characterized as PH.
+At position 642 to 836, the domain is characterized as Rab-GAP TBC.
+At position 133 to 411, the domain is characterized as Protein kinase.
+At position 129 to 168, the domain is characterized as UBA.
+At position 271 to 446, the domain is characterized as B30.2/SPRY.
+At position 286 to 468, the domain is characterized as PPIase cyclophilin-type.
+At position 17 to 178, the domain is characterized as NAC.
+At position 148 to 435, the domain is characterized as ABC transmembrane type-1.
+At position 470 to 707, the domain is characterized as ABC transporter.
+At position 33 to 296, the domain is characterized as Tyrosine-protein phosphatase.
+At position 16 to 152, the domain is characterized as MPN.
+At position 104 to 169, the domain is characterized as OVATE.
+At position 435 to 614, the domain is characterized as Lon proteolytic.
+At position 89 to 307, the domain is characterized as Radical SAM core.
+At position 55 to 235, the domain is characterized as Guanylate kinase-like.
+At position 32 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 865 to 1010, the domain is characterized as TIR.
+At position 38 to 98, the domain is characterized as SH3.
+At position 100 to 191, the domain is characterized as SH2.
+At position 31 to 119, the domain is characterized as GOLD.
+At position 63 to 218, the domain is characterized as CRAL-TRIO.
+At position 244 to 431, the domain is characterized as Rho-GAP.
+At position 142 to 301, the domain is characterized as F5/8 type C.
+At position 200 to 452, the domain is characterized as Lon N-terminal.
+At position 895 to 1081, the domain is characterized as Lon proteolytic.
+At position 88 to 261, the domain is characterized as PXA.
+At position 311 to 422, the domain is characterized as PX.
+At position 9 to 696, the domain is characterized as Myosin motor.
+At position 813 to 1006, the domain is characterized as TH1.
+At position 40 to 166, the domain is characterized as MARVEL.
+At position 32 to 701, the domain is characterized as PFL.
+At position 708 to 831, the domain is characterized as Glycine radical.
+At position 453 to 682, the domain is characterized as PH.
+At position 679 to 822, the domain is characterized as Arf-GAP.
+At position 294 to 472, the domain is characterized as VWFA.
+At position 488 to 577, the domain is characterized as Cache.
+At position 35 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 275 to 435, the domain is characterized as Helicase ATP-binding.
+At position 454 to 614, the domain is characterized as Helicase C-terminal.
+At position 134 to 175, the domain is characterized as EGF-like; calcium-binding.
+At position 245 to 290, the domain is characterized as Collagen-like 1.
+At position 300 to 333, the domain is characterized as Collagen-like 2.
+At position 182 to 254, the domain is characterized as DRBM 2.
+At position 162 to 348, the domain is characterized as CheB-type methylesterase.
+At position 246 to 317, the domain is characterized as HARP 1.
+At position 349 to 420, the domain is characterized as HARP 2.
+At position 466 to 621, the domain is characterized as Helicase ATP-binding.
+At position 737 to 890, the domain is characterized as Helicase C-terminal.
+At position 6 to 171, the domain is characterized as Exonuclease.
+At position 19 to 47, the domain is characterized as Antistasin-like.
+At position 105 to 134, the domain is characterized as IQ.
+At position 679 to 750, the domain is characterized as PAS.
+At position 822 to 1051, the domain is characterized as Histidine kinase.
+At position 172 to 242, the domain is characterized as MBD.
+At position 304 to 378, the domain is characterized as Pre-SET.
+At position 381 to 672, the domain is characterized as SET.
+At position 11 to 259, the domain is characterized as Lon N-terminal.
+At position 118 to 172, the domain is characterized as bHLH.
+At position 929 to 1021, the domain is characterized as Fibronectin type-III 1.
+At position 1246 to 1354, the domain is characterized as CBM20.
+At position 1677 to 1740, the domain is characterized as SLH 1.
+At position 1741 to 1799, the domain is characterized as SLH 2.
+At position 1802 to 1861, the domain is characterized as SLH 3.
+At position 422 to 537, the domain is characterized as Toprim.
+At position 14 to 126, the domain is characterized as HotDog ACOT-type.
+At position 88 to 136, the domain is characterized as bHLH.
+At position 23 to 111, the domain is characterized as GS beta-grasp.
+At position 119 to 491, the domain is characterized as GS catalytic.
+At position 205 to 287, the domain is characterized as RCK C-terminal 1.
+At position 294 to 376, the domain is characterized as RCK C-terminal 2.
+At position 21 to 72, the domain is characterized as LCN-type CS-alpha/beta.
+At position 136 to 214, the domain is characterized as RRM 1.
+At position 230 to 308, the domain is characterized as RRM 2.
+At position 119 to 171, the domain is characterized as bHLH.
+At position 414 to 476, the domain is characterized as SH3 1.
+At position 494 to 553, the domain is characterized as SH3 2.
+At position 570 to 629, the domain is characterized as SH3 3.
+At position 660 to 719, the domain is characterized as SH3 4.
+At position 729 to 788, the domain is characterized as SH3 5.
+At position 194 to 229, the domain is characterized as EF-hand 1.
+At position 238 to 273, the domain is characterized as EF-hand 2.
+At position 357 to 514, the domain is characterized as Ferric oxidoreductase.
+At position 548 to 670, the domain is characterized as FAD-binding FR-type.
+At position 60 to 425, the domain is characterized as Peptidase A1.
+At position 556 to 620, the domain is characterized as KH.
+At position 630 to 701, the domain is characterized as S1 motif.
+At position 3 to 56, the domain is characterized as bHLH.
+At position 5 to 252, the domain is characterized as Pyruvate carboxyltransferase.
+At position 40 to 268, the domain is characterized as Radical SAM core.
+At position 775 to 1098, the domain is characterized as PDEase.
+At position 287 to 599, the domain is characterized as Protein kinase.
+At position 210 to 475, the domain is characterized as Protein kinase.
+At position 7 to 206, the domain is characterized as tr-type G.
+At position 29 to 254, the domain is characterized as Glutamine amidotransferase type-2.
+At position 19 to 151, the domain is characterized as Ephrin RBD.
+At position 12 to 99, the domain is characterized as MtN3/slv 1.
+At position 7 to 61, the domain is characterized as Myosin N-terminal SH3-like.
+At position 65 to 749, the domain is characterized as Myosin motor.
+At position 753 to 773, the domain is characterized as IQ 1.
+At position 776 to 796, the domain is characterized as IQ 2.
+At position 801 to 821, the domain is characterized as IQ 3.
+At position 824 to 844, the domain is characterized as IQ 4.
+At position 849 to 869, the domain is characterized as IQ 5.
+At position 872 to 892, the domain is characterized as IQ 6.
+At position 1171 to 1417, the domain is characterized as Dilute.
+At position 2 to 177, the domain is characterized as PBS-linker.
+At position 217 to 269, the domain is characterized as CpcD-like.
+At position 125 to 172, the domain is characterized as UPAR/Ly6.
+At position 540 to 569, the domain is characterized as IQ.
+At position 6 to 223, the domain is characterized as ABC transporter.
+At position 10 to 203, the domain is characterized as DPCK.
+At position 364 to 613, the domain is characterized as TLDc.
+At position 12 to 86, the domain is characterized as ACT.
+At position 5 to 78, the domain is characterized as DWNN.
+At position 606 to 946, the domain is characterized as PUM-HD.
+At position 22 to 206, the domain is characterized as RNase H type-2.
+At position 232 to 312, the domain is characterized as DEP.
+At position 344 to 474, the domain is characterized as RGS.
+At position 13 to 119, the domain is characterized as PRD.
+At position 159 to 412, the domain is characterized as Tyrosine-protein phosphatase.
+At position 301 to 435, the domain is characterized as Nudix hydrolase.
+At position 199 to 374, the domain is characterized as OTU.
+At position 360 to 706, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 1019 to 1306, the domain is characterized as CNH.
+At position 243 to 514, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 26 to 136, the domain is characterized as MTTase N-terminal.
+At position 153 to 389, the domain is characterized as Radical SAM core.
+At position 392 to 458, the domain is characterized as TRAM.
+At position 68 to 142, the domain is characterized as Cadherin 1.
+At position 143 to 264, the domain is characterized as Cadherin 2.
+At position 277 to 387, the domain is characterized as Cadherin 3.
+At position 388 to 500, the domain is characterized as Cadherin 4.
+At position 519 to 604, the domain is characterized as Cadherin 5.
+At position 605 to 704, the domain is characterized as Cadherin 6.
+At position 707 to 807, the domain is characterized as Cadherin 7.
+At position 808 to 908, the domain is characterized as Cadherin 8.
+At position 909 to 1005, the domain is characterized as Cadherin 9.
+At position 1038 to 1148, the domain is characterized as Cadherin 10.
+At position 1156 to 1270, the domain is characterized as Cadherin 11.
+At position 158 to 200, the domain is characterized as CUE 1.
+At position 253 to 296, the domain is characterized as CUE 2.
+At position 511 to 679, the domain is characterized as Helicase ATP-binding.
+At position 860 to 1012, the domain is characterized as Helicase C-terminal.
+At position 7 to 38, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 244 to 482, the domain is characterized as Grh/CP2 DB.
+At position 717 to 767, the domain is characterized as bHLH.
+At position 9 to 66, the domain is characterized as HTH cro/C1-type.
+At position 72 to 379, the domain is characterized as SAM-dependent MTase C5-type.
+At position 158 to 306, the domain is characterized as TRUD.
+At position 397 to 682, the domain is characterized as Protein kinase.
+At position 22 to 127, the domain is characterized as Ig-like 1.
+At position 131 to 215, the domain is characterized as Ig-like 2.
+At position 142 to 395, the domain is characterized as NR LBD.
+At position 27 to 177, the domain is characterized as UBC core.
+At position 18 to 265, the domain is characterized as SET.
+At position 288 to 492, the domain is characterized as Helicase ATP-binding.
+At position 520 to 666, the domain is characterized as Helicase C-terminal.
+At position 7 to 222, the domain is characterized as ABC transporter.
+At position 36 to 231, the domain is characterized as Thioredoxin.
+At position 309 to 368, the domain is characterized as Tudor 1.
+At position 542 to 599, the domain is characterized as Tudor 2.
+At position 820 to 879, the domain is characterized as Tudor 3.
+At position 1038 to 1092, the domain is characterized as Tudor 4.
+At position 1358 to 1417, the domain is characterized as Tudor 5.
+At position 1570 to 1630, the domain is characterized as Tudor 6.
+At position 27 to 108, the domain is characterized as GST N-terminal.
+At position 86 to 230, the domain is characterized as GST C-terminal.
+At position 36 to 119, the domain is characterized as DEP 1.
+At position 145 to 219, the domain is characterized as DEP 2.
+At position 330 to 407, the domain is characterized as PDZ.
+At position 384 to 447, the domain is characterized as bZIP.
+At position 280 to 405, the domain is characterized as DBINO.
+At position 530 to 701, the domain is characterized as Helicase ATP-binding.
+At position 1105 to 1260, the domain is characterized as Helicase C-terminal.
+At position 7 to 328, the domain is characterized as DhaK.
+At position 147 to 185, the domain is characterized as LRRCT.
+At position 53 to 238, the domain is characterized as BPL/LPL catalytic.
+At position 253 to 283, the domain is characterized as EGF-like 2.
+At position 364 to 401, the domain is characterized as EGF-like 5.
+At position 111 to 317, the domain is characterized as ATP-grasp.
+At position 267 to 338, the domain is characterized as PAS.
+At position 539 to 875, the domain is characterized as PDEase.
+At position 603 to 688, the domain is characterized as Smr.
+At position 428 to 849, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1345 to 1663, the domain is characterized as PKS/mFAS DH.
+At position 1711 to 1785, the domain is characterized as Carrier.
+At position 463 to 785, the domain is characterized as UvrD-like helicase C-terminal.
+At position 946 to 1239, the domain is characterized as Protein kinase.
+At position 8 to 51, the domain is characterized as SpoVT-AbrB 1.
+At position 90 to 140, the domain is characterized as SpoVT-AbrB 2.
+At position 93 to 272, the domain is characterized as FAD-binding PCMH-type.
+At position 12 to 179, the domain is characterized as Miro 1.
+At position 195 to 230, the domain is characterized as EF-hand 1.
+At position 315 to 350, the domain is characterized as EF-hand 2.
+At position 423 to 592, the domain is characterized as Miro 2.
+At position 366 to 646, the domain is characterized as Autotransporter.
+At position 336 to 745, the domain is characterized as Single-minded C-terminal.
+At position 1 to 124, the domain is characterized as MsrB.
+At position 27 to 610, the domain is characterized as Peptidase M2.
+At position 442 to 705, the domain is characterized as Protein kinase.
+At position 724 to 797, the domain is characterized as U-box.
+At position 27 to 144, the domain is characterized as DSCP-N.
+At position 148 to 170, the domain is characterized as Follistatin-like 1.
+At position 175 to 197, the domain is characterized as Follistatin-like 2.
+At position 209 to 231, the domain is characterized as Follistatin-like 3.
+At position 240 to 262, the domain is characterized as Follistatin-like 4.
+At position 276 to 298, the domain is characterized as Follistatin-like 5.
+At position 304 to 327, the domain is characterized as Follistatin-like 6.
+At position 332 to 354, the domain is characterized as Follistatin-like 7.
+At position 362 to 384, the domain is characterized as Follistatin-like 8.
+At position 49 to 97, the domain is characterized as F-box.
+At position 72 to 101, the domain is characterized as IQ 1.
+At position 128 to 157, the domain is characterized as IQ 2.
+At position 293 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 130, the domain is characterized as Nudix hydrolase.
+At position 109 to 340, the domain is characterized as Era-type G.
+At position 370 to 447, the domain is characterized as KH type-2.
+At position 314 to 620, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 31 to 129, the domain is characterized as Fibronectin type-III 1.
+At position 142 to 240, the domain is characterized as Fibronectin type-III 2.
+At position 12 to 132, the domain is characterized as C-type lectin.
+At position 5 to 338, the domain is characterized as MACPF.
+At position 52 to 215, the domain is characterized as SIS.
+At position 104 to 124, the domain is characterized as UIM 2.
+At position 3 to 112, the domain is characterized as STAS.
+At position 35 to 194, the domain is characterized as Cupin type-1 1.
+At position 536 to 576, the domain is characterized as UBA.
+At position 194 to 363, the domain is characterized as tr-type G.
+At position 150 to 258, the domain is characterized as C-type lectin.
+At position 150 to 215, the domain is characterized as HTH luxR-type.
+At position 24 to 140, the domain is characterized as MTTase N-terminal.
+At position 164 to 410, the domain is characterized as Radical SAM core.
+At position 413 to 476, the domain is characterized as TRAM.
+At position 22 to 196, the domain is characterized as EngB-type G.
+At position 32 to 148, the domain is characterized as Cadherin 1.
+At position 149 to 249, the domain is characterized as Cadherin 2.
+At position 675 to 839, the domain is characterized as PCI.
+At position 435 to 509, the domain is characterized as GW 1.
+At position 511 to 585, the domain is characterized as GW 2.
+At position 604 to 678, the domain is characterized as GW 3.
+At position 680 to 754, the domain is characterized as GW 4.
+At position 776 to 851, the domain is characterized as GW 5.
+At position 853 to 928, the domain is characterized as GW 6.
+At position 935 to 1009, the domain is characterized as GW 7.
+At position 464 to 749, the domain is characterized as Protein kinase.
+At position 821 to 951, the domain is characterized as Guanylate cyclase.
+At position 129 to 158, the domain is characterized as NR LBD.
+At position 1 to 277, the domain is characterized as GH84.
+At position 2 to 187, the domain is characterized as KARI N-terminal Rossmann.
+At position 188 to 333, the domain is characterized as KARI C-terminal knotted.
+At position 133 to 363, the domain is characterized as Radical SAM core.
+At position 366 to 435, the domain is characterized as TRAM.
+At position 10 to 164, the domain is characterized as Tyrosine-protein phosphatase.
+At position 31 to 163, the domain is characterized as MARVEL 1.
+At position 168 to 319, the domain is characterized as MARVEL 2.
+At position 527 to 616, the domain is characterized as EH.
+At position 7 to 449, the domain is characterized as ABC transporter.
+At position 33 to 192, the domain is characterized as Thioredoxin.
+At position 46 to 273, the domain is characterized as ABC transmembrane type-2.
+At position 283 to 516, the domain is characterized as NR LBD.
+At position 183 to 468, the domain is characterized as Deacetylase sirtuin-type.
+At position 140 to 221, the domain is characterized as BRX 1.
+At position 315 to 370, the domain is characterized as BRX 2.
+At position 205 to 290, the domain is characterized as KH.
+At position 331 to 424, the domain is characterized as HD.
+At position 1 to 51, the domain is characterized as Rubredoxin-like.
+At position 12 to 135, the domain is characterized as Toprim.
+At position 186 to 341, the domain is characterized as C1q.
+At position 171 to 412, the domain is characterized as Protein kinase.
+At position 593 to 829, the domain is characterized as EAL.
+At position 7 to 88, the domain is characterized as Plastocyanin-like 1.
+At position 98 to 225, the domain is characterized as Plastocyanin-like 2.
+At position 318 to 451, the domain is characterized as Plastocyanin-like 3.
+At position 632 to 826, the domain is characterized as Roc.
+At position 1242 to 1525, the domain is characterized as Protein kinase.
+At position 289 to 390, the domain is characterized as PH.
+At position 776 to 945, the domain is characterized as VASt.
+At position 97 to 195, the domain is characterized as Cadherin 1.
+At position 204 to 301, the domain is characterized as Cadherin 2.
+At position 311 to 412, the domain is characterized as Cadherin 3.
+At position 420 to 522, the domain is characterized as Cadherin 4.
+At position 532 to 633, the domain is characterized as Cadherin 5.
+At position 631 to 733, the domain is characterized as Cadherin 6.
+At position 741 to 835, the domain is characterized as Cadherin 7.
+At position 1084 to 1123, the domain is characterized as EGF-like.
+At position 1125 to 1313, the domain is characterized as Laminin G-like.
+At position 60 to 234, the domain is characterized as VWFD 1.
+At position 326 to 381, the domain is characterized as TIL 1.
+At position 450 to 501, the domain is characterized as TIL 2.
+At position 539 to 706, the domain is characterized as VWFD 2.
+At position 820 to 870, the domain is characterized as TIL 3.
+At position 947 to 1127, the domain is characterized as VWFA 1.
+At position 1167 to 1334, the domain is characterized as VWFA 2.
+At position 1360 to 1540, the domain is characterized as VWFA 3.
+At position 1617 to 1793, the domain is characterized as VWFD 3.
+At position 1924 to 1997, the domain is characterized as VWFC 1.
+At position 2098 to 2164, the domain is characterized as VWFC 2.
+At position 2249 to 2314, the domain is characterized as VWFC 3.
+At position 2393 to 2481, the domain is characterized as CTCK.
+At position 13 to 109, the domain is characterized as EthD.
+At position 86 to 115, the domain is characterized as EGF-like.
+At position 72 to 263, the domain is characterized as Rab-GAP TBC.
+At position 107 to 142, the domain is characterized as QLQ.
+At position 158 to 202, the domain is characterized as WRC.
+At position 6 to 104, the domain is characterized as SH2.
+At position 63 to 126, the domain is characterized as BTB.
+At position 32 to 312, the domain is characterized as FERM.
+At position 55 to 466, the domain is characterized as USP.
+At position 32 to 222, the domain is characterized as GH11.
+At position 868 to 931, the domain is characterized as SAM.
+At position 119 to 497, the domain is characterized as Protein kinase.
+At position 267 to 506, the domain is characterized as NR LBD.
+At position 33 to 131, the domain is characterized as Ig-like V-type.
+At position 4 to 90, the domain is characterized as KRAB.
+At position 226 to 590, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 301 to 543, the domain is characterized as Glutamine amidotransferase type-1.
+At position 17 to 123, the domain is characterized as PH.
+At position 133 to 327, the domain is characterized as Rho-GAP.
+At position 194 to 253, the domain is characterized as Mop 2.
+At position 508 to 585, the domain is characterized as IPT/TIG.
+At position 19 to 50, the domain is characterized as LRRNT.
+At position 180 to 231, the domain is characterized as LRRCT.
+At position 232 to 343, the domain is characterized as Ig-like.
+At position 72 to 215, the domain is characterized as HD.
+At position 221 to 661, the domain is characterized as Myotubularin phosphatase.
+At position 753 to 860, the domain is characterized as PH.
+At position 147 to 174, the domain is characterized as PLD phosphodiesterase.
+At position 5 to 93, the domain is characterized as Ig-like C1-type.
+At position 6 to 332, the domain is characterized as Asparaginase/glutaminase.
+At position 105 to 181, the domain is characterized as PRC barrel.
+At position 100 to 199, the domain is characterized as Rieske.
+At position 61 to 162, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 25 to 286, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 8 to 102, the domain is characterized as ACB.
+At position 264 to 355, the domain is characterized as RRM 1.
+At position 372 to 454, the domain is characterized as RRM 2.
+At position 38 to 589, the domain is characterized as PLA2c.
+At position 46 to 274, the domain is characterized as ATP-grasp.
+At position 523 to 577, the domain is characterized as LRRCT.
+At position 633 to 776, the domain is characterized as TIR.
+At position 79 to 390, the domain is characterized as IF rod.
+At position 300 to 346, the domain is characterized as G-patch.
+At position 195 to 368, the domain is characterized as EngA-type G 2.
+At position 27 to 71, the domain is characterized as CAP-Gly.
+At position 343 to 381, the domain is characterized as LRRCT.
+At position 30 to 299, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 193 to 355, the domain is characterized as JmjC.
+At position 1 to 317, the domain is characterized as 5'-3' exonuclease.
+At position 318 to 494, the domain is characterized as 3'-5' exonuclease.
+At position 2 to 59, the domain is characterized as 4Fe-4S.
+At position 63 to 138, the domain is characterized as BTB.
+At position 4 to 146, the domain is characterized as Clp R.
+At position 661 to 949, the domain is characterized as ABC transmembrane type-1 2.
+At position 160 to 200, the domain is characterized as LRRCT.
+At position 450 to 557, the domain is characterized as Rhodanese.
+At position 197 to 216, the domain is characterized as UIM 1.
+At position 221 to 240, the domain is characterized as UIM 2.
+At position 37 to 394, the domain is characterized as PIPK.
+At position 142 to 456, the domain is characterized as Kinesin motor.
+At position 416 to 480, the domain is characterized as S4 RNA-binding.
+At position 33 to 353, the domain is characterized as G-alpha.
+At position 140 to 205, the domain is characterized as HTH luxR-type.
+At position 3 to 157, the domain is characterized as N-acetyltransferase.
+At position 45 to 189, the domain is characterized as SCP.
+At position 190 to 457, the domain is characterized as SF4 helicase.
+At position 9 to 160, the domain is characterized as YEATS.
+At position 133 to 511, the domain is characterized as USP.
+At position 64 to 134, the domain is characterized as Chitin-binding type R&R.
+At position 139 to 245, the domain is characterized as Gnk2-homologous 2.
+At position 325 to 608, the domain is characterized as Protein kinase.
+At position 46 to 234, the domain is characterized as Peptidase M12A.
+At position 29 to 156, the domain is characterized as PLAT.
+At position 595 to 928, the domain is characterized as Reverse transcriptase.
+At position 1 to 110, the domain is characterized as BRCT.
+At position 818 to 935, the domain is characterized as TIR.
+At position 68 to 320, the domain is characterized as GB1/RHD3-type G.
+At position 2 to 115, the domain is characterized as STAS.
+At position 7 to 191, the domain is characterized as Guanylate kinase-like.
+At position 55 to 123, the domain is characterized as POTRA.
+At position 722 to 798, the domain is characterized as Carrier.
+At position 296 to 380, the domain is characterized as RRM 1.
+At position 384 to 462, the domain is characterized as RRM 2.
+At position 6 to 420, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 558 to 851, the domain is characterized as Protein kinase.
+At position 982 to 1289, the domain is characterized as SEC63 1.
+At position 1340 to 1515, the domain is characterized as Helicase ATP-binding 2.
+At position 1548 to 1756, the domain is characterized as Helicase C-terminal 2.
+At position 1815 to 2127, the domain is characterized as SEC63 2.
+At position 248 to 303, the domain is characterized as DEK-C.
+At position 307 to 448, the domain is characterized as Tyrosine-protein phosphatase.
+At position 23 to 244, the domain is characterized as ABC transporter.
+At position 744 to 914, the domain is characterized as Helicase ATP-binding.
+At position 1160 to 1334, the domain is characterized as Helicase C-terminal.
+At position 120 to 478, the domain is characterized as TTL.
+At position 91 to 140, the domain is characterized as bHLH.
+At position 408 to 536, the domain is characterized as Guanylate cyclase.
+At position 438 to 661, the domain is characterized as Guanylate cyclase 1.
+At position 1189 to 1311, the domain is characterized as Guanylate cyclase 2.
+At position 22 to 167, the domain is characterized as VOC 1.
+At position 182 to 322, the domain is characterized as VOC 2.
+At position 27 to 148, the domain is characterized as Calponin-homology (CH).
+At position 203 to 275, the domain is characterized as GAR.
+At position 353 to 496, the domain is characterized as RCK N-terminal.
+At position 43 to 165, the domain is characterized as FZ.
+At position 20 to 59, the domain is characterized as EGF-like 1.
+At position 62 to 106, the domain is characterized as EGF-like 2.
+At position 109 to 265, the domain is characterized as F5/8 type C 1.
+At position 270 to 427, the domain is characterized as F5/8 type C 2.
+At position 199 to 266, the domain is characterized as SCA7.
+At position 122 to 226, the domain is characterized as Fibronectin type-III.
+At position 3 to 148, the domain is characterized as UBC core.
+At position 29 to 217, the domain is characterized as BPL/LPL catalytic.
+At position 557 to 665, the domain is characterized as Thioredoxin 3.
+At position 671 to 776, the domain is characterized as Thioredoxin 4.
+At position 15 to 229, the domain is characterized as HORMA.
+At position 974 to 1255, the domain is characterized as ABC transmembrane type-1 2.
+At position 1292 to 1526, the domain is characterized as ABC transporter 2.
+At position 283 to 509, the domain is characterized as TLDc.
+At position 30 to 151, the domain is characterized as EamA 1.
+At position 170 to 291, the domain is characterized as EamA 2.
+At position 554 to 615, the domain is characterized as SH3.
+At position 633 to 697, the domain is characterized as SAM 1.
+At position 1177 to 1241, the domain is characterized as SAM 2.
+At position 18 to 306, the domain is characterized as Radical SAM core.
+At position 49 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 699 to 823, the domain is characterized as DMAP1-binding.
+At position 984 to 1019, the domain is characterized as EF-hand.
+At position 108 to 148, the domain is characterized as EGF-like 1.
+At position 195 to 236, the domain is characterized as EGF-like 3.
+At position 237 to 276, the domain is characterized as EGF-like 4.
+At position 322 to 362, the domain is characterized as EGF-like 5.
+At position 371 to 505, the domain is characterized as FAS1 1.
+At position 515 to 652, the domain is characterized as FAS1 2.
+At position 736 to 776, the domain is characterized as EGF-like 6.
+At position 826 to 866, the domain is characterized as EGF-like 7.
+At position 867 to 909, the domain is characterized as EGF-like 8.
+At position 910 to 952, the domain is characterized as EGF-like 9.
+At position 953 to 992, the domain is characterized as EGF-like 10.
+At position 994 to 1127, the domain is characterized as FAS1 3.
+At position 1137 to 1265, the domain is characterized as FAS1 4.
+At position 1343 to 1408, the domain is characterized as Laminin EGF-like 1.
+At position 1432 to 1470, the domain is characterized as EGF-like 11.
+At position 1471 to 1512, the domain is characterized as EGF-like 12.
+At position 1513 to 1554, the domain is characterized as EGF-like 13.
+At position 1555 to 1594, the domain is characterized as EGF-like 14.
+At position 1596 to 1724, the domain is characterized as FAS1 5.
+At position 1740 to 1881, the domain is characterized as FAS1 6.
+At position 1957 to 2022, the domain is characterized as Laminin EGF-like 2.
+At position 2047 to 2081, the domain is characterized as EGF-like 15.
+At position 2082 to 2122, the domain is characterized as EGF-like 16.
+At position 2123 to 2165, the domain is characterized as EGF-like 17.
+At position 2198 to 2291, the domain is characterized as Link.
+At position 2311 to 2446, the domain is characterized as FAS1 7.
+At position 140 to 397, the domain is characterized as Olfactomedin-like.
+At position 27 to 145, the domain is characterized as Response regulatory.
+At position 191 to 393, the domain is characterized as CheB-type methylesterase.
+At position 1756 to 1817, the domain is characterized as PWWP.
+At position 79 to 299, the domain is characterized as VWFA.
+At position 165 to 544, the domain is characterized as GRAS.
+At position 28 to 242, the domain is characterized as ABC transporter.
+At position 73 to 125, the domain is characterized as HAMP.
+At position 616 to 644, the domain is characterized as IQ.
+At position 211 to 393, the domain is characterized as Helicase ATP-binding.
+At position 430 to 585, the domain is characterized as Helicase C-terminal.
+At position 6 to 205, the domain is characterized as DPCK.
+At position 214 to 346, the domain is characterized as DCD.
+At position 45 to 280, the domain is characterized as Glutamine amidotransferase type-1.
+At position 487 to 561, the domain is characterized as RRM 3.
+At position 569 to 644, the domain is characterized as RRM 4.
+At position 19 to 258, the domain is characterized as ABC transporter.
+At position 247 to 390, the domain is characterized as FCP1 homology.
+At position 647 to 737, the domain is characterized as BRCT 2.
+At position 758 to 840, the domain is characterized as BRCT 3.
+At position 6 to 147, the domain is characterized as TsaA-like.
+At position 645 to 899, the domain is characterized as Protein kinase.
+At position 2 to 226, the domain is characterized as BAR.
+At position 288 to 421, the domain is characterized as PH.
+At position 467 to 603, the domain is characterized as Arf-GAP.
+At position 132 to 232, the domain is characterized as Rhodanese.
+At position 14 to 165, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 48 to 136, the domain is characterized as PPIase FKBP-type.
+At position 65 to 373, the domain is characterized as IF rod.
+At position 122 to 406, the domain is characterized as SET.
+At position 536 to 611, the domain is characterized as HSA.
+At position 995 to 1048, the domain is characterized as Myb-like.
+At position 126 to 326, the domain is characterized as ATP-grasp.
+At position 33 to 255, the domain is characterized as Phosphatase tensin-type.
+At position 11 to 101, the domain is characterized as Acylphosphatase-like.
+At position 5 to 197, the domain is characterized as Peptidase M12B.
+At position 280 to 389, the domain is characterized as DEUBAD.
+At position 2 to 113, the domain is characterized as RRM 1.
+At position 227 to 298, the domain is characterized as RRM 2.
+At position 38 to 74, the domain is characterized as LRRNT.
+At position 444 to 495, the domain is characterized as LRRCT.
+At position 499 to 598, the domain is characterized as Ig-like C2-type 1.
+At position 603 to 692, the domain is characterized as Ig-like C2-type 2.
+At position 697 to 783, the domain is characterized as Ig-like C2-type 3.
+At position 193 to 253, the domain is characterized as KH.
+At position 319 to 412, the domain is characterized as HD.
+At position 20 to 158, the domain is characterized as DAC.
+At position 109 to 282, the domain is characterized as EngB-type G.
+At position 20 to 127, the domain is characterized as Calponin-homology (CH).
+At position 600 to 680, the domain is characterized as DIX.
+At position 446 to 457, the domain is characterized as EGF-like.
+At position 1442 to 1694, the domain is characterized as Autotransporter.
+At position 275 to 347, the domain is characterized as Cyclin N-terminal.
+At position 295 to 497, the domain is characterized as SEC7.
+At position 681 to 804, the domain is characterized as PH.
+At position 40 to 269, the domain is characterized as Peptidase S1.
+At position 292 to 486, the domain is characterized as B30.2/SPRY.
+At position 198 to 457, the domain is characterized as GP-PDE.
+At position 9 to 97, the domain is characterized as MtN3/slv 1.
+At position 87 to 302, the domain is characterized as RNase H type-2.
+At position 280 to 424, the domain is characterized as SIS 1.
+At position 457 to 597, the domain is characterized as SIS 2.
+At position 531 to 624, the domain is characterized as FDX-ACB.
+At position 597 to 676, the domain is characterized as BRCT.
+At position 36 to 347, the domain is characterized as GH26.
+At position 27 to 146, the domain is characterized as Ig-like V-type.
+At position 338 to 396, the domain is characterized as S4 RNA-binding.
+At position 286 to 377, the domain is characterized as PDZ 1.
+At position 413 to 497, the domain is characterized as PDZ 2.
+At position 73 to 273, the domain is characterized as TR mART core.
+At position 378 to 467, the domain is characterized as PDZ 2.
+At position 558 to 705, the domain is characterized as MOSC.
+At position 150 to 212, the domain is characterized as KH 1.
+At position 222 to 284, the domain is characterized as KH 2.
+At position 295 to 357, the domain is characterized as KH 3.
+At position 364 to 424, the domain is characterized as KH 4.
+At position 435 to 497, the domain is characterized as KH 5.
+At position 507 to 570, the domain is characterized as KH 6.
+At position 581 to 643, the domain is characterized as KH 7.
+At position 653 to 716, the domain is characterized as KH 8.
+At position 727 to 790, the domain is characterized as KH 9.
+At position 800 to 863, the domain is characterized as KH 10.
+At position 873 to 967, the domain is characterized as KH 11.
+At position 972 to 1034, the domain is characterized as KH 12.
+At position 1052 to 1117, the domain is characterized as KH 13.
+At position 1127 to 1190, the domain is characterized as KH 14.
+At position 62 to 264, the domain is characterized as Peptidase M12A.
+At position 251 to 307, the domain is characterized as EGF-like.
+At position 308 to 414, the domain is characterized as CUB.
+At position 31 to 517, the domain is characterized as Sema.
+At position 114 to 208, the domain is characterized as Ig-like C1-type.
+At position 122 to 234, the domain is characterized as PilZ.
+At position 19 to 212, the domain is characterized as RNase H type-2.
+At position 44 to 268, the domain is characterized as Peptidase S1.
+At position 20 to 305, the domain is characterized as Protein kinase.
+At position 325 to 408, the domain is characterized as RRM.
+At position 585 to 758, the domain is characterized as NTF2.
+At position 788 to 841, the domain is characterized as TAP-C.
+At position 31 to 224, the domain is characterized as VWFA.
+At position 24 to 154, the domain is characterized as FZ.
+At position 47 to 102, the domain is characterized as FHA.
+At position 162 to 444, the domain is characterized as Protein kinase.
+At position 12 to 43, the domain is characterized as RIIa.
+At position 9 to 295, the domain is characterized as tr-type G.
+At position 26 to 78, the domain is characterized as HTH myb-type 1.
+At position 79 to 133, the domain is characterized as HTH myb-type 2.
+At position 314 to 372, the domain is characterized as AFP-like.
+At position 84 to 213, the domain is characterized as TIR.
+At position 1026 to 1170, the domain is characterized as RUN.
+At position 1445 to 1504, the domain is characterized as SH3.
+At position 90 to 321, the domain is characterized as AIG1-type G.
+At position 31 to 103, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 188, the domain is characterized as Ig-like C2-type 2.
+At position 112 to 312, the domain is characterized as ATP-grasp.
+At position 165 to 272, the domain is characterized as PH.
+At position 1609 to 2036, the domain is characterized as DOCKER.
+At position 7 to 213, the domain is characterized as ABC transporter.
+At position 374 to 439, the domain is characterized as TRAM.
+At position 1110 to 1186, the domain is characterized as Carrier.
+At position 5 to 90, the domain is characterized as MtN3/slv 1.
+At position 124 to 204, the domain is characterized as MtN3/slv 2.
+At position 5 to 59, the domain is characterized as HTH lacI-type.
+At position 32 to 145, the domain is characterized as C-type lectin.
+At position 239 to 289, the domain is characterized as bHLH.
+At position 702 to 796, the domain is characterized as PH 1.
+At position 810 to 918, the domain is characterized as PH 2.
+At position 954 to 1109, the domain is characterized as MyTH4.
+At position 1120 to 1449, the domain is characterized as FERM.
+At position 201 to 233, the domain is characterized as ShKT.
+At position 23 to 256, the domain is characterized as PABS.
+At position 246 to 328, the domain is characterized as POTRA.
+At position 7 to 150, the domain is characterized as Nudix hydrolase.
+At position 89 to 185, the domain is characterized as K-box.
+At position 87 to 291, the domain is characterized as Helicase ATP-binding.
+At position 310 to 525, the domain is characterized as Helicase C-terminal.
+At position 550 to 712, the domain is characterized as Toprim.
+At position 1070 to 1199, the domain is characterized as DOD-type homing endonuclease.
+At position 20 to 133, the domain is characterized as AB hydrolase-1.
+At position 336 to 571, the domain is characterized as ABC transporter.
+At position 38 to 241, the domain is characterized as BPL/LPL catalytic.
+At position 326 to 365, the domain is characterized as PLD phosphodiesterase 1.
+At position 655 to 682, the domain is characterized as PLD phosphodiesterase 2.
+At position 1 to 43, the domain is characterized as Peptidase M12B.
+At position 39 to 105, the domain is characterized as PQ-loop 1.
+At position 159 to 216, the domain is characterized as PQ-loop 2.
+At position 9 to 78, the domain is characterized as Sm.
+At position 86 to 184, the domain is characterized as AD.
+At position 24 to 252, the domain is characterized as Phosphagen kinase C-terminal.
+At position 64 to 142, the domain is characterized as GIY-YIG.
+At position 252 to 287, the domain is characterized as UVR.
+At position 197 to 353, the domain is characterized as JmjC.
+At position 191 to 405, the domain is characterized as Peptidase M12B.
+At position 371 to 474, the domain is characterized as Rhodanese.
+At position 184 to 264, the domain is characterized as RRM 1.
+At position 274 to 350, the domain is characterized as RRM 2.
+At position 359 to 455, the domain is characterized as RRM 3.
+At position 470 to 547, the domain is characterized as RRM 4.
+At position 732 to 813, the domain is characterized as PABC.
+At position 22 to 277, the domain is characterized as Protein kinase.
+At position 309 to 335, the domain is characterized as NAF.
+At position 497 to 684, the domain is characterized as Rho-GAP.
+At position 81 to 175, the domain is characterized as AD.
+At position 48 to 119, the domain is characterized as KRAB.
+At position 352 to 374, the domain is characterized as Follistatin-like 1.
+At position 507 to 530, the domain is characterized as Follistatin-like 2.
+At position 1307 to 1343, the domain is characterized as EGF-like 15.
+At position 266 to 471, the domain is characterized as SMP-LTD.
+At position 462 to 584, the domain is characterized as C2 1.
+At position 738 to 858, the domain is characterized as C2 2.
+At position 1060 to 1177, the domain is characterized as C2 3.
+At position 19 to 149, the domain is characterized as EamA 1.
+At position 697 to 790, the domain is characterized as FDX-ACB.
+At position 597 to 680, the domain is characterized as BRCT.
+At position 16 to 81, the domain is characterized as SH3.
+At position 98 to 360, the domain is characterized as Protein kinase.
+At position 198 to 387, the domain is characterized as Glutamine amidotransferase type-1.
+At position 75 to 183, the domain is characterized as PA.
+At position 2 to 119, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 235 to 458, the domain is characterized as Fibrinogen C-terminal.
+At position 37 to 105, the domain is characterized as Importin N-terminal.
+At position 40 to 306, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 317 to 570, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 37 to 320, the domain is characterized as ABC transmembrane type-1.
+At position 352 to 586, the domain is characterized as ABC transporter.
+At position 225 to 379, the domain is characterized as TrmE-type G.
+At position 20 to 98, the domain is characterized as RRM 1.
+At position 244 to 322, the domain is characterized as RRM 3.
+At position 31 to 354, the domain is characterized as G-alpha.
+At position 12 to 73, the domain is characterized as HTH tetR-type.
+At position 93 to 157, the domain is characterized as KH 1.
+At position 178 to 243, the domain is characterized as KH 2.
+At position 320 to 385, the domain is characterized as KH 3.
+At position 335 to 466, the domain is characterized as Nudix hydrolase.
+At position 28 to 218, the domain is characterized as GH16.
+At position 25 to 123, the domain is characterized as HTH hxlR-type.
+At position 114 to 172, the domain is characterized as TCP.
+At position 246 to 263, the domain is characterized as R.
+At position 97 to 159, the domain is characterized as SH3.
+At position 172 to 253, the domain is characterized as Fibronectin type-III.
+At position 264 to 597, the domain is characterized as GH18.
+At position 38 to 146, the domain is characterized as Toprim.
+At position 4 to 70, the domain is characterized as PQ-loop.
+At position 1 to 282, the domain is characterized as Deacetylase sirtuin-type.
+At position 667 to 948, the domain is characterized as Protein kinase.
+At position 312 to 590, the domain is characterized as Protein kinase.
+At position 37 to 294, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 66 to 144, the domain is characterized as GIY-YIG.
+At position 238 to 373, the domain is characterized as PAS 1.
+At position 391 to 497, the domain is characterized as PAS 2.
+At position 57 to 108, the domain is characterized as HTH psq-type.
+At position 122 to 195, the domain is characterized as HTH CENPB-type.
+At position 240 to 365, the domain is characterized as DDE-1.
+At position 115 to 164, the domain is characterized as bHLH.
+At position 1 to 121, the domain is characterized as MGS-like.
+At position 386 to 605, the domain is characterized as FtsK.
+At position 7 to 43, the domain is characterized as LDL-receptor class A 1.
+At position 56 to 97, the domain is characterized as LDL-receptor class A 2.
+At position 101 to 214, the domain is characterized as CUB.
+At position 216 to 253, the domain is characterized as LDL-receptor class A 3.
+At position 254 to 291, the domain is characterized as LDL-receptor class A 4.
+At position 292 to 328, the domain is characterized as LDL-receptor class A 5.
+At position 19 to 394, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 30 to 131, the domain is characterized as Thioredoxin.
+At position 140 to 453, the domain is characterized as IF rod.
+At position 365 to 515, the domain is characterized as YDG.
+At position 585 to 644, the domain is characterized as Pre-SET.
+At position 647 to 764, the domain is characterized as SET.
+At position 778 to 794, the domain is characterized as Post-SET.
+At position 15 to 137, the domain is characterized as EamA 1.
+At position 167 to 285, the domain is characterized as EamA 2.
+At position 81 to 149, the domain is characterized as POTRA.
+At position 164 to 243, the domain is characterized as RRM.
+At position 128 to 209, the domain is characterized as Kringle 1.
+At position 219 to 300, the domain is characterized as Kringle 2.
+At position 315 to 565, the domain is characterized as Peptidase S1.
+At position 41 to 192, the domain is characterized as VOC 1.
+At position 208 to 368, the domain is characterized as VOC 2.
+At position 88 to 175, the domain is characterized as PB1.
+At position 33 to 414, the domain is characterized as Alpha-carbonic anhydrase.
+At position 177 to 399, the domain is characterized as Helicase ATP-binding.
+At position 110 to 636, the domain is characterized as GBD/FH3.
+At position 953 to 1368, the domain is characterized as FH2.
+At position 215 to 259, the domain is characterized as CUE.
+At position 485 to 567, the domain is characterized as Smr.
+At position 351 to 602, the domain is characterized as SF4 helicase.
+At position 22 to 79, the domain is characterized as Sushi 1.
+At position 118 to 181, the domain is characterized as Sushi 2.
+At position 134 to 268, the domain is characterized as Fatty acid hydroxylase.
+At position 26 to 348, the domain is characterized as Brix.
+At position 1 to 136, the domain is characterized as Flavodoxin-like.
+At position 28 to 104, the domain is characterized as Ig-like 1.
+At position 114 to 181, the domain is characterized as Ig-like 2.
+At position 35 to 144, the domain is characterized as Ig-like V-type 1.
+At position 37 to 165, the domain is characterized as ALOG.
+At position 32 to 122, the domain is characterized as Fibronectin type-III 1.
+At position 159 to 331, the domain is characterized as VWFA 1.
+At position 356 to 445, the domain is characterized as Fibronectin type-III 2.
+At position 446 to 537, the domain is characterized as Fibronectin type-III 3.
+At position 538 to 625, the domain is characterized as Fibronectin type-III 4.
+At position 627 to 716, the domain is characterized as Fibronectin type-III 5.
+At position 738 to 830, the domain is characterized as Fibronectin type-III 6.
+At position 832 to 922, the domain is characterized as Fibronectin type-III 7.
+At position 923 to 1014, the domain is characterized as Fibronectin type-III 8.
+At position 1033 to 1206, the domain is characterized as VWFA 2.
+At position 1230 to 1425, the domain is characterized as Laminin G-like.
+At position 1463 to 1511, the domain is characterized as Collagen-like 1.
+At position 1515 to 1571, the domain is characterized as Collagen-like 2.
+At position 1572 to 1610, the domain is characterized as Collagen-like 3.
+At position 1655 to 1706, the domain is characterized as Collagen-like 4.
+At position 1708 to 1758, the domain is characterized as Collagen-like 5.
+At position 47 to 172, the domain is characterized as C-type lectin.
+At position 1 to 30, the domain is characterized as LEM.
+At position 194 to 323, the domain is characterized as Galectin 2.
+At position 156 to 283, the domain is characterized as Galectin 2.
+At position 29 to 247, the domain is characterized as Peptidase S1.
+At position 359 to 468, the domain is characterized as BRCT.
+At position 111 to 145, the domain is characterized as EF-hand 1.
+At position 146 to 181, the domain is characterized as EF-hand 2.
+At position 120 to 153, the domain is characterized as WW.
+At position 75 to 204, the domain is characterized as HD.
+At position 37 to 137, the domain is characterized as SRCR 1.
+At position 186 to 286, the domain is characterized as SRCR 2.
+At position 324 to 424, the domain is characterized as SRCR 3.
+At position 463 to 563, the domain is characterized as SRCR 4.
+At position 602 to 702, the domain is characterized as SRCR 5.
+At position 741 to 841, the domain is characterized as SRCR 6.
+At position 880 to 980, the domain is characterized as SRCR 7.
+At position 1023 to 1132, the domain is characterized as CUB 1.
+At position 1139 to 1248, the domain is characterized as CUB 2.
+At position 1265 to 1374, the domain is characterized as CUB 3.
+At position 1381 to 1490, the domain is characterized as CUB 4.
+At position 1510 to 1610, the domain is characterized as SRCR 8.
+At position 1633 to 1742, the domain is characterized as CUB 5.
+At position 1751 to 1999, the domain is characterized as ZP.
+At position 188 to 248, the domain is characterized as DDT.
+At position 2573 to 2643, the domain is characterized as Bromo.
+At position 35 to 253, the domain is characterized as Cupin type-1 1.
+At position 83 to 228, the domain is characterized as Clp R.
+At position 130 to 288, the domain is characterized as 3'-5' exonuclease.
+At position 27 to 207, the domain is characterized as FAD-binding PCMH-type.
+At position 285 to 483, the domain is characterized as B30.2/SPRY.
+At position 29 to 93, the domain is characterized as SAM.
+At position 186 to 438, the domain is characterized as Protein kinase.
+At position 176 to 336, the domain is characterized as Upf1 CH-rich.
+At position 46 to 100, the domain is characterized as FHA.
+At position 145 to 411, the domain is characterized as Protein kinase.
+At position 217 to 387, the domain is characterized as GAF.
+At position 595 to 666, the domain is characterized as PAS 1.
+At position 732 to 803, the domain is characterized as PAS 2.
+At position 877 to 1096, the domain is characterized as Histidine kinase.
+At position 231 to 342, the domain is characterized as SCP.
+At position 33 to 111, the domain is characterized as EMI.
+At position 110 to 141, the domain is characterized as EGF-like 1.
+At position 143 to 183, the domain is characterized as EGF-like 2; calcium-binding.
+At position 40 to 93, the domain is characterized as TSP type-1.
+At position 97 to 134, the domain is characterized as LDL-receptor class A.
+At position 136 to 518, the domain is characterized as MACPF.
+At position 519 to 549, the domain is characterized as EGF-like.
+At position 30 to 208, the domain is characterized as Eph LBD.
+At position 327 to 437, the domain is characterized as Fibronectin type-III 1.
+At position 438 to 533, the domain is characterized as Fibronectin type-III 2.
+At position 634 to 895, the domain is characterized as Protein kinase.
+At position 929 to 993, the domain is characterized as SAM.
+At position 630 to 726, the domain is characterized as Zinc-hook.
+At position 19 to 102, the domain is characterized as RRM 1.
+At position 222 to 292, the domain is characterized as RRM 2.
+At position 401 to 474, the domain is characterized as RRM 3.
+At position 599 to 681, the domain is characterized as BRCT.
+At position 610 to 716, the domain is characterized as tRNA-binding.
+At position 185 to 466, the domain is characterized as GH84.
+At position 781 to 953, the domain is characterized as F5/8 type C.
+At position 1573 to 1628, the domain is characterized as Dockerin.
+At position 30 to 140, the domain is characterized as AB hydrolase-1.
+At position 24 to 104, the domain is characterized as KRAB.
+At position 27 to 129, the domain is characterized as Rieske.
+At position 91 to 149, the domain is characterized as S4 RNA-binding.
+At position 4 to 179, the domain is characterized as Prephenate dehydratase.
+At position 194 to 269, the domain is characterized as ACT.
+At position 37 to 153, the domain is characterized as MTTase N-terminal.
+At position 175 to 406, the domain is characterized as Radical SAM core.
+At position 408 to 476, the domain is characterized as TRAM.
+At position 468 to 581, the domain is characterized as PH.
+At position 297 to 358, the domain is characterized as SH3.
+At position 9 to 234, the domain is characterized as Radical SAM core.
+At position 245 to 782, the domain is characterized as PLA2c.
+At position 598 to 676, the domain is characterized as Carrier.
+At position 95 to 171, the domain is characterized as Ubiquitin-like.
+At position 272 to 296, the domain is characterized as C-type lectin.
+At position 532 to 873, the domain is characterized as HECT.
+At position 50 to 178, the domain is characterized as Runt.
+At position 23 to 123, the domain is characterized as Ig-like 1.
+At position 131 to 265, the domain is characterized as Ig-like 2.
+At position 270 to 352, the domain is characterized as Ig-like 3.
+At position 357 to 433, the domain is characterized as Ig-like 4.
+At position 441 to 540, the domain is characterized as Ig-like 5.
+At position 119 to 163, the domain is characterized as LysM.
+At position 40 to 226, the domain is characterized as BPL/LPL catalytic.
+At position 90 to 170, the domain is characterized as RRM 1.
+At position 180 to 259, the domain is characterized as RRM 2.
+At position 284 to 356, the domain is characterized as RRM 3.
+At position 147 to 322, the domain is characterized as Helicase ATP-binding.
+At position 350 to 497, the domain is characterized as Helicase C-terminal.
+At position 20 to 150, the domain is characterized as Thioredoxin.
+At position 32 to 388, the domain is characterized as Protein kinase.
+At position 278 to 610, the domain is characterized as Kinesin motor.
+At position 376 to 438, the domain is characterized as TRAM.
+At position 71 to 151, the domain is characterized as RRM 1.
+At position 209 to 293, the domain is characterized as RRM 2.
+At position 490 to 536, the domain is characterized as G-patch.
+At position 74 to 765, the domain is characterized as Peptidase M13.
+At position 710 to 977, the domain is characterized as Protein kinase.
+At position 31 to 106, the domain is characterized as UPAR/Ly6.
+At position 1 to 377, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 89 to 124, the domain is characterized as EF-hand 2.
+At position 184 to 219, the domain is characterized as EF-hand 4.
+At position 601 to 683, the domain is characterized as BRCT.
+At position 199 to 335, the domain is characterized as Nudix hydrolase.
+At position 87 to 247, the domain is characterized as FAS1.
+At position 614 to 692, the domain is characterized as TFIIS N-terminal.
+At position 26 to 218, the domain is characterized as Velvet.
+At position 210 to 350, the domain is characterized as CBM21.
+At position 29 to 99, the domain is characterized as PAS 1.
+At position 150 to 220, the domain is characterized as PAS 2.
+At position 271 to 342, the domain is characterized as PAS 3.
+At position 391 to 462, the domain is characterized as PAS 4.
+At position 523 to 729, the domain is characterized as Histidine kinase.
+At position 175 to 281, the domain is characterized as Cytochrome c.
+At position 196 to 228, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 30 to 191, the domain is characterized as MAM.
+At position 193 to 284, the domain is characterized as Ig-like C2-type.
+At position 291 to 384, the domain is characterized as Fibronectin type-III 1.
+At position 389 to 483, the domain is characterized as Fibronectin type-III 2.
+At position 484 to 590, the domain is characterized as Fibronectin type-III 3.
+At position 591 to 726, the domain is characterized as Fibronectin type-III 4.
+At position 889 to 1143, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1175 to 1437, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 55 to 134, the domain is characterized as RRM.
+At position 35 to 173, the domain is characterized as Thioredoxin.
+At position 160 to 343, the domain is characterized as OBG-type G.
+At position 363 to 447, the domain is characterized as OCT.
+At position 26 to 208, the domain is characterized as Chitin-binding type-4.
+At position 20 to 333, the domain is characterized as GH10.
+At position 371 to 407, the domain is characterized as CBM1.
+At position 146 to 328, the domain is characterized as Helicase ATP-binding.
+At position 357 to 500, the domain is characterized as Helicase C-terminal.
+At position 350 to 517, the domain is characterized as tr-type G.
+At position 1 to 166, the domain is characterized as TCTP.
+At position 147 to 332, the domain is characterized as Helicase ATP-binding.
+At position 523 to 673, the domain is characterized as Helicase C-terminal.
+At position 551 to 751, the domain is characterized as VWFA.
+At position 96 to 129, the domain is characterized as WW.
+At position 386 to 505, the domain is characterized as PH.
+At position 610 to 827, the domain is characterized as Rho-GAP.
+At position 15 to 197, the domain is characterized as tr-type G.
+At position 34 to 100, the domain is characterized as Chitin-binding type R&R.
+At position 137 to 302, the domain is characterized as TNase-like.
+At position 66 to 279, the domain is characterized as VWFA.
+At position 228 to 286, the domain is characterized as Plastocyanin-like.
+At position 455 to 624, the domain is characterized as tr-type G.
+At position 52 to 106, the domain is characterized as F-box.
+At position 30 to 157, the domain is characterized as ALOG.
+At position 29 to 146, the domain is characterized as MARVEL.
+At position 20 to 133, the domain is characterized as Ig-like.
+At position 27 to 67, the domain is characterized as Fibronectin type-I 1.
+At position 72 to 115, the domain is characterized as Fibronectin type-I 2.
+At position 116 to 159, the domain is characterized as Fibronectin type-I 3.
+At position 161 to 205, the domain is characterized as Fibronectin type-I 4.
+At position 206 to 250, the domain is characterized as Fibronectin type-I 5.
+At position 283 to 322, the domain is characterized as Fibronectin type-I 6.
+At position 332 to 380, the domain is characterized as Fibronectin type-II 1.
+At position 392 to 440, the domain is characterized as Fibronectin type-II 2.
+At position 421 to 475, the domain is characterized as Fibronectin type-I 7.
+At position 480 to 522, the domain is characterized as Fibronectin type-I 8.
+At position 523 to 566, the domain is characterized as Fibronectin type-I 9.
+At position 574 to 669, the domain is characterized as Fibronectin type-III 1.
+At position 681 to 776, the domain is characterized as Fibronectin type-III 2.
+At position 777 to 866, the domain is characterized as Fibronectin type-III 3.
+At position 873 to 964, the domain is characterized as Fibronectin type-III 4.
+At position 965 to 1052, the domain is characterized as Fibronectin type-III 5.
+At position 1053 to 1139, the domain is characterized as Fibronectin type-III 6.
+At position 1140 to 1234, the domain is characterized as Fibronectin type-III 7.
+At position 1235 to 1323, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1324 to 1414, the domain is characterized as Fibronectin type-III 9.
+At position 1415 to 1505, the domain is characterized as Fibronectin type-III 10.
+At position 1506 to 1581, the domain is characterized as Fibronectin type-III 11.
+At position 1583 to 1673, the domain is characterized as Fibronectin type-III 12.
+At position 1674 to 1766, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1767 to 1856, the domain is characterized as Fibronectin type-III 14.
+At position 1857 to 1949, the domain is characterized as Fibronectin type-III 15.
+At position 2025 to 2071, the domain is characterized as Fibronectin type-I 10.
+At position 2072 to 2114, the domain is characterized as Fibronectin type-I 11.
+At position 2116 to 2156, the domain is characterized as Fibronectin type-I 12.
+At position 40 to 105, the domain is characterized as NAC-A/B.
+At position 294 to 344, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 21 to 100, the domain is characterized as Importin N-terminal.
+At position 372 to 439, the domain is characterized as TRAM.
+At position 189 to 316, the domain is characterized as Thioredoxin.
+At position 637 to 695, the domain is characterized as Tudor 1.
+At position 873 to 932, the domain is characterized as Tudor 2.
+At position 1139 to 1196, the domain is characterized as Tudor 3.
+At position 1390 to 1450, the domain is characterized as Tudor 4.
+At position 554 to 651, the domain is characterized as tRNA-binding.
+At position 377 to 436, the domain is characterized as SH3.
+At position 80 to 391, the domain is characterized as YjeF C-terminal.
+At position 12 to 209, the domain is characterized as Lon N-terminal.
+At position 439 to 529, the domain is characterized as CARD.
+At position 23 to 337, the domain is characterized as GH26.
+At position 37 to 110, the domain is characterized as POTRA.
+At position 4 to 99, the domain is characterized as DUSP.
+At position 279 to 869, the domain is characterized as USP.
+At position 124 to 156, the domain is characterized as LisH.
+At position 162 to 220, the domain is characterized as CTLH.
+At position 40 to 142, the domain is characterized as Gnk2-homologous 1.
+At position 643 to 820, the domain is characterized as MOSC.
+At position 16 to 100, the domain is characterized as BMC 1.
+At position 120 to 204, the domain is characterized as BMC 2.
+At position 14 to 78, the domain is characterized as TRAM.
+At position 40 to 94, the domain is characterized as EMI.
+At position 97 to 230, the domain is characterized as FAS1 1.
+At position 234 to 365, the domain is characterized as FAS1 2.
+At position 368 to 492, the domain is characterized as FAS1 3.
+At position 496 to 628, the domain is characterized as FAS1 4.
+At position 280 to 371, the domain is characterized as PDZ 1.
+At position 377 to 466, the domain is characterized as PDZ 2.
+At position 11 to 125, the domain is characterized as Response regulatory.
+At position 191 to 381, the domain is characterized as GMPS ATP-PPase.
+At position 80 to 298, the domain is characterized as Radical SAM core.
+At position 61 to 172, the domain is characterized as Expansin-like EG45.
+At position 142 to 223, the domain is characterized as Expansin-like CBD.
+At position 4 to 375, the domain is characterized as Trm1 methyltransferase.
+At position 9 to 84, the domain is characterized as CTLH.
+At position 30 to 99, the domain is characterized as POTRA.
+At position 171 to 245, the domain is characterized as Toprim.
+At position 135 to 229, the domain is characterized as Ig-like C2-type 2.
+At position 261 to 350, the domain is characterized as Ig-like C2-type 3.
+At position 643 to 738, the domain is characterized as Fibronectin type-III 1.
+At position 740 to 837, the domain is characterized as Fibronectin type-III 2.
+At position 842 to 944, the domain is characterized as Fibronectin type-III 3.
+At position 948 to 1045, the domain is characterized as Fibronectin type-III 4.
+At position 158 to 399, the domain is characterized as Protein kinase.
+At position 3 to 116, the domain is characterized as PTS EIIA type-5.
+At position 205 to 315, the domain is characterized as PX.
+At position 346 to 549, the domain is characterized as BAR.
+At position 5 to 347, the domain is characterized as Kinesin motor.
+At position 520 to 587, the domain is characterized as FHA.
+At position 19 to 790, the domain is characterized as Vitellogenin.
+At position 1410 to 1597, the domain is characterized as VWFD.
+At position 432 to 504, the domain is characterized as ACT-like 1.
+At position 526 to 597, the domain is characterized as ACT-like 2.
+At position 53 to 105, the domain is characterized as LIM zinc-binding 1.
+At position 115 to 168, the domain is characterized as LIM zinc-binding 2.
+At position 31 to 90, the domain is characterized as VWFC.
+At position 1215 to 1450, the domain is characterized as Fibrillar collagen NC1.
+At position 13 to 168, the domain is characterized as CRAL-TRIO.
+At position 195 to 381, the domain is characterized as Rho-GAP.
+At position 9 to 114, the domain is characterized as Rieske.
+At position 272 to 373, the domain is characterized as FAD-binding FR-type.
+At position 503 to 588, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 170 to 250, the domain is characterized as PPIase FKBP-type.
+At position 440 to 604, the domain is characterized as PI-PLC X-box.
+At position 49 to 151, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 232, the domain is characterized as Ig-like C2-type 2.
+At position 250 to 333, the domain is characterized as Ig-like C2-type 3.
+At position 341 to 428, the domain is characterized as Ig-like C2-type 4.
+At position 438 to 532, the domain is characterized as Fibronectin type-III 1.
+At position 535 to 630, the domain is characterized as Fibronectin type-III 2.
+At position 681 to 955, the domain is characterized as Roc.
+At position 1312 to 1396, the domain is characterized as Death.
+At position 84 to 252, the domain is characterized as Helicase ATP-binding.
+At position 277 to 450, the domain is characterized as Helicase C-terminal.
+At position 29 to 144, the domain is characterized as Ig-like V-type.
+At position 2 to 76, the domain is characterized as Carrier.
+At position 110 to 216, the domain is characterized as HTH APSES-type.
+At position 409 to 568, the domain is characterized as Exonuclease.
+At position 501 to 809, the domain is characterized as Protein kinase.
+At position 867 to 997, the domain is characterized as Guanylate cyclase.
+At position 609 to 689, the domain is characterized as BRCT.
+At position 279 to 323, the domain is characterized as LEM.
+At position 370 to 485, the domain is characterized as GIY-YIG.
+At position 67 to 245, the domain is characterized as Helicase ATP-binding.
+At position 274 to 467, the domain is characterized as Helicase C-terminal.
+At position 20 to 304, the domain is characterized as Protein kinase.
+At position 316 to 453, the domain is characterized as C-CAP/cofactor C-like.
+At position 144 to 453, the domain is characterized as NB-ARC.
+At position 66 to 142, the domain is characterized as RRM.
+At position 357 to 469, the domain is characterized as PLAT.
+At position 632 to 801, the domain is characterized as tr-type G.
+At position 1579 to 1756, the domain is characterized as VWFD.
+At position 1 to 196, the domain is characterized as tr-type G.
+At position 68 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 418 to 479, the domain is characterized as SAM.
+At position 333 to 463, the domain is characterized as MPN.
+At position 43 to 166, the domain is characterized as Thioredoxin.
+At position 410 to 513, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 189 to 523, the domain is characterized as Protein kinase.
+At position 311 to 594, the domain is characterized as ABC transmembrane type-1 1.
+At position 629 to 851, the domain is characterized as ABC transporter 1.
+At position 971 to 1252, the domain is characterized as ABC transmembrane type-1 2.
+At position 1291 to 1523, the domain is characterized as ABC transporter 2.
+At position 4 to 133, the domain is characterized as Ras-associating.
+At position 100 to 128, the domain is characterized as ITAM 2.
+At position 131 to 159, the domain is characterized as ITAM 3.
+At position 219 to 271, the domain is characterized as CpcD-like.
+At position 287 to 448, the domain is characterized as Helicase C-terminal.
+At position 266 to 325, the domain is characterized as SH3.
+At position 39 to 112, the domain is characterized as CSD.
+At position 11 to 255, the domain is characterized as Lon N-terminal.
+At position 692 to 877, the domain is characterized as Lon proteolytic.
+At position 31 to 144, the domain is characterized as Expansin-like EG45.
+At position 117 to 237, the domain is characterized as RCK N-terminal.
+At position 252 to 336, the domain is characterized as RCK C-terminal.
+At position 12 to 127, the domain is characterized as Guanylate cyclase.
+At position 146 to 290, the domain is characterized as Jacalin-type lectin 2.
+At position 298 to 442, the domain is characterized as Jacalin-type lectin 3.
+At position 195 to 275, the domain is characterized as RRM Nup35-type.
+At position 143 to 286, the domain is characterized as FCP1 homology.
+At position 30 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 541 to 618, the domain is characterized as PABC.
+At position 176 to 350, the domain is characterized as EngA-type G 2.
+At position 116 to 167, the domain is characterized as C-type lectin; atypical.
+At position 42 to 76, the domain is characterized as EF-hand 2.
+At position 973 to 1064, the domain is characterized as SET.
+At position 17 to 96, the domain is characterized as CIDE-N.
+At position 121 to 205, the domain is characterized as Ig-like 2.
+At position 312 to 450, the domain is characterized as FZ.
+At position 575 to 856, the domain is characterized as Protein kinase.
+At position 789 to 818, the domain is characterized as IQ 2.
+At position 862 to 883, the domain is characterized as IQ 5.
+At position 885 to 914, the domain is characterized as IQ 6.
+At position 1534 to 1810, the domain is characterized as Dilute.
+At position 553 to 614, the domain is characterized as SAM.
+At position 279 to 449, the domain is characterized as tr-type G.
+At position 124 to 216, the domain is characterized as PPIase FKBP-type.
+At position 349 to 426, the domain is characterized as OCT.
+At position 9 to 382, the domain is characterized as Trm1 methyltransferase.
+At position 182 to 526, the domain is characterized as PDEase.
+At position 4 to 54, the domain is characterized as Rubredoxin-like.
+At position 249 to 315, the domain is characterized as HMA.
+At position 1750 to 1980, the domain is characterized as Alpha-type protein kinase.
+At position 117 to 193, the domain is characterized as RRM.
+At position 214 to 310, the domain is characterized as PH 1.
+At position 406 to 497, the domain is characterized as PH 2.
+At position 97 to 148, the domain is characterized as SANT.
+At position 313 to 411, the domain is characterized as SWIRM.
+At position 517 to 651, the domain is characterized as MPN.
+At position 4 to 119, the domain is characterized as PINc.
+At position 120 to 204, the domain is characterized as PPIase FKBP-type.
+At position 57 to 713, the domain is characterized as Peptidase M13.
+At position 1 to 236, the domain is characterized as Peptidase S1.
+At position 29 to 132, the domain is characterized as Gnk2-homologous 1.
+At position 138 to 248, the domain is characterized as Gnk2-homologous 2.
+At position 272 to 488, the domain is characterized as RNase H type-1.
+At position 154 to 427, the domain is characterized as ABC transporter 1.
+At position 825 to 1077, the domain is characterized as ABC transporter 2.
+At position 1150 to 1364, the domain is characterized as ABC transmembrane type-2 2.
+At position 168 to 481, the domain is characterized as IF rod.
+At position 40 to 123, the domain is characterized as Ig-like V-type.
+At position 157 to 240, the domain is characterized as Ig-like C2-type 1.
+At position 246 to 344, the domain is characterized as Ig-like C2-type 2.
+At position 36 to 109, the domain is characterized as U-box 1.
+At position 131 to 204, the domain is characterized as U-box 2.
+At position 16 to 181, the domain is characterized as CP-type G.
+At position 33 to 73, the domain is characterized as Chitin-binding type-1.
+At position 5 to 138, the domain is characterized as B12-binding.
+At position 41 to 132, the domain is characterized as Ig-like.
+At position 427 to 504, the domain is characterized as S1 motif.
+At position 194 to 214, the domain is characterized as ELK.
+At position 8 to 81, the domain is characterized as KRAB.
+At position 8 to 151, the domain is characterized as N-acetyltransferase.
+At position 31 to 75, the domain is characterized as CAP-Gly.
+At position 17 to 201, the domain is characterized as tr-type G.
+At position 1 to 39, the domain is characterized as SCAN box.
+At position 1 to 62, the domain is characterized as SH3.
+At position 250 to 360, the domain is characterized as PX.
+At position 392 to 595, the domain is characterized as BAR.
+At position 237 to 280, the domain is characterized as LRRCT.
+At position 504 to 775, the domain is characterized as Protein kinase.
+At position 353 to 452, the domain is characterized as BRCT.
+At position 55 to 201, the domain is characterized as Cupin type-1.
+At position 325 to 381, the domain is characterized as GGDEF.
+At position 40 to 77, the domain is characterized as PAS 1.
+At position 117 to 169, the domain is characterized as PAC 1.
+At position 209 to 246, the domain is characterized as PAS 2.
+At position 250 to 302, the domain is characterized as PAC 2.
+At position 314 to 458, the domain is characterized as GAF 1.
+At position 469 to 540, the domain is characterized as PAS 3.
+At position 609 to 752, the domain is characterized as GAF 2.
+At position 783 to 998, the domain is characterized as Histidine kinase.
+At position 207 to 303, the domain is characterized as PH.
+At position 213 to 310, the domain is characterized as Fe2OG dioxygenase.
+At position 141 to 325, the domain is characterized as CP-type G.
+At position 59 to 114, the domain is characterized as bHLH.
+At position 136 to 171, the domain is characterized as Orange.
+At position 20 to 118, the domain is characterized as HTH hxlR-type.
+At position 19 to 60, the domain is characterized as JmjN.
+At position 84 to 174, the domain is characterized as ARID.
+At position 437 to 603, the domain is characterized as JmjC.
+At position 71 to 143, the domain is characterized as J.
+At position 13 to 151, the domain is characterized as Tyrosine-protein phosphatase.
+At position 122 to 151, the domain is characterized as IQ.
+At position 353 to 408, the domain is characterized as EGF-like.
+At position 82 to 180, the domain is characterized as Mis18.
+At position 25 to 170, the domain is characterized as Helicase ATP-binding.
+At position 26 to 86, the domain is characterized as LCN-type CS-alpha/beta.
+At position 33 to 192, the domain is characterized as SIS.
+At position 82 to 334, the domain is characterized as Protein kinase.
+At position 503 to 581, the domain is characterized as POLO box 1.
+At position 601 to 685, the domain is characterized as POLO box 2.
+At position 471 to 738, the domain is characterized as Ras-GEF.
+At position 1751 to 1853, the domain is characterized as PH.
+At position 1872 to 2070, the domain is characterized as Rho-GAP.
+At position 195 to 351, the domain is characterized as JmjC.
+At position 439 to 501, the domain is characterized as FIP-RBD.
+At position 11 to 66, the domain is characterized as HTH cro/C1-type.
+At position 44 to 239, the domain is characterized as Lon N-terminal.
+At position 626 to 807, the domain is characterized as Lon proteolytic.
+At position 1 to 118, the domain is characterized as MTTase N-terminal.
+At position 129 to 356, the domain is characterized as Radical SAM core.
+At position 359 to 418, the domain is characterized as TRAM.
+At position 2 to 224, the domain is characterized as ABC transporter.
+At position 7 to 111, the domain is characterized as Longin.
+At position 126 to 186, the domain is characterized as v-SNARE coiled-coil homology.
+At position 522 to 664, the domain is characterized as Flavodoxin-like.
+At position 703 to 952, the domain is characterized as FAD-binding FR-type.
+At position 88 to 147, the domain is characterized as LIM zinc-binding 2.
+At position 50 to 93, the domain is characterized as SMB 1.
+At position 94 to 138, the domain is characterized as SMB 2.
+At position 23 to 298, the domain is characterized as PPM-type phosphatase.
+At position 261 to 307, the domain is characterized as G-patch.
+At position 781 to 863, the domain is characterized as DIX.
+At position 194 to 285, the domain is characterized as PpiC.
+At position 26 to 302, the domain is characterized as Protein kinase.
+At position 75 to 286, the domain is characterized as ABC transmembrane type-1.
+At position 417 to 484, the domain is characterized as TRAM.
+At position 594 to 675, the domain is characterized as BRCT.
+At position 24 to 143, the domain is characterized as C-type lectin.
+At position 702 to 785, the domain is characterized as BRCT.
+At position 38 to 109, the domain is characterized as KRAB.
+At position 2 to 105, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 173 to 303, the domain is characterized as EamA.
+At position 40 to 316, the domain is characterized as Dynamin-type G.
+At position 538 to 627, the domain is characterized as GED.
+At position 128 to 224, the domain is characterized as PPIase FKBP-type.
+At position 150 to 188, the domain is characterized as EGF-like 1.
+At position 241 to 282, the domain is characterized as EGF-like 2; calcium-binding.
+At position 21 to 125, the domain is characterized as Ig-like V-type.
+At position 473 to 528, the domain is characterized as Kazal-like.
+At position 124 to 338, the domain is characterized as PNPLA.
+At position 146 to 407, the domain is characterized as WH1.
+At position 25 to 360, the domain is characterized as Kinesin motor.
+At position 454 to 622, the domain is characterized as tr-type G.
+At position 10 to 171, the domain is characterized as TIR.
+At position 187 to 452, the domain is characterized as NB-ARC.
+At position 7 to 169, the domain is characterized as UBC core.
+At position 681 to 780, the domain is characterized as BRCT 1.
+At position 836 to 941, the domain is characterized as BRCT 2.
+At position 437 to 531, the domain is characterized as ASCH.
+At position 72 to 346, the domain is characterized as Protein kinase.
+At position 19 to 125, the domain is characterized as PH.
+At position 135 to 329, the domain is characterized as Rho-GAP.
+At position 218 to 380, the domain is characterized as TrmE-type G.
+At position 317 to 403, the domain is characterized as BRCT.
+At position 427 to 463, the domain is characterized as CBM1.
+At position 176 to 247, the domain is characterized as GRAM.
+At position 189 to 286, the domain is characterized as BEACH-type PH.
+At position 290 to 575, the domain is characterized as BEACH.
+At position 30 to 85, the domain is characterized as Clip.
+At position 148 to 400, the domain is characterized as Peptidase S1.
+At position 409 to 462, the domain is characterized as PAP-associated.
+At position 340 to 396, the domain is characterized as EGF-like.
+At position 576 to 681, the domain is characterized as PilZ.
+At position 426 to 551, the domain is characterized as Arf-GAP.
+At position 126 to 418, the domain is characterized as NR LBD.
+At position 68 to 454, the domain is characterized as GRAS.
+At position 34 to 290, the domain is characterized as Protein kinase.
+At position 681 to 871, the domain is characterized as ATP-grasp 2.
+At position 944 to 1073, the domain is characterized as MGS-like.
+At position 36 to 181, the domain is characterized as UBC core.
+At position 94 to 179, the domain is characterized as Ig-like.
+At position 75 to 260, the domain is characterized as RNase H type-2.
+At position 220 to 382, the domain is characterized as Helicase ATP-binding.
+At position 436 to 594, the domain is characterized as Helicase C-terminal.
+At position 130 to 238, the domain is characterized as CBM21.
+At position 35 to 303, the domain is characterized as PPM-type phosphatase.
+At position 85 to 187, the domain is characterized as Plastocyanin-like.
+At position 213 to 373, the domain is characterized as TrmE-type G.
+At position 14 to 250, the domain is characterized as ABC transporter 1.
+At position 261 to 504, the domain is characterized as ABC transporter 2.
+At position 30 to 252, the domain is characterized as AB hydrolase-1.
+At position 194 to 423, the domain is characterized as Sigma-54 factor interaction.
+At position 1 to 119, the domain is characterized as Peptidase M12B.
+At position 127 to 213, the domain is characterized as Disintegrin.
+At position 44 to 297, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 68 to 164, the domain is characterized as Plastocyanin-like.
+At position 158 to 229, the domain is characterized as KH 1.
+At position 230 to 302, the domain is characterized as KH 2.
+At position 303 to 371, the domain is characterized as KH 3.
+At position 372 to 442, the domain is characterized as KH 4.
+At position 443 to 514, the domain is characterized as KH 5.
+At position 515 to 588, the domain is characterized as KH 6.
+At position 589 to 660, the domain is characterized as KH 7.
+At position 661 to 734, the domain is characterized as KH 8.
+At position 735 to 807, the domain is characterized as KH 9.
+At position 808 to 880, the domain is characterized as KH 10.
+At position 881 to 979, the domain is characterized as KH 11.
+At position 980 to 1059, the domain is characterized as KH 12.
+At position 1060 to 1134, the domain is characterized as KH 13.
+At position 1135 to 1209, the domain is characterized as KH 14.
+At position 54 to 124, the domain is characterized as H15.
+At position 126 to 376, the domain is characterized as NR LBD.
+At position 53 to 121, the domain is characterized as R3H.
+At position 218 to 384, the domain is characterized as Helicase ATP-binding.
+At position 627 to 799, the domain is characterized as Helicase C-terminal.
+At position 1303 to 1433, the domain is characterized as YTH.
+At position 58 to 130, the domain is characterized as Thyroglobulin type-1.
+At position 100 to 269, the domain is characterized as FAS1.
+At position 107 to 415, the domain is characterized as IF rod.
+At position 56 to 98, the domain is characterized as CHCH.
+At position 224 to 415, the domain is characterized as PCI.
+At position 42 to 234, the domain is characterized as Cupin type-1 1.
+At position 283 to 432, the domain is characterized as Cupin type-1 2.
+At position 280 to 341, the domain is characterized as CBS 1.
+At position 388 to 417, the domain is characterized as IQ.
+At position 5 to 101, the domain is characterized as CS.
+At position 32 to 94, the domain is characterized as Sushi 1.
+At position 95 to 159, the domain is characterized as Sushi 2.
+At position 160 to 221, the domain is characterized as Sushi 3.
+At position 222 to 284, the domain is characterized as Sushi 4.
+At position 131 to 159, the domain is characterized as IQ 1.
+At position 160 to 182, the domain is characterized as IQ 2.
+At position 116 to 174, the domain is characterized as RRM.
+At position 19 to 127, the domain is characterized as Ig-like V-type.
+At position 223 to 351, the domain is characterized as Nudix hydrolase.
+At position 1 to 16, the domain is characterized as Phosphagen kinase C-terminal.
+At position 139 to 205, the domain is characterized as KH.
+At position 163 to 226, the domain is characterized as LIM zinc-binding.
+At position 663 to 810, the domain is characterized as bMERB.
+At position 122 to 238, the domain is characterized as Calponin-homology (CH) 1.
+At position 266 to 377, the domain is characterized as Calponin-homology (CH) 2.
+At position 396 to 505, the domain is characterized as Calponin-homology (CH) 3.
+At position 517 to 626, the domain is characterized as Calponin-homology (CH) 4.
+At position 43 to 162, the domain is characterized as Bulb-type lectin.
+At position 298 to 334, the domain is characterized as EGF-like; atypical.
+At position 353 to 439, the domain is characterized as PAN.
+At position 520 to 803, the domain is characterized as Protein kinase.
+At position 250 to 495, the domain is characterized as ABC transporter 2.
+At position 36 to 169, the domain is characterized as RUN.
+At position 1296 to 1425, the domain is characterized as GOLD.
+At position 150 to 328, the domain is characterized as Helicase ATP-binding.
+At position 339 to 503, the domain is characterized as Helicase C-terminal.
+At position 71 to 353, the domain is characterized as Protein kinase.
+At position 583 to 708, the domain is characterized as DBINO.
+At position 833 to 1005, the domain is characterized as Helicase ATP-binding.
+At position 216 to 320, the domain is characterized as RRM.
+At position 282 to 523, the domain is characterized as MHD.
+At position 175 to 414, the domain is characterized as MIF4G.
+At position 9 to 190, the domain is characterized as YrdC-like.
+At position 323 to 382, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 392 to 583, the domain is characterized as E2.
+At position 10 to 113, the domain is characterized as PH.
+At position 144 to 570, the domain is characterized as G-alpha.
+At position 55 to 278, the domain is characterized as Radical SAM core.
+At position 296 to 334, the domain is characterized as LRRCT.
+At position 444 to 634, the domain is characterized as B30.2/SPRY.
+At position 154 to 571, the domain is characterized as Myotubularin phosphatase.
+At position 874 to 1146, the domain is characterized as Protein kinase.
+At position 79 to 227, the domain is characterized as Toprim.
+At position 1 to 52, the domain is characterized as SPR.
+At position 583 to 685, the domain is characterized as tRNA-binding.
+At position 95 to 155, the domain is characterized as S4 RNA-binding.
+At position 36 to 287, the domain is characterized as Protein kinase.
+At position 405 to 484, the domain is characterized as POLO box 1.
+At position 506 to 588, the domain is characterized as POLO box 2.
+At position 41 to 104, the domain is characterized as TGS.
+At position 41 to 221, the domain is characterized as PCI.
+At position 204 to 368, the domain is characterized as UBC core.
+At position 17 to 132, the domain is characterized as DUSP.
+At position 301 to 880, the domain is characterized as USP.
+At position 305 to 356, the domain is characterized as Collagen-like.
+At position 389 to 489, the domain is characterized as SRCR.
+At position 161 to 289, the domain is characterized as GST C-terminal.
+At position 28 to 70, the domain is characterized as EGF-like 1.
+At position 71 to 122, the domain is characterized as EGF-like 2; calcium-binding.
+At position 123 to 171, the domain is characterized as EGF-like 3; calcium-binding.
+At position 390 to 440, the domain is characterized as GPS.
+At position 405 to 476, the domain is characterized as ACT.
+At position 288 to 500, the domain is characterized as B30.2/SPRY.
+At position 8 to 468, the domain is characterized as ABC transporter.
+At position 147 to 377, the domain is characterized as tr-type G.
+At position 225 to 399, the domain is characterized as Helicase ATP-binding.
+At position 429 to 573, the domain is characterized as Helicase C-terminal.
+At position 7 to 213, the domain is characterized as Lon N-terminal.
+At position 615 to 795, the domain is characterized as Lon proteolytic.
+At position 91 to 238, the domain is characterized as C2 1.
+At position 554 to 674, the domain is characterized as MHD1.
+At position 785 to 892, the domain is characterized as MHD2.
+At position 909 to 1034, the domain is characterized as C2 2.
+At position 976 to 1082, the domain is characterized as Fibronectin type-III.
+At position 338 to 409, the domain is characterized as ACT-like 1.
+At position 432 to 504, the domain is characterized as ACT-like 2.
+At position 561 to 675, the domain is characterized as Fe2OG dioxygenase.
+At position 90 to 206, the domain is characterized as RGS.
+At position 226 to 259, the domain is characterized as WW 1.
+At position 390 to 423, the domain is characterized as WW 3.
+At position 479 to 812, the domain is characterized as HECT.
+At position 380 to 393, the domain is characterized as CRIB.
+At position 683 to 934, the domain is characterized as Protein kinase.
+At position 88 to 246, the domain is characterized as TNase-like.
+At position 23 to 293, the domain is characterized as PPM-type phosphatase.
+At position 72 to 113, the domain is characterized as LDL-receptor class A 2.
+At position 413 to 514, the domain is characterized as MRH.
+At position 147 to 470, the domain is characterized as NACHT.
+At position 1 to 292, the domain is characterized as Peptidase A1.
+At position 537 to 689, the domain is characterized as MRH.
+At position 123 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 5 to 141, the domain is characterized as N-acetyltransferase 1.
+At position 31 to 72, the domain is characterized as CHCH.
+At position 157 to 325, the domain is characterized as OBG-type G.
+At position 123 to 197, the domain is characterized as PRC barrel.
+At position 424 to 646, the domain is characterized as TRUD.
+At position 142 to 348, the domain is characterized as ATP-grasp.
+At position 44 to 348, the domain is characterized as Protein kinase.
+At position 85 to 191, the domain is characterized as GST C-terminal.
+At position 156 to 278, the domain is characterized as MPN.
+At position 132 to 572, the domain is characterized as Urease.
+At position 13 to 90, the domain is characterized as Ubiquitin-like.
+At position 225 to 360, the domain is characterized as PADR1 zinc-binding.
+At position 386 to 477, the domain is characterized as BRCT.
+At position 71 to 153, the domain is characterized as Kringle.
+At position 3 to 153, the domain is characterized as Flavodoxin-like.
+At position 152 to 454, the domain is characterized as NB-ARC.
+At position 47 to 189, the domain is characterized as RNase III.
+At position 216 to 286, the domain is characterized as DRBM.
+At position 2 to 27, the domain is characterized as Antistasin-like.
+At position 149 to 430, the domain is characterized as Rab-GAP TBC.
+At position 118 to 151, the domain is characterized as EF-hand 1.
+At position 184 to 212, the domain is characterized as EF-hand 3.
+At position 213 to 247, the domain is characterized as EF-hand 4.
+At position 29 to 137, the domain is characterized as Thioredoxin 1.
+At position 139 to 256, the domain is characterized as Thioredoxin 2.
+At position 537 to 648, the domain is characterized as MaoC-like.
+At position 692 to 968, the domain is characterized as Protein kinase.
+At position 159 to 188, the domain is characterized as IQ.
+At position 278 to 472, the domain is characterized as MH2.
+At position 60 to 174, the domain is characterized as Expansin-like EG45.
+At position 184 to 264, the domain is characterized as Expansin-like CBD.
+At position 65 to 133, the domain is characterized as POTRA.
+At position 25 to 89, the domain is characterized as Sushi 1.
+At position 90 to 149, the domain is characterized as Sushi 2.
+At position 152 to 211, the domain is characterized as Sushi 3.
+At position 212 to 270, the domain is characterized as Sushi 4.
+At position 273 to 330, the domain is characterized as Sushi 5.
+At position 335 to 392, the domain is characterized as Sushi 6.
+At position 454 to 517, the domain is characterized as Sushi 8.
+At position 523 to 581, the domain is characterized as Sushi 9.
+At position 582 to 648, the domain is characterized as Sushi 10.
+At position 394 to 444, the domain is characterized as HAMP.
+At position 471 to 603, the domain is characterized as Guanylate cyclase.
+At position 211 to 408, the domain is characterized as GMPS ATP-PPase.
+At position 320 to 503, the domain is characterized as Helicase ATP-binding.
+At position 531 to 676, the domain is characterized as Helicase C-terminal.
+At position 145 to 379, the domain is characterized as Radical SAM core.
+At position 33 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 257 to 500, the domain is characterized as ABC transporter 2.
+At position 25 to 203, the domain is characterized as EngB-type G.
+At position 264 to 458, the domain is characterized as GATase cobBQ-type.
+At position 74 to 225, the domain is characterized as PID.
+At position 1 to 301, the domain is characterized as Deacetylase sirtuin-type.
+At position 94 to 354, the domain is characterized as Protein kinase.
+At position 19 to 234, the domain is characterized as tr-type G.
+At position 2 to 178, the domain is characterized as Prephenate dehydratase.
+At position 194 to 270, the domain is characterized as ACT.
+At position 754 to 843, the domain is characterized as SUEL-type lectin.
+At position 79 to 284, the domain is characterized as B30.2/SPRY.
+At position 317 to 844, the domain is characterized as USP.
+At position 633 to 676, the domain is characterized as UBA 1.
+At position 708 to 748, the domain is characterized as UBA 2.
+At position 297 to 347, the domain is characterized as Myb-like.
+At position 40 to 233, the domain is characterized as Glutamine amidotransferase type-1.
+At position 234 to 426, the domain is characterized as GMPS ATP-PPase.
+At position 40 to 155, the domain is characterized as sHSP.
+At position 293 to 356, the domain is characterized as bZIP.
+At position 331 to 391, the domain is characterized as MIR 1.
+At position 399 to 458, the domain is characterized as MIR 2.
+At position 464 to 521, the domain is characterized as MIR 3.
+At position 15 to 101, the domain is characterized as WSC.
+At position 72 to 302, the domain is characterized as Helicase ATP-binding.
+At position 330 to 480, the domain is characterized as Helicase C-terminal.
+At position 11 to 73, the domain is characterized as SAM.
+At position 44 to 129, the domain is characterized as Myb-like.
+At position 39 to 422, the domain is characterized as Helicase ATP-binding.
+At position 52 to 158, the domain is characterized as Expansin-like EG45.
+At position 172 to 255, the domain is characterized as Expansin-like CBD.
+At position 157 to 310, the domain is characterized as Plastocyanin-like 2.
+At position 412 to 551, the domain is characterized as Plastocyanin-like 3.
+At position 9 to 135, the domain is characterized as Response regulatory.
+At position 163 to 330, the domain is characterized as OBG-type G.
+At position 169 to 280, the domain is characterized as PINc.
+At position 295 to 356, the domain is characterized as TRAM.
+At position 10 to 135, the domain is characterized as Thioredoxin.
+At position 242 to 422, the domain is characterized as PBS-linker 1.
+At position 498 to 680, the domain is characterized as PBS-linker 2.
+At position 694 to 871, the domain is characterized as PBS-linker 3.
+At position 79 to 199, the domain is characterized as PLAT.
+At position 202 to 896, the domain is characterized as Lipoxygenase.
+At position 4 to 134, the domain is characterized as Galectin.
+At position 3 to 33, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 37 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 68 to 97, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 613 to 787, the domain is characterized as PCI.
+At position 345 to 620, the domain is characterized as Protein kinase.
+At position 273 to 361, the domain is characterized as PDZ 1.
+At position 750 to 836, the domain is characterized as PDZ 2.
+At position 127 to 205, the domain is characterized as RRM 1.
+At position 213 to 293, the domain is characterized as RRM 2.
+At position 80 to 279, the domain is characterized as Peptidase M12A.
+At position 52 to 130, the domain is characterized as H15.
+At position 101 to 400, the domain is characterized as ABC transmembrane type-1 1.
+At position 445 to 688, the domain is characterized as ABC transporter 1.
+At position 797 to 1094, the domain is characterized as ABC transmembrane type-1 2.
+At position 1136 to 1377, the domain is characterized as ABC transporter 2.
+At position 349 to 429, the domain is characterized as KH-like.
+At position 123 to 216, the domain is characterized as Rhodanese.
+At position 2 to 136, the domain is characterized as PINc.
+At position 53 to 216, the domain is characterized as EngA-type G 1.
+At position 228 to 401, the domain is characterized as EngA-type G 2.
+At position 402 to 484, the domain is characterized as KH-like.
+At position 1009 to 1093, the domain is characterized as PB1.
+At position 26 to 66, the domain is characterized as Chitin-binding type-1 1.
+At position 69 to 108, the domain is characterized as Chitin-binding type-1 2.
+At position 84 to 163, the domain is characterized as RRM.
+At position 13 to 180, the domain is characterized as PNPLA.
+At position 104 to 283, the domain is characterized as Tyr recombinase.
+At position 128 to 383, the domain is characterized as Radical SAM core.
+At position 435 to 486, the domain is characterized as SANT 1.
+At position 623 to 674, the domain is characterized as SANT 2.
+At position 15 to 144, the domain is characterized as VHS.
+At position 200 to 579, the domain is characterized as GRAS.
+At position 118 to 372, the domain is characterized as Protein kinase.
+At position 419 to 453, the domain is characterized as EF-hand 1.
+At position 454 to 489, the domain is characterized as EF-hand 2.
+At position 528 to 562, the domain is characterized as EF-hand 4.
+At position 57 to 228, the domain is characterized as Laminin G-like.
+At position 399 to 447, the domain is characterized as Collagen-like 1.
+At position 487 to 545, the domain is characterized as Collagen-like 2.
+At position 546 to 590, the domain is characterized as Collagen-like 3.
+At position 805 to 862, the domain is characterized as Collagen-like 4.
+At position 863 to 899, the domain is characterized as Collagen-like 5.
+At position 1099 to 1156, the domain is characterized as Collagen-like 6.
+At position 1157 to 1172, the domain is characterized as Collagen-like 7.
+At position 1441 to 1499, the domain is characterized as Collagen-like 8.
+At position 1541 to 1735, the domain is characterized as Fibrillar collagen NC1.
+At position 208 to 350, the domain is characterized as VLRF1.
+At position 44 to 723, the domain is characterized as Myosin motor.
+At position 727 to 747, the domain is characterized as IQ 1.
+At position 748 to 773, the domain is characterized as IQ 2.
+At position 781 to 977, the domain is characterized as TH1.
+At position 9 to 96, the domain is characterized as MtN3/slv 1.
+At position 132 to 214, the domain is characterized as MtN3/slv 2.
+At position 34 to 79, the domain is characterized as WAP.
+At position 29 to 302, the domain is characterized as Dynamin-type G.
+At position 539 to 625, the domain is characterized as GED.
+At position 56 to 207, the domain is characterized as CP-type G.
+At position 11 to 246, the domain is characterized as ABC transporter 1.
+At position 257 to 503, the domain is characterized as ABC transporter 2.
+At position 23 to 208, the domain is characterized as RNase H type-2.
+At position 254 to 289, the domain is characterized as DMA.
+At position 582 to 855, the domain is characterized as Protein kinase.
+At position 1 to 55, the domain is characterized as IBB.
+At position 40 to 158, the domain is characterized as BTB.
+At position 290 to 322, the domain is characterized as WW.
+At position 413 to 580, the domain is characterized as PID 1.
+At position 586 to 738, the domain is characterized as PID 2.
+At position 3 to 55, the domain is characterized as HTH psq-type.
+At position 67 to 137, the domain is characterized as HTH CENPB-type.
+At position 167 to 360, the domain is characterized as DDE-1.
+At position 4 to 293, the domain is characterized as Protein kinase.
+At position 47 to 189, the domain is characterized as Thioredoxin.
+At position 68 to 262, the domain is characterized as SMP-LTD.
+At position 267 to 381, the domain is characterized as C2.
+At position 122 to 323, the domain is characterized as ATP-grasp.
+At position 634 to 663, the domain is characterized as IQ.
+At position 109 to 173, the domain is characterized as SANT.
+At position 24 to 165, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 73, the domain is characterized as TGS.
+At position 585 to 644, the domain is characterized as KH.
+At position 656 to 728, the domain is characterized as S1 motif.
+At position 22 to 142, the domain is characterized as MTTase N-terminal.
+At position 169 to 401, the domain is characterized as Radical SAM core.
+At position 404 to 466, the domain is characterized as TRAM.
+At position 162 to 291, the domain is characterized as EamA 2.
+At position 1 to 56, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 613 to 727, the domain is characterized as SMC hinge.
+At position 183 to 202, the domain is characterized as UIM 1.
+At position 208 to 227, the domain is characterized as UIM 2.
+At position 233 to 252, the domain is characterized as UIM 3.
+At position 336 to 413, the domain is characterized as RRM 4.
+At position 23 to 112, the domain is characterized as Ig-like.
+At position 1477 to 1547, the domain is characterized as Bromo.
+At position 14 to 254, the domain is characterized as UmuC.
+At position 276 to 342, the domain is characterized as HMA 4.
+At position 376 to 442, the domain is characterized as HMA 5.
+At position 478 to 544, the domain is characterized as HMA 6.
+At position 554 to 620, the domain is characterized as HMA 7.
+At position 63 to 281, the domain is characterized as Radical SAM core.
+At position 85 to 269, the domain is characterized as ATP-grasp.
+At position 12 to 129, the domain is characterized as Response regulatory.
+At position 51 to 197, the domain is characterized as Cupin type-1.
+At position 2 to 93, the domain is characterized as BLUF.
+At position 155 to 403, the domain is characterized as EAL.
+At position 12 to 46, the domain is characterized as EF-hand 1.
+At position 80 to 114, the domain is characterized as EF-hand 2.
+At position 12 to 196, the domain is characterized as UmuC.
+At position 95 to 302, the domain is characterized as TLC.
+At position 10 to 60, the domain is characterized as SpoVT-AbrB.
+At position 771 to 912, the domain is characterized as CID.
+At position 43 to 210, the domain is characterized as Laminin G-like.
+At position 304 to 343, the domain is characterized as EGF-like 1.
+At position 344 to 381, the domain is characterized as EGF-like 2; calcium-binding.
+At position 397 to 434, the domain is characterized as EGF-like 3; calcium-binding.
+At position 438 to 481, the domain is characterized as EGF-like 4.
+At position 750 to 964, the domain is characterized as TSP C-terminal.
+At position 122 to 269, the domain is characterized as SIS.
+At position 356 to 369, the domain is characterized as CRIB.
+At position 570 to 823, the domain is characterized as Protein kinase.
+At position 185 to 292, the domain is characterized as Ig-like.
+At position 10 to 298, the domain is characterized as Protein kinase.
+At position 4 to 424, the domain is characterized as Helicase ATP-binding.
+At position 565 to 625, the domain is characterized as KH.
+At position 635 to 709, the domain is characterized as S1 motif.
+At position 115 to 273, the domain is characterized as Cupin type-1 1.
+At position 332 to 494, the domain is characterized as Cupin type-1 2.
+At position 46 to 170, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 5 to 51, the domain is characterized as F-box.
+At position 741 to 832, the domain is characterized as SUEL-type lectin.
+At position 207 to 309, the domain is characterized as Fe2OG dioxygenase.
+At position 286 to 602, the domain is characterized as Asparagine synthetase.
+At position 1 to 254, the domain is characterized as Deacetylase sirtuin-type.
+At position 57 to 145, the domain is characterized as PPIase FKBP-type 1.
+At position 173 to 262, the domain is characterized as PPIase FKBP-type 2.
+At position 290 to 383, the domain is characterized as PPIase FKBP-type 3.
+At position 552 to 624, the domain is characterized as ACT.
+At position 131 to 163, the domain is characterized as Gla.
+At position 6 to 273, the domain is characterized as Pyruvate carboxyltransferase.
+At position 34 to 191, the domain is characterized as SIS.
+At position 266 to 392, the domain is characterized as G8.
+At position 15 to 159, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 290 to 429, the domain is characterized as C2.
+At position 682 to 800, the domain is characterized as RGS.
+At position 23 to 799, the domain is characterized as Vitellogenin.
+At position 1466 to 1675, the domain is characterized as VWFD.
+At position 28 to 141, the domain is characterized as Cystatin fetuin-B-type 1.
+At position 152 to 264, the domain is characterized as Cystatin fetuin-B-type 2.
+At position 57 to 206, the domain is characterized as MPN.
+At position 31 to 222, the domain is characterized as RNase H type-2.
+At position 402 to 525, the domain is characterized as Ricin B-type lectin.
+At position 102 to 429, the domain is characterized as Asparaginase/glutaminase.
+At position 891 to 1134, the domain is characterized as ABC transporter 2.
+At position 121 to 248, the domain is characterized as SLD.
+At position 186 to 378, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 881 to 1006, the domain is characterized as DBINO.
+At position 1130 to 1302, the domain is characterized as Helicase ATP-binding.
+At position 1702 to 1858, the domain is characterized as Helicase C-terminal.
+At position 60 to 168, the domain is characterized as FAD-binding FR-type.
+At position 29 to 112, the domain is characterized as Ig-like V-type.
+At position 616 to 697, the domain is characterized as BRCT.
+At position 3 to 48, the domain is characterized as SpoVT-AbrB.
+At position 125 to 221, the domain is characterized as Rhodanese.
+At position 56 to 237, the domain is characterized as tr-type G.
+At position 119 to 307, the domain is characterized as ATP-grasp.
+At position 395 to 517, the domain is characterized as Guanylate cyclase 1.
+At position 1168 to 1296, the domain is characterized as Guanylate cyclase 2.
+At position 298 to 494, the domain is characterized as Histidine kinase.
+At position 50 to 336, the domain is characterized as Rab-GAP TBC.
+At position 1 to 176, the domain is characterized as FAD-binding PCMH-type.
+At position 14 to 81, the domain is characterized as S4 RNA-binding.
+At position 18 to 108, the domain is characterized as N-acetyltransferase.
+At position 17 to 131, the domain is characterized as Ig-like V-type.
+At position 68 to 180, the domain is characterized as Thioredoxin.
+At position 3 to 215, the domain is characterized as ABC transporter.
+At position 17 to 184, the domain is characterized as Era-type G.
+At position 36 to 230, the domain is characterized as Cupin type-1 1.
+At position 324 to 453, the domain is characterized as Cupin type-1 2.
+At position 30 to 134, the domain is characterized as Gnk2-homologous 1.
+At position 140 to 249, the domain is characterized as Gnk2-homologous 2.
+At position 357 to 637, the domain is characterized as Protein kinase.
+At position 172 to 202, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 47 to 226, the domain is characterized as FAD-binding PCMH-type.
+At position 42 to 98, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 73 to 357, the domain is characterized as Protein kinase.
+At position 23 to 166, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 91 to 411, the domain is characterized as Kinesin motor.
+At position 938 to 1077, the domain is characterized as MGS-like.
+At position 18 to 69, the domain is characterized as bHLH.
+At position 192 to 443, the domain is characterized as Protein kinase.
+At position 3 to 85, the domain is characterized as GST N-terminal.
+At position 91 to 224, the domain is characterized as GST C-terminal.
+At position 17 to 52, the domain is characterized as CBM1.
+At position 112 to 201, the domain is characterized as Histone-fold.
+At position 29 to 256, the domain is characterized as Peptidase S1.
+At position 248 to 333, the domain is characterized as Ig-like C2-type 1.
+At position 347 to 439, the domain is characterized as Ig-like C2-type 2.
+At position 3 to 65, the domain is characterized as J.
+At position 11 to 194, the domain is characterized as YrdC-like.
+At position 1317 to 1392, the domain is characterized as DEP.
+At position 22 to 242, the domain is characterized as Peptidase S1.
+At position 30 to 246, the domain is characterized as tr-type G.
+At position 365 to 440, the domain is characterized as DEP.
+At position 1758 to 2084, the domain is characterized as PIPK.
+At position 130 to 260, the domain is characterized as Galectin.
+At position 46 to 229, the domain is characterized as PCI.
+At position 175 to 278, the domain is characterized as Fe2OG dioxygenase.
+At position 22 to 243, the domain is characterized as ABC transporter.
+At position 346 to 415, the domain is characterized as SH3b.
+At position 22 to 116, the domain is characterized as Ig-like 1.
+At position 126 to 219, the domain is characterized as Ig-like 2.
+At position 152 to 308, the domain is characterized as TRUD.
+At position 5 to 196, the domain is characterized as DPCK.
+At position 7 to 42, the domain is characterized as RPE1 insert.
+At position 44 to 222, the domain is characterized as Guanylate kinase-like.
+At position 803 to 871, the domain is characterized as Carrier.
+At position 46 to 277, the domain is characterized as Radical SAM core.
+At position 4 to 80, the domain is characterized as Ubiquitin-like.
+At position 105 to 483, the domain is characterized as USP.
+At position 393 to 736, the domain is characterized as Kinesin motor.
+At position 860 to 911, the domain is characterized as FHA.
+At position 166 to 235, the domain is characterized as OVATE.
+At position 59 to 123, the domain is characterized as KH 1.
+At position 167 to 232, the domain is characterized as KH 2.
+At position 283 to 354, the domain is characterized as KH 3.
+At position 11 to 85, the domain is characterized as HTH merR-type.
+At position 145 to 450, the domain is characterized as Peptidase S8.
+At position 37 to 431, the domain is characterized as Glutamine amidotransferase type-2.
+At position 140 to 381, the domain is characterized as Radical SAM core.
+At position 156 to 243, the domain is characterized as HPr.
+At position 503 to 605, the domain is characterized as CXC.
+At position 612 to 727, the domain is characterized as SET.
+At position 11 to 172, the domain is characterized as Exonuclease.
+At position 46 to 173, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 98 to 161, the domain is characterized as HMA 2.
+At position 166 to 236, the domain is characterized as RRM.
+At position 12 to 161, the domain is characterized as Reelin.
+At position 475 to 661, the domain is characterized as VWFA.
+At position 110 to 188, the domain is characterized as RRM 1.
+At position 196 to 276, the domain is characterized as RRM 2.
+At position 118 to 155, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 706 to 780, the domain is characterized as Smr.
+At position 205 to 292, the domain is characterized as RCK C-terminal 1.
+At position 2 to 184, the domain is characterized as RNase H type-2.
+At position 106 to 179, the domain is characterized as PRC barrel.
+At position 100 to 369, the domain is characterized as Protein kinase.
+At position 370 to 440, the domain is characterized as AGC-kinase C-terminal.
+At position 1059 to 1177, the domain is characterized as PH.
+At position 1203 to 1489, the domain is characterized as CNH.
+At position 1546 to 1559, the domain is characterized as CRIB.
+At position 52 to 92, the domain is characterized as Fibronectin type-I 1.
+At position 97 to 140, the domain is characterized as Fibronectin type-I 2.
+At position 141 to 184, the domain is characterized as Fibronectin type-I 3.
+At position 186 to 230, the domain is characterized as Fibronectin type-I 4.
+At position 231 to 275, the domain is characterized as Fibronectin type-I 5.
+At position 311 to 350, the domain is characterized as Fibronectin type-I 6.
+At position 360 to 408, the domain is characterized as Fibronectin type-II 1.
+At position 420 to 468, the domain is characterized as Fibronectin type-II 2.
+At position 473 to 516, the domain is characterized as Fibronectin type-I 7.
+At position 521 to 563, the domain is characterized as Fibronectin type-I 8.
+At position 564 to 607, the domain is characterized as Fibronectin type-I 9.
+At position 615 to 708, the domain is characterized as Fibronectin type-III 1.
+At position 723 to 812, the domain is characterized as Fibronectin type-III 2.
+At position 815 to 906, the domain is characterized as Fibronectin type-III 3.
+At position 913 to 1002, the domain is characterized as Fibronectin type-III 4.
+At position 1003 to 1091, the domain is characterized as Fibronectin type-III 5.
+At position 1093 to 1179, the domain is characterized as Fibronectin type-III 6.
+At position 1180 to 1274, the domain is characterized as Fibronectin type-III 7.
+At position 1275 to 1363, the domain is characterized as Fibronectin type-III 8.
+At position 1275 to 1363, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1364 to 1456, the domain is characterized as Fibronectin type-III 9.
+At position 1457 to 1544, the domain is characterized as Fibronectin type-III 10.
+At position 1545 to 1638, the domain is characterized as Fibronectin type-III 11.
+At position 1639 to 1730, the domain is characterized as Fibronectin type-III 12.
+At position 1731 to 1818, the domain is characterized as Fibronectin type-III 13.
+At position 1731 to 1818, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1819 to 1912, the domain is characterized as Fibronectin type-III 14.
+At position 1913 to 2000, the domain is characterized as Fibronectin type-III 15.
+At position 2001 to 2092, the domain is characterized as Fibronectin type-III 16.
+At position 2200 to 2292, the domain is characterized as Fibronectin type-III 17.
+At position 2300 to 2344, the domain is characterized as Fibronectin type-I 10.
+At position 2345 to 2387, the domain is characterized as Fibronectin type-I 11.
+At position 2389 to 2429, the domain is characterized as Fibronectin type-I 12.
+At position 319 to 439, the domain is characterized as MATH.
+At position 104 to 325, the domain is characterized as PE-PPE.
+At position 23 to 244, the domain is characterized as NHR.
+At position 250 to 285, the domain is characterized as SOCS box.
+At position 152 to 341, the domain is characterized as CheB-type methylesterase.
+At position 351 to 470, the domain is characterized as BRCT.
+At position 578 to 679, the domain is characterized as tRNA-binding.
+At position 7 to 109, the domain is characterized as FAD-binding FR-type.
+At position 234 to 319, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 133 to 317, the domain is characterized as ATP-grasp.
+At position 14 to 51, the domain is characterized as UBA-like.
+At position 70 to 266, the domain is characterized as DCUN1.
+At position 125 to 308, the domain is characterized as FAD-binding PCMH-type.
+At position 226 to 428, the domain is characterized as Pentraxin (PTX).
+At position 349 to 427, the domain is characterized as Cytochrome b5 heme-binding.
+At position 109 to 241, the domain is characterized as NlpC/P60.
+At position 113 to 384, the domain is characterized as SET.
+At position 85 to 172, the domain is characterized as MANSC.
+At position 193 to 287, the domain is characterized as PKD.
+At position 293 to 329, the domain is characterized as LDL-receptor class A.
+At position 22 to 223, the domain is characterized as GH16.
+At position 84 to 403, the domain is characterized as BRO1.
+At position 25 to 222, the domain is characterized as GH16.
+At position 44 to 159, the domain is characterized as tRNA-binding.
+At position 428 to 510, the domain is characterized as B5.
+At position 758 to 851, the domain is characterized as FDX-ACB.
+At position 90 to 148, the domain is characterized as K-box; partial.
+At position 23 to 73, the domain is characterized as Tudor-knot.
+At position 156 to 427, the domain is characterized as MYST-type HAT.
+At position 31 to 95, the domain is characterized as Sushi.
+At position 315 to 406, the domain is characterized as PUA.
+At position 34 to 156, the domain is characterized as Bulb-type lectin.
+At position 350 to 430, the domain is characterized as PAN.
+At position 16 to 157, the domain is characterized as RNase H type-1.
+At position 28 to 221, the domain is characterized as Thioredoxin.
+At position 256 to 396, the domain is characterized as RanBD1.
+At position 439 to 542, the domain is characterized as SH2.
+At position 582 to 854, the domain is characterized as Protein kinase 1.
+At position 874 to 1152, the domain is characterized as Protein kinase 2.
+At position 2 to 21, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 27 to 139, the domain is characterized as Thioredoxin 1.
+At position 161 to 275, the domain is characterized as Thioredoxin 2.
+At position 17 to 81, the domain is characterized as LIM zinc-binding 1.
+At position 76 to 135, the domain is characterized as LIM zinc-binding 2.
+At position 780 to 966, the domain is characterized as Rho-GAP.
+At position 32 to 149, the domain is characterized as C-type lectin.
+At position 317 to 370, the domain is characterized as HAMP 1.
+At position 437 to 490, the domain is characterized as HAMP 2.
+At position 509 to 745, the domain is characterized as Methyl-accepting transducer.
+At position 25 to 61, the domain is characterized as ATP-grasp.
+At position 429 to 480, the domain is characterized as Rubredoxin-like.
+At position 1 to 300, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 280 to 590, the domain is characterized as UvrD-like helicase C-terminal.
+At position 481 to 608, the domain is characterized as Guanylate cyclase.
+At position 224 to 387, the domain is characterized as TrmE-type G.
+At position 42 to 382, the domain is characterized as G-alpha.
+At position 120 to 480, the domain is characterized as PTS EIIC type-1.
+At position 81 to 376, the domain is characterized as Protein kinase.
+At position 154 to 348, the domain is characterized as ATP-grasp.
+At position 72 to 137, the domain is characterized as TGS.
+At position 165 to 253, the domain is characterized as PDZ.
+At position 138 to 377, the domain is characterized as Radical SAM core.
+At position 30 to 170, the domain is characterized as Ephrin RBD.
+At position 434 to 617, the domain is characterized as Thioredoxin.
+At position 15 to 165, the domain is characterized as UBC core.
+At position 16 to 306, the domain is characterized as Protein kinase.
+At position 124 to 414, the domain is characterized as ABC transmembrane type-1.
+At position 449 to 690, the domain is characterized as ABC transporter.
+At position 215 to 267, the domain is characterized as HAMP.
+At position 272 to 501, the domain is characterized as Methyl-accepting transducer.
+At position 6 to 389, the domain is characterized as Kinesin motor.
+At position 255 to 314, the domain is characterized as CBS 1.
+At position 711 to 793, the domain is characterized as ACT 1.
+At position 819 to 893, the domain is characterized as ACT 2.
+At position 110 to 194, the domain is characterized as PPIase FKBP-type.
+At position 165 to 351, the domain is characterized as CheB-type methylesterase.
+At position 29 to 142, the domain is characterized as Plastocyanin-like 1.
+At position 171 to 359, the domain is characterized as Plastocyanin-like 2.
+At position 468 to 598, the domain is characterized as Plastocyanin-like 3.
+At position 193 to 265, the domain is characterized as PDZ.
+At position 148 to 303, the domain is characterized as F5/8 type C 1.
+At position 308 to 463, the domain is characterized as F5/8 type C 2.
+At position 29 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 58 to 346, the domain is characterized as ABC transmembrane type-1 1.
+At position 381 to 617, the domain is characterized as ABC transporter 1.
+At position 710 to 997, the domain is characterized as ABC transmembrane type-1 2.
+At position 1032 to 1271, the domain is characterized as ABC transporter 2.
+At position 451 to 576, the domain is characterized as CRC.
+At position 15 to 102, the domain is characterized as J.
+At position 112 to 168, the domain is characterized as DPH-type MB.
+At position 23 to 257, the domain is characterized as ABC transporter.
+At position 232 to 403, the domain is characterized as PCI.
+At position 26 to 93, the domain is characterized as Importin N-terminal.
+At position 127 to 208, the domain is characterized as Kringle 1.
+At position 215 to 296, the domain is characterized as Kringle 2.
+At position 1 to 52, the domain is characterized as HTH myb-type 1.
+At position 53 to 107, the domain is characterized as HTH myb-type 2.
+At position 1 to 108, the domain is characterized as MTTase N-terminal.
+At position 110 to 339, the domain is characterized as Radical SAM core.
+At position 94 to 341, the domain is characterized as NR LBD.
+At position 4 to 83, the domain is characterized as RRM.
+At position 90 to 183, the domain is characterized as PH.
+At position 92 to 167, the domain is characterized as Smr.
+At position 437 to 577, the domain is characterized as Thioredoxin.
+At position 238 to 456, the domain is characterized as Fibrinogen C-terminal.
+At position 318 to 403, the domain is characterized as B5.
+At position 625 to 718, the domain is characterized as FDX-ACB.
+At position 175 to 293, the domain is characterized as AB hydrolase-1.
+At position 191 to 260, the domain is characterized as Chromo 1.
+At position 288 to 349, the domain is characterized as Chromo 2.
+At position 387 to 557, the domain is characterized as Helicase ATP-binding.
+At position 694 to 852, the domain is characterized as Helicase C-terminal.
+At position 549 to 641, the domain is characterized as BRCT 1.
+At position 655 to 765, the domain is characterized as BRCT 2.
+At position 92 to 195, the domain is characterized as C-type lectin.
+At position 703 to 796, the domain is characterized as FDX-ACB.
+At position 50 to 247, the domain is characterized as Cupin type-1 1.
+At position 315 to 464, the domain is characterized as Cupin type-1 2.
+At position 364 to 543, the domain is characterized as Helicase ATP-binding.
+At position 601 to 748, the domain is characterized as Helicase C-terminal.
+At position 45 to 79, the domain is characterized as Plastocyanin-like 1.
+At position 99 to 174, the domain is characterized as Plastocyanin-like 2.
+At position 242 to 317, the domain is characterized as Plastocyanin-like 3.
+At position 372 to 506, the domain is characterized as Plastocyanin-like 4.
+At position 519 to 753, the domain is characterized as NR LBD.
+At position 435 to 532, the domain is characterized as Fibronectin type-III 2.
+At position 620 to 883, the domain is characterized as Protein kinase.
+At position 912 to 976, the domain is characterized as SAM.
+At position 32 to 219, the domain is characterized as RNase H type-2.
+At position 68 to 185, the domain is characterized as Plastocyanin-like 1.
+At position 191 to 337, the domain is characterized as Plastocyanin-like 2.
+At position 396 to 525, the domain is characterized as Plastocyanin-like 3.
+At position 21 to 62, the domain is characterized as Chitin-binding type-1.
+At position 17 to 252, the domain is characterized as ABC transporter 1.
+At position 263 to 505, the domain is characterized as ABC transporter 2.
+At position 3 to 122, the domain is characterized as ADF-H.
+At position 362 to 409, the domain is characterized as FBD.
+At position 34 to 81, the domain is characterized as F-box.
+At position 560 to 638, the domain is characterized as TFIIS N-terminal.
+At position 65 to 105, the domain is characterized as EGF-like.
+At position 201 to 234, the domain is characterized as WW 1.
+At position 236 to 269, the domain is characterized as WW 2.
+At position 323 to 370, the domain is characterized as SARAH.
+At position 1 to 110, the domain is characterized as BMC circularly permuted 1.
+At position 111 to 217, the domain is characterized as BMC circularly permuted 2.
+At position 32 to 323, the domain is characterized as ABC transmembrane type-1.
+At position 355 to 591, the domain is characterized as ABC transporter.
+At position 43 to 133, the domain is characterized as BRCT.
+At position 243 to 436, the domain is characterized as GATase cobBQ-type.
+At position 67 to 249, the domain is characterized as SMP-LTD.
+At position 240 to 363, the domain is characterized as C2 1.
+At position 401 to 521, the domain is characterized as C2 2.
+At position 57 to 274, the domain is characterized as Radical SAM core.
+At position 126 to 399, the domain is characterized as Peptidase S8.
+At position 37 to 66, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 162 to 306, the domain is characterized as PI-PLC X-box.
+At position 385 to 501, the domain is characterized as PI-PLC Y-box.
+At position 501 to 625, the domain is characterized as C2.
+At position 252 to 331, the domain is characterized as BCNT-C.
+At position 12 to 84, the domain is characterized as J.
+At position 249 to 505, the domain is characterized as ABC transporter 2.
+At position 240 to 286, the domain is characterized as LRRCT.
+At position 287 to 373, the domain is characterized as Ig-like.
+At position 414 to 503, the domain is characterized as Fibronectin type-III.
+At position 100 to 275, the domain is characterized as Prephenate dehydratase.
+At position 289 to 375, the domain is characterized as ACT.
+At position 65 to 107, the domain is characterized as CUE.
+At position 223 to 273, the domain is characterized as F-box.
+At position 108 to 135, the domain is characterized as PLD phosphodiesterase 1.
+At position 285 to 312, the domain is characterized as PLD phosphodiesterase 2.
+At position 1 to 272, the domain is characterized as Protein kinase 1.
+At position 1177 to 1433, the domain is characterized as Protein kinase 2.
+At position 26 to 206, the domain is characterized as FAD-binding PCMH-type.
+At position 33 to 91, the domain is characterized as TCP.
+At position 53 to 458, the domain is characterized as GBD/FH3.
+At position 487 to 615, the domain is characterized as FH1.
+At position 616 to 1013, the domain is characterized as FH2.
+At position 1053 to 1133, the domain is characterized as DAD.
+At position 587 to 653, the domain is characterized as CBS 1.
+At position 684 to 742, the domain is characterized as CBS 2.
+At position 2 to 438, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 143 to 369, the domain is characterized as Sigma-54 factor interaction.
+At position 273 to 316, the domain is characterized as STI1.
+At position 363 to 403, the domain is characterized as UBA 2.
+At position 32 to 85, the domain is characterized as Sushi.
+At position 1239 to 1306, the domain is characterized as Sushi.
+At position 28 to 260, the domain is characterized as GB1/RHD3-type G.
+At position 267 to 449, the domain is characterized as GAF.
+At position 668 to 739, the domain is characterized as PAS 1.
+At position 802 to 873, the domain is characterized as PAS 2.
+At position 950 to 1170, the domain is characterized as Histidine kinase.
+At position 154 to 224, the domain is characterized as SANT.
+At position 38 to 189, the domain is characterized as CBM-cenC 1.
+At position 195 to 343, the domain is characterized as CBM-cenC 2.
+At position 352 to 675, the domain is characterized as GH10.
+At position 1051 to 1114, the domain is characterized as SLH 1.
+At position 1115 to 1157, the domain is characterized as SLH 2.
+At position 104 to 298, the domain is characterized as Tyr recombinase.
+At position 53 to 96, the domain is characterized as Collagen-like.
+At position 105 to 238, the domain is characterized as C1q.
+At position 13 to 251, the domain is characterized as Protein kinase.
+At position 71 to 269, the domain is characterized as ABC transmembrane type-1.
+At position 14 to 201, the domain is characterized as Reticulon.
+At position 111 to 379, the domain is characterized as SET.
+At position 145 to 171, the domain is characterized as KH.
+At position 256 to 290, the domain is characterized as ShKT.
+At position 296 to 381, the domain is characterized as Ig-like C2-type.
+At position 20 to 170, the domain is characterized as MARVEL.
+At position 600 to 698, the domain is characterized as tRNA-binding.
+At position 54 to 132, the domain is characterized as EMI.
+At position 815 to 943, the domain is characterized as C1q.
+At position 4 to 218, the domain is characterized as Radical SAM core.
+At position 735 to 1124, the domain is characterized as FH1.
+At position 1139 to 1554, the domain is characterized as FH2.
+At position 11 to 97, the domain is characterized as GS beta-grasp.
+At position 188 to 332, the domain is characterized as FCP1 homology.
+At position 38 to 197, the domain is characterized as PPIase cyclophilin-type.
+At position 163 to 236, the domain is characterized as HTH crp-type.
+At position 49 to 207, the domain is characterized as Cupin type-1 1.
+At position 249 to 407, the domain is characterized as Cupin type-1 2.
+At position 8 to 123, the domain is characterized as VOC.
+At position 41 to 165, the domain is characterized as RWD.
+At position 4 to 151, the domain is characterized as UBC core.
+At position 198 to 271, the domain is characterized as KRAB.
+At position 21 to 111, the domain is characterized as Core-binding (CB).
+At position 140 to 336, the domain is characterized as Tyr recombinase.
+At position 22 to 56, the domain is characterized as WW 1.
+At position 126 to 157, the domain is characterized as WW 2.
+At position 426 to 503, the domain is characterized as BAG.
+At position 36 to 486, the domain is characterized as Biotin carboxylation.
+At position 156 to 353, the domain is characterized as ATP-grasp.
+At position 563 to 832, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1109 to 1178, the domain is characterized as Biotinyl-binding.
+At position 65 to 100, the domain is characterized as EF-hand.
+At position 52 to 249, the domain is characterized as Peptidase M12A.
+At position 176 to 302, the domain is characterized as C-type lectin.
+At position 60 to 151, the domain is characterized as SH2.
+At position 152 to 211, the domain is characterized as SH3 2.
+At position 5 to 256, the domain is characterized as Pyruvate carboxyltransferase.
+At position 316 to 359, the domain is characterized as CUE.
+At position 526 to 608, the domain is characterized as Carrier.
+At position 96 to 146, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 156 to 206, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 103 to 174, the domain is characterized as PRC barrel.
+At position 135 to 406, the domain is characterized as ABC transporter 1.
+At position 484 to 697, the domain is characterized as ABC transmembrane type-2 1.
+At position 791 to 1043, the domain is characterized as ABC transporter 2.
+At position 1116 to 1330, the domain is characterized as ABC transmembrane type-2 2.
+At position 183 to 320, the domain is characterized as C-type lectin.
+At position 561 to 632, the domain is characterized as BRCT.
+At position 7 to 433, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 946 to 1254, the domain is characterized as PKS/mFAS DH.
+At position 2455 to 2532, the domain is characterized as Carrier.
+At position 351 to 448, the domain is characterized as ERCC4.
+At position 12 to 117, the domain is characterized as Calponin-homology (CH) 1.
+At position 125 to 227, the domain is characterized as Calponin-homology (CH) 2.
+At position 158 to 706, the domain is characterized as Protein kinase.
+At position 50 to 104, the domain is characterized as HTH myb-type.
+At position 3 to 258, the domain is characterized as Deacetylase sirtuin-type.
+At position 4 to 78, the domain is characterized as Carrier.
+At position 29 to 172, the domain is characterized as SIS.
+At position 24 to 245, the domain is characterized as Peptidase S1.
+At position 73 to 213, the domain is characterized as PX.
+At position 3 to 187, the domain is characterized as YrdC-like.
+At position 463 to 570, the domain is characterized as SEA.
+At position 58 to 149, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 38 to 133, the domain is characterized as HPt.
+At position 268 to 427, the domain is characterized as SSD.
+At position 415 to 580, the domain is characterized as Miro 2.
+At position 137 to 197, the domain is characterized as MADS-box.
+At position 168 to 363, the domain is characterized as Helicase ATP-binding.
+At position 401 to 626, the domain is characterized as Helicase C-terminal.
+At position 355 to 440, the domain is characterized as KH-like.
+At position 1 to 143, the domain is characterized as N-acetyltransferase.
+At position 318 to 424, the domain is characterized as PDZ.
+At position 31 to 298, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 295 to 558, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 355 to 567, the domain is characterized as DDE-1.
+At position 34 to 90, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 454 to 595, the domain is characterized as SIS 2.
+At position 18 to 150, the domain is characterized as VHS.
+At position 274 to 293, the domain is characterized as UIM 1.
+At position 324 to 343, the domain is characterized as UIM 2.
+At position 531 to 727, the domain is characterized as Helicase ATP-binding.
+At position 1017 to 1181, the domain is characterized as Helicase C-terminal.
+At position 123 to 155, the domain is characterized as EF-hand 4.
+At position 136 to 408, the domain is characterized as Protein kinase.
+At position 51 to 303, the domain is characterized as Protein kinase.
+At position 408 to 486, the domain is characterized as POLO box 1.
+At position 508 to 590, the domain is characterized as POLO box 2.
+At position 930 to 1071, the domain is characterized as MGS-like.
+At position 486 to 553, the domain is characterized as CBS.
+At position 1422 to 1586, the domain is characterized as PNPLA.
+At position 210 to 270, the domain is characterized as KH.
+At position 24 to 93, the domain is characterized as BTB.
+At position 33 to 109, the domain is characterized as Carrier.
+At position 35 to 401, the domain is characterized as PRONE.
+At position 8 to 144, the domain is characterized as Nudix hydrolase.
+At position 13 to 416, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 113 to 213, the domain is characterized as Fe2OG dioxygenase.
+At position 116 to 208, the domain is characterized as Ig-like C2-type 2.
+At position 213 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 314 to 411, the domain is characterized as Ig-like C2-type 4.
+At position 94 to 297, the domain is characterized as DCUN1.
+At position 611 to 864, the domain is characterized as NB-ARC.
+At position 1209 to 1278, the domain is characterized as HMA.
+At position 174 to 257, the domain is characterized as RRM.
+At position 889 to 963, the domain is characterized as RRM.
+At position 475 to 555, the domain is characterized as Kringle 5.
+At position 577 to 804, the domain is characterized as Peptidase S1.
+At position 284 to 453, the domain is characterized as SUN.
+At position 300 to 390, the domain is characterized as Rhodanese.
+At position 39 to 166, the domain is characterized as Ricin B-type lectin.
+At position 598 to 683, the domain is characterized as BRCT.
+At position 5 to 268, the domain is characterized as Peptidase S8.
+At position 10 to 129, the domain is characterized as RWD.
+At position 271 to 431, the domain is characterized as UBC core.
+At position 119 to 193, the domain is characterized as H15.
+At position 73 to 262, the domain is characterized as Peptidase M12A.
+At position 256 to 295, the domain is characterized as EGF-like.
+At position 96 to 431, the domain is characterized as Kinesin motor.
+At position 85 to 348, the domain is characterized as F-BAR.
+At position 553 to 756, the domain is characterized as Rho-GAP.
+At position 8 to 148, the domain is characterized as N-acetyltransferase.
+At position 8 to 37, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 38 to 67, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 72, the domain is characterized as Carrier 1.
+At position 988 to 1065, the domain is characterized as Carrier 2.
+At position 336 to 371, the domain is characterized as EF-hand 2.
+At position 15 to 229, the domain is characterized as ABC transporter.
+At position 286 to 427, the domain is characterized as GST C-terminal.
+At position 239 to 424, the domain is characterized as FAD-binding PCMH-type.
+At position 40 to 225, the domain is characterized as BPL/LPL catalytic.
+At position 23 to 89, the domain is characterized as Chitin-binding type R&R.
+At position 77 to 159, the domain is characterized as Pre-SET.
+At position 162 to 297, the domain is characterized as SET.
+At position 315 to 331, the domain is characterized as Post-SET.
+At position 1 to 321, the domain is characterized as SMP-LTD.
+At position 9 to 289, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 290 to 560, the domain is characterized as UvrD-like helicase C-terminal.
+At position 121 to 215, the domain is characterized as Ig-like C1-type.
+At position 128 to 244, the domain is characterized as SCP.
+At position 139 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 331, the domain is characterized as Fibronectin type-III 1.
+At position 336 to 428, the domain is characterized as Fibronectin type-III 2.
+At position 536 to 807, the domain is characterized as Protein kinase.
+At position 153 to 249, the domain is characterized as SWIRM.
+At position 76 to 123, the domain is characterized as TSP type-1 1.
+At position 341 to 402, the domain is characterized as TSP type-1 2.
+At position 404 to 459, the domain is characterized as TSP type-1 3.
+At position 461 to 525, the domain is characterized as TSP type-1 4.
+At position 585 to 643, the domain is characterized as TSP type-1 5.
+At position 645 to 702, the domain is characterized as TSP type-1 6.
+At position 1089 to 1141, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 1150 to 1202, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 1271 to 1321, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 1375 to 1425, the domain is characterized as BPTI/Kunitz inhibitor 4.
+At position 1447 to 1497, the domain is characterized as BPTI/Kunitz inhibitor 5.
+At position 1504 to 1554, the domain is characterized as BPTI/Kunitz inhibitor 6.
+At position 1621 to 1671, the domain is characterized as BPTI/Kunitz inhibitor 7.
+At position 1731 to 1781, the domain is characterized as BPTI/Kunitz inhibitor 8.
+At position 1790 to 1840, the domain is characterized as BPTI/Kunitz inhibitor 9.
+At position 1853 to 1903, the domain is characterized as BPTI/Kunitz inhibitor 10.
+At position 1914 to 1964, the domain is characterized as BPTI/Kunitz inhibitor 11.
+At position 2124 to 2163, the domain is characterized as PLAC.
+At position 82 to 334, the domain is characterized as ABC transporter.
+At position 434 to 644, the domain is characterized as ABC transmembrane type-2.
+At position 68 to 282, the domain is characterized as Radical SAM core.
+At position 116 to 249, the domain is characterized as Ricin B-type lectin 2.
+At position 460 to 627, the domain is characterized as tr-type G.
+At position 220 to 367, the domain is characterized as TrmE-type G.
+At position 38 to 149, the domain is characterized as MTTase N-terminal.
+At position 173 to 402, the domain is characterized as Radical SAM core.
+At position 3 to 76, the domain is characterized as DWNN.
+At position 55 to 122, the domain is characterized as Oxytoxin-type inhibitor cystine knot (ICK).
+At position 27 to 96, the domain is characterized as BTB.
+At position 201 to 474, the domain is characterized as NPH3.
+At position 5 to 290, the domain is characterized as CN hydrolase.
+At position 353 to 559, the domain is characterized as MCM.
+At position 339 to 401, the domain is characterized as S4 RNA-binding.
+At position 72 to 298, the domain is characterized as tr-type G.
+At position 9 to 202, the domain is characterized as tr-type G.
+At position 577 to 850, the domain is characterized as Protein kinase.
+At position 1 to 57, the domain is characterized as Myb-like 1.
+At position 58 to 108, the domain is characterized as Myb-like 2.
+At position 109 to 160, the domain is characterized as Myb-like 3.
+At position 120 to 225, the domain is characterized as PRD 1.
+At position 229 to 336, the domain is characterized as PRD 2.
+At position 206 to 248, the domain is characterized as CHCH.
+At position 79 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 119 to 148, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 33 to 167, the domain is characterized as SIS.
+At position 211 to 288, the domain is characterized as TFIIS N-terminal.
+At position 101 to 332, the domain is characterized as ATP-grasp.
+At position 233 to 408, the domain is characterized as PCI.
+At position 10 to 130, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 36 to 112, the domain is characterized as H15.
+At position 315 to 595, the domain is characterized as GH10.
+At position 703 to 883, the domain is characterized as Helicase C-terminal.
+At position 461 to 884, the domain is characterized as FH2.
+At position 559 to 662, the domain is characterized as tRNA-binding.
+At position 15 to 278, the domain is characterized as Protein kinase.
+At position 317 to 342, the domain is characterized as NAF.
+At position 773 to 879, the domain is characterized as EH.
+At position 102 to 186, the domain is characterized as PDZ.
+At position 48 to 78, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 91 to 122, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 71 to 172, the domain is characterized as ULD.
+At position 175 to 248, the domain is characterized as CUTL.
+At position 73 to 425, the domain is characterized as IF rod.
+At position 456 to 574, the domain is characterized as LTD.
+At position 988 to 1056, the domain is characterized as R3H.
+At position 540 to 656, the domain is characterized as PAZ.
+At position 841 to 1145, the domain is characterized as Piwi.
+At position 16 to 186, the domain is characterized as Era-type G.
+At position 217 to 294, the domain is characterized as KH type-2.
+At position 218 to 461, the domain is characterized as Sigma-54 factor interaction.
+At position 112 to 284, the domain is characterized as Helicase ATP-binding.
+At position 307 to 461, the domain is characterized as Helicase C-terminal.
+At position 66 to 324, the domain is characterized as Protein kinase.
+At position 367 to 402, the domain is characterized as EF-hand 1.
+At position 403 to 438, the domain is characterized as EF-hand 2.
+At position 439 to 474, the domain is characterized as EF-hand 3.
+At position 475 to 509, the domain is characterized as EF-hand 4.
+At position 37 to 127, the domain is characterized as CTCK.
+At position 6 to 200, the domain is characterized as RNase H type-2.
+At position 16 to 63, the domain is characterized as F-box.
+At position 149 to 357, the domain is characterized as Histidine kinase.
+At position 44 to 250, the domain is characterized as BPL/LPL catalytic.
+At position 145 to 434, the domain is characterized as Protein kinase.
+At position 119 to 214, the domain is characterized as PTS EIIB type-2 2.
+At position 241 to 576, the domain is characterized as PTS EIIC type-2.
+At position 6 to 121, the domain is characterized as Response regulatory.
+At position 158 to 263, the domain is characterized as HTH LytTR-type.
+At position 40 to 128, the domain is characterized as Ig-like 1.
+At position 134 to 241, the domain is characterized as Ig-like 2.
+At position 246 to 334, the domain is characterized as Ig-like 3.
+At position 341 to 429, the domain is characterized as Ig-like 4.
+At position 434 to 527, the domain is characterized as Fibronectin type-III 1.
+At position 555 to 646, the domain is characterized as Fibronectin type-III 2.
+At position 43 to 72, the domain is characterized as IQ 1.
+At position 99 to 128, the domain is characterized as IQ 2.
+At position 64 to 180, the domain is characterized as RGS.
+At position 141 to 273, the domain is characterized as Nudix hydrolase.
+At position 7 to 29, the domain is characterized as OCA.
+At position 160 to 342, the domain is characterized as OBG-type G.
+At position 1163 to 1238, the domain is characterized as DEP.
+At position 224 to 413, the domain is characterized as Ku.
+At position 359 to 381, the domain is characterized as WH2.
+At position 22 to 151, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 28 to 250, the domain is characterized as Peptidase S1.
+At position 224 to 288, the domain is characterized as SEP.
+At position 43 to 82, the domain is characterized as Chitin-binding type-1 2.
+At position 105 to 391, the domain is characterized as ABC transmembrane type-1 1.
+At position 423 to 647, the domain is characterized as ABC transporter 1.
+At position 726 to 1016, the domain is characterized as ABC transmembrane type-1 2.
+At position 1053 to 1287, the domain is characterized as ABC transporter 2.
+At position 604 to 665, the domain is characterized as SH3.
+At position 677 to 813, the domain is characterized as PID.
+At position 203 to 290, the domain is characterized as Ig-like C1-type.
+At position 342 to 496, the domain is characterized as PPIase cyclophilin-type.
+At position 270 to 470, the domain is characterized as Ku.
+At position 588 to 622, the domain is characterized as SAP.
+At position 65 to 140, the domain is characterized as ACT.
+At position 108 to 344, the domain is characterized as Radical SAM core.
+At position 23 to 131, the domain is characterized as PH.
+At position 141 to 176, the domain is characterized as EF-hand 1.
+At position 177 to 212, the domain is characterized as EF-hand 2.
+At position 213 to 244, the domain is characterized as EF-hand 3.
+At position 297 to 442, the domain is characterized as PI-PLC X-box.
+At position 503 to 619, the domain is characterized as PI-PLC Y-box.
+At position 619 to 746, the domain is characterized as C2.
+At position 9 to 87, the domain is characterized as Cytochrome b5 heme-binding.
+At position 77 to 147, the domain is characterized as HTH iclR-type.
+At position 505 to 675, the domain is characterized as tr-type G.
+At position 176 to 400, the domain is characterized as MIF4G.
+At position 582 to 704, the domain is characterized as MI.
+At position 116 to 176, the domain is characterized as FHA.
+At position 108 to 349, the domain is characterized as Radical SAM core.
+At position 8 to 251, the domain is characterized as AB hydrolase-1.
+At position 19 to 133, the domain is characterized as EamA 1.
+At position 150 to 269, the domain is characterized as EamA 2.
+At position 55 to 167, the domain is characterized as PA.
+At position 415 to 465, the domain is characterized as EGF-like 1.
+At position 468 to 515, the domain is characterized as EGF-like 2.
+At position 516 to 558, the domain is characterized as EGF-like 3; calcium-binding.
+At position 45 to 141, the domain is characterized as Plastocyanin-like 1.
+At position 270 to 372, the domain is characterized as Plastocyanin-like 2.
+At position 463 to 602, the domain is characterized as Plastocyanin-like 3.
+At position 17 to 133, the domain is characterized as MTTase N-terminal.
+At position 156 to 392, the domain is characterized as Radical SAM core.
+At position 395 to 461, the domain is characterized as TRAM.
+At position 80 to 325, the domain is characterized as SET.
+At position 997 to 1122, the domain is characterized as SH2.
+At position 24 to 58, the domain is characterized as EF-hand.
+At position 95 to 770, the domain is characterized as Myosin motor.
+At position 80 to 115, the domain is characterized as EF-hand 1.
+At position 116 to 151, the domain is characterized as EF-hand 2.
+At position 110 to 186, the domain is characterized as RRM.
+At position 64 to 397, the domain is characterized as Peptidase S8.
+At position 397 to 494, the domain is characterized as Zinc-hook.
+At position 321 to 373, the domain is characterized as FBD.
+At position 55 to 278, the domain is characterized as Flo11.
+At position 30 to 152, the domain is characterized as BTB.
+At position 165 to 184, the domain is characterized as UIM 1.
+At position 189 to 208, the domain is characterized as UIM 2.
+At position 13 to 58, the domain is characterized as F-box.
+At position 460 to 497, the domain is characterized as EGF-like.
+At position 709 to 769, the domain is characterized as Sushi.
+At position 768 to 821, the domain is characterized as TSP type-1.
+At position 819 to 859, the domain is characterized as LDL-receptor class A.
+At position 60 to 221, the domain is characterized as SIS.
+At position 19 to 318, the domain is characterized as Protein kinase.
+At position 8 to 236, the domain is characterized as ABC transporter.
+At position 12 to 41, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 42 to 70, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 143 to 265, the domain is characterized as FAD-binding FR-type.
+At position 1008 to 1080, the domain is characterized as Bromo.
+At position 79 to 247, the domain is characterized as TNase-like.
+At position 483 to 502, the domain is characterized as UIM 1.
+At position 519 to 538, the domain is characterized as UIM 2.
+At position 549 to 568, the domain is characterized as UIM 3.
+At position 574 to 590, the domain is characterized as UIM 4.
+At position 31 to 283, the domain is characterized as Protein kinase.
+At position 176 to 274, the domain is characterized as SWIRM.
+At position 398 to 449, the domain is characterized as SANT.
+At position 802 to 901, the domain is characterized as PH.
+At position 40 to 350, the domain is characterized as Protein kinase.
+At position 16 to 140, the domain is characterized as Toprim.
+At position 79 to 152, the domain is characterized as POTRA.
+At position 34 to 125, the domain is characterized as SH2.
+At position 84 to 120, the domain is characterized as EF-hand 2.
+At position 177 to 212, the domain is characterized as EF-hand 4.
+At position 224 to 259, the domain is characterized as EF-hand 5.
+At position 283 to 304, the domain is characterized as EF-hand 6.
+At position 172 to 347, the domain is characterized as EngA-type G 2.
+At position 201 to 395, the domain is characterized as Peptidase M12B.
+At position 7 to 206, the domain is characterized as MIF4G.
+At position 33 to 96, the domain is characterized as BTB.
+At position 29 to 301, the domain is characterized as Septin-type G.
+At position 524 to 615, the domain is characterized as WSC 1.
+At position 627 to 718, the domain is characterized as WSC 2.
+At position 128 to 225, the domain is characterized as PPIase FKBP-type.
+At position 456 to 506, the domain is characterized as DHHC.
+At position 12 to 90, the domain is characterized as GST N-terminal.
+At position 91 to 235, the domain is characterized as GST C-terminal.
+At position 1937 to 2031, the domain is characterized as Peptidase C50.
+At position 61 to 90, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 100 to 129, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 67 to 426, the domain is characterized as Peptidase A1.
+At position 4 to 115, the domain is characterized as MTTase N-terminal.
+At position 368 to 424, the domain is characterized as TRAM.
+At position 30 to 177, the domain is characterized as VHS.
+At position 314 to 333, the domain is characterized as UIM 1.
+At position 369 to 388, the domain is characterized as UIM 2.
+At position 2 to 138, the domain is characterized as N-acetyltransferase 1.
+At position 141 to 292, the domain is characterized as N-acetyltransferase 2.
+At position 36 to 138, the domain is characterized as Rhodanese 1.
+At position 164 to 270, the domain is characterized as Rhodanese 2.
+At position 304 to 425, the domain is characterized as Rhodanese 3.
+At position 22 to 113, the domain is characterized as Ig-like.
+At position 85 to 158, the domain is characterized as PAS 1.
+At position 1 to 169, the domain is characterized as Macro.
+At position 175 to 257, the domain is characterized as PPIase FKBP-type.
+At position 9 to 151, the domain is characterized as Nudix hydrolase.
+At position 194 to 390, the domain is characterized as Peptidase M12B.
+At position 398 to 479, the domain is characterized as Disintegrin.
+At position 138 to 317, the domain is characterized as CP-type G.
+At position 232 to 479, the domain is characterized as Protein kinase.
+At position 181 to 216, the domain is characterized as EF-hand.
+At position 81 to 108, the domain is characterized as Oxidoreductase-like.
+At position 22 to 240, the domain is characterized as tr-type G.
+At position 65 to 200, the domain is characterized as N-terminal Ras-GEF.
+At position 247 to 505, the domain is characterized as Ras-GEF.
+At position 613 to 700, the domain is characterized as Ras-associating.
+At position 5 to 403, the domain is characterized as BRO1.
+At position 1 to 68, the domain is characterized as BMV.
+At position 171 to 258, the domain is characterized as PPIase FKBP-type.
+At position 11 to 130, the domain is characterized as C-type lectin.
+At position 8 to 86, the domain is characterized as MIT.
+At position 163 to 244, the domain is characterized as PRC barrel.
+At position 21 to 72, the domain is characterized as HTH psq-type.
+At position 219 to 376, the domain is characterized as TrmE-type G.
+At position 6 to 231, the domain is characterized as tr-type G.
+At position 14 to 49, the domain is characterized as EF-hand.
+At position 484 to 692, the domain is characterized as Rab-GAP TBC.
+At position 298 to 542, the domain is characterized as ABC transporter 1.
+At position 619 to 834, the domain is characterized as ABC transporter 2.
+At position 126 to 304, the domain is characterized as Helicase ATP-binding.
+At position 317 to 541, the domain is characterized as Helicase C-terminal.
+At position 13 to 97, the domain is characterized as Core-binding (CB).
+At position 118 to 302, the domain is characterized as Tyr recombinase.
+At position 1 to 71, the domain is characterized as SCAN box.
+At position 330 to 395, the domain is characterized as G protein gamma.
+At position 421 to 537, the domain is characterized as RGS.
+At position 600 to 677, the domain is characterized as BRCT.
+At position 38 to 134, the domain is characterized as IGFBP N-terminal.
+At position 224 to 306, the domain is characterized as Thyroglobulin type-1.
+At position 22 to 144, the domain is characterized as FAS1 1.
+At position 166 to 310, the domain is characterized as FAS1 2.
+At position 317 to 463, the domain is characterized as FAS1 3.
+At position 467 to 616, the domain is characterized as FAS1 4.
+At position 728 to 804, the domain is characterized as Carrier.
+At position 110 to 363, the domain is characterized as ABC transporter 1.
+At position 802 to 1044, the domain is characterized as ABC transporter 2.
+At position 207 to 301, the domain is characterized as Fe2OG dioxygenase.
+At position 30 to 260, the domain is characterized as Peptidase S1.
+At position 23 to 203, the domain is characterized as Guanylate kinase-like.
+At position 96 to 317, the domain is characterized as Radical SAM core.
+At position 315 to 344, the domain is characterized as IQ.
+At position 644 to 837, the domain is characterized as SEC7.
+At position 850 to 983, the domain is characterized as PH.
+At position 122 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 313, the domain is characterized as Ig-like C2-type 3.
+At position 408 to 497, the domain is characterized as Ig-like C2-type 5.
+At position 499 to 593, the domain is characterized as Ig-like C2-type 6.
+At position 902 to 998, the domain is characterized as Fibronectin type-III 4.
+At position 162 to 656, the domain is characterized as USP.
+At position 585 to 759, the domain is characterized as PCI.
+At position 850 to 1010, the domain is characterized as UBC core.
+At position 6 to 271, the domain is characterized as Radical SAM core.
+At position 17 to 111, the domain is characterized as Ig-like V-type.
+At position 119 to 208, the domain is characterized as Ig-like C2-type.
+At position 55 to 373, the domain is characterized as USP.
+At position 309 to 424, the domain is characterized as C-type lectin.
+At position 36 to 200, the domain is characterized as Helicase ATP-binding.
+At position 235 to 439, the domain is characterized as Helicase C-terminal.
+At position 19 to 319, the domain is characterized as Protein kinase.
+At position 8 to 89, the domain is characterized as RRM.
+At position 133 to 229, the domain is characterized as BACK.
+At position 57 to 307, the domain is characterized as Protein kinase.
+At position 33 to 204, the domain is characterized as FAD-binding PCMH-type.
+At position 59 to 165, the domain is characterized as Ig-like V-type.
+At position 170 to 258, the domain is characterized as Ig-like C2-type 1.
+At position 269 to 354, the domain is characterized as Ig-like C2-type 2.
+At position 6 to 143, the domain is characterized as Toprim.
+At position 178 to 208, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 40 to 160, the domain is characterized as C-type lectin.
+At position 357 to 433, the domain is characterized as RRM.
+At position 487 to 793, the domain is characterized as Calpain catalytic.
+At position 56 to 159, the domain is characterized as FAD-binding FR-type.
+At position 160 to 353, the domain is characterized as CheB-type methylesterase.
+At position 9 to 107, the domain is characterized as Rieske.
+At position 357 to 686, the domain is characterized as PDEase.
+At position 228 to 382, the domain is characterized as TrmE-type G.
+At position 144 to 394, the domain is characterized as Radical SAM core.
+At position 108 to 500, the domain is characterized as GRAS.
+At position 92 to 214, the domain is characterized as RGS.
+At position 753 to 835, the domain is characterized as DIX.
+At position 552 to 601, the domain is characterized as bHLH.
+At position 80 to 181, the domain is characterized as Toprim.
+At position 14 to 47, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 337 to 398, the domain is characterized as S4 RNA-binding.
+At position 98 to 216, the domain is characterized as PLAT.
+At position 219 to 917, the domain is characterized as Lipoxygenase.
+At position 375 to 438, the domain is characterized as TRAM.
+At position 348 to 619, the domain is characterized as AB hydrolase-1.
+At position 481 to 744, the domain is characterized as Protein kinase.
+At position 762 to 834, the domain is characterized as U-box.
+At position 163 to 318, the domain is characterized as C-CAP/cofactor C-like.
+At position 49 to 164, the domain is characterized as DOMON.
+At position 170 to 369, the domain is characterized as Cytochrome b561.
+At position 4 to 63, the domain is characterized as AFP-like 1.
+At position 74 to 133, the domain is characterized as AFP-like 2.
+At position 557 to 618, the domain is characterized as KH.
+At position 72 to 144, the domain is characterized as J.
+At position 36 to 730, the domain is characterized as Myosin motor.
+At position 1155 to 1217, the domain is characterized as SH3.
+At position 114 to 256, the domain is characterized as PA14.
+At position 72 to 106, the domain is characterized as SAP.
+At position 126 to 302, the domain is characterized as Exonuclease.
+At position 48 to 204, the domain is characterized as PPIase cyclophilin-type.
+At position 44 to 90, the domain is characterized as Chitin-binding type-2.
+At position 1 to 130, the domain is characterized as FAS1.
+At position 30 to 66, the domain is characterized as EGF-like 1.
+At position 67 to 108, the domain is characterized as EGF-like 2; calcium-binding.
+At position 109 to 150, the domain is characterized as EGF-like 3; calcium-binding.
+At position 295 to 326, the domain is characterized as EGF-like 4.
+At position 337 to 592, the domain is characterized as ZP.
+At position 24 to 269, the domain is characterized as ABC transporter.
+At position 361 to 573, the domain is characterized as ABC transmembrane type-2.
+At position 73 to 350, the domain is characterized as Protein kinase.
+At position 1041 to 1295, the domain is characterized as Glutamine amidotransferase type-1.
+At position 64 to 163, the domain is characterized as Cadherin 1.
+At position 164 to 272, the domain is characterized as Cadherin 2.
+At position 273 to 380, the domain is characterized as Cadherin 3.
+At position 381 to 485, the domain is characterized as Cadherin 4.
+At position 486 to 595, the domain is characterized as Cadherin 5.
+At position 611 to 707, the domain is characterized as Cadherin 6.
+At position 11 to 193, the domain is characterized as CRAL-TRIO.
+At position 619 to 822, the domain is characterized as DH.
+At position 834 to 954, the domain is characterized as PH.
+At position 34 to 286, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 102 to 232, the domain is characterized as GST C-terminal.
+At position 18 to 208, the domain is characterized as RNase H type-2.
+At position 33 to 299, the domain is characterized as CN hydrolase.
+At position 265 to 372, the domain is characterized as PH.
+At position 389 to 574, the domain is characterized as Rho-GAP.
+At position 728 to 786, the domain is characterized as SH3.
+At position 129 to 159, the domain is characterized as EF-hand 3.
+At position 27 to 471, the domain is characterized as Hexokinase 1.
+At position 477 to 912, the domain is characterized as Hexokinase 2.
+At position 822 to 935, the domain is characterized as PH.
+At position 1101 to 1168, the domain is characterized as RBD.
+At position 1184 to 1273, the domain is characterized as PDZ.
+At position 1425 to 1619, the domain is characterized as DH.
+At position 48 to 167, the domain is characterized as RNase III.
+At position 38 to 108, the domain is characterized as KH type-2.
+At position 5 to 147, the domain is characterized as RNase III.
+At position 174 to 244, the domain is characterized as DRBM.
+At position 153 to 224, the domain is characterized as POTRA.
+At position 301 to 731, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1213 to 1523, the domain is characterized as PKS/mFAS DH.
+At position 1586 to 1663, the domain is characterized as Carrier.
+At position 8 to 173, the domain is characterized as N-acetyltransferase.
+At position 1 to 40, the domain is characterized as C-type lectin.
+At position 115 to 387, the domain is characterized as Dynamin-type G.
+At position 623 to 711, the domain is characterized as GED.
+At position 123 to 175, the domain is characterized as FHA.
+At position 49 to 434, the domain is characterized as Peptidase A1.
+At position 25 to 88, the domain is characterized as HMA 1.
+At position 132 to 195, the domain is characterized as HMA 2.
+At position 22 to 93, the domain is characterized as KH type-2.
+At position 4 to 100, the domain is characterized as SH2 1.
+At position 110 to 213, the domain is characterized as SH2 2.
+At position 244 to 515, the domain is characterized as Tyrosine-protein phosphatase.
+At position 393 to 427, the domain is characterized as SAP.
+At position 395 to 833, the domain is characterized as Urease.
+At position 41 to 172, the domain is characterized as Nudix hydrolase.
+At position 304 to 345, the domain is characterized as UBA.
+At position 107 to 146, the domain is characterized as LRRCT.
+At position 209 to 447, the domain is characterized as NR LBD.
+At position 154 to 315, the domain is characterized as 3'-5' exonuclease.
+At position 245 to 468, the domain is characterized as tr-type G.
+At position 39 to 172, the domain is characterized as SCP.
+At position 306 to 474, the domain is characterized as Helicase ATP-binding.
+At position 644 to 818, the domain is characterized as Helicase C-terminal.
+At position 1932 to 2266, the domain is characterized as PIPK.
+At position 32 to 244, the domain is characterized as BPL/LPL catalytic.
+At position 618 to 675, the domain is characterized as RAP.
+At position 387 to 555, the domain is characterized as GRAM 1.
+At position 438 to 530, the domain is characterized as PH.
+At position 862 to 933, the domain is characterized as GRAM 2.
+At position 574 to 855, the domain is characterized as Protein kinase.
+At position 593 to 696, the domain is characterized as tRNA-binding.
+At position 3 to 144, the domain is characterized as N-acetyltransferase.
+At position 215 to 556, the domain is characterized as PUM-HD.
+At position 14 to 168, the domain is characterized as CP-type G.
+At position 706 to 799, the domain is characterized as FDX-ACB.
+At position 52 to 232, the domain is characterized as Helicase ATP-binding.
+At position 261 to 488, the domain is characterized as Helicase C-terminal.
+At position 44 to 107, the domain is characterized as S5 DRBM.
+At position 137 to 232, the domain is characterized as PpiC.
+At position 1049 to 1302, the domain is characterized as Glutamine amidotransferase type-1.
+At position 198 to 283, the domain is characterized as KH type-2.
+At position 2 to 91, the domain is characterized as Thioredoxin.
+At position 551 to 809, the domain is characterized as Protein kinase.
+At position 73 to 320, the domain is characterized as ABC transporter 1.
+At position 412 to 622, the domain is characterized as ABC transmembrane type-2 1.
+At position 758 to 1001, the domain is characterized as ABC transporter 2.
+At position 1071 to 1286, the domain is characterized as ABC transmembrane type-2 2.
+At position 171 to 213, the domain is characterized as PAS.
+At position 333 to 385, the domain is characterized as HAMP 5.
+At position 390 to 619, the domain is characterized as Methyl-accepting transducer.
+At position 161 to 268, the domain is characterized as Cadherin 1.
+At position 269 to 383, the domain is characterized as Cadherin 2.
+At position 384 to 498, the domain is characterized as Cadherin 3.
+At position 499 to 604, the domain is characterized as Cadherin 4.
+At position 605 to 714, the domain is characterized as Cadherin 5.
+At position 416 to 673, the domain is characterized as Protein kinase 2.
+At position 40 to 118, the domain is characterized as H15.
+At position 311 to 385, the domain is characterized as POU-specific.
+At position 12 to 93, the domain is characterized as GS beta-grasp.
+At position 99 to 439, the domain is characterized as GS catalytic.
+At position 8 to 225, the domain is characterized as ThyX.
+At position 249 to 380, the domain is characterized as MPN.
+At position 6 to 317, the domain is characterized as GT23.
+At position 32 to 404, the domain is characterized as PIPK.
+At position 118 to 211, the domain is characterized as Fibronectin type-III.
+At position 248 to 311, the domain is characterized as KH.
+At position 374 to 467, the domain is characterized as HD.
+At position 91 to 366, the domain is characterized as tr-type G.
+At position 147 to 196, the domain is characterized as bHLH.
+At position 232 to 351, the domain is characterized as PAZ.
+At position 520 to 821, the domain is characterized as Piwi.
+At position 34 to 222, the domain is characterized as GH11.
+At position 255 to 290, the domain is characterized as CBM1.
+At position 63 to 372, the domain is characterized as AB hydrolase-1.
+At position 288 to 452, the domain is characterized as SUN.
+At position 305 to 587, the domain is characterized as ABC transmembrane type-1 1.
+At position 622 to 849, the domain is characterized as ABC transporter 1.
+At position 959 to 1245, the domain is characterized as ABC transmembrane type-1 2.
+At position 1282 to 1516, the domain is characterized as ABC transporter 2.
+At position 85 to 430, the domain is characterized as TTL.
+At position 182 to 558, the domain is characterized as Myotubularin phosphatase.
+At position 30 to 257, the domain is characterized as ABC transporter.
+At position 162 to 224, the domain is characterized as LIM zinc-binding.
+At position 661 to 808, the domain is characterized as bMERB.
+At position 65 to 306, the domain is characterized as Peptidase M12B.
+At position 315 to 402, the domain is characterized as Disintegrin.
+At position 3 to 82, the domain is characterized as KHA.
+At position 89 to 161, the domain is characterized as BTB.
+At position 224 to 256, the domain is characterized as Pentapeptide repeat 1.
+At position 258 to 297, the domain is characterized as Pentapeptide repeat 2.
+At position 338 to 376, the domain is characterized as Pentapeptide repeat 3.
+At position 81 to 339, the domain is characterized as Protein kinase.
+At position 382 to 417, the domain is characterized as EF-hand 1.
+At position 418 to 453, the domain is characterized as EF-hand 2.
+At position 459 to 486, the domain is characterized as EF-hand 3.
+At position 487 to 522, the domain is characterized as EF-hand 4.
+At position 294 to 368, the domain is characterized as POU-specific.
+At position 8 to 210, the domain is characterized as ABC transporter.
+At position 195 to 450, the domain is characterized as Protein kinase.
+At position 42 to 123, the domain is characterized as GOLD.
+At position 282 to 355, the domain is characterized as RRM.
+At position 126 to 405, the domain is characterized as Peptidase S8.
+At position 344 to 603, the domain is characterized as Protein kinase.
+At position 142 to 307, the domain is characterized as JmjC.
+At position 26 to 148, the domain is characterized as C2 1.
+At position 261 to 419, the domain is characterized as C2 2.
+At position 504 to 698, the domain is characterized as Ras-GAP.
+At position 762 to 860, the domain is characterized as PH.
+At position 211 to 277, the domain is characterized as KH.
+At position 116 to 188, the domain is characterized as Death.
+At position 66 to 436, the domain is characterized as AB hydrolase-1.
+At position 695 to 834, the domain is characterized as Tyrosine-protein phosphatase.
+At position 145 to 390, the domain is characterized as Radical SAM core.
+At position 393 to 461, the domain is characterized as TRAM.
+At position 191 to 423, the domain is characterized as Protein kinase.
+At position 445 to 555, the domain is characterized as PH.
+At position 472 to 575, the domain is characterized as Cadherin 4.
+At position 576 to 682, the domain is characterized as Cadherin 5.
+At position 3 to 150, the domain is characterized as UBC core.
+At position 2 to 248, the domain is characterized as Glutamine amidotransferase type-2.
+At position 12 to 147, the domain is characterized as Cyclin N-terminal.
+At position 4 to 276, the domain is characterized as YjeF C-terminal.
+At position 799 to 850, the domain is characterized as GPS.
+At position 23 to 114, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 156 to 186, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 104 to 160, the domain is characterized as EamA.
+At position 2 to 74, the domain is characterized as RRM 1.
+At position 97 to 168, the domain is characterized as RRM 2.
+At position 1005 to 1043, the domain is characterized as LRRCT.
+At position 17 to 285, the domain is characterized as Protein kinase.
+At position 25 to 145, the domain is characterized as Bulb-type lectin.
+At position 279 to 315, the domain is characterized as EGF-like; atypical.
+At position 491 to 776, the domain is characterized as Protein kinase.
+At position 18 to 74, the domain is characterized as CpcD-like.
+At position 120 to 245, the domain is characterized as FAD-binding FR-type.
+At position 186 to 292, the domain is characterized as Fe2OG dioxygenase.
+At position 42 to 227, the domain is characterized as tr-type G.
+At position 136 to 312, the domain is characterized as Helicase ATP-binding.
+At position 326 to 496, the domain is characterized as Helicase C-terminal.
+At position 343 to 953, the domain is characterized as USP.
+At position 706 to 725, the domain is characterized as UIM 1.
+At position 808 to 827, the domain is characterized as UIM 2.
+At position 830 to 849, the domain is characterized as UIM 3.
+At position 47 to 193, the domain is characterized as UBC core.
+At position 249 to 276, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 160 to 267, the domain is characterized as Cadherin 1.
+At position 268 to 382, the domain is characterized as Cadherin 2.
+At position 383 to 497, the domain is characterized as Cadherin 3.
+At position 498 to 603, the domain is characterized as Cadherin 4.
+At position 604 to 714, the domain is characterized as Cadherin 5.
+At position 75 to 121, the domain is characterized as F-box.
+At position 566 to 754, the domain is characterized as DH.
+At position 6 to 152, the domain is characterized as Jacalin-type lectin.
+At position 8 to 126, the domain is characterized as MaoC-like.
+At position 125 to 382, the domain is characterized as SMP-LTD.
+At position 41 to 123, the domain is characterized as Lipoyl-binding.
+At position 328 to 417, the domain is characterized as HTH La-type RNA-binding.
+At position 715 to 963, the domain is characterized as DDHD.
+At position 25 to 126, the domain is characterized as Phytocyanin.
+At position 174 to 225, the domain is characterized as LRRCT.
+At position 178 to 463, the domain is characterized as Protein kinase.
+At position 316 to 749, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1230 to 1539, the domain is characterized as PKS/mFAS DH.
+At position 1580 to 1658, the domain is characterized as Carrier 1.
+At position 1699 to 1776, the domain is characterized as Carrier 2.
+At position 81 to 297, the domain is characterized as RNase H type-2.
+At position 47 to 194, the domain is characterized as Tyrosine-protein phosphatase.
+At position 468 to 569, the domain is characterized as CBM20.
+At position 755 to 1043, the domain is characterized as ABC transmembrane type-1 2.
+At position 1078 to 1316, the domain is characterized as ABC transporter 2.
+At position 138 to 175, the domain is characterized as LDL-receptor class A.
+At position 876 to 934, the domain is characterized as Kazal-like 2.
+At position 149 to 439, the domain is characterized as Protein kinase.
+At position 137 to 342, the domain is characterized as ATP-grasp.
+At position 1 to 50, the domain is characterized as SAND.
+At position 374 to 534, the domain is characterized as PA14.
+At position 203 to 255, the domain is characterized as HAMP.
+At position 260 to 330, the domain is characterized as PAS.
+At position 324 to 377, the domain is characterized as PAC.
+At position 381 to 599, the domain is characterized as Histidine kinase.
+At position 67 to 108, the domain is characterized as bZIP.
+At position 3 to 137, the domain is characterized as B12-binding.
+At position 85 to 163, the domain is characterized as RRM.
+At position 2 to 82, the domain is characterized as PUA.
+At position 1 to 441, the domain is characterized as SMP-LTD.
+At position 840 to 1070, the domain is characterized as NR LBD.
+At position 83 to 158, the domain is characterized as MIT.
+At position 360 to 688, the domain is characterized as GH10.
+At position 720 to 851, the domain is characterized as CBM-cenC 1.
+At position 895 to 1040, the domain is characterized as CBM-cenC 2.
+At position 7 to 212, the domain is characterized as RNase H type-2.
+At position 193 to 385, the domain is characterized as Peptidase M12A.
+At position 380 to 420, the domain is characterized as EGF-like.
+At position 421 to 546, the domain is characterized as CUB.
+At position 547 to 596, the domain is characterized as TSP type-1.
+At position 24 to 174, the domain is characterized as NAC.
+At position 23 to 157, the domain is characterized as Ephrin RBD.
+At position 155 to 290, the domain is characterized as YTH.
+At position 303 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 26 to 76, the domain is characterized as PSI.
+At position 140 to 378, the domain is characterized as VWFA.
+At position 439 to 501, the domain is characterized as EGF-like 1.
+At position 502 to 554, the domain is characterized as EGF-like 2.
+At position 555 to 591, the domain is characterized as EGF-like 3.
+At position 592 to 635, the domain is characterized as EGF-like 4.
+At position 358 to 455, the domain is characterized as Rhodanese.
+At position 74 to 263, the domain is characterized as ABC transmembrane type-1.
+At position 228 to 365, the domain is characterized as GAF 1.
+At position 397 to 536, the domain is characterized as GAF 2.
+At position 566 to 890, the domain is characterized as PDEase.
+At position 30 to 95, the domain is characterized as Collagen-like.
+At position 99 to 238, the domain is characterized as C1q.
+At position 349 to 431, the domain is characterized as OCT.
+At position 194 to 392, the domain is characterized as Helicase ATP-binding.
+At position 403 to 565, the domain is characterized as Helicase C-terminal.
+At position 149 to 199, the domain is characterized as LRRCT.
+At position 43 to 280, the domain is characterized as Grh/CP2 DB.
+At position 10 to 369, the domain is characterized as Kinesin motor.
+At position 2 to 126, the domain is characterized as PTS EIIA type-4.
+At position 160 to 323, the domain is characterized as PTS EIIB type-4.
+At position 9 to 184, the domain is characterized as Ku.
+At position 54 to 125, the domain is characterized as KRAB.
+At position 150 to 447, the domain is characterized as NR LBD.
+At position 2 to 73, the domain is characterized as RRM.
+At position 656 to 832, the domain is characterized as PCI.
+At position 10 to 81, the domain is characterized as KRAB.
+At position 59 to 229, the domain is characterized as FAD-binding PCMH-type.
+At position 258 to 533, the domain is characterized as DDHD.
+At position 421 to 458, the domain is characterized as EGF-like.
+At position 514 to 705, the domain is characterized as VWFA.
+At position 108 to 415, the domain is characterized as SET.
+At position 51 to 101, the domain is characterized as Myosin N-terminal SH3-like.
+At position 105 to 800, the domain is characterized as Myosin motor.
+At position 803 to 832, the domain is characterized as IQ.
+At position 242 to 333, the domain is characterized as Ig-like C1-type.
+At position 130 to 217, the domain is characterized as PDZ 1.
+At position 226 to 311, the domain is characterized as PDZ 2.
+At position 379 to 465, the domain is characterized as PDZ 3.
+At position 501 to 571, the domain is characterized as SH3.
+At position 627 to 802, the domain is characterized as Guanylate kinase-like.
+At position 7 to 56, the domain is characterized as Myosin N-terminal SH3-like.
+At position 61 to 738, the domain is characterized as Myosin motor.
+At position 741 to 770, the domain is characterized as IQ 1.
+At position 764 to 793, the domain is characterized as IQ 2.
+At position 789 to 818, the domain is characterized as IQ 3.
+At position 812 to 841, the domain is characterized as IQ 4.
+At position 837 to 866, the domain is characterized as IQ 5.
+At position 860 to 889, the domain is characterized as IQ 6.
+At position 1158 to 1463, the domain is characterized as Dilute.
+At position 22 to 135, the domain is characterized as FZ.
+At position 24 to 180, the domain is characterized as UBC core.
+At position 9 to 60, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 36 to 282, the domain is characterized as ABC transporter.
+At position 162 to 342, the domain is characterized as Helicase ATP-binding.
+At position 353 to 515, the domain is characterized as Helicase C-terminal.
+At position 1060 to 1209, the domain is characterized as Exonuclease.
+At position 174 to 281, the domain is characterized as PRD 2.
+At position 66 to 434, the domain is characterized as PIPK.
+At position 411 to 633, the domain is characterized as Rab-GAP TBC.
+At position 14 to 137, the domain is characterized as MsrB.
+At position 95 to 200, the domain is characterized as FAD-binding FR-type.
+At position 1 to 49, the domain is characterized as Kazal-like.
+At position 62 to 143, the domain is characterized as GS beta-grasp.
+At position 150 to 399, the domain is characterized as GS catalytic.
+At position 718 to 1019, the domain is characterized as Protein kinase.
+At position 1020 to 1106, the domain is characterized as AGC-kinase C-terminal.
+At position 406 to 482, the domain is characterized as B5.
+At position 698 to 790, the domain is characterized as FDX-ACB.
+At position 177 to 214, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 140 to 395, the domain is characterized as Protein kinase.
+At position 396 to 466, the domain is characterized as AGC-kinase C-terminal.
+At position 552 to 706, the domain is characterized as SEC7.
+At position 5 to 92, the domain is characterized as Pyrin.
+At position 21 to 246, the domain is characterized as AMMECR1.
+At position 20 to 126, the domain is characterized as WAC.
+At position 604 to 668, the domain is characterized as DDT.
+At position 1356 to 1426, the domain is characterized as Bromo.
+At position 562 to 645, the domain is characterized as S1 motif.
+At position 167 to 267, the domain is characterized as PpiC.
+At position 126 to 397, the domain is characterized as Protein kinase.
+At position 6 to 136, the domain is characterized as Galectin.
+At position 147 to 222, the domain is characterized as Rho RNA-BD.
+At position 5 to 176, the domain is characterized as Thioredoxin.
+At position 1 to 177, the domain is characterized as FAD-binding PCMH-type.
+At position 80 to 187, the domain is characterized as Toprim.
+At position 83 to 358, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 175 to 227, the domain is characterized as bHLH.
+At position 281 to 396, the domain is characterized as PAZ.
+At position 565 to 872, the domain is characterized as Piwi.
+At position 68 to 258, the domain is characterized as Rab-GAP TBC.
+At position 97 to 340, the domain is characterized as Radical SAM core.
+At position 96 to 195, the domain is characterized as Cytochrome b5 heme-binding.
+At position 134 to 393, the domain is characterized as Olfactomedin-like.
+At position 802 to 853, the domain is characterized as GPS.
+At position 1 to 265, the domain is characterized as Protein kinase.
+At position 552 to 877, the domain is characterized as Reverse transcriptase.
+At position 200 to 460, the domain is characterized as Protein kinase.
+At position 305 to 402, the domain is characterized as CS.
+At position 72 to 220, the domain is characterized as HD.
+At position 87 to 334, the domain is characterized as PPM-type phosphatase.
+At position 99 to 320, the domain is characterized as Radical SAM core.
+At position 181 to 210, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 29 to 312, the domain is characterized as ABC transmembrane type-1.
+At position 346 to 580, the domain is characterized as ABC transporter.
+At position 272 to 378, the domain is characterized as HTH APSES-type.
+At position 705 to 788, the domain is characterized as Ubiquitin-like.
+At position 13 to 276, the domain is characterized as Protein kinase.
+At position 35 to 279, the domain is characterized as AB hydrolase-1.
+At position 75 to 150, the domain is characterized as Cytochrome b5 heme-binding.
+At position 12 to 145, the domain is characterized as UBC core.
+At position 67 to 181, the domain is characterized as Plastocyanin-like 1.
+At position 191 to 344, the domain is characterized as Plastocyanin-like 2.
+At position 425 to 568, the domain is characterized as Plastocyanin-like 3.
+At position 189 to 267, the domain is characterized as PDZ.
+At position 21 to 175, the domain is characterized as MARVEL.
+At position 659 to 846, the domain is characterized as DH.
+At position 1034 to 1336, the domain is characterized as CNH.
+At position 33 to 106, the domain is characterized as Inhibitor I9.
+At position 110 to 617, the domain is characterized as Peptidase S8.
+At position 385 to 469, the domain is characterized as PA.
+At position 1 to 35, the domain is characterized as WW.
+At position 39 to 150, the domain is characterized as PpiC.
+At position 258 to 357, the domain is characterized as CBM20.
+At position 505 to 630, the domain is characterized as DBINO.
+At position 749 to 921, the domain is characterized as Helicase ATP-binding.
+At position 1315 to 1470, the domain is characterized as Helicase C-terminal.
+At position 109 to 141, the domain is characterized as EGF-like 1.
+At position 277 to 331, the domain is characterized as TB 1.
+At position 355 to 395, the domain is characterized as EGF-like 2; calcium-binding.
+At position 403 to 455, the domain is characterized as TB 2.
+At position 574 to 615, the domain is characterized as EGF-like 3.
+At position 616 to 659, the domain is characterized as EGF-like 4; calcium-binding.
+At position 660 to 702, the domain is characterized as EGF-like 5; calcium-binding.
+At position 744 to 784, the domain is characterized as EGF-like 6; calcium-binding.
+At position 785 to 825, the domain is characterized as EGF-like 7; calcium-binding.
+At position 826 to 865, the domain is characterized as EGF-like 8; calcium-binding.
+At position 866 to 908, the domain is characterized as EGF-like 9; calcium-binding.
+At position 917 to 971, the domain is characterized as TB 3.
+At position 993 to 1035, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1036 to 1076, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1082 to 1122, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1136 to 1186, the domain is characterized as TB 4.
+At position 1254 to 1298, the domain is characterized as EGF-like 13; calcium-binding.
+At position 45 to 139, the domain is characterized as Ig-like V-type.
+At position 144 to 238, the domain is characterized as Ig-like C2-type 1.
+At position 243 to 329, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 314, the domain is characterized as PUA.
+At position 81 to 153, the domain is characterized as Bromo.
+At position 147 to 376, the domain is characterized as NR LBD.
+At position 80 to 443, the domain is characterized as Protein kinase.
+At position 444 to 493, the domain is characterized as AGC-kinase C-terminal.
+At position 60 to 203, the domain is characterized as RNase III.
+At position 218 to 294, the domain is characterized as DRBM 1.
+At position 313 to 387, the domain is characterized as DRBM 2.
+At position 2 to 130, the domain is characterized as PTS EIIA type-4.
+At position 166 to 330, the domain is characterized as PTS EIIB type-4.
+At position 282 to 317, the domain is characterized as CBS 2.
+At position 444 to 617, the domain is characterized as tr-type G.
+At position 40 to 221, the domain is characterized as Rab-GAP TBC.
+At position 330 to 442, the domain is characterized as Rhodanese.
+At position 23 to 102, the domain is characterized as Sm.
+At position 138 to 215, the domain is characterized as GRAM.
+At position 6 to 108, the domain is characterized as SSB.
+At position 7 to 176, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 85, the domain is characterized as Acylphosphatase-like.
+At position 238 to 402, the domain is characterized as SUN.
+At position 232 to 295, the domain is characterized as bZIP.
+At position 22 to 141, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 266, the domain is characterized as Ig-like C2-type 2.
+At position 279 to 388, the domain is characterized as Ig-like C2-type 3.
+At position 408 to 529, the domain is characterized as Ig-like C2-type 4.
+At position 539 to 657, the domain is characterized as Ig-like C2-type 5.
+At position 670 to 797, the domain is characterized as Ig-like C2-type 6.
+At position 806 to 941, the domain is characterized as Ig-like C2-type 7.
+At position 3 to 91, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 143 to 371, the domain is characterized as Radical SAM core.
+At position 41 to 339, the domain is characterized as AB hydrolase-1.
+At position 287 to 364, the domain is characterized as PUA.
+At position 32 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 232, the domain is characterized as Ig-like C2-type 2.
+At position 563 to 606, the domain is characterized as CUE.
+At position 92 to 249, the domain is characterized as Tyrosine-protein phosphatase.
+At position 43 to 160, the domain is characterized as FZ.
+At position 35 to 231, the domain is characterized as TLC.
+At position 539 to 624, the domain is characterized as RWP-RK.
+At position 741 to 823, the domain is characterized as PB1.
+At position 327 to 419, the domain is characterized as PH.
+At position 442 to 565, the domain is characterized as Arf-GAP.
+At position 130 to 419, the domain is characterized as ABC transmembrane type-1.
+At position 453 to 687, the domain is characterized as ABC transporter.
+At position 197 to 368, the domain is characterized as EngA-type G 2.
+At position 118 to 236, the domain is characterized as PilZ.
+At position 20 to 127, the domain is characterized as Rhodanese 1.
+At position 161 to 281, the domain is characterized as Rhodanese 2.
+At position 351 to 608, the domain is characterized as Clu.
+At position 14 to 75, the domain is characterized as S4 RNA-binding.
+At position 26 to 141, the domain is characterized as Ig-like V-type.
+At position 142 to 233, the domain is characterized as Ig-like C1-type.
+At position 40 to 161, the domain is characterized as tRNA-binding.
+At position 413 to 486, the domain is characterized as B5.
+At position 710 to 804, the domain is characterized as FDX-ACB.
+At position 32 to 49, the domain is characterized as WH2.
+At position 116 to 232, the domain is characterized as Calponin-homology (CH) 1.
+At position 260 to 365, the domain is characterized as Calponin-homology (CH) 2.
+At position 379 to 488, the domain is characterized as Calponin-homology (CH) 3.
+At position 501 to 608, the domain is characterized as Calponin-homology (CH) 4.
+At position 184 to 266, the domain is characterized as SPOR.
+At position 420 to 736, the domain is characterized as FERM.
+At position 12 to 100, the domain is characterized as RH1.
+At position 520 to 594, the domain is characterized as RH2.
+At position 385 to 448, the domain is characterized as bZIP.
+At position 295 to 329, the domain is characterized as EGF-like.
+At position 339 to 449, the domain is characterized as CUB 1.
+At position 484 to 595, the domain is characterized as CUB 2.
+At position 600 to 689, the domain is characterized as BRCT.
+At position 148 to 457, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 2 to 108, the domain is characterized as FAD-binding FR-type.
+At position 230 to 317, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 188 to 313, the domain is characterized as BAH.
+At position 345 to 876, the domain is characterized as SAM-dependent MTase C5-type.
+At position 445 to 508, the domain is characterized as Chromo.
+At position 23 to 139, the domain is characterized as Thioredoxin 1.
+At position 351 to 480, the domain is characterized as Thioredoxin 2.
+At position 238 to 378, the domain is characterized as MPN.
+At position 88 to 277, the domain is characterized as Rho-GAP.
+At position 7 to 284, the domain is characterized as tr-type G.
+At position 598 to 675, the domain is characterized as BRCT.
+At position 18 to 47, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 61 to 143, the domain is characterized as Lipoyl-binding.
+At position 684 to 859, the domain is characterized as Helicase ATP-binding.
+At position 885 to 1032, the domain is characterized as Helicase C-terminal.
+At position 1217 to 1297, the domain is characterized as HRDC.
+At position 924 to 1209, the domain is characterized as PKS/mFAS DH.
+At position 47 to 617, the domain is characterized as Lipoxygenase.
+At position 133 to 225, the domain is characterized as EH 2.
+At position 8 to 74, the domain is characterized as Ubiquitin-like.
+At position 459 to 658, the domain is characterized as MAGE 1.
+At position 706 to 897, the domain is characterized as MAGE 2.
+At position 92 to 231, the domain is characterized as GST C-terminal.
+At position 60 to 118, the domain is characterized as SH2.
+At position 9 to 101, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 118 to 408, the domain is characterized as ABC transmembrane type-1 1.
+At position 443 to 688, the domain is characterized as ABC transporter 1.
+At position 779 to 1068, the domain is characterized as ABC transmembrane type-1 2.
+At position 1103 to 1341, the domain is characterized as ABC transporter 2.
+At position 125 to 325, the domain is characterized as ATP-grasp.
+At position 21 to 98, the domain is characterized as Ubiquitin-like.
+At position 29 to 111, the domain is characterized as RRM 1.
+At position 114 to 193, the domain is characterized as RRM 2.
+At position 285 to 371, the domain is characterized as PI3K-RBD.
+At position 541 to 689, the domain is characterized as C2 PI3K-type.
+At position 704 to 880, the domain is characterized as PIK helical.
+At position 949 to 1227, the domain is characterized as PI3K/PI4K catalytic.
+At position 1260 to 1372, the domain is characterized as PX.
+At position 1381 to 1506, the domain is characterized as C2.
+At position 661 to 960, the domain is characterized as Protein kinase.
+At position 99 to 175, the domain is characterized as PRC barrel.
+At position 68 to 227, the domain is characterized as Thioredoxin.
+At position 189 to 273, the domain is characterized as PDZ.
+At position 147 to 414, the domain is characterized as NR LBD.
+At position 39 to 72, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 118 to 266, the domain is characterized as PA14.
+At position 521 to 623, the domain is characterized as SMC hinge.
+At position 134 to 203, the domain is characterized as UPAR/Ly6 1.
+At position 322 to 393, the domain is characterized as UPAR/Ly6 2.
+At position 511 to 581, the domain is characterized as UPAR/Ly6 3.
+At position 705 to 774, the domain is characterized as UPAR/Ly6 4.
+At position 46 to 157, the domain is characterized as Thioredoxin.
+At position 123 to 210, the domain is characterized as Core-binding (CB).
+At position 233 to 418, the domain is characterized as Tyr recombinase.
+At position 13 to 255, the domain is characterized as ABC transporter.
+At position 11 to 245, the domain is characterized as ABC transporter.
+At position 749 to 836, the domain is characterized as WWE.
+At position 1885 to 1992, the domain is characterized as HECT.
+At position 148 to 249, the domain is characterized as BACK.
+At position 2 to 144, the domain is characterized as N-acetyltransferase.
+At position 420 to 492, the domain is characterized as ACT-like 1.
+At position 514 to 585, the domain is characterized as ACT-like 2.
+At position 129 to 412, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 22 to 262, the domain is characterized as ABC transporter.
+At position 25 to 224, the domain is characterized as Pentraxin (PTX).
+At position 375 to 443, the domain is characterized as TRAM.
+At position 2 to 72, the domain is characterized as PAS 1.
+At position 108 to 178, the domain is characterized as PAS 2.
+At position 215 to 284, the domain is characterized as PAS 3.
+At position 542 to 805, the domain is characterized as Protein kinase.
+At position 1399 to 1463, the domain is characterized as FHA.
+At position 349 to 402, the domain is characterized as TSP type-1.
+At position 83 to 393, the domain is characterized as IF rod.
+At position 57 to 124, the domain is characterized as J.
+At position 10 to 179, the domain is characterized as TIR.
+At position 198 to 417, the domain is characterized as NB-ARC.
+At position 36 to 90, the domain is characterized as HTH myb-type.
+At position 3 to 41, the domain is characterized as Ig-like C1-type.
+At position 190 to 429, the domain is characterized as RMT2.
+At position 343 to 601, the domain is characterized as Protein kinase.
+At position 602 to 671, the domain is characterized as AGC-kinase C-terminal.
+At position 158 to 263, the domain is characterized as FAD-binding FR-type.
+At position 740 to 890, the domain is characterized as RNase NYN.
+At position 1247 to 1393, the domain is characterized as RNase H type-1.
+At position 1552 to 1724, the domain is characterized as Integrase catalytic.
+At position 49 to 233, the domain is characterized as BPL/LPL catalytic.
+At position 98 to 295, the domain is characterized as ABC transmembrane type-1.
+At position 33 to 101, the domain is characterized as BTB.
+At position 48 to 165, the domain is characterized as SEA.
+At position 189 to 419, the domain is characterized as Peptidase S1.
+At position 244 to 271, the domain is characterized as WW.
+At position 27 to 236, the domain is characterized as Saposin B-type.
+At position 3 to 76, the domain is characterized as Sm.
+At position 14 to 175, the domain is characterized as C2 PI3K-type.
+At position 272 to 447, the domain is characterized as PIK helical.
+At position 531 to 797, the domain is characterized as PI3K/PI4K catalytic.
+At position 65 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 170 to 207, the domain is characterized as UBA.
+At position 150 to 274, the domain is characterized as OTU.
+At position 624 to 691, the domain is characterized as S1 motif.
+At position 24 to 380, the domain is characterized as IF rod.
+At position 438 to 559, the domain is characterized as LTD.
+At position 126 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 31 to 89, the domain is characterized as Clip.
+At position 119 to 373, the domain is characterized as Peptidase S1.
+At position 114 to 135, the domain is characterized as LRRCT.
+At position 133 to 568, the domain is characterized as Urease.
+At position 193 to 422, the domain is characterized as Sigma-54 factor interaction.
+At position 49 to 130, the domain is characterized as PDZ 1.
+At position 157 to 235, the domain is characterized as PDZ 2.
+At position 263 to 346, the domain is characterized as PDZ 3.
+At position 394 to 475, the domain is characterized as PDZ 4.
+At position 29 to 169, the domain is characterized as Nudix hydrolase.
+At position 48 to 97, the domain is characterized as Clip.
+At position 147 to 399, the domain is characterized as Peptidase S1.
+At position 1 to 65, the domain is characterized as IBB.
+At position 32 to 141, the domain is characterized as Thioredoxin.
+At position 187 to 311, the domain is characterized as Fatty acid hydroxylase.
+At position 19 to 151, the domain is characterized as Jacalin-type lectin.
+At position 115 to 159, the domain is characterized as LysM.
+At position 1 to 42, the domain is characterized as Chitin-binding type-1.
+At position 96 to 404, the domain is characterized as IF rod.
+At position 117 to 213, the domain is characterized as Rieske.
+At position 564 to 645, the domain is characterized as BRCT.
+At position 1209 to 1552, the domain is characterized as CNH.
+At position 78 to 230, the domain is characterized as Thioredoxin.
+At position 85 to 780, the domain is characterized as Myosin motor.
+At position 8 to 200, the domain is characterized as AMMECR1.
+At position 173 to 235, the domain is characterized as t-SNARE coiled-coil homology.
+At position 26 to 325, the domain is characterized as GH10.
+At position 158 to 271, the domain is characterized as Fe2OG dioxygenase.
+At position 27 to 334, the domain is characterized as KAP NTPase.
+At position 329 to 380, the domain is characterized as Collagen-like.
+At position 827 to 1115, the domain is characterized as Protein kinase.
+At position 26 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 42 to 93, the domain is characterized as TIL.
+At position 4 to 183, the domain is characterized as KARI N-terminal Rossmann.
+At position 198 to 286, the domain is characterized as PDZ.
+At position 274 to 591, the domain is characterized as NB-ARC.
+At position 48 to 207, the domain is characterized as DH.
+At position 1 to 68, the domain is characterized as HTH gntR-type.
+At position 454 to 660, the domain is characterized as FtsK 1.
+At position 808 to 994, the domain is characterized as FtsK 2.
+At position 1080 to 1268, the domain is characterized as FtsK 3.
+At position 26 to 277, the domain is characterized as Protein kinase.
+At position 302 to 342, the domain is characterized as UBA.
+At position 25 to 68, the domain is characterized as P-type 1.
+At position 73 to 117, the domain is characterized as P-type 2.
+At position 123 to 167, the domain is characterized as P-type 3.
+At position 173 to 216, the domain is characterized as P-type 4.
+At position 243 to 345, the domain is characterized as Cadherin 3.
+At position 346 to 450, the domain is characterized as Cadherin 4.
+At position 568 to 673, the domain is characterized as Cadherin 6.
+At position 166 to 230, the domain is characterized as KH.
+At position 73 to 148, the domain is characterized as ACT.
+At position 852 to 936, the domain is characterized as PB1.
+At position 1 to 237, the domain is characterized as ABC transporter.
+At position 488 to 617, the domain is characterized as Peptidase C51.
+At position 171 to 287, the domain is characterized as THUMP.
+At position 125 to 186, the domain is characterized as v-SNARE coiled-coil homology.
+At position 23 to 86, the domain is characterized as HMA 1.
+At position 153 to 216, the domain is characterized as HMA 2.
+At position 45 to 241, the domain is characterized as tr-type G.
+At position 4 to 89, the domain is characterized as GIY-YIG.
+At position 1 to 122, the domain is characterized as CBM20.
+At position 344 to 654, the domain is characterized as GP-PDE.
+At position 22 to 386, the domain is characterized as GH18.
+At position 415 to 464, the domain is characterized as Chitin-binding type-2.
+At position 57 to 142, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 450 to 511, the domain is characterized as MIR 1.
+At position 522 to 579, the domain is characterized as MIR 2.
+At position 585 to 642, the domain is characterized as MIR 3.
+At position 101 to 268, the domain is characterized as Integrase catalytic.
+At position 274 to 420, the domain is characterized as N-acetyltransferase.
+At position 55 to 147, the domain is characterized as Glutaredoxin.
+At position 149 to 334, the domain is characterized as NodB homology.
+At position 389 to 435, the domain is characterized as LysM.
+At position 195 to 257, the domain is characterized as Chromo 1.
+At position 285 to 350, the domain is characterized as Chromo 2.
+At position 388 to 562, the domain is characterized as Helicase ATP-binding.
+At position 699 to 860, the domain is characterized as Helicase C-terminal.
+At position 68 to 577, the domain is characterized as Biotin carboxylation.
+At position 226 to 418, the domain is characterized as ATP-grasp.
+At position 704 to 778, the domain is characterized as Biotinyl-binding.
+At position 1524 to 1863, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1867 to 2181, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 47 to 155, the domain is characterized as Jacalin-type lectin.
+At position 2 to 30, the domain is characterized as LCN-type CS-alpha/beta.
+At position 150 to 391, the domain is characterized as SMP-LTD.
+At position 108 to 478, the domain is characterized as Protein kinase.
+At position 542 to 562, the domain is characterized as WH2.
+At position 10 to 136, the domain is characterized as MATH.
+At position 1555 to 1872, the domain is characterized as Protein kinase.
+At position 1873 to 1958, the domain is characterized as AGC-kinase C-terminal.
+At position 160 to 335, the domain is characterized as OBG-type G.
+At position 662 to 860, the domain is characterized as SUN.
+At position 83 to 167, the domain is characterized as Saposin B-type.
+At position 154 to 198, the domain is characterized as DSL.
+At position 199 to 232, the domain is characterized as EGF-like 1.
+At position 233 to 263, the domain is characterized as EGF-like 2.
+At position 265 to 303, the domain is characterized as EGF-like 3.
+At position 305 to 341, the domain is characterized as EGF-like 4; calcium-binding.
+At position 343 to 380, the domain is characterized as EGF-like 5.
+At position 382 to 418, the domain is characterized as EGF-like 6.
+At position 420 to 456, the domain is characterized as EGF-like 7; calcium-binding.
+At position 458 to 494, the domain is characterized as EGF-like 8.
+At position 255 to 502, the domain is characterized as ABC transporter 2.
+At position 217 to 365, the domain is characterized as TrmE-type G.
+At position 320 to 360, the domain is characterized as NAF.
+At position 43 to 221, the domain is characterized as uDENN.
+At position 46 to 168, the domain is characterized as CMP/dCMP-type deaminase.
+At position 770 to 921, the domain is characterized as HNH Cas9-type.
+At position 542 to 665, the domain is characterized as MI.
+At position 719 to 903, the domain is characterized as W2.
+At position 131 to 220, the domain is characterized as CS.
+At position 11 to 159, the domain is characterized as UBC core.
+At position 4 to 80, the domain is characterized as KRAB.
+At position 4 to 96, the domain is characterized as KRAB.
+At position 4 to 66, the domain is characterized as SH3 1.
+At position 68 to 128, the domain is characterized as SH3 2.
+At position 356 to 417, the domain is characterized as SH3 3.
+At position 108 to 309, the domain is characterized as ATP-grasp.
+At position 232 to 488, the domain is characterized as Fibrinogen C-terminal.
+At position 255 to 298, the domain is characterized as LysM 1.
+At position 336 to 379, the domain is characterized as LysM 2.
+At position 412 to 455, the domain is characterized as LysM 3.
+At position 487 to 530, the domain is characterized as LysM 4.
+At position 563 to 606, the domain is characterized as LysM 5.
+At position 621 to 664, the domain is characterized as LysM 6.
+At position 25 to 371, the domain is characterized as GH10.
+At position 28 to 126, the domain is characterized as SWIRM.
+At position 23 to 112, the domain is characterized as CFEM.
+At position 3 to 255, the domain is characterized as Pyruvate carboxyltransferase.
+At position 20 to 129, the domain is characterized as Cystatin fetuin-A-type 1.
+At position 140 to 253, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 22 to 191, the domain is characterized as EngB-type G.
+At position 35 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 145 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 328 to 401, the domain is characterized as Ig-like C2-type 4.
+At position 499 to 591, the domain is characterized as Ig-like C2-type 6.
+At position 1 to 33, the domain is characterized as Ferritin-like diiron.
+At position 1543 to 1619, the domain is characterized as RRM.
+At position 31 to 82, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 97 to 132, the domain is characterized as EF-hand 1.
+At position 136 to 171, the domain is characterized as EF-hand 2.
+At position 232 to 267, the domain is characterized as EF-hand 4.
+At position 277 to 312, the domain is characterized as EF-hand 5.
+At position 313 to 348, the domain is characterized as EF-hand 6.
+At position 14 to 111, the domain is characterized as Chorein N-terminal.
+At position 190 to 241, the domain is characterized as bHLH.
+At position 399 to 833, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1323 to 1634, the domain is characterized as PKS/mFAS DH.
+At position 1715 to 1789, the domain is characterized as Carrier.
+At position 350 to 429, the domain is characterized as KH-like.
+At position 7 to 107, the domain is characterized as Glutaredoxin.
+At position 30 to 145, the domain is characterized as Ig-like V-type.
+At position 148 to 248, the domain is characterized as Ig-like C1-type 1.
+At position 255 to 348, the domain is characterized as Ig-like C1-type 2.
+At position 58 to 241, the domain is characterized as CNNM transmembrane.
+At position 260 to 321, the domain is characterized as CBS 1.
+At position 322 to 387, the domain is characterized as CBS 2.
+At position 9 to 66, the domain is characterized as HTH myb-type 1.
+At position 18 to 207, the domain is characterized as Glutamine amidotransferase type-1.
+At position 208 to 405, the domain is characterized as GMPS ATP-PPase.
+At position 47 to 229, the domain is characterized as Helicase ATP-binding.
+At position 242 to 474, the domain is characterized as Helicase C-terminal.
+At position 9 to 481, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 508 to 798, the domain is characterized as UvrD-like helicase C-terminal.
+At position 14 to 55, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 57 to 99, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 31 to 275, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 2 to 53, the domain is characterized as Myosin N-terminal SH3-like.
+At position 57 to 771, the domain is characterized as Myosin motor.
+At position 813 to 842, the domain is characterized as IQ.
+At position 4 to 142, the domain is characterized as RNase III 1.
+At position 307 to 382, the domain is characterized as DRBM 1.
+At position 415 to 551, the domain is characterized as RNase III 2.
+At position 566 to 645, the domain is characterized as DRBM 2.
+At position 837 to 912, the domain is characterized as DRBM 3.
+At position 38 to 148, the domain is characterized as MTTase N-terminal.
+At position 166 to 403, the domain is characterized as Radical SAM core.
+At position 406 to 472, the domain is characterized as TRAM.
+At position 344 to 421, the domain is characterized as Death.
+At position 598 to 681, the domain is characterized as BRCT.
+At position 52 to 84, the domain is characterized as C2.
+At position 289 to 352, the domain is characterized as bZIP.
+At position 310 to 364, the domain is characterized as MIR 1.
+At position 374 to 433, the domain is characterized as MIR 2.
+At position 48 to 188, the domain is characterized as BAH.
+At position 35 to 267, the domain is characterized as ABC transmembrane type-2.
+At position 269 to 449, the domain is characterized as B30.2/SPRY.
+At position 79 to 276, the domain is characterized as Pentraxin (PTX).
+At position 507 to 556, the domain is characterized as GPS.
+At position 10 to 118, the domain is characterized as Glutamine amidotransferase type-1.
+At position 119 to 304, the domain is characterized as GMPS ATP-PPase.
+At position 586 to 767, the domain is characterized as SSD.
+At position 395 to 445, the domain is characterized as DHHC.
+At position 37 to 257, the domain is characterized as VWFA.
+At position 227 to 260, the domain is characterized as WW 1.
+At position 331 to 364, the domain is characterized as WW 2.
+At position 391 to 424, the domain is characterized as WW 3.
+At position 480 to 813, the domain is characterized as HECT.
+At position 233 to 296, the domain is characterized as KH.
+At position 359 to 452, the domain is characterized as HD.
+At position 377 to 429, the domain is characterized as bHLH.
+At position 580 to 638, the domain is characterized as PASTA.
+At position 54 to 121, the domain is characterized as CSD.
+At position 167 to 217, the domain is characterized as GRAM 1.
+At position 218 to 315, the domain is characterized as PH.
+At position 568 to 634, the domain is characterized as GRAM 2.
+At position 126 to 431, the domain is characterized as Protein kinase.
+At position 432 to 505, the domain is characterized as AGC-kinase C-terminal.
+At position 628 to 698, the domain is characterized as Bromo.
+At position 1305 to 1378, the domain is characterized as PWWP.
+At position 104 to 308, the domain is characterized as ATP-grasp.
+At position 219 to 369, the domain is characterized as TrmE-type G.
+At position 388 to 422, the domain is characterized as EGF-like.
+At position 4 to 71, the domain is characterized as SAM.
+At position 40 to 72, the domain is characterized as EF-hand 2.
+At position 372 to 655, the domain is characterized as Histidine kinase.
+At position 818 to 965, the domain is characterized as Response regulatory.
+At position 40 to 258, the domain is characterized as Radical SAM core.
+At position 124 to 474, the domain is characterized as PTS EIIC type-1.
+At position 22 to 54, the domain is characterized as LisH.
+At position 60 to 117, the domain is characterized as CTLH.
+At position 421 to 509, the domain is characterized as PI3K-RBD.
+At position 682 to 841, the domain is characterized as C2 PI3K-type.
+At position 861 to 1037, the domain is characterized as PIK helical.
+At position 1105 to 1383, the domain is characterized as PI3K/PI4K catalytic.
+At position 1422 to 1538, the domain is characterized as PX.
+At position 1555 to 1678, the domain is characterized as C2.
+At position 485 to 657, the domain is characterized as SSD.
+At position 967 to 1133, the domain is characterized as PNPLA.
+At position 108 to 176, the domain is characterized as BTB.
+At position 220 to 330, the domain is characterized as Fe2OG dioxygenase.
+At position 26 to 113, the domain is characterized as Ig-like C1-type.
+At position 4 to 281, the domain is characterized as DegV.
+At position 19 to 259, the domain is characterized as ABC transporter.
+At position 269 to 327, the domain is characterized as COS.
+At position 216 to 309, the domain is characterized as PH.
+At position 487 to 622, the domain is characterized as DAGKc.
+At position 691 to 777, the domain is characterized as BRCT.
+At position 63 to 184, the domain is characterized as FAD-binding FR-type.
+At position 457 to 542, the domain is characterized as Ig-like C2-type.
+At position 561 to 599, the domain is characterized as EGF-like.
+At position 66 to 136, the domain is characterized as BTB.
+At position 342 to 614, the domain is characterized as Protein kinase.
+At position 281 to 326, the domain is characterized as PDZ.
+At position 78 to 293, the domain is characterized as RNase H type-2.
+At position 10 to 232, the domain is characterized as BAR.
+At position 279 to 345, the domain is characterized as SH3.
+At position 52 to 117, the domain is characterized as NAC-A/B.
+At position 175 to 214, the domain is characterized as UBA.
+At position 57 to 240, the domain is characterized as CNNM transmembrane.
+At position 259 to 320, the domain is characterized as CBS 1.
+At position 321 to 386, the domain is characterized as CBS 2.
+At position 320 to 595, the domain is characterized as ABC transmembrane type-1 1.
+At position 629 to 852, the domain is characterized as ABC transporter 1.
+At position 950 to 1220, the domain is characterized as ABC transmembrane type-1 2.
+At position 1267 to 1501, the domain is characterized as ABC transporter 2.
+At position 684 to 879, the domain is characterized as DH.
+At position 895 to 1001, the domain is characterized as PH.
+At position 1507 to 1651, the domain is characterized as VPS9.
+At position 55 to 271, the domain is characterized as Radical SAM core.
+At position 32 to 156, the domain is characterized as Ig-like V-type.
+At position 162 to 256, the domain is characterized as Ig-like C2-type 1.
+At position 1200 to 1375, the domain is characterized as Helicase ATP-binding.
+At position 1401 to 1559, the domain is characterized as Helicase C-terminal.
+At position 19 to 213, the domain is characterized as RNase H type-2.
+At position 227 to 630, the domain is characterized as PPM-type phosphatase.
+At position 245 to 447, the domain is characterized as GATase cobBQ-type.
+At position 94 to 227, the domain is characterized as Nudix hydrolase.
+At position 24 to 158, the domain is characterized as C-type lectin.
+At position 258 to 340, the domain is characterized as Toprim.
+At position 17 to 107, the domain is characterized as HPt.
+At position 227 to 453, the domain is characterized as Lon N-terminal.
+At position 452 to 561, the domain is characterized as CULT.
+At position 292 to 531, the domain is characterized as Glutamine amidotransferase type-1.
+At position 36 to 276, the domain is characterized as Helicase ATP-binding.
+At position 440 to 606, the domain is characterized as Helicase C-terminal.
+At position 37 to 169, the domain is characterized as Nudix hydrolase.
+At position 145 to 191, the domain is characterized as G-patch.
+At position 168 to 322, the domain is characterized as YDG.
+At position 448 to 620, the domain is characterized as tr-type G.
+At position 930 to 1056, the domain is characterized as MGS-like.
+At position 230 to 280, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 286 to 336, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 43 to 353, the domain is characterized as AB hydrolase-1.
+At position 10 to 438, the domain is characterized as Kinesin motor.
+At position 217 to 381, the domain is characterized as PCI.
+At position 123 to 191, the domain is characterized as COMM.
+At position 511 to 708, the domain is characterized as VWFA 1.
+At position 959 to 1131, the domain is characterized as VWFA 2.
+At position 143 to 198, the domain is characterized as BRX 1.
+At position 319 to 374, the domain is characterized as BRX 2.
+At position 19 to 308, the domain is characterized as ABC transmembrane type-1.
+At position 338 to 574, the domain is characterized as ABC transporter.
+At position 172 to 480, the domain is characterized as USP.
+At position 3 to 278, the domain is characterized as DegV.
+At position 52 to 153, the domain is characterized as THUMP.
+At position 28 to 511, the domain is characterized as Sema.
+At position 571 to 655, the domain is characterized as Ig-like C2-type.
+At position 84 to 183, the domain is characterized as Toprim.
+At position 12 to 265, the domain is characterized as Pyruvate carboxyltransferase.
+At position 10 to 467, the domain is characterized as ADPK.
+At position 12 to 179, the domain is characterized as Reelin.
+At position 217 to 330, the domain is characterized as DOMON.
+At position 334 to 533, the domain is characterized as Cytochrome b561.
+At position 78 to 158, the domain is characterized as RRM.
+At position 42 to 298, the domain is characterized as Protein kinase.
+At position 17 to 212, the domain is characterized as Glutamine amidotransferase type-1.
+At position 213 to 416, the domain is characterized as GMPS ATP-PPase.
+At position 220 to 384, the domain is characterized as JmjC.
+At position 974 to 1187, the domain is characterized as FtsK.
+At position 10 to 289, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 290 to 570, the domain is characterized as UvrD-like helicase C-terminal.
+At position 376 to 577, the domain is characterized as MIF4G.
+At position 1105 to 1123, the domain is characterized as WH2.
+At position 10 to 105, the domain is characterized as J.
+At position 126 to 193, the domain is characterized as DPH-type MB.
+At position 224 to 417, the domain is characterized as B30.2/SPRY.
+At position 1053 to 1145, the domain is characterized as ELM2.
+At position 1160 to 1211, the domain is characterized as SANT.
+At position 56 to 359, the domain is characterized as PPM-type phosphatase.
+At position 116 to 311, the domain is characterized as Peptidase M12A.
+At position 306 to 346, the domain is characterized as EGF-like.
+At position 356 to 471, the domain is characterized as CUB.
+At position 138 to 170, the domain is characterized as EF-hand 3.
+At position 196 to 354, the domain is characterized as Cupin type-1 1.
+At position 406 to 567, the domain is characterized as Cupin type-1 2.
+At position 300 to 574, the domain is characterized as ABC transporter 1.
+At position 594 to 912, the domain is characterized as ABC transporter 2.
+At position 1254 to 1474, the domain is characterized as ABC transporter 3.
+At position 19 to 105, the domain is characterized as PAN.
+At position 292 to 370, the domain is characterized as Kringle 3.
+At position 379 to 457, the domain is characterized as Kringle 4.
+At position 489 to 714, the domain is characterized as Peptidase S1.
+At position 9 to 234, the domain is characterized as ATP-grasp.
+At position 167 to 223, the domain is characterized as BTB 1.
+At position 306 to 373, the domain is characterized as BTB 2.
+At position 17 to 91, the domain is characterized as S1-like.
+At position 651 to 764, the domain is characterized as FAD-binding FR-type.
+At position 15 to 239, the domain is characterized as BAR.
+At position 103 to 181, the domain is characterized as RRM.
+At position 9 to 350, the domain is characterized as YjeF C-terminal.
+At position 141 to 264, the domain is characterized as Nudix hydrolase.
+At position 703 to 786, the domain is characterized as PB1.
+At position 290 to 340, the domain is characterized as bHLH.
+At position 6 to 414, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 34 to 64, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 78 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 169, the domain is characterized as Brix.
+At position 422 to 904, the domain is characterized as Protein kinase.
+At position 30 to 389, the domain is characterized as GH18.
+At position 5 to 352, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 357 to 686, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 9 to 129, the domain is characterized as CMP/dCMP-type deaminase.
+At position 102 to 291, the domain is characterized as ABC transmembrane type-1.
+At position 388 to 476, the domain is characterized as PDZ 2.
+At position 40 to 326, the domain is characterized as GH18.
+At position 180 to 278, the domain is characterized as ELM2.
+At position 102 to 175, the domain is characterized as PRC barrel.
+At position 85 to 243, the domain is characterized as PPIase cyclophilin-type.
+At position 1 to 61, the domain is characterized as Disintegrin.
+At position 30 to 223, the domain is characterized as BPL/LPL catalytic.
+At position 25 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 244, the domain is characterized as Ig-like C2-type 2.
+At position 255 to 343, the domain is characterized as Ig-like C2-type 3.
+At position 352 to 442, the domain is characterized as Ig-like C2-type 4.
+At position 453 to 583, the domain is characterized as Ig-like C2-type 5.
+At position 583 to 690, the domain is characterized as Ig-like C2-type 6.
+At position 699 to 785, the domain is characterized as Ig-like C2-type 7.
+At position 866 to 1181, the domain is characterized as Protein kinase.
+At position 294 to 378, the domain is characterized as RCK C-terminal.
+At position 482 to 574, the domain is characterized as PH 1.
+At position 587 to 679, the domain is characterized as PH 2.
+At position 676 to 811, the domain is characterized as Arf-GAP.
+At position 878 to 1003, the domain is characterized as PH 3.
+At position 1014 to 1114, the domain is characterized as PH 4.
+At position 1116 to 1297, the domain is characterized as Rho-GAP.
+At position 1326 to 1420, the domain is characterized as Ras-associating.
+At position 1434 to 1537, the domain is characterized as PH 5.
+At position 756 to 838, the domain is characterized as DIX.
+At position 2 to 164, the domain is characterized as PPIase cyclophilin-type.
+At position 218 to 372, the domain is characterized as TrmE-type G.
+At position 21 to 78, the domain is characterized as Chitin-binding type-2 1.
+At position 125 to 182, the domain is characterized as Chitin-binding type-2 2.
+At position 217 to 274, the domain is characterized as Chitin-binding type-2 3.
+At position 279 to 334, the domain is characterized as Chitin-binding type-2 4.
+At position 367 to 423, the domain is characterized as Chitin-binding type-2 5.
+At position 436 to 491, the domain is characterized as Chitin-binding type-2 6.
+At position 150 to 337, the domain is characterized as Helicase ATP-binding.
+At position 368 to 554, the domain is characterized as Helicase C-terminal.
+At position 6 to 67, the domain is characterized as LIM zinc-binding 1.
+At position 68 to 129, the domain is characterized as LIM zinc-binding 2.
+At position 216 to 546, the domain is characterized as Protein kinase.
+At position 236 to 291, the domain is characterized as DEK-C.
+At position 295 to 436, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 120, the domain is characterized as Jacalin-type lectin.
+At position 10 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 36 to 76, the domain is characterized as Anaphylatoxin-like 1.
+At position 77 to 111, the domain is characterized as Anaphylatoxin-like 2.
+At position 112 to 144, the domain is characterized as Anaphylatoxin-like 3.
+At position 176 to 215, the domain is characterized as EGF-like 1.
+At position 216 to 261, the domain is characterized as EGF-like 2; calcium-binding.
+At position 262 to 307, the domain is characterized as EGF-like 3; calcium-binding.
+At position 308 to 355, the domain is characterized as EGF-like 4; calcium-binding.
+At position 356 to 398, the domain is characterized as EGF-like 5; calcium-binding.
+At position 399 to 440, the domain is characterized as EGF-like 6; calcium-binding.
+At position 441 to 480, the domain is characterized as EGF-like 7; calcium-binding.
+At position 481 to 524, the domain is characterized as EGF-like 8; calcium-binding.
+At position 525 to 578, the domain is characterized as EGF-like 9; calcium-binding.
+At position 196 to 394, the domain is characterized as HIN-200.
+At position 504 to 814, the domain is characterized as Pterin-binding.
+At position 31 to 324, the domain is characterized as ABC transmembrane type-1.
+At position 356 to 592, the domain is characterized as ABC transporter.
+At position 244 to 544, the domain is characterized as Protein kinase.
+At position 163 to 212, the domain is characterized as bHLH.
+At position 14 to 81, the domain is characterized as POTRA 1.
+At position 82 to 159, the domain is characterized as POTRA 2.
+At position 162 to 248, the domain is characterized as POTRA 3.
+At position 251 to 329, the domain is characterized as POTRA 4.
+At position 332 to 404, the domain is characterized as POTRA 5.
+At position 356 to 420, the domain is characterized as S4 RNA-binding.
+At position 634 to 691, the domain is characterized as RAP.
+At position 56 to 120, the domain is characterized as Inhibitor I9.
+At position 122 to 623, the domain is characterized as Peptidase S8.
+At position 379 to 472, the domain is characterized as PA.
+At position 314 to 349, the domain is characterized as DMA.
+At position 460 to 659, the domain is characterized as FtsK.
+At position 53 to 110, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 1 to 140, the domain is characterized as HTH marR-type.
+At position 153 to 303, the domain is characterized as N-acetyltransferase.
+At position 903 to 1016, the domain is characterized as PH.
+At position 1103 to 1295, the domain is characterized as Rho-GAP.
+At position 24 to 206, the domain is characterized as FAD-binding PCMH-type.
+At position 5 to 268, the domain is characterized as YEATS.
+At position 299 to 519, the domain is characterized as BAR.
+At position 658 to 739, the domain is characterized as RRM 3; atypical.
+At position 148 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 452, the domain is characterized as TRAM.
+At position 605 to 640, the domain is characterized as EF-hand 1.
+At position 641 to 676, the domain is characterized as EF-hand 2.
+At position 3 to 92, the domain is characterized as PE.
+At position 12 to 41, the domain is characterized as IQ 1.
+At position 68 to 97, the domain is characterized as IQ 2.
+At position 131 to 272, the domain is characterized as MPN.
+At position 382 to 815, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1303 to 1616, the domain is characterized as PKS/mFAS DH.
+At position 1679 to 1756, the domain is characterized as Carrier 1.
+At position 1783 to 1865, the domain is characterized as Carrier 2.
+At position 3 to 138, the domain is characterized as Jacalin-type lectin 1.
+At position 144 to 264, the domain is characterized as Jacalin-type lectin 2.
+At position 270 to 392, the domain is characterized as Jacalin-type lectin 3.
+At position 80 to 197, the domain is characterized as HD.
+At position 108 to 444, the domain is characterized as GS catalytic.
+At position 80 to 273, the domain is characterized as Peptidase M12A.
+At position 348 to 382, the domain is characterized as ShKT.
+At position 727 to 809, the domain is characterized as SUEL-type lectin.
+At position 158 to 368, the domain is characterized as CP-type G.
+At position 103 to 314, the domain is characterized as Radical SAM core.
+At position 457 to 522, the domain is characterized as SAM 1.
+At position 535 to 599, the domain is characterized as SAM 2.
+At position 623 to 686, the domain is characterized as SAM 3.
+At position 225 to 301, the domain is characterized as Ubiquitin-like.
+At position 1 to 117, the domain is characterized as Ig-like.
+At position 201 to 254, the domain is characterized as HAMP.
+At position 259 to 495, the domain is characterized as Methyl-accepting transducer.
+At position 195 to 387, the domain is characterized as GMPS ATP-PPase.
+At position 165 to 271, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 8, the domain is characterized as SoHo.
+At position 22 to 35, the domain is characterized as SH3.
+At position 7 to 71, the domain is characterized as Histone-fold.
+At position 118 to 317, the domain is characterized as ATP-grasp.
+At position 81 to 127, the domain is characterized as F-box.
+At position 75 to 383, the domain is characterized as Peptidase A1.
+At position 13 to 179, the domain is characterized as FAD-binding PCMH-type.
+At position 530 to 594, the domain is characterized as R3H.
+At position 662 to 705, the domain is characterized as G-patch.
+At position 214 to 366, the domain is characterized as TrmE-type G.
+At position 683 to 968, the domain is characterized as Protein kinase.
+At position 109 to 198, the domain is characterized as Cytochrome c 1.
+At position 206 to 287, the domain is characterized as Cytochrome c 2.
+At position 3 to 163, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 14 to 121, the domain is characterized as SAND.
+At position 9 to 126, the domain is characterized as C2 B9-type.
+At position 332 to 490, the domain is characterized as N-acetyltransferase.
+At position 69 to 379, the domain is characterized as Protein kinase.
+At position 256 to 547, the domain is characterized as ABC transmembrane type-1.
+At position 581 to 815, the domain is characterized as ABC transporter.
+At position 208 to 258, the domain is characterized as bHLH.
+At position 46 to 354, the domain is characterized as Cbl-PTB.
+At position 18 to 119, the domain is characterized as Rhodanese.
+At position 229 to 463, the domain is characterized as BEACH.
+At position 706 to 753, the domain is characterized as GPS.
+At position 435 to 462, the domain is characterized as PLD phosphodiesterase 1.
+At position 704 to 731, the domain is characterized as PLD phosphodiesterase 2.
+At position 960 to 1022, the domain is characterized as PWWP 2.
+At position 1093 to 1143, the domain is characterized as AWS.
+At position 1145 to 1262, the domain is characterized as SET.
+At position 1269 to 1285, the domain is characterized as Post-SET.
+At position 538 to 826, the domain is characterized as Protein kinase.
+At position 897 to 1027, the domain is characterized as Guanylate cyclase.
+At position 3 to 94, the domain is characterized as HIG1.
+At position 26 to 313, the domain is characterized as FAE.
+At position 41 to 105, the domain is characterized as BTB.
+At position 217 to 469, the domain is characterized as NPH3.
+At position 102 to 341, the domain is characterized as Radical SAM core.
+At position 391 to 519, the domain is characterized as Guanylate cyclase.
+At position 27 to 200, the domain is characterized as CP-type G.
+At position 2103 to 2234, the domain is characterized as MPN.
+At position 265 to 425, the domain is characterized as SUN.
+At position 156 to 310, the domain is characterized as Plastocyanin-like 2.
+At position 419 to 561, the domain is characterized as Plastocyanin-like 3.
+At position 9 to 173, the domain is characterized as TIR 1.
+At position 187 to 418, the domain is characterized as NB-ARC 1.
+At position 488 to 585, the domain is characterized as ALOG.
+At position 574 to 737, the domain is characterized as TIR 2.
+At position 755 to 987, the domain is characterized as NB-ARC 2.
+At position 265 to 654, the domain is characterized as GRAS.
+At position 355 to 421, the domain is characterized as PASTA 1.
+At position 422 to 489, the domain is characterized as PASTA 2.
+At position 490 to 556, the domain is characterized as PASTA 3.
+At position 557 to 625, the domain is characterized as PASTA 4.
+At position 160 to 271, the domain is characterized as STAS.
+At position 86 to 218, the domain is characterized as GST C-terminal.
+At position 16 to 38, the domain is characterized as OCA.
+At position 93 to 128, the domain is characterized as EGF-like 1.
+At position 130 to 161, the domain is characterized as EGF-like 2.
+At position 163 to 195, the domain is characterized as EGF-like 3.
+At position 208 to 243, the domain is characterized as EGF-like 4.
+At position 245 to 280, the domain is characterized as EGF-like 5.
+At position 282 to 315, the domain is characterized as EGF-like 6.
+At position 185 to 322, the domain is characterized as OTU.
+At position 71 to 348, the domain is characterized as Protein kinase.
+At position 123 to 175, the domain is characterized as HTH cro/C1-type.
+At position 96 to 131, the domain is characterized as Tify.
+At position 8 to 100, the domain is characterized as Acylphosphatase-like.
+At position 90 to 275, the domain is characterized as Helicase ATP-binding.
+At position 288 to 543, the domain is characterized as Helicase C-terminal.
+At position 308 to 796, the domain is characterized as USP.
+At position 613 to 654, the domain is characterized as UBA 1.
+At position 670 to 710, the domain is characterized as UBA 2.
+At position 42 to 510, the domain is characterized as Sema.
+At position 512 to 563, the domain is characterized as PSI.
+At position 580 to 635, the domain is characterized as Ig-like C2-type.
+At position 256 to 315, the domain is characterized as OVATE.
+At position 164 to 257, the domain is characterized as PAZ.
+At position 426 to 699, the domain is characterized as Piwi.
+At position 31 to 138, the domain is characterized as WH1.
+At position 200 to 213, the domain is characterized as CRIB.
+At position 401 to 418, the domain is characterized as WH2 1.
+At position 429 to 446, the domain is characterized as WH2 2.
+At position 243 to 303, the domain is characterized as HTH myb-type.
+At position 216 to 339, the domain is characterized as MsrB.
+At position 98 to 277, the domain is characterized as FAD-binding PCMH-type.
+At position 402 to 525, the domain is characterized as CMP/dCMP-type deaminase.
+At position 373 to 808, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1297 to 1606, the domain is characterized as PKS/mFAS DH.
+At position 1660 to 1738, the domain is characterized as Carrier.
+At position 80 to 134, the domain is characterized as Kazal-like.
+At position 173 to 208, the domain is characterized as EF-hand 1.
+At position 225 to 247, the domain is characterized as EF-hand 2.
+At position 250 to 336, the domain is characterized as Ig-like 1.
+At position 340 to 425, the domain is characterized as Ig-like 2.
+At position 4 to 148, the domain is characterized as Clp R.
+At position 83 to 137, the domain is characterized as bHLH.
+At position 8 to 158, the domain is characterized as PPIase cyclophilin-type.
+At position 164 to 274, the domain is characterized as Ig-like.
+At position 99 to 150, the domain is characterized as bHLH.
+At position 117 to 289, the domain is characterized as 3'-5' exonuclease.
+At position 210 to 420, the domain is characterized as B30.2/SPRY.
+At position 20 to 462, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 958 to 1269, the domain is characterized as PKS/mFAS DH.
+At position 2273 to 2347, the domain is characterized as Carrier.
+At position 176 to 230, the domain is characterized as HAMP.
+At position 238 to 450, the domain is characterized as Histidine kinase.
+At position 61 to 113, the domain is characterized as bHLH.
+At position 155 to 311, the domain is characterized as TRUD.
+At position 2 to 296, the domain is characterized as FERM.
+At position 145 to 296, the domain is characterized as Exonuclease.
+At position 331 to 410, the domain is characterized as RRM 1.
+At position 469 to 549, the domain is characterized as RRM 2.
+At position 608 to 688, the domain is characterized as RRM 3.
+At position 28 to 248, the domain is characterized as GH16.
+At position 267 to 334, the domain is characterized as Dockerin.
+At position 79 to 143, the domain is characterized as Myb-like.
+At position 6 to 99, the domain is characterized as Ig-like 1.
+At position 116 to 206, the domain is characterized as Ig-like 2.
+At position 219 to 321, the domain is characterized as Ig-like 3.
+At position 40 to 118, the domain is characterized as Sm.
+At position 28 to 114, the domain is characterized as Thioredoxin.
+At position 66 to 313, the domain is characterized as Dynamin-type G.
+At position 68 to 248, the domain is characterized as FAD-binding PCMH-type.
+At position 266 to 449, the domain is characterized as ATP-grasp.
+At position 79 to 378, the domain is characterized as Calpain catalytic.
+At position 610 to 636, the domain is characterized as EF-hand 1.
+At position 640 to 675, the domain is characterized as EF-hand 2.
+At position 69 to 287, the domain is characterized as Radical SAM core.
+At position 68 to 250, the domain is characterized as IRG-type G.
+At position 595 to 676, the domain is characterized as RWP-RK.
+At position 811 to 894, the domain is characterized as PB1.
+At position 168 to 192, the domain is characterized as HhH.
+At position 58 to 141, the domain is characterized as RRM 1.
+At position 150 to 230, the domain is characterized as RRM 2.
+At position 451 to 529, the domain is characterized as RRM 3.
+At position 63 to 733, the domain is characterized as Myosin motor.
+At position 736 to 758, the domain is characterized as IQ 1.
+At position 759 to 788, the domain is characterized as IQ 2.
+At position 805 to 827, the domain is characterized as IQ 3.
+At position 828 to 857, the domain is characterized as IQ 4.
+At position 1008 to 1245, the domain is characterized as MyTH4 1.
+At position 1250 to 1560, the domain is characterized as FERM 1.
+At position 1558 to 1627, the domain is characterized as SH3.
+At position 1701 to 1849, the domain is characterized as MyTH4 2.
+At position 1855 to 2158, the domain is characterized as FERM 2.
+At position 30 to 224, the domain is characterized as Lon N-terminal.
+At position 54 to 359, the domain is characterized as AB hydrolase-1.
+At position 28 to 168, the domain is characterized as Nudix hydrolase.
+At position 201 to 259, the domain is characterized as CTLH.
+At position 147 to 314, the domain is characterized as Helicase ATP-binding.
+At position 325 to 493, the domain is characterized as Helicase C-terminal.
+At position 78 to 150, the domain is characterized as PUB.
+At position 31 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 81 to 163, the domain is characterized as SAND.
+At position 60 to 114, the domain is characterized as TCP.
+At position 29 to 210, the domain is characterized as Rab-GAP TBC.
+At position 318 to 426, the domain is characterized as Rhodanese.
+At position 521 to 584, the domain is characterized as bZIP.
+At position 210 to 307, the domain is characterized as bHLH.
+At position 21 to 81, the domain is characterized as SLH.
+At position 51 to 275, the domain is characterized as Radical SAM core.
+At position 412 to 458, the domain is characterized as F-box.
+At position 343 to 510, the domain is characterized as tr-type G.
+At position 400 to 693, the domain is characterized as Protein kinase.
+At position 9 to 404, the domain is characterized as PUM-HD.
+At position 4 to 144, the domain is characterized as PTS EIIA type-2.
+At position 78 to 222, the domain is characterized as Clp R.
+At position 77 to 262, the domain is characterized as TNase-like.
+At position 66 to 229, the domain is characterized as Laminin G-like.
+At position 425 to 478, the domain is characterized as Collagen-like 1.
+At position 493 to 552, the domain is characterized as Collagen-like 2.
+At position 556 to 615, the domain is characterized as Collagen-like 3.
+At position 622 to 681, the domain is characterized as Collagen-like 4.
+At position 685 to 744, the domain is characterized as Collagen-like 5.
+At position 748 to 807, the domain is characterized as Collagen-like 6.
+At position 811 to 870, the domain is characterized as Collagen-like 7.
+At position 892 to 951, the domain is characterized as Collagen-like 8.
+At position 952 to 1011, the domain is characterized as Collagen-like 9.
+At position 1024 to 1083, the domain is characterized as Collagen-like 10.
+At position 1084 to 1137, the domain is characterized as Collagen-like 11.
+At position 1139 to 1198, the domain is characterized as Collagen-like 12.
+At position 1199 to 1258, the domain is characterized as Collagen-like 13.
+At position 1268 to 1327, the domain is characterized as Collagen-like 14.
+At position 1361 to 1420, the domain is characterized as Collagen-like 15.
+At position 1458 to 1658, the domain is characterized as Fibrillar collagen NC1.
+At position 2 to 242, the domain is characterized as ABC transporter 1.
+At position 262 to 494, the domain is characterized as ABC transporter 2.
+At position 200 to 278, the domain is characterized as PDZ.
+At position 190 to 349, the domain is characterized as Helicase C-terminal.
+At position 54 to 225, the domain is characterized as Laminin G-like.
+At position 269 to 328, the domain is characterized as VWFC 1.
+At position 395 to 437, the domain is characterized as EGF-like 1.
+At position 438 to 479, the domain is characterized as EGF-like 2; calcium-binding.
+At position 480 to 520, the domain is characterized as EGF-like 3; calcium-binding.
+At position 521 to 551, the domain is characterized as EGF-like 4.
+At position 553 to 592, the domain is characterized as EGF-like 5; calcium-binding.
+At position 600 to 635, the domain is characterized as EGF-like 6; calcium-binding.
+At position 636 to 691, the domain is characterized as VWFC 2.
+At position 696 to 754, the domain is characterized as VWFC 3.
+At position 30 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 323, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 417, the domain is characterized as Ig-like C2-type 4.
+At position 424 to 545, the domain is characterized as Ig-like C2-type 5.
+At position 552 to 644, the domain is characterized as Ig-like C2-type 6.
+At position 651 to 737, the domain is characterized as Ig-like C2-type 7.
+At position 819 to 1151, the domain is characterized as Protein kinase.
+At position 6 to 200, the domain is characterized as DPCK.
+At position 690 to 987, the domain is characterized as Protein kinase.
+At position 173 to 359, the domain is characterized as CheB-type methylesterase.
+At position 164 to 227, the domain is characterized as R3H.
+At position 228 to 300, the domain is characterized as SUZ.
+At position 1 to 95, the domain is characterized as SUEL-type lectin 1.
+At position 105 to 195, the domain is characterized as SUEL-type lectin 2.
+At position 45 to 288, the domain is characterized as Lon N-terminal.
+At position 674 to 855, the domain is characterized as Lon proteolytic.
+At position 10 to 246, the domain is characterized as DOG1.
+At position 566 to 699, the domain is characterized as C1q.
+At position 603 to 717, the domain is characterized as PAZ.
+At position 885 to 1186, the domain is characterized as Piwi.
+At position 290 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1090 to 1260, the domain is characterized as Laminin G-like 6.
+At position 257 to 353, the domain is characterized as RRM 1.
+At position 358 to 438, the domain is characterized as RRM 2.
+At position 475 to 555, the domain is characterized as RRM 3.
+At position 31 to 207, the domain is characterized as Flo11.
+At position 70 to 373, the domain is characterized as PPM-type phosphatase.
+At position 7 to 74, the domain is characterized as Sm.
+At position 69 to 167, the domain is characterized as AD.
+At position 185 to 287, the domain is characterized as PpiC 1.
+At position 235 to 356, the domain is characterized as C2 2.
+At position 399 to 530, the domain is characterized as C2 3.
+At position 943 to 1068, the domain is characterized as C2 4.
+At position 1115 to 1241, the domain is characterized as C2 5.
+At position 5 to 161, the domain is characterized as PPIase cyclophilin-type.
+At position 257 to 512, the domain is characterized as KaiC 2.
+At position 56 to 138, the domain is characterized as RRM 1.
+At position 14 to 82, the domain is characterized as HTH gntR-type.
+At position 191 to 332, the domain is characterized as FCP1 homology.
+At position 166 to 331, the domain is characterized as Thioredoxin.
+At position 306 to 433, the domain is characterized as C-type lectin.
+At position 1 to 202, the domain is characterized as MARVEL.
+At position 1 to 239, the domain is characterized as CN hydrolase.
+At position 223 to 388, the domain is characterized as TrmE-type G.
+At position 153 to 203, the domain is characterized as DHHC.
+At position 4 to 133, the domain is characterized as ADF-H.
+At position 220 to 272, the domain is characterized as HAMP.
+At position 281 to 351, the domain is characterized as PAS.
+At position 429 to 656, the domain is characterized as Histidine kinase.
+At position 173 to 241, the domain is characterized as DRBM.
+At position 499 to 770, the domain is characterized as Protein kinase.
+At position 844 to 974, the domain is characterized as Guanylate cyclase.
+At position 35 to 54, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 395 to 414, the domain is characterized as UIM.
+At position 33 to 77, the domain is characterized as CAP-Gly.
+At position 441 to 481, the domain is characterized as LRRCT.
+At position 135 to 392, the domain is characterized as Protein kinase.
+At position 393 to 463, the domain is characterized as AGC-kinase C-terminal.
+At position 275 to 402, the domain is characterized as Guanylate cyclase 1.
+At position 963 to 1107, the domain is characterized as Guanylate cyclase 2.
+At position 14 to 177, the domain is characterized as C2 PI3K-type.
+At position 533 to 799, the domain is characterized as PI3K/PI4K catalytic.
+At position 21 to 46, the domain is characterized as Antistasin-like 1.
+At position 49 to 75, the domain is characterized as Antistasin-like 2.
+At position 61 to 146, the domain is characterized as Cytochrome b5 heme-binding.
+At position 18 to 135, the domain is characterized as Response regulatory.
+At position 162 to 355, the domain is characterized as CheB-type methylesterase.
+At position 719 to 957, the domain is characterized as NR LBD.
+At position 50 to 360, the domain is characterized as AB hydrolase-1.
+At position 62 to 122, the domain is characterized as CWF21.
+At position 74 to 201, the domain is characterized as TBDR plug.
+At position 209 to 999, the domain is characterized as TBDR beta-barrel.
+At position 286 to 401, the domain is characterized as C-type lectin.
+At position 96 to 203, the domain is characterized as Rieske.
+At position 308 to 421, the domain is characterized as PH.
+At position 773 to 978, the domain is characterized as VASt.
+At position 178 to 248, the domain is characterized as MBD.
+At position 310 to 384, the domain is characterized as Pre-SET.
+At position 387 to 678, the domain is characterized as SET.
+At position 23 to 244, the domain is characterized as AB hydrolase-1.
+At position 9 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 172 to 278, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 357, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 53 to 220, the domain is characterized as FCP1 homology.
+At position 122 to 173, the domain is characterized as bHLH.
+At position 244 to 320, the domain is characterized as ACT.
+At position 314 to 589, the domain is characterized as ABC transmembrane type-1 1.
+At position 623 to 846, the domain is characterized as ABC transporter 1.
+At position 945 to 1215, the domain is characterized as ABC transmembrane type-1 2.
+At position 1262 to 1496, the domain is characterized as ABC transporter 2.
+At position 761 to 827, the domain is characterized as HP.
+At position 46 to 60, the domain is characterized as UIM.
+At position 348 to 636, the domain is characterized as Protein kinase.
+At position 1 to 133, the domain is characterized as MGS-like.
+At position 1 to 105, the domain is characterized as Plastocyanin-like.
+At position 20 to 69, the domain is characterized as F-box.
+At position 16 to 78, the domain is characterized as LCN-type CS-alpha/beta.
+At position 25 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 341 to 574, the domain is characterized as ABC transporter.
+At position 4 to 130, the domain is characterized as Galectin.
+At position 31 to 97, the domain is characterized as KH.
+At position 12 to 325, the domain is characterized as SAM-dependent MTase C5-type.
+At position 99 to 190, the domain is characterized as Ig-like C2-type 1.
+At position 196 to 282, the domain is characterized as Ig-like C2-type 2.
+At position 300 to 385, the domain is characterized as Ig-like C2-type 3.
+At position 390 to 474, the domain is characterized as Ig-like C2-type 4.
+At position 480 to 569, the domain is characterized as Ig-like C2-type 5.
+At position 571 to 660, the domain is characterized as Ig-like C2-type 6.
+At position 673 to 771, the domain is characterized as Fibronectin type-III 1.
+At position 776 to 873, the domain is characterized as Fibronectin type-III 2.
+At position 878 to 972, the domain is characterized as Fibronectin type-III 3.
+At position 977 to 1067, the domain is characterized as Fibronectin type-III 4.
+At position 25 to 227, the domain is characterized as HORMA.
+At position 1 to 146, the domain is characterized as Ferritin-like diiron.
+At position 14 to 90, the domain is characterized as KRAB.
+At position 144 to 365, the domain is characterized as Radical SAM core.
+At position 37 to 147, the domain is characterized as HIT.
+At position 127 to 211, the domain is characterized as MEIS N-terminal.
+At position 145 to 202, the domain is characterized as TRAM.
+At position 64 to 177, the domain is characterized as DOMON.
+At position 184 to 377, the domain is characterized as Cytochrome b561.
+At position 2 to 25, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 26 to 54, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 25 to 351, the domain is characterized as Transferrin-like 1.
+At position 364 to 689, the domain is characterized as Transferrin-like 2.
+At position 158 to 459, the domain is characterized as Deacetylase sirtuin-type.
+At position 141 to 362, the domain is characterized as Radical SAM core.
+At position 38 to 260, the domain is characterized as AB hydrolase-1.
+At position 324 to 553, the domain is characterized as MH2.
+At position 19 to 139, the domain is characterized as Thioredoxin 1.
+At position 159 to 276, the domain is characterized as Thioredoxin 2.
+At position 1 to 330, the domain is characterized as GBD/FH3.
+At position 432 to 592, the domain is characterized as FH1.
+At position 593 to 981, the domain is characterized as FH2.
+At position 1009 to 1024, the domain is characterized as WH2.
+At position 40 to 220, the domain is characterized as Integrase catalytic.
+At position 785 to 876, the domain is characterized as ELM2.
+At position 891 to 942, the domain is characterized as SANT.
+At position 83 to 265, the domain is characterized as ABC transmembrane type-1 1.
+At position 352 to 540, the domain is characterized as ABC transmembrane type-1 2.
+At position 24 to 117, the domain is characterized as UPAR/Ly6 1.
+At position 117 to 212, the domain is characterized as UPAR/Ly6 2.
+At position 213 to 298, the domain is characterized as UPAR/Ly6 3.
+At position 545 to 609, the domain is characterized as FHA.
+At position 39 to 117, the domain is characterized as Inhibitor I9.
+At position 122 to 611, the domain is characterized as Peptidase S8.
+At position 158 to 232, the domain is characterized as RRM 2.
+At position 13 to 180, the domain is characterized as Era-type G.
+At position 211 to 288, the domain is characterized as KH type-2.
+At position 57 to 154, the domain is characterized as sHSP.
+At position 32 to 188, the domain is characterized as Helicase ATP-binding.
+At position 208 to 417, the domain is characterized as Helicase C-terminal.
+At position 117 to 315, the domain is characterized as ATP-grasp.
+At position 174 to 549, the domain is characterized as USP.
+At position 227 to 262, the domain is characterized as DMA.
+At position 36 to 124, the domain is characterized as MaoC-like.
+At position 17 to 186, the domain is characterized as FAD-binding PCMH-type.
+At position 51 to 285, the domain is characterized as Radical SAM core.
+At position 358 to 480, the domain is characterized as RNase NYN.
+At position 226 to 278, the domain is characterized as HAMP.
+At position 280 to 490, the domain is characterized as HD-GYP.
+At position 88 to 119, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 121 to 144, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 28 to 62, the domain is characterized as Chitin-binding type-1.
+At position 562 to 620, the domain is characterized as RAP.
+At position 29 to 128, the domain is characterized as Cystatin.
+At position 251 to 304, the domain is characterized as HTH myb-type 1.
+At position 305 to 363, the domain is characterized as HTH myb-type 2.
+At position 1 to 41, the domain is characterized as Kazal-like 1.
+At position 79 to 132, the domain is characterized as Laminin EGF-like 1.
+At position 133 to 179, the domain is characterized as Laminin EGF-like 2.
+At position 201 to 257, the domain is characterized as Kazal-like 2.
+At position 411 to 533, the domain is characterized as SEA.
+At position 608 to 644, the domain is characterized as EGF-like 1.
+At position 649 to 825, the domain is characterized as Laminin G-like 1.
+At position 865 to 902, the domain is characterized as EGF-like 2.
+At position 914 to 1096, the domain is characterized as Laminin G-like 2.
+At position 1097 to 1135, the domain is characterized as EGF-like 3.
+At position 1146 to 1324, the domain is characterized as Laminin G-like 3.
+At position 299 to 499, the domain is characterized as HIN-200.
+At position 71 to 266, the domain is characterized as Peptidase M12A.
+At position 148 to 175, the domain is characterized as PLD phosphodiesterase 1.
+At position 357 to 383, the domain is characterized as PLD phosphodiesterase 2.
+At position 8 to 56, the domain is characterized as F-box; degenerate.
+At position 104 to 273, the domain is characterized as tr-type G.
+At position 74 to 109, the domain is characterized as EF-hand.
+At position 138 to 361, the domain is characterized as Radical SAM core.
+At position 18 to 262, the domain is characterized as ABC transporter.
+At position 11 to 145, the domain is characterized as ADF-H.
+At position 538 to 578, the domain is characterized as CUE.
+At position 50 to 211, the domain is characterized as SIS.
+At position 16 to 278, the domain is characterized as Helicase ATP-binding.
+At position 458 to 634, the domain is characterized as Helicase C-terminal.
+At position 120 to 352, the domain is characterized as NR LBD.
+At position 27 to 309, the domain is characterized as ABC transmembrane type-1.
+At position 375 to 405, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 415 to 444, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 204 to 268, the domain is characterized as KH.
+At position 330 to 423, the domain is characterized as HD.
+At position 1 to 38, the domain is characterized as Rubredoxin-like.
+At position 373 to 409, the domain is characterized as CBM1.
+At position 335 to 477, the domain is characterized as Thioredoxin 2.
+At position 135 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 245 to 327, the domain is characterized as Ig-like C2-type 3.
+At position 334 to 424, the domain is characterized as Fibronectin type-III 1.
+At position 429 to 523, the domain is characterized as Fibronectin type-III 2.
+At position 527 to 616, the domain is characterized as Fibronectin type-III 3.
+At position 621 to 718, the domain is characterized as Fibronectin type-III 4.
+At position 723 to 831, the domain is characterized as Fibronectin type-III 5.
+At position 832 to 930, the domain is characterized as Fibronectin type-III 6.
+At position 931 to 1033, the domain is characterized as Fibronectin type-III 7.
+At position 1036 to 1120, the domain is characterized as Fibronectin type-III 8.
+At position 1393 to 1648, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1680 to 1939, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 174 to 350, the domain is characterized as EngA-type G 2.
+At position 65 to 135, the domain is characterized as Chitin-binding type R&R.
+At position 205 to 376, the domain is characterized as PCI.
+At position 75 to 215, the domain is characterized as MPN.
+At position 101 to 158, the domain is characterized as VWFC.
+At position 307 to 344, the domain is characterized as LRRNT.
+At position 164 to 286, the domain is characterized as Fatty acid hydroxylase.
+At position 193 to 256, the domain is characterized as bZIP.
+At position 36 to 150, the domain is characterized as MTTase N-terminal.
+At position 171 to 403, the domain is characterized as Radical SAM core.
+At position 406 to 475, the domain is characterized as TRAM.
+At position 278 to 467, the domain is characterized as Helicase ATP-binding.
+At position 477 to 638, the domain is characterized as Helicase C-terminal.
+At position 2 to 182, the domain is characterized as YrdC-like.
+At position 53 to 294, the domain is characterized as ABC transporter 1.
+At position 364 to 583, the domain is characterized as ABC transporter 2.
+At position 208 to 272, the domain is characterized as KH 1.
+At position 296 to 362, the domain is characterized as KH 2.
+At position 385 to 449, the domain is characterized as KH 3.
+At position 486 to 553, the domain is characterized as KH 4.
+At position 45 to 109, the domain is characterized as Chromo 1.
+At position 142 to 201, the domain is characterized as Chromo 2.
+At position 237 to 405, the domain is characterized as Helicase ATP-binding.
+At position 528 to 679, the domain is characterized as Helicase C-terminal.
+At position 188 to 405, the domain is characterized as JmjC.
+At position 1 to 323, the domain is characterized as 5'-3' exonuclease.
+At position 324 to 517, the domain is characterized as 3'-5' exonuclease.
+At position 81 to 174, the domain is characterized as N-acetyltransferase.
+At position 321 to 711, the domain is characterized as PIPK.
+At position 64 to 195, the domain is characterized as THUMP.
+At position 7 to 195, the domain is characterized as Flavodoxin-like.
+At position 107 to 315, the domain is characterized as ATP-grasp.
+At position 53 to 271, the domain is characterized as Radical SAM core.
+At position 358 to 701, the domain is characterized as Kinesin motor.
+At position 825 to 891, the domain is characterized as FHA.
+At position 233 to 296, the domain is characterized as bZIP.
+At position 8 to 158, the domain is characterized as C2 NT-type.
+At position 443 to 548, the domain is characterized as Calponin-homology (CH).
+At position 1056 to 1212, the domain is characterized as bMERB.
+At position 73 to 292, the domain is characterized as Radical SAM core.
+At position 171 to 269, the domain is characterized as HTH araC/xylS-type.
+At position 7 to 75, the domain is characterized as HTH gntR-type.
+At position 154 to 267, the domain is characterized as Fe2OG dioxygenase.
+At position 136 to 499, the domain is characterized as MACPF.
+At position 499 to 530, the domain is characterized as EGF-like.
+At position 540 to 584, the domain is characterized as TSP type-1 2.
+At position 630 to 711, the domain is characterized as BRCT.
+At position 219 to 288, the domain is characterized as Ubiquitin-like.
+At position 590 to 667, the domain is characterized as BRCT.
+At position 34 to 79, the domain is characterized as F-box.
+At position 36 to 117, the domain is characterized as Saposin B-type.
+At position 15 to 78, the domain is characterized as R3H.
+At position 227 to 396, the domain is characterized as Helicase ATP-binding.
+At position 561 to 735, the domain is characterized as Helicase C-terminal.
+At position 43 to 296, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 277 to 329, the domain is characterized as HAMP.
+At position 143 to 220, the domain is characterized as RRM 2.
+At position 236 to 314, the domain is characterized as RRM 3.
+At position 340 to 470, the domain is characterized as RRM 4.
+At position 662 to 739, the domain is characterized as PABC.
+At position 570 to 675, the domain is characterized as tRNA-binding.
+At position 285 to 348, the domain is characterized as bZIP.
+At position 5 to 61, the domain is characterized as HTH deoR-type.
+At position 429 to 598, the domain is characterized as SSD.
+At position 74 to 120, the domain is characterized as UBX.
+At position 6 to 121, the domain is characterized as PpiC.
+At position 28 to 208, the domain is characterized as Laminin G-like 1.
+At position 198 to 236, the domain is characterized as EGF-like 1.
+At position 263 to 460, the domain is characterized as Laminin G-like 2.
+At position 467 to 661, the domain is characterized as Laminin G-like 3.
+At position 665 to 702, the domain is characterized as EGF-like 2.
+At position 707 to 880, the domain is characterized as Laminin G-like 4.
+At position 894 to 1069, the domain is characterized as Laminin G-like 5.
+At position 1072 to 1109, the domain is characterized as EGF-like 3.
+At position 1113 to 1314, the domain is characterized as Laminin G-like 6.
+At position 95 to 328, the domain is characterized as Radical SAM core.
+At position 203 to 312, the domain is characterized as Calponin-homology (CH).
+At position 1109 to 1243, the domain is characterized as CKK.
+At position 227 to 373, the domain is characterized as YDG.
+At position 454 to 516, the domain is characterized as Pre-SET.
+At position 519 to 660, the domain is characterized as SET.
+At position 677 to 693, the domain is characterized as Post-SET.
+At position 191 to 378, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 256, the domain is characterized as ABC transporter.
+At position 68 to 183, the domain is characterized as THUMP.
+At position 75 to 255, the domain is characterized as ABC transmembrane type-1.
+At position 348 to 691, the domain is characterized as GH16.
+At position 159 to 449, the domain is characterized as NR LBD.
+At position 10 to 65, the domain is characterized as L27 1.
+At position 67 to 122, the domain is characterized as L27 2.
+At position 30 to 104, the domain is characterized as SH3b.
+At position 120 to 195, the domain is characterized as RRM 2.
+At position 14 to 297, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 34 to 217, the domain is characterized as RNase H type-2.
+At position 76 to 315, the domain is characterized as GB1/RHD3-type G.
+At position 521 to 587, the domain is characterized as DRBM 2.
+At position 63 to 337, the domain is characterized as Protein kinase.
+At position 115 to 209, the domain is characterized as Ig-like C1-type.
+At position 94 to 277, the domain is characterized as tr-type G.
+At position 1 to 42, the domain is characterized as F-box.
+At position 212 to 376, the domain is characterized as PID.
+At position 389 to 475, the domain is characterized as PDZ 1.
+At position 480 to 554, the domain is characterized as PDZ 2.
+At position 248 to 338, the domain is characterized as PDZ 1.
+At position 205 to 243, the domain is characterized as LRRCT.
+At position 509 to 791, the domain is characterized as Protein kinase.
+At position 859 to 989, the domain is characterized as Guanylate cyclase.
+At position 23 to 139, the domain is characterized as HD.
+At position 22 to 440, the domain is characterized as GH18.
+At position 64 to 507, the domain is characterized as Kinesin motor.
+At position 351 to 425, the domain is characterized as ACT.
+At position 49 to 266, the domain is characterized as Radical SAM core.
+At position 16 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 91 to 322, the domain is characterized as tr-type G.
+At position 353 to 585, the domain is characterized as Peptidase M12B.
+At position 26 to 94, the domain is characterized as PAS.
+At position 152 to 316, the domain is characterized as GAF.
+At position 529 to 747, the domain is characterized as Histidine kinase.
+At position 18 to 202, the domain is characterized as RNase H type-2.
+At position 52 to 189, the domain is characterized as GAF.
+At position 203 to 265, the domain is characterized as PAS.
+At position 327 to 552, the domain is characterized as Sigma-54 factor interaction.
+At position 129 to 195, the domain is characterized as HMA 2.
+At position 204 to 270, the domain is characterized as HMA 3; degenerate.
+At position 139 to 377, the domain is characterized as Radical SAM core.
+At position 69 to 469, the domain is characterized as Glutamine amidotransferase type-2.
+At position 221 to 276, the domain is characterized as LIM zinc-binding 4.
+At position 6 to 82, the domain is characterized as RRM 1.
+At position 120 to 197, the domain is characterized as RRM 2.
+At position 25 to 152, the domain is characterized as C-type lectin.
+At position 119 to 335, the domain is characterized as SMP-LTD.
+At position 22 to 56, the domain is characterized as SAP.
+At position 384 to 462, the domain is characterized as RRM.
+At position 86 to 228, the domain is characterized as RNase III.
+At position 236 to 306, the domain is characterized as DRBM.
+At position 516 to 684, the domain is characterized as HNH Cas9-type.
+At position 605 to 741, the domain is characterized as C2.
+At position 2 to 243, the domain is characterized as PPM-type phosphatase.
+At position 1012 to 1117, the domain is characterized as Calponin-homology (CH).
+At position 456 to 536, the domain is characterized as RRM.
+At position 1051 to 1097, the domain is characterized as G-patch.
+At position 158 to 305, the domain is characterized as TRUD.
+At position 144 to 263, the domain is characterized as C-type lectin.
+At position 68 to 352, the domain is characterized as Protein kinase.
+At position 303 to 419, the domain is characterized as C2.
+At position 243 to 286, the domain is characterized as LysM 1.
+At position 319 to 362, the domain is characterized as LysM 2.
+At position 393 to 436, the domain is characterized as LysM 3.
+At position 527 to 622, the domain is characterized as MRH.
+At position 151 to 291, the domain is characterized as MRH.
+At position 35 to 135, the domain is characterized as Ig-like V-type.
+At position 145 to 230, the domain is characterized as Ig-like C2-type.
+At position 37 to 90, the domain is characterized as WAP.
+At position 124 to 175, the domain is characterized as Kazal-like.
+At position 208 to 301, the domain is characterized as Ig-like C2-type.
+At position 326 to 376, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 384 to 434, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 443 to 564, the domain is characterized as NTR.
+At position 23 to 95, the domain is characterized as KH type-2.
+At position 47 to 267, the domain is characterized as GB1/RHD3-type G.
+At position 582 to 683, the domain is characterized as tRNA-binding.
+At position 633 to 697, the domain is characterized as Tudor 1.
+At position 724 to 780, the domain is characterized as Tudor 2.
+At position 938 to 1009, the domain is characterized as MBD.
+At position 1075 to 1148, the domain is characterized as Pre-SET.
+At position 1151 to 1411, the domain is characterized as SET.
+At position 1420 to 1436, the domain is characterized as Post-SET.
+At position 285 to 362, the domain is characterized as PUA.
+At position 18 to 89, the domain is characterized as S1 motif.
+At position 289 to 540, the domain is characterized as Protein kinase.
+At position 92 to 288, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 286, the domain is characterized as RNase H type-2.
+At position 116 to 316, the domain is characterized as ATP-grasp.
+At position 530 to 763, the domain is characterized as ABC transporter 1.
+At position 1381 to 1614, the domain is characterized as ABC transporter 2.
+At position 128 to 401, the domain is characterized as Deacetylase sirtuin-type.
+At position 24 to 53, the domain is characterized as LRRNT.
+At position 351 to 405, the domain is characterized as LRRCT.
+At position 406 to 495, the domain is characterized as Ig-like C2-type.
+At position 187 to 237, the domain is characterized as LRRCT.
+At position 242 to 340, the domain is characterized as Ig-like.
+At position 698 to 749, the domain is characterized as GPS.
+At position 33 to 107, the domain is characterized as Cytochrome b5 heme-binding.
+At position 543 to 578, the domain is characterized as EF-hand 1.
+At position 587 to 620, the domain is characterized as EF-hand 2.
+At position 617 to 652, the domain is characterized as EF-hand 3.
+At position 682 to 716, the domain is characterized as EF-hand 4.
+At position 363 to 424, the domain is characterized as SH3.
+At position 1 to 60, the domain is characterized as SH3.
+At position 489 to 623, the domain is characterized as N-terminal Ras-GEF.
+At position 663 to 894, the domain is characterized as Ras-GEF.
+At position 77 to 183, the domain is characterized as sHSP.
+At position 11 to 173, the domain is characterized as Tyrosine-protein phosphatase.
+At position 30 to 97, the domain is characterized as Histone-fold.
+At position 1 to 112, the domain is characterized as SET.
+At position 17 to 256, the domain is characterized as ABC transporter.
+At position 489 to 605, the domain is characterized as HD.
+At position 729 to 810, the domain is characterized as ACT 1.
+At position 840 to 921, the domain is characterized as ACT 2.
+At position 24 to 346, the domain is characterized as Kinesin motor.
+At position 4 to 79, the domain is characterized as U-box.
+At position 70 to 178, the domain is characterized as FAD-binding FR-type.
+At position 403 to 572, the domain is characterized as tr-type G.
+At position 250 to 342, the domain is characterized as Cytochrome c.
+At position 39 to 490, the domain is characterized as Hexokinase.
+At position 416 to 689, the domain is characterized as Protein kinase.
+At position 60 to 126, the domain is characterized as TGS.
+At position 617 to 716, the domain is characterized as Zinc-hook.
+At position 93 to 250, the domain is characterized as PID.
+At position 1796 to 2004, the domain is characterized as Rap-GAP.
+At position 259 to 466, the domain is characterized as Ku.
+At position 571 to 605, the domain is characterized as SAP.
+At position 54 to 100, the domain is characterized as bZIP 1.
+At position 329 to 392, the domain is characterized as bZIP 2.
+At position 493 to 813, the domain is characterized as Protein kinase.
+At position 885 to 1015, the domain is characterized as Guanylate cyclase.
+At position 63 to 271, the domain is characterized as Glutamine amidotransferase type-1.
+At position 315 to 351, the domain is characterized as CBM1.
+At position 17 to 58, the domain is characterized as LRRNT.
+At position 88 to 247, the domain is characterized as CP-type G.
+At position 39 to 110, the domain is characterized as SH3.
+At position 3 to 77, the domain is characterized as Ubiquitin-like 1.
+At position 86 to 159, the domain is characterized as Ubiquitin-like 2.
+At position 27 to 242, the domain is characterized as Radical SAM core.
+At position 220 to 271, the domain is characterized as bHLH.
+At position 2067 to 2117, the domain is characterized as AWS.
+At position 2119 to 2240, the domain is characterized as SET.
+At position 66 to 191, the domain is characterized as Thioredoxin.
+At position 433 to 462, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 463 to 490, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 26 to 129, the domain is characterized as Cytochrome c 1.
+At position 173 to 289, the domain is characterized as Cytochrome c 2.
+At position 312 to 403, the domain is characterized as Cytochrome c 3.
+At position 33 to 192, the domain is characterized as Tyrosine-protein phosphatase.
+At position 223 to 289, the domain is characterized as RRM 1.
+At position 602 to 679, the domain is characterized as RRM 2.
+At position 79 to 407, the domain is characterized as Peptidase A1.
+At position 11 to 127, the domain is characterized as LRAT.
+At position 34 to 217, the domain is characterized as SIS.
+At position 360 to 417, the domain is characterized as S4 RNA-binding.
+At position 143 to 265, the domain is characterized as Cyclin N-terminal.
+At position 1 to 44, the domain is characterized as LEM.
+At position 1 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 79, the domain is characterized as LRRNT.
+At position 160 to 212, the domain is characterized as LRRCT.
+At position 53 to 304, the domain is characterized as Protein kinase.
+At position 323 to 362, the domain is characterized as UBA.
+At position 727 to 776, the domain is characterized as KA1.
+At position 75 to 251, the domain is characterized as IRG-type G.
+At position 395 to 447, the domain is characterized as LRRCT.
+At position 44 to 95, the domain is characterized as HTH myb-type 1.
+At position 96 to 150, the domain is characterized as HTH myb-type 2.
+At position 102 to 231, the domain is characterized as JmjC.
+At position 302 to 575, the domain is characterized as Protein kinase.
+At position 47 to 130, the domain is characterized as Ig-like C2-type.
+At position 35 to 211, the domain is characterized as BPL/LPL catalytic.
+At position 168 to 362, the domain is characterized as B30.2/SPRY.
+At position 42 to 228, the domain is characterized as CP-type G.
+At position 33 to 415, the domain is characterized as G-alpha.
+At position 54 to 188, the domain is characterized as MPN.
+At position 234 to 385, the domain is characterized as Exonuclease.
+At position 1 to 249, the domain is characterized as Deacetylase sirtuin-type.
+At position 235 to 522, the domain is characterized as GH18.
+At position 161 to 383, the domain is characterized as Histidine kinase.
+At position 18 to 241, the domain is characterized as Peptidase S1.
+At position 53 to 361, the domain is characterized as YjeF C-terminal.
+At position 165 to 305, the domain is characterized as TRUD.
+At position 19 to 60, the domain is characterized as UBA.
+At position 238 to 303, the domain is characterized as SH3.
+At position 792 to 865, the domain is characterized as RRM.
+At position 272 to 462, the domain is characterized as B30.2/SPRY.
+At position 101 to 270, the domain is characterized as tr-type G.
+At position 20 to 149, the domain is characterized as RNase III.
+At position 175 to 244, the domain is characterized as DRBM.
+At position 499 to 562, the domain is characterized as bZIP.
+At position 52 to 736, the domain is characterized as Peptidase M13.
+At position 414 to 500, the domain is characterized as Fibronectin type-III.
+At position 100 to 174, the domain is characterized as PRC barrel.
+At position 289 to 346, the domain is characterized as CBS 2.
+At position 46 to 246, the domain is characterized as AIG1-type G 1.
+At position 281 to 471, the domain is characterized as AIG1-type G 2.
+At position 472 to 681, the domain is characterized as AIG1-type G 3.
+At position 493 to 750, the domain is characterized as Olfactomedin-like.
+At position 71 to 124, the domain is characterized as Cadherin 1.
+At position 125 to 237, the domain is characterized as Cadherin 2.
+At position 249 to 354, the domain is characterized as Cadherin 3.
+At position 355 to 459, the domain is characterized as Cadherin 4.
+At position 132 to 269, the domain is characterized as Thioredoxin.
+At position 140 to 347, the domain is characterized as ATP-grasp.
+At position 5 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 125 to 395, the domain is characterized as Protein kinase.
+At position 131 to 169, the domain is characterized as LRRCT.
+At position 581 to 684, the domain is characterized as Ricin B-type lectin.
+At position 794 to 871, the domain is characterized as Carrier 1.
+At position 1875 to 1951, the domain is characterized as Carrier 2.
+At position 102 to 217, the domain is characterized as Ferric oxidoreductase.
+At position 247 to 369, the domain is characterized as FAD-binding FR-type.
+At position 34 to 161, the domain is characterized as N-terminal Ras-GEF.
+At position 205 to 453, the domain is characterized as Ras-GEF.
+At position 160 to 354, the domain is characterized as Rho-GAP.
+At position 2 to 335, the domain is characterized as SPX.
+At position 593 to 784, the domain is characterized as EXS.
+At position 162 to 214, the domain is characterized as bHLH.
+At position 118 to 295, the domain is characterized as SMP-LTD.
+At position 292 to 412, the domain is characterized as C2 1.
+At position 430 to 570, the domain is characterized as C2 2.
+At position 759 to 881, the domain is characterized as C2 3.
+At position 49 to 350, the domain is characterized as ABC transmembrane type-1 1.
+At position 386 to 622, the domain is characterized as ABC transporter 1.
+At position 693 to 980, the domain is characterized as ABC transmembrane type-1 2.
+At position 1015 to 1253, the domain is characterized as ABC transporter 2.
+At position 83 to 311, the domain is characterized as ABC transmembrane type-1.
+At position 62 to 314, the domain is characterized as Protein kinase.
+At position 463 to 541, the domain is characterized as POLO box 1.
+At position 562 to 645, the domain is characterized as POLO box 2.
+At position 609 to 718, the domain is characterized as PH.
+At position 86 to 138, the domain is characterized as Kazal-like 1.
+At position 177 to 230, the domain is characterized as Kazal-like 2.
+At position 264 to 304, the domain is characterized as EGF-like.
+At position 117 to 241, the domain is characterized as CRC.
+At position 253 to 411, the domain is characterized as FCP1 homology.
+At position 312 to 397, the domain is characterized as Ig-like C2-type 4.
+At position 514 to 595, the domain is characterized as Ig-like C2-type 6.
+At position 601 to 682, the domain is characterized as Ig-like C2-type 7.
+At position 45 to 186, the domain is characterized as Nudix hydrolase.
+At position 39 to 303, the domain is characterized as Laminin N-terminal.
+At position 405 to 497, the domain is characterized as Laminin EGF-like 1.
+At position 498 to 560, the domain is characterized as Laminin EGF-like 2.
+At position 561 to 610, the domain is characterized as Laminin EGF-like 3.
+At position 649 to 792, the domain is characterized as NTR.
+At position 259 to 374, the domain is characterized as CobW C-terminal.
+At position 568 to 674, the domain is characterized as EH.
+At position 15 to 147, the domain is characterized as ADF-H.
+At position 326 to 372, the domain is characterized as G-patch.
+At position 365 to 448, the domain is characterized as Death.
+At position 45 to 105, the domain is characterized as Sushi 1.
+At position 106 to 168, the domain is characterized as Sushi 2.
+At position 169 to 234, the domain is characterized as Sushi 3.
+At position 235 to 294, the domain is characterized as Sushi 4.
+At position 8 to 314, the domain is characterized as IF rod.
+At position 64 to 92, the domain is characterized as EF-hand 2.
+At position 49 to 104, the domain is characterized as F-box.
+At position 55 to 264, the domain is characterized as Cupin type-1 1.
+At position 348 to 496, the domain is characterized as Cupin type-1 2.
+At position 119 to 485, the domain is characterized as PRONE.
+At position 217 to 359, the domain is characterized as PPC.
+At position 73 to 779, the domain is characterized as GH81.
+At position 84 to 181, the domain is characterized as WGR.
+At position 207 to 324, the domain is characterized as PARP alpha-helical.
+At position 332 to 559, the domain is characterized as PARP catalytic.
+At position 7 to 106, the domain is characterized as HTH hxlR-type.
+At position 11 to 131, the domain is characterized as MaoC-like.
+At position 82 to 323, the domain is characterized as Calpain catalytic.
+At position 22 to 233, the domain is characterized as GH16.
+At position 346 to 543, the domain is characterized as Lon proteolytic.
+At position 8 to 212, the domain is characterized as YjeF N-terminal.
+At position 32 to 102, the domain is characterized as GED.
+At position 327 to 536, the domain is characterized as BAR.
+At position 582 to 645, the domain is characterized as SH3 1.
+At position 713 to 776, the domain is characterized as SH3 2.
+At position 96 to 174, the domain is characterized as GRAM.
+At position 1 to 132, the domain is characterized as CMP/dCMP-type deaminase.
+At position 53 to 128, the domain is characterized as Carrier.
+At position 307 to 515, the domain is characterized as PCI.
+At position 49 to 155, the domain is characterized as B30.2/SPRY.
+At position 475 to 671, the domain is characterized as FtsK.
+At position 131 to 264, the domain is characterized as JmjC.
+At position 512 to 798, the domain is characterized as UvrD-like helicase C-terminal.
+At position 26 to 415, the domain is characterized as Helicase ATP-binding.
+At position 139 to 811, the domain is characterized as Peptidase M13.
+At position 1049 to 1158, the domain is characterized as PH.
+At position 572 to 673, the domain is characterized as tRNA-binding.
+At position 234 to 623, the domain is characterized as GRAS.
+At position 92 to 162, the domain is characterized as PRC barrel.
+At position 81 to 449, the domain is characterized as PIPK.
+At position 38 to 151, the domain is characterized as sHSP.
+At position 103 to 257, the domain is characterized as Guanylate cyclase.
+At position 69 to 312, the domain is characterized as ABC transporter 1.
+At position 445 to 722, the domain is characterized as ABC transmembrane type-2 1.
+At position 814 to 1053, the domain is characterized as ABC transporter 2.
+At position 1201 to 1471, the domain is characterized as ABC transmembrane type-2 2.
+At position 454 to 571, the domain is characterized as Toprim.
+At position 2 to 80, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 80 to 119, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 217 to 273, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 851 to 1104, the domain is characterized as Protein kinase.
+At position 74 to 244, the domain is characterized as Helicase ATP-binding.
+At position 254 to 414, the domain is characterized as Helicase C-terminal.
+At position 20 to 225, the domain is characterized as Radical SAM core.
+At position 773 to 808, the domain is characterized as EF-hand.
+At position 46 to 218, the domain is characterized as Laminin G-like 1.
+At position 225 to 391, the domain is characterized as Laminin G-like 2.
+At position 131 to 284, the domain is characterized as C2 NT-type.
+At position 134 to 667, the domain is characterized as USP.
+At position 122 to 203, the domain is characterized as RRM 1.
+At position 609 to 642, the domain is characterized as WW.
+At position 32 to 416, the domain is characterized as FERM.
+At position 435 to 540, the domain is characterized as SH2; atypical.
+At position 580 to 846, the domain is characterized as Protein kinase 1.
+At position 872 to 1150, the domain is characterized as Protein kinase 2.
+At position 158 to 229, the domain is characterized as PAS.
+At position 272 to 502, the domain is characterized as Sigma-54 factor interaction.
+At position 848 to 1119, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1150 to 1410, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 470 to 597, the domain is characterized as Guanylate cyclase 1.
+At position 1072 to 1211, the domain is characterized as Guanylate cyclase 2.
+At position 515 to 691, the domain is characterized as Helicase ATP-binding.
+At position 839 to 998, the domain is characterized as Helicase C-terminal.
+At position 36 to 65, the domain is characterized as LRRNT.
+At position 363 to 417, the domain is characterized as LRRCT.
+At position 405 to 507, the domain is characterized as Ig-like C2-type.
+At position 34 to 223, the domain is characterized as RHD.
+At position 771 to 857, the domain is characterized as Death.
+At position 1398 to 1532, the domain is characterized as MaoC-like.
+At position 1 to 131, the domain is characterized as PX.
+At position 266 to 338, the domain is characterized as MIT.
+At position 279 to 550, the domain is characterized as ABC transmembrane type-1 1.
+At position 601 to 829, the domain is characterized as ABC transporter 1.
+At position 882 to 1161, the domain is characterized as ABC transmembrane type-1 2.
+At position 1197 to 1428, the domain is characterized as ABC transporter 2.
+At position 131 to 574, the domain is characterized as Urease.
+At position 399 to 521, the domain is characterized as Arf-GAP.
+At position 4 to 231, the domain is characterized as ABC transporter.
+At position 422 to 543, the domain is characterized as RCK N-terminal.
+At position 216 to 397, the domain is characterized as CRAL-TRIO.
+At position 45 to 77, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 77 to 106, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 110 to 143, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 202 to 377, the domain is characterized as CRAL-TRIO.
+At position 353 to 487, the domain is characterized as GOLD.
+At position 15 to 56, the domain is characterized as JmjN.
+At position 80 to 170, the domain is characterized as ARID.
+At position 439 to 605, the domain is characterized as JmjC.
+At position 139 to 320, the domain is characterized as Macro.
+At position 4 to 329, the domain is characterized as Asparaginase/glutaminase.
+At position 24 to 179, the domain is characterized as C-CAP/cofactor C-like.
+At position 595 to 677, the domain is characterized as BRCT.
+At position 38 to 96, the domain is characterized as Chitin-binding type-2.
+At position 4 to 106, the domain is characterized as PINc.
+At position 13 to 74, the domain is characterized as HTH iclR-type.
+At position 89 to 258, the domain is characterized as IclR-ED.
+At position 37 to 155, the domain is characterized as C-type lectin.
+At position 346 to 420, the domain is characterized as ACT-like.
+At position 41 to 100, the domain is characterized as S4 RNA-binding.
+At position 12 to 156, the domain is characterized as PTS EIIA type-2.
+At position 7 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 54 to 384, the domain is characterized as Protein kinase.
+At position 32 to 94, the domain is characterized as t-SNARE coiled-coil homology.
+At position 340 to 545, the domain is characterized as Protein kinase.
+At position 290 to 319, the domain is characterized as IQ.
+At position 14 to 70, the domain is characterized as HTH lysR-type.
+At position 45 to 137, the domain is characterized as Ig-like C2-type.
+At position 1450 to 1702, the domain is characterized as Autotransporter.
+At position 30 to 83, the domain is characterized as bHLH.
+At position 104 to 175, the domain is characterized as PAS 1.
+At position 297 to 367, the domain is characterized as PAS 2.
+At position 372 to 413, the domain is characterized as PAC.
+At position 234 to 405, the domain is characterized as Helicase ATP-binding.
+At position 416 to 579, the domain is characterized as Helicase C-terminal.
+At position 203 to 249, the domain is characterized as F-box.
+At position 607 to 671, the domain is characterized as KH.
+At position 758 to 817, the domain is characterized as Tudor.
+At position 35 to 342, the domain is characterized as YjeF C-terminal.
+At position 29 to 134, the domain is characterized as Bulb-type lectin 1.
+At position 148 to 255, the domain is characterized as Bulb-type lectin 2.
+At position 21 to 191, the domain is characterized as EngB-type G.
+At position 428 to 488, the domain is characterized as SH3.
+At position 114 to 163, the domain is characterized as F-box.
+At position 57 to 772, the domain is characterized as Myosin motor.
+At position 814 to 843, the domain is characterized as IQ.
+At position 3 to 109, the domain is characterized as LOB.
+At position 4 to 65, the domain is characterized as HTH dtxR-type.
+At position 235 to 463, the domain is characterized as NR LBD.
+At position 237 to 327, the domain is characterized as Ig-like C2-type 2.
+At position 332 to 410, the domain is characterized as Ig-like C2-type 3.
+At position 11 to 280, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 282 to 534, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 546 to 787, the domain is characterized as Fibrinogen C-terminal.
+At position 92 to 182, the domain is characterized as PB1.
+At position 57 to 273, the domain is characterized as Radical SAM core.
+At position 212 to 486, the domain is characterized as Protein kinase.
+At position 28 to 134, the domain is characterized as Gnk2-homologous 1.
+At position 353 to 619, the domain is characterized as Protein kinase.
+At position 81 to 433, the domain is characterized as IF rod.
+At position 462 to 581, the domain is characterized as LTD.
+At position 67 to 243, the domain is characterized as uDENN FNIP1/2-type.
+At position 251 to 601, the domain is characterized as cDENN FNIP1/2-type.
+At position 607 to 687, the domain is characterized as dDENN FNIP1/2-type.
+At position 640 to 719, the domain is characterized as Cytochrome c.
+At position 491 to 811, the domain is characterized as Protein kinase.
+At position 883 to 1013, the domain is characterized as Guanylate cyclase.
+At position 197 to 268, the domain is characterized as RRM.
+At position 2 to 239, the domain is characterized as ABC transporter 1.
+At position 251 to 493, the domain is characterized as ABC transporter 2.
+At position 293 to 378, the domain is characterized as SCD.
+At position 56 to 227, the domain is characterized as MENTAL.
+At position 263 to 573, the domain is characterized as START.
+At position 71 to 170, the domain is characterized as Cytochrome b5 heme-binding.
+At position 168 to 231, the domain is characterized as R3H.
+At position 232 to 302, the domain is characterized as SUZ.
+At position 154 to 303, the domain is characterized as Cupin type-1 1.
+At position 350 to 513, the domain is characterized as Cupin type-1 2.
+At position 142 to 298, the domain is characterized as PPIase cyclophilin-type.
+At position 1703 to 1888, the domain is characterized as Rho-GAP.
+At position 12 to 240, the domain is characterized as Phosphagen kinase C-terminal.
+At position 325 to 460, the domain is characterized as Fido.
+At position 141 to 471, the domain is characterized as PI3K/PI4K catalytic.
+At position 906 to 1052, the domain is characterized as N-acetyltransferase.
+At position 226 to 385, the domain is characterized as TrmE-type G.
+At position 13 to 333, the domain is characterized as Hcy-binding.
+At position 364 to 625, the domain is characterized as Pterin-binding.
+At position 766 to 883, the domain is characterized as B12-binding.
+At position 916 to 1256, the domain is characterized as AdoMet activation.
+At position 198 to 271, the domain is characterized as RRM 1.
+At position 283 to 356, the domain is characterized as RRM 2.
+At position 132 to 298, the domain is characterized as Helicase ATP-binding.
+At position 326 to 477, the domain is characterized as Helicase C-terminal.
+At position 332 to 418, the domain is characterized as PPIase FKBP-type.
+At position 1 to 125, the domain is characterized as PINc.
+At position 3 to 134, the domain is characterized as Galectin.
+At position 117 to 351, the domain is characterized as Radical SAM core.
+At position 7 to 148, the domain is characterized as Peptidase C51.
+At position 198 to 323, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 398 to 466, the domain is characterized as SH3b.
+At position 108 to 163, the domain is characterized as Collagen-like 1.
+At position 242 to 297, the domain is characterized as Collagen-like 3.
+At position 3 to 337, the domain is characterized as Kinesin motor.
+At position 321 to 609, the domain is characterized as Protein kinase.
+At position 71 to 109, the domain is characterized as LRRNT.
+At position 94 to 456, the domain is characterized as GBD/FH3.
+At position 541 to 611, the domain is characterized as FH1.
+At position 616 to 1014, the domain is characterized as FH2.
+At position 1037 to 1067, the domain is characterized as DAD.
+At position 26 to 106, the domain is characterized as RRM 1.
+At position 392 to 464, the domain is characterized as RRM 3.
+At position 1 to 195, the domain is characterized as Glutamine amidotransferase type-1.
+At position 595 to 671, the domain is characterized as BRCT.
+At position 486 to 924, the domain is characterized as USP.
+At position 1709 to 1825, the domain is characterized as PI-PLC Y-box.
+At position 1830 to 1955, the domain is characterized as C2.
+At position 1991 to 2093, the domain is characterized as Ras-associating 1.
+At position 2114 to 2217, the domain is characterized as Ras-associating 2.
+At position 162 to 250, the domain is characterized as 5'-3' exonuclease.
+At position 29 to 243, the domain is characterized as GH16.
+At position 111 to 284, the domain is characterized as Helicase ATP-binding.
+At position 295 to 468, the domain is characterized as Helicase C-terminal.
+At position 49 to 162, the domain is characterized as Expansin-like EG45.
+At position 172 to 252, the domain is characterized as Expansin-like CBD.
+At position 534 to 734, the domain is characterized as SEC7.
+At position 785 to 898, the domain is characterized as PH.
+At position 212 to 262, the domain is characterized as HAMP.
+At position 260 to 305, the domain is characterized as PAS.
+At position 326 to 382, the domain is characterized as PAC.
+At position 395 to 602, the domain is characterized as Histidine kinase.
+At position 157 to 412, the domain is characterized as ABC transporter 1.
+At position 857 to 1099, the domain is characterized as ABC transporter 2.
+At position 23 to 85, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 147 to 209, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 199 to 315, the domain is characterized as Fe2OG dioxygenase.
+At position 132 to 206, the domain is characterized as Ig-like C2-type.
+At position 1044 to 1086, the domain is characterized as Bromo.
+At position 69 to 161, the domain is characterized as FAR1.
+At position 292 to 388, the domain is characterized as MULE.
+At position 83 to 283, the domain is characterized as Laminin G-like.
+At position 72 to 124, the domain is characterized as bHLH.
+At position 4 to 31, the domain is characterized as Lipoyl-binding.
+At position 69 to 109, the domain is characterized as VM.
+At position 270 to 305, the domain is characterized as EF-hand 1.
+At position 337 to 358, the domain is characterized as EF-hand 2.
+At position 465 to 500, the domain is characterized as EF-hand 3.
+At position 45 to 90, the domain is characterized as AWS.
+At position 92 to 209, the domain is characterized as SET.
+At position 216 to 232, the domain is characterized as Post-SET.
+At position 501 to 534, the domain is characterized as WW.
+At position 91 to 160, the domain is characterized as BTB.
+At position 195 to 296, the domain is characterized as BACK.
+At position 46 to 112, the domain is characterized as Importin N-terminal.
+At position 127 to 176, the domain is characterized as bHLH.
+At position 625 to 688, the domain is characterized as S1 motif.
+At position 4 to 67, the domain is characterized as Thyroglobulin type-1 1.
+At position 72 to 127, the domain is characterized as Thyroglobulin type-1 2.
+At position 13 to 124, the domain is characterized as CMP/dCMP-type deaminase.
+At position 49 to 107, the domain is characterized as TCP.
+At position 39 to 138, the domain is characterized as Cytochrome b5 heme-binding.
+At position 22 to 281, the domain is characterized as Protein kinase.
+At position 45 to 104, the domain is characterized as Collagen-like.
+At position 150 to 266, the domain is characterized as C-type lectin.
+At position 24 to 796, the domain is characterized as Vitellogenin.
+At position 1402 to 1591, the domain is characterized as VWFD.
+At position 1175 to 1250, the domain is characterized as DEP.
+At position 52 to 189, the domain is characterized as MOSC.
+At position 237 to 342, the domain is characterized as FAD-binding FR-type.
+At position 474 to 561, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 21 to 107, the domain is characterized as Acylphosphatase-like.
+At position 46 to 171, the domain is characterized as PLAT.
+At position 174 to 864, the domain is characterized as Lipoxygenase.
+At position 493 to 666, the domain is characterized as tr-type G.
+At position 244 to 272, the domain is characterized as HhH.
+At position 2 to 100, the domain is characterized as ABM.
+At position 212 to 351, the domain is characterized as TrmE-type G.
+At position 88 to 396, the domain is characterized as Protein kinase.
+At position 36 to 147, the domain is characterized as sHSP.
+At position 7 to 55, the domain is characterized as Tudor-knot.
+At position 122 to 327, the domain is characterized as MRG.
+At position 148 to 285, the domain is characterized as OTU.
+At position 73 to 256, the domain is characterized as RNase H type-2.
+At position 132 to 460, the domain is characterized as Peptidase A1.
+At position 453 to 558, the domain is characterized as Calponin-homology (CH).
+At position 1059 to 1212, the domain is characterized as bMERB.
+At position 304 to 600, the domain is characterized as Protein kinase.
+At position 4 to 237, the domain is characterized as GP-PDE.
+At position 5 to 90, the domain is characterized as Toprim.
+At position 340 to 406, the domain is characterized as S4 RNA-binding.
+At position 639 to 730, the domain is characterized as Fe2OG dioxygenase.
+At position 40 to 264, the domain is characterized as Radical SAM core.
+At position 280 to 329, the domain is characterized as F-box.
+At position 15 to 239, the domain is characterized as Sigma-54 factor interaction; truncated.
+At position 2 to 197, the domain is characterized as Glutamine amidotransferase type-1.
+At position 331 to 477, the domain is characterized as SEFIR.
+At position 169 to 482, the domain is characterized as IF rod.
+At position 338 to 544, the domain is characterized as PNPLA.
+At position 50 to 334, the domain is characterized as Protein kinase.
+At position 81 to 246, the domain is characterized as Laminin G-like.
+At position 619 to 673, the domain is characterized as Collagen-like 1.
+At position 682 to 741, the domain is characterized as Collagen-like 2.
+At position 751 to 810, the domain is characterized as Collagen-like 3.
+At position 826 to 885, the domain is characterized as Collagen-like 4.
+At position 886 to 945, the domain is characterized as Collagen-like 5.
+At position 946 to 1005, the domain is characterized as Collagen-like 6.
+At position 1006 to 1047, the domain is characterized as Collagen-like 7.
+At position 1048 to 1105, the domain is characterized as Collagen-like 8.
+At position 1108 to 1155, the domain is characterized as Collagen-like 9.
+At position 1156 to 1215, the domain is characterized as Collagen-like 10.
+At position 1216 to 1275, the domain is characterized as Collagen-like 11.
+At position 1276 to 1330, the domain is characterized as Collagen-like 12.
+At position 1334 to 1393, the domain is characterized as Collagen-like 13.
+At position 1433 to 1492, the domain is characterized as Collagen-like 14.
+At position 1493 to 1552, the domain is characterized as Collagen-like 15.
+At position 1553 to 1612, the domain is characterized as Collagen-like 16.
+At position 1655 to 1855, the domain is characterized as Fibrillar collagen NC1.
+At position 16 to 266, the domain is characterized as Protein kinase.
+At position 1 to 241, the domain is characterized as Radical SAM core.
+At position 260 to 375, the domain is characterized as C-type lectin.
+At position 273 to 407, the domain is characterized as Ferric oxidoreductase.
+At position 408 to 527, the domain is characterized as FAD-binding FR-type.
+At position 96 to 275, the domain is characterized as FAD-binding PCMH-type.
+At position 553 to 679, the domain is characterized as G8.
+At position 43 to 240, the domain is characterized as Lon N-terminal.
+At position 635 to 817, the domain is characterized as Lon proteolytic.
+At position 112 to 323, the domain is characterized as ATP-grasp.
+At position 2323 to 2358, the domain is characterized as EF-hand 1.
+At position 2366 to 2401, the domain is characterized as EF-hand 2.
+At position 2404 to 2439, the domain is characterized as EF-hand 3.
+At position 317 to 455, the domain is characterized as C-CAP/cofactor C-like.
+At position 220 to 431, the domain is characterized as PCI.
+At position 121 to 167, the domain is characterized as F-box.
+At position 2 to 88, the domain is characterized as Disintegrin.
+At position 1 to 131, the domain is characterized as N-acetyltransferase.
+At position 505 to 692, the domain is characterized as Rab-GAP TBC.
+At position 5 to 65, the domain is characterized as TRAM.
+At position 224 to 491, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 184 to 376, the domain is characterized as Glutamine amidotransferase type-1.
+At position 423 to 604, the domain is characterized as RUN.
+At position 335 to 385, the domain is characterized as FBD.
+At position 4 to 486, the domain is characterized as ADPK.
+At position 7 to 66, the domain is characterized as HTH iclR-type.
+At position 81 to 251, the domain is characterized as IclR-ED.
+At position 186 to 627, the domain is characterized as Protein kinase.
+At position 491 to 749, the domain is characterized as Protein kinase.
+At position 1 to 265, the domain is characterized as CheR-type methyltransferase.
+At position 586 to 699, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 700 to 813, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 886 to 964, the domain is characterized as POLO box.
+At position 11 to 188, the domain is characterized as Helicase ATP-binding.
+At position 539 to 669, the domain is characterized as RLR CTR.
+At position 282 to 472, the domain is characterized as Ku.
+At position 610 to 644, the domain is characterized as SAP.
+At position 200 to 371, the domain is characterized as EngA-type G 2.
+At position 15 to 150, the domain is characterized as Ferritin-like diiron.
+At position 299 to 496, the domain is characterized as Peptidase M12B.
+At position 502 to 588, the domain is characterized as Disintegrin.
+At position 732 to 769, the domain is characterized as EGF-like.
+At position 174 to 259, the domain is characterized as PPIase FKBP-type.
+At position 705 to 788, the domain is characterized as ACT 1.
+At position 815 to 891, the domain is characterized as ACT 2.
+At position 1 to 45, the domain is characterized as Rubredoxin-like.
+At position 15 to 53, the domain is characterized as EGF-like 1.
+At position 54 to 104, the domain is characterized as EGF-like 2; calcium-binding.
+At position 138 to 185, the domain is characterized as GPS.
+At position 38 to 266, the domain is characterized as Radical SAM core.
+At position 7 to 326, the domain is characterized as Helicase ATP-binding.
+At position 18 to 152, the domain is characterized as VOC 1.
+At position 134 to 163, the domain is characterized as KOW.
+At position 25 to 210, the domain is characterized as Lon proteolytic.
+At position 127 to 311, the domain is characterized as CP-type G.
+At position 207 to 362, the domain is characterized as N-acetyltransferase.
+At position 22 to 91, the domain is characterized as H15.
+At position 573 to 670, the domain is characterized as SH2.
+At position 321 to 413, the domain is characterized as ARID.
+At position 17 to 142, the domain is characterized as EamA 1.
+At position 166 to 296, the domain is characterized as EamA 2.
+At position 412 to 446, the domain is characterized as SAP.
+At position 7 to 52, the domain is characterized as SpoVT-AbrB.
+At position 20 to 214, the domain is characterized as DPCK.
+At position 130 to 228, the domain is characterized as Ig-like C2-type 1.
+At position 233 to 315, the domain is characterized as Ig-like C2-type 2.
+At position 227 to 475, the domain is characterized as CN hydrolase.
+At position 199 to 287, the domain is characterized as GAT.
+At position 421 to 518, the domain is characterized as Ricin B-type lectin.
+At position 270 to 460, the domain is characterized as B30.2/SPRY.
+At position 89 to 147, the domain is characterized as TCP.
+At position 23 to 68, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 35 to 248, the domain is characterized as ABC transmembrane type-2.
+At position 115 to 209, the domain is characterized as Toprim.
+At position 165 to 395, the domain is characterized as CP-type G.
+At position 383 to 552, the domain is characterized as tr-type G.
+At position 57 to 194, the domain is characterized as N-terminal Ras-GEF.
+At position 324 to 586, the domain is characterized as Ras-GEF.
+At position 736 to 823, the domain is characterized as Ras-associating.
+At position 113 to 132, the domain is characterized as HhH.
+At position 748 to 1025, the domain is characterized as Autotransporter.
+At position 91 to 511, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 975 to 1260, the domain is characterized as PKS/mFAS DH.
+At position 2468 to 2546, the domain is characterized as Carrier.
+At position 1230 to 1464, the domain is characterized as Fibrillar collagen NC1.
+At position 154 to 346, the domain is characterized as ATP-grasp 1.
+At position 698 to 890, the domain is characterized as ATP-grasp 2.
+At position 960 to 1118, the domain is characterized as MGS-like.
+At position 8 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 235 to 430, the domain is characterized as GMPS ATP-PPase.
+At position 64 to 387, the domain is characterized as Peptidase S8.
+At position 6 to 141, the domain is characterized as SprT-like.
+At position 60 to 294, the domain is characterized as Radical SAM core.
+At position 167 to 240, the domain is characterized as HTH crp-type.
+At position 185 to 229, the domain is characterized as bZIP.
+At position 252 to 469, the domain is characterized as DOG1.
+At position 203 to 305, the domain is characterized as Fe2OG dioxygenase.
+At position 258 to 454, the domain is characterized as GATase cobBQ-type.
+At position 61 to 220, the domain is characterized as TNase-like.
+At position 191 to 443, the domain is characterized as NB-ARC.
+At position 248 to 479, the domain is characterized as NR LBD.
+At position 151 to 363, the domain is characterized as TRUD.
+At position 15 to 66, the domain is characterized as HTH psq-type.
+At position 322 to 414, the domain is characterized as ARID.
+At position 1123 to 1356, the domain is characterized as Fibrillar collagen NC1.
+At position 54 to 122, the domain is characterized as BTB.
+At position 1099 to 1348, the domain is characterized as Glutamine amidotransferase type-1.
+At position 115 to 147, the domain is characterized as LisH.
+At position 221 to 335, the domain is characterized as N-terminal Ras-GEF.
+At position 365 to 591, the domain is characterized as Ras-GEF.
+At position 1 to 102, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 103 to 176, the domain is characterized as H15.
+At position 715 to 989, the domain is characterized as MYST-type HAT.
+At position 66 to 160, the domain is characterized as RRM.
+At position 284 to 359, the domain is characterized as PUA.
+At position 240 to 355, the domain is characterized as C-type lectin.
+At position 181 to 567, the domain is characterized as Peptidase S53.
+At position 374 to 471, the domain is characterized as BEN.
+At position 238 to 274, the domain is characterized as DFDF.
+At position 220 to 297, the domain is characterized as SWIB/MDM2.
+At position 331 to 609, the domain is characterized as ABC transporter 1.
+At position 629 to 958, the domain is characterized as ABC transporter 2.
+At position 174 to 227, the domain is characterized as HAMP.
+At position 364 to 559, the domain is characterized as Histidine kinase.
+At position 166 to 259, the domain is characterized as PDZ.
+At position 346 to 611, the domain is characterized as Protein kinase.
+At position 4 to 233, the domain is characterized as Sigma-54 factor interaction.
+At position 448 to 519, the domain is characterized as PAS.
+At position 319 to 502, the domain is characterized as Helicase ATP-binding.
+At position 530 to 675, the domain is characterized as Helicase C-terminal.
+At position 75 to 152, the domain is characterized as RRM.
+At position 215 to 370, the domain is characterized as DOD-type homing endonuclease.
+At position 32 to 132, the domain is characterized as Glutaredoxin.
+At position 111 to 178, the domain is characterized as BTB.
+At position 213 to 314, the domain is characterized as BACK.
+At position 981 to 1001, the domain is characterized as WH2 1.
+At position 1021 to 1041, the domain is characterized as WH2 2.
+At position 1109 to 1129, the domain is characterized as WH2 3.
+At position 39 to 223, the domain is characterized as tr-type G.
+At position 22 to 150, the domain is characterized as Plastocyanin-like.
+At position 308 to 453, the domain is characterized as JmjC.
+At position 573 to 786, the domain is characterized as FtsK.
+At position 43 to 93, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 65 to 183, the domain is characterized as MTTase N-terminal.
+At position 206 to 436, the domain is characterized as Radical SAM core.
+At position 439 to 502, the domain is characterized as TRAM.
+At position 109 to 138, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 148 to 177, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 47 to 281, the domain is characterized as Radical SAM core.
+At position 8 to 84, the domain is characterized as PDZ.
+At position 88 to 244, the domain is characterized as MyTH4.
+At position 249 to 563, the domain is characterized as FERM.
+At position 872 to 1193, the domain is characterized as Kinesin motor.
+At position 535 to 612, the domain is characterized as Carrier.
+At position 8 to 287, the domain is characterized as CN hydrolase.
+At position 20 to 73, the domain is characterized as F-box.
+At position 113 to 208, the domain is characterized as TAFH.
+At position 164 to 214, the domain is characterized as DHHC.
+At position 172 to 240, the domain is characterized as DRBM.
+At position 6 to 171, the domain is characterized as 3'-5' exonuclease.
+At position 213 to 292, the domain is characterized as HRDC.
+At position 592 to 674, the domain is characterized as Fibronectin type-III 4.
+At position 74 to 418, the domain is characterized as Calpain catalytic.
+At position 650 to 684, the domain is characterized as EF-hand 1.
+At position 693 to 726, the domain is characterized as EF-hand 2.
+At position 723 to 758, the domain is characterized as EF-hand 3.
+At position 788 to 822, the domain is characterized as EF-hand 4.
+At position 389 to 661, the domain is characterized as Protein kinase.
+At position 57 to 174, the domain is characterized as RGS.
+At position 189 to 451, the domain is characterized as Protein kinase.
+At position 452 to 517, the domain is characterized as AGC-kinase C-terminal.
+At position 180 to 441, the domain is characterized as Pterin-binding.
+At position 249 to 323, the domain is characterized as IPT/TIG 1.
+At position 603 to 680, the domain is characterized as IPT/TIG 2.
+At position 704 to 788, the domain is characterized as IPT/TIG 3.
+At position 1171 to 1283, the domain is characterized as Rab-GAP TBC.
+At position 113 to 166, the domain is characterized as Oxytoxin-type inhibitor cystine knot (ICK).
+At position 21 to 118, the domain is characterized as Ig-like.
+At position 438 to 496, the domain is characterized as Kazal-like.
+At position 3 to 263, the domain is characterized as PTS EIID.
+At position 3 to 206, the domain is characterized as MurNAc-LAA.
+At position 20 to 388, the domain is characterized as GBD/FH3.
+At position 601 to 998, the domain is characterized as FH2.
+At position 1134 to 1158, the domain is characterized as DAD.
+At position 247 to 366, the domain is characterized as SET.
+At position 184 to 527, the domain is characterized as PUM-HD.
+At position 8 to 91, the domain is characterized as Phosphagen kinase N-terminal.
+At position 91 to 169, the domain is characterized as RRM.
+At position 49 to 149, the domain is characterized as PA.
+At position 24 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 244, the domain is characterized as Ig-like C2-type 2.
+At position 472 to 761, the domain is characterized as Protein kinase.
+At position 480 to 514, the domain is characterized as ShKT 1.
+At position 523 to 557, the domain is characterized as ShKT 2.
+At position 331 to 402, the domain is characterized as AGC-kinase C-terminal.
+At position 784 to 846, the domain is characterized as RhoBD.
+At position 961 to 1171, the domain is characterized as PH.
+At position 370 to 482, the domain is characterized as PLAT.
+At position 77 to 111, the domain is characterized as EF-hand.
+At position 5 to 201, the domain is characterized as DPCK.
+At position 28 to 111, the domain is characterized as EF-hand-like.
+At position 112 to 256, the domain is characterized as PI-PLC X-box.
+At position 314 to 430, the domain is characterized as PI-PLC Y-box.
+At position 430 to 560, the domain is characterized as C2.
+At position 1 to 55, the domain is characterized as HTH lacI-type.
+At position 17 to 655, the domain is characterized as Vitellogenin.
+At position 1490 to 1675, the domain is characterized as VWFD.
+At position 81 to 359, the domain is characterized as Rab-GAP TBC.
+At position 12 to 60, the domain is characterized as GYF.
+At position 241 to 457, the domain is characterized as Helicase ATP-binding.
+At position 497 to 665, the domain is characterized as Helicase C-terminal.
+At position 324 to 498, the domain is characterized as PCI.
+At position 1 to 40, the domain is characterized as Chitin-binding type-1.
+At position 39 to 278, the domain is characterized as Peptidase S1.
+At position 71 to 270, the domain is characterized as Glutamine amidotransferase type-1.
+At position 76 to 206, the domain is characterized as Fido.
+At position 509 to 624, the domain is characterized as SMC hinge.
+At position 32 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 87 to 179, the domain is characterized as FAR1.
+At position 299 to 395, the domain is characterized as MULE.
+At position 629 to 712, the domain is characterized as BRCT.
+At position 2 to 75, the domain is characterized as Lipoyl-binding 1.
+At position 105 to 178, the domain is characterized as Lipoyl-binding 2.
+At position 206 to 279, the domain is characterized as Lipoyl-binding 3.
+At position 328 to 365, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 229 to 476, the domain is characterized as Ku.
+At position 35 to 155, the domain is characterized as Bulb-type lectin.
+At position 350 to 433, the domain is characterized as PAN.
+At position 528 to 779, the domain is characterized as Protein kinase.
+At position 17 to 201, the domain is characterized as RNase H type-2.
+At position 368 to 430, the domain is characterized as HTH myb-type 1.
+At position 431 to 482, the domain is characterized as HTH myb-type 2.
+At position 484 to 546, the domain is characterized as Myb-like.
+At position 436 to 546, the domain is characterized as STAS.
+At position 74 to 160, the domain is characterized as PB1.
+At position 71 to 518, the domain is characterized as Biotin carboxylation.
+At position 190 to 387, the domain is characterized as ATP-grasp.
+At position 658 to 737, the domain is characterized as Biotinyl-binding.
+At position 240 to 294, the domain is characterized as SOCS box.
+At position 771 to 845, the domain is characterized as Carrier 1.
+At position 2282 to 2357, the domain is characterized as Carrier 2.
+At position 30 to 79, the domain is characterized as KH.
+At position 15 to 328, the domain is characterized as Tyrosine-protein phosphatase.
+At position 217 to 411, the domain is characterized as Peptidase M12B.
+At position 418 to 467, the domain is characterized as Disintegrin.
+At position 77 to 252, the domain is characterized as FAD-binding PCMH-type.
+At position 25 to 155, the domain is characterized as Nudix hydrolase.
+At position 31 to 78, the domain is characterized as WAP.
+At position 3 to 277, the domain is characterized as Tyrosine-protein phosphatase.
+At position 124 to 178, the domain is characterized as bHLH.
+At position 21 to 247, the domain is characterized as Radical SAM core.
+At position 1 to 154, the domain is characterized as SPX.
+At position 47 to 262, the domain is characterized as Rab-GAP TBC.
+At position 343 to 554, the domain is characterized as TLDc.
+At position 7 to 64, the domain is characterized as S4 RNA-binding.
+At position 49 to 114, the domain is characterized as NAC-A/B.
+At position 170 to 209, the domain is characterized as UBA.
+At position 232 to 375, the domain is characterized as VPS9.
+At position 558 to 620, the domain is characterized as KH.
+At position 228 to 287, the domain is characterized as SH3.
+At position 213 to 311, the domain is characterized as HTH araC/xylS-type.
+At position 76 to 161, the domain is characterized as RCK C-terminal.
+At position 298 to 438, the domain is characterized as NTR.
+At position 47 to 332, the domain is characterized as Protein kinase.
+At position 68 to 127, the domain is characterized as CBS 1.
+At position 134 to 189, the domain is characterized as CBS 2.
+At position 235 to 294, the domain is characterized as CBS 3.
+At position 302 to 360, the domain is characterized as CBS 4.
+At position 414 to 502, the domain is characterized as PB1.
+At position 656 to 714, the domain is characterized as PAP-associated.
+At position 30 to 154, the domain is characterized as C2.
+At position 221 to 254, the domain is characterized as WW 1.
+At position 414 to 447, the domain is characterized as WW 2.
+At position 526 to 559, the domain is characterized as WW 3.
+At position 577 to 610, the domain is characterized as WW 4.
+At position 669 to 1003, the domain is characterized as HECT.
+At position 420 to 503, the domain is characterized as RRM 2.
+At position 21 to 74, the domain is characterized as SANT.
+At position 126 to 182, the domain is characterized as HTH myb-type.
+At position 346 to 516, the domain is characterized as tr-type G.
+At position 4 to 67, the domain is characterized as HTH asnC-type.
+At position 292 to 370, the domain is characterized as B5.
+At position 41 to 235, the domain is characterized as Helicase ATP-binding.
+At position 265 to 429, the domain is characterized as Helicase C-terminal.
+At position 69 to 88, the domain is characterized as UIM 1.
+At position 101 to 120, the domain is characterized as UIM 2.
+At position 170 to 230, the domain is characterized as LIM zinc-binding.
+At position 27 to 68, the domain is characterized as Chitin-binding type-1 1.
+At position 69 to 111, the domain is characterized as Chitin-binding type-1 2.
+At position 112 to 154, the domain is characterized as Chitin-binding type-1 3.
+At position 155 to 197, the domain is characterized as Chitin-binding type-1 4.
+At position 86 to 159, the domain is characterized as J.
+At position 447 to 509, the domain is characterized as SANT 1.
+At position 757 to 821, the domain is characterized as SAM.
+At position 413 to 630, the domain is characterized as B30.2/SPRY.
+At position 52 to 172, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 191 to 296, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 259 to 425, the domain is characterized as NIDO.
+At position 656 to 807, the domain is characterized as AMOP.
+At position 820 to 1028, the domain is characterized as VWFD.
+At position 1119 to 1179, the domain is characterized as Sushi.
+At position 54 to 146, the domain is characterized as PPIase FKBP-type.
+At position 352 to 415, the domain is characterized as bZIP.
+At position 44 to 313, the domain is characterized as Septin-type G.
+At position 257 to 448, the domain is characterized as B30.2/SPRY.
+At position 24 to 119, the domain is characterized as HTH arsR-type.
+At position 4 to 57, the domain is characterized as Kazal-like.
+At position 154 to 611, the domain is characterized as Urease.
+At position 223 to 434, the domain is characterized as Peptidase M12B.
+At position 444 to 519, the domain is characterized as Disintegrin.
+At position 520 to 575, the domain is characterized as TSP type-1 1.
+At position 801 to 860, the domain is characterized as TSP type-1 2.
+At position 861 to 917, the domain is characterized as TSP type-1 3.
+At position 922 to 975, the domain is characterized as TSP type-1 4.
+At position 1320 to 1368, the domain is characterized as TSP type-1 5.
+At position 1371 to 1431, the domain is characterized as TSP type-1 6.
+At position 1433 to 1476, the domain is characterized as TSP type-1 7.
+At position 1478 to 1538, the domain is characterized as TSP type-1 8.
+At position 1541 to 1581, the domain is characterized as PLAC.
+At position 448 to 522, the domain is characterized as POU-specific.
+At position 526 to 602, the domain is characterized as Carrier 1.
+At position 1584 to 1662, the domain is characterized as Carrier 2.
+At position 10 to 72, the domain is characterized as TRAM.
+At position 372 to 425, the domain is characterized as Collagen-like 5.
+At position 447 to 505, the domain is characterized as Collagen-like 6.
+At position 571 to 630, the domain is characterized as Collagen-like 7.
+At position 482 to 700, the domain is characterized as tr-type G.
+At position 130 to 159, the domain is characterized as KOW.
+At position 310 to 450, the domain is characterized as RanBD1.
+At position 659 to 736, the domain is characterized as RRM 3.
+At position 60 to 151, the domain is characterized as Cadherin 1.
+At position 152 to 259, the domain is characterized as Cadherin 2.
+At position 375 to 480, the domain is characterized as Cadherin 4.
+At position 481 to 589, the domain is characterized as Cadherin 5.
+At position 88 to 266, the domain is characterized as ABC transmembrane type-1.
+At position 756 to 1082, the domain is characterized as Protein kinase.
+At position 1083 to 1203, the domain is characterized as AGC-kinase C-terminal.
+At position 29 to 56, the domain is characterized as LRRNT.
+At position 606 to 643, the domain is characterized as LRRCT.
+At position 196 to 365, the domain is characterized as PCI.
+At position 23 to 349, the domain is characterized as Transferrin-like 1.
+At position 363 to 691, the domain is characterized as Transferrin-like 2.
+At position 47 to 407, the domain is characterized as Peptidase A1.
+At position 32 to 61, the domain is characterized as LRRNT.
+At position 148 to 196, the domain is characterized as LRRCT.
+At position 197 to 282, the domain is characterized as Ig-like C2-type 1.
+At position 295 to 365, the domain is characterized as Ig-like C2-type 2.
+At position 537 to 806, the domain is characterized as Protein kinase.
+At position 51 to 233, the domain is characterized as FAD-binding PCMH-type.
+At position 538 to 669, the domain is characterized as AXH.
+At position 451 to 516, the domain is characterized as SAM 1.
+At position 529 to 593, the domain is characterized as SAM 2.
+At position 617 to 684, the domain is characterized as SAM 3.
+At position 131 to 231, the domain is characterized as Fibronectin type-III 1.
+At position 322 to 417, the domain is characterized as Fibronectin type-III 2.
+At position 419 to 511, the domain is characterized as Fibronectin type-III 3.
+At position 144 to 254, the domain is characterized as Cystatin fetuin-A-type 2.
+At position 2 to 269, the domain is characterized as Glutamine amidotransferase type-2.
+At position 353 to 492, the domain is characterized as SIS 1.
+At position 524 to 667, the domain is characterized as SIS 2.
+At position 420 to 604, the domain is characterized as N-acetyltransferase.
+At position 21 to 142, the domain is characterized as C-type lysozyme.
+At position 358 to 489, the domain is characterized as Plus3.
+At position 521 to 823, the domain is characterized as NB-ARC.
+At position 1248 to 1312, the domain is characterized as HMA.
+At position 97 to 131, the domain is characterized as SAP.
+At position 3 to 152, the domain is characterized as N-acetyltransferase.
+At position 47 to 84, the domain is characterized as ShKT.
+At position 209 to 409, the domain is characterized as Rho-GAP.
+At position 100 to 272, the domain is characterized as Helicase ATP-binding.
+At position 73 to 394, the domain is characterized as Peptidase A1.
+At position 237 to 250, the domain is characterized as CRIB.
+At position 472 to 723, the domain is characterized as Protein kinase.
+At position 793 to 844, the domain is characterized as GPS.
+At position 320 to 537, the domain is characterized as ABC transporter 2.
+At position 148 to 357, the domain is characterized as ATP-grasp.
+At position 263 to 372, the domain is characterized as PAZ.
+At position 538 to 829, the domain is characterized as Piwi.
+At position 561 to 622, the domain is characterized as KH.
+At position 642 to 711, the domain is characterized as S1 motif.
+At position 23 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 115 to 663, the domain is characterized as Lipoxygenase.
+At position 73 to 382, the domain is characterized as Peptidase A1.
+At position 23 to 249, the domain is characterized as PARP catalytic.
+At position 238 to 305, the domain is characterized as RST.
+At position 171 to 249, the domain is characterized as Thyroglobulin type-1.
+At position 2329 to 2406, the domain is characterized as Carrier.
+At position 1531 to 1758, the domain is characterized as Rap-GAP.
+At position 52 to 564, the domain is characterized as Protein kinase.
+At position 496 to 672, the domain is characterized as Helicase C-terminal.
+At position 61 to 143, the domain is characterized as Core-binding (CB).
+At position 164 to 362, the domain is characterized as Tyr recombinase.
+At position 2 to 68, the domain is characterized as Thioredoxin.
+At position 1 to 179, the domain is characterized as PBS-linker.
+At position 8 to 313, the domain is characterized as IF rod.
+At position 18 to 100, the domain is characterized as SUEL-type lectin 1.
+At position 107 to 196, the domain is characterized as SUEL-type lectin 2.
+At position 191 to 478, the domain is characterized as Dynamin-type G.
+At position 214 to 522, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 215 to 297, the domain is characterized as SPAZ 1.
+At position 359 to 507, the domain is characterized as SPAZ 2.
+At position 42 to 83, the domain is characterized as Chitin-binding type-1 1.
+At position 84 to 127, the domain is characterized as Chitin-binding type-1 2.
+At position 128 to 170, the domain is characterized as Chitin-binding type-1 3.
+At position 171 to 211, the domain is characterized as Chitin-binding type-1 4.
+At position 212 to 252, the domain is characterized as Chitin-binding type-1 5.
+At position 253 to 293, the domain is characterized as Chitin-binding type-1 6.
+At position 294 to 335, the domain is characterized as Chitin-binding type-1 7.
+At position 23 to 165, the domain is characterized as SprT-like.
+At position 325 to 498, the domain is characterized as PCI.
+At position 103 to 174, the domain is characterized as KRAB.
+At position 56 to 325, the domain is characterized as Protein kinase.
+At position 372 to 407, the domain is characterized as EF-hand 1.
+At position 416 to 451, the domain is characterized as EF-hand 2.
+At position 452 to 487, the domain is characterized as EF-hand 3.
+At position 488 to 521, the domain is characterized as EF-hand 4.
+At position 339 to 416, the domain is characterized as Carrier.
+At position 76 to 198, the domain is characterized as HD.
+At position 48 to 329, the domain is characterized as GH18.
+At position 11 to 227, the domain is characterized as DHFR.
+At position 14 to 124, the domain is characterized as MTTase N-terminal.
+At position 392 to 468, the domain is characterized as TRAM.
+At position 116 to 325, the domain is characterized as TLC.
+At position 289 to 474, the domain is characterized as GATase cobBQ-type.
+At position 190 to 239, the domain is characterized as KH.
+At position 5 to 66, the domain is characterized as HTH IS21-type.
+At position 111 to 285, the domain is characterized as Integrase catalytic.
+At position 341 to 410, the domain is characterized as ACT.
+At position 1 to 102, the domain is characterized as PTS EIIB type-3.
+At position 474 to 966, the domain is characterized as USP.
+At position 1036 to 1208, the domain is characterized as Exonuclease.
+At position 34 to 112, the domain is characterized as Carrier.
+At position 430 to 624, the domain is characterized as SSD.
+At position 84 to 248, the domain is characterized as FAS1.
+At position 30 to 497, the domain is characterized as Sema.
+At position 499 to 552, the domain is characterized as PSI.
+At position 557 to 645, the domain is characterized as Ig-like C2-type.
+At position 76 to 152, the domain is characterized as ACT.
+At position 472 to 532, the domain is characterized as Kazal-like.
+At position 352 to 441, the domain is characterized as Ig-like.
+At position 229 to 496, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 63 to 146, the domain is characterized as AB hydrolase-1.
+At position 297 to 408, the domain is characterized as Guanylate cyclase.
+At position 30 to 187, the domain is characterized as PPIase cyclophilin-type.
+At position 21 to 301, the domain is characterized as ABC transmembrane type-1 1.
+At position 334 to 568, the domain is characterized as ABC transporter 1.
+At position 628 to 910, the domain is characterized as ABC transmembrane type-1 2.
+At position 942 to 1177, the domain is characterized as ABC transporter 2.
+At position 139 to 369, the domain is characterized as Radical SAM core.
+At position 89 to 131, the domain is characterized as LDL-receptor class A.
+At position 1 to 253, the domain is characterized as Radical SAM core.
+At position 10 to 204, the domain is characterized as YrdC-like.
+At position 21 to 46, the domain is characterized as IQ.
+At position 572 to 607, the domain is characterized as EF-hand 1.
+At position 656 to 691, the domain is characterized as EF-hand 2.
+At position 696 to 731, the domain is characterized as EF-hand 3.
+At position 419 to 538, the domain is characterized as SMC hinge.
+At position 1 to 221, the domain is characterized as Peptidase S1.
+At position 382 to 626, the domain is characterized as Clu.
+At position 84 to 789, the domain is characterized as Myosin motor.
+At position 792 to 821, the domain is characterized as IQ.
+At position 41 to 114, the domain is characterized as H15.
+At position 267 to 468, the domain is characterized as B30.2/SPRY.
+At position 332 to 382, the domain is characterized as FBD.
+At position 143 to 415, the domain is characterized as Protein kinase.
+At position 384 to 435, the domain is characterized as FBD.
+At position 25 to 198, the domain is characterized as N-acetyltransferase.
+At position 47 to 92, the domain is characterized as F-box.
+At position 30 to 122, the domain is characterized as 3'-5' exonuclease.
+At position 4 to 60, the domain is characterized as TIL.
+At position 240 to 411, the domain is characterized as PCI.
+At position 457 to 676, the domain is characterized as FtsK.
+At position 70 to 150, the domain is characterized as GS beta-grasp.
+At position 154 to 423, the domain is characterized as GS catalytic.
+At position 288 to 520, the domain is characterized as TLDc.
+At position 404 to 479, the domain is characterized as RRM 3.
+At position 1 to 146, the domain is characterized as Alpha-carbonic anhydrase.
+At position 67 to 171, the domain is characterized as PRD 1.
+At position 172 to 278, the domain is characterized as PRD 2.
+At position 32 to 167, the domain is characterized as MPN.
+At position 41 to 166, the domain is characterized as PLAT.
+At position 169 to 861, the domain is characterized as Lipoxygenase.
+At position 167 to 253, the domain is characterized as Toprim.
+At position 98 to 360, the domain is characterized as AB hydrolase-1.
+At position 23 to 288, the domain is characterized as PPM-type phosphatase.
+At position 204 to 233, the domain is characterized as GS.
+At position 234 to 525, the domain is characterized as Protein kinase.
+At position 32 to 120, the domain is characterized as Ig-like C2-type.
+At position 174 to 202, the domain is characterized as ITAM.
+At position 152 to 251, the domain is characterized as SH2.
+At position 538 to 805, the domain is characterized as Ras-GEF.
+At position 384 to 631, the domain is characterized as ABC transporter.
+At position 793 to 1044, the domain is characterized as ABC transmembrane type-2.
+At position 60 to 246, the domain is characterized as Rab-GAP TBC.
+At position 19 to 179, the domain is characterized as uDENN.
+At position 199 to 330, the domain is characterized as cDENN.
+At position 332 to 437, the domain is characterized as dDENN.
+At position 275 to 495, the domain is characterized as Fibrinogen C-terminal.
+At position 135 to 215, the domain is characterized as PDZ 2.
+At position 76 to 263, the domain is characterized as B30.2/SPRY.
+At position 32 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 775 to 958, the domain is characterized as PCI.
+At position 324 to 411, the domain is characterized as PPIase FKBP-type.
+At position 341 to 421, the domain is characterized as OCT.
+At position 259 to 589, the domain is characterized as Protein kinase.
+At position 190 to 240, the domain is characterized as LRRCT.
+At position 247 to 344, the domain is characterized as Ig-like.
+At position 707 to 758, the domain is characterized as GPS.
+At position 1 to 289, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 411 to 602, the domain is characterized as FtsK.
+At position 232 to 409, the domain is characterized as NodB homology.
+At position 219 to 282, the domain is characterized as bZIP.
+At position 88 to 175, the domain is characterized as Rieske.
+At position 284 to 361, the domain is characterized as TFIIS N-terminal.
+At position 43 to 161, the domain is characterized as tRNA-binding.
+At position 436 to 519, the domain is characterized as B5.
+At position 736 to 828, the domain is characterized as FDX-ACB.
+At position 832 to 899, the domain is characterized as SH3 1.
+At position 995 to 1083, the domain is characterized as Fibronectin type-III 1.
+At position 1088 to 1184, the domain is characterized as Fibronectin type-III 2.
+At position 1452 to 1520, the domain is characterized as SH3 2.
+At position 1569 to 1636, the domain is characterized as SH3 3.
+At position 31 to 252, the domain is characterized as L-type lectin-like.
+At position 11 to 73, the domain is characterized as SH3.
+At position 17 to 283, the domain is characterized as OBG-type G.
+At position 312 to 398, the domain is characterized as TGS.
+At position 321 to 412, the domain is characterized as PUA.
+At position 382 to 517, the domain is characterized as YTH.
+At position 359 to 471, the domain is characterized as PLAT.
+At position 75 to 133, the domain is characterized as Cadherin 1.
+At position 130 to 208, the domain is characterized as Ig-like C2-type 1.
+At position 209 to 318, the domain is characterized as Ig-like C2-type 2.
+At position 319 to 374, the domain is characterized as Ig-like C2-type 3.
+At position 145 to 199, the domain is characterized as HTH myb-type 1.
+At position 225 to 279, the domain is characterized as HTH myb-type 2.
+At position 525 to 624, the domain is characterized as SWIRM.
+At position 778 to 921, the domain is characterized as MPN.
+At position 324 to 503, the domain is characterized as PCI.
+At position 8 to 251, the domain is characterized as ABC transporter.
+At position 156 to 510, the domain is characterized as Protein kinase.
+At position 246 to 488, the domain is characterized as ATP-grasp.
+At position 75 to 570, the domain is characterized as Peptidase S8.
+At position 383 to 469, the domain is characterized as SANTA.
+At position 875 to 930, the domain is characterized as SANT.
+At position 425 to 511, the domain is characterized as DEP.
+At position 540 to 685, the domain is characterized as RGS.
+At position 305 to 345, the domain is characterized as UBA.
+At position 48 to 82, the domain is characterized as ShKT.
+At position 456 to 639, the domain is characterized as Lon proteolytic.
+At position 522 to 639, the domain is characterized as SMC hinge.
+At position 320 to 579, the domain is characterized as Protein kinase.
+At position 8 to 207, the domain is characterized as Lon N-terminal.
+At position 595 to 774, the domain is characterized as Lon proteolytic.
+At position 69 to 134, the domain is characterized as NAC-A/B.
+At position 175 to 212, the domain is characterized as UBA.
+At position 34 to 223, the domain is characterized as uDENN FNIP1/2-type.
+At position 231 to 723, the domain is characterized as cDENN FNIP1/2-type.
+At position 731 to 836, the domain is characterized as dDENN FNIP1/2-type.
+At position 1077 to 1113, the domain is characterized as LDL-receptor class A 1.
+At position 1116 to 1154, the domain is characterized as LDL-receptor class A 2.
+At position 1157 to 1193, the domain is characterized as LDL-receptor class A 3.
+At position 1234 to 1272, the domain is characterized as LDL-receptor class A 5.
+At position 1274 to 1316, the domain is characterized as LDL-receptor class A 6.
+At position 1324 to 1360, the domain is characterized as LDL-receptor class A 7.
+At position 1367 to 1404, the domain is characterized as LDL-receptor class A 8.
+At position 1418 to 1454, the domain is characterized as LDL-receptor class A 9.
+At position 1470 to 1507, the domain is characterized as LDL-receptor class A 10.
+At position 1513 to 1550, the domain is characterized as LDL-receptor class A 11.
+At position 1747 to 1843, the domain is characterized as Fibronectin type-III 3.
+At position 333 to 418, the domain is characterized as PDZ.
+At position 652 to 764, the domain is characterized as FAD-binding FR-type.
+At position 16 to 148, the domain is characterized as ENTH.
+At position 183 to 225, the domain is characterized as CAP-Gly.
+At position 229 to 460, the domain is characterized as Peptidase S1.
+At position 327 to 361, the domain is characterized as EGF-like 1; incomplete.
+At position 362 to 402, the domain is characterized as EGF-like 2; calcium-binding.
+At position 403 to 443, the domain is characterized as EGF-like 3.
+At position 441 to 483, the domain is characterized as EGF-like 4.
+At position 747 to 787, the domain is characterized as EGF-like 5.
+At position 838 to 876, the domain is characterized as EGF-like 6.
+At position 877 to 918, the domain is characterized as EGF-like 7; calcium-binding.
+At position 919 to 959, the domain is characterized as EGF-like 8; calcium-binding.
+At position 978 to 1019, the domain is characterized as EGF-like 9.
+At position 70 to 375, the domain is characterized as Protein kinase.
+At position 242 to 355, the domain is characterized as C-type lectin.
+At position 405 to 729, the domain is characterized as MCM.
+At position 768 to 1045, the domain is characterized as Protein kinase.
+At position 290 to 534, the domain is characterized as Glutamine amidotransferase type-1.
+At position 20 to 84, the domain is characterized as NAC-A/B.
+At position 54 to 132, the domain is characterized as RRM 1.
+At position 142 to 219, the domain is characterized as RRM 2.
+At position 235 to 312, the domain is characterized as RRM 3.
+At position 338 to 472, the domain is characterized as RRM 4.
+At position 658 to 731, the domain is characterized as PABC.
+At position 106 to 158, the domain is characterized as SANT.
+At position 476 to 567, the domain is characterized as SWIRM.
+At position 27 to 206, the domain is characterized as VWFA 1.
+At position 229 to 411, the domain is characterized as VWFA 2.
+At position 436 to 606, the domain is characterized as VWFA 3.
+At position 622 to 791, the domain is characterized as VWFA 4.
+At position 809 to 982, the domain is characterized as VWFA 5.
+At position 1000 to 1171, the domain is characterized as VWFA 6.
+At position 1187 to 1371, the domain is characterized as VWFA 7.
+At position 1757 to 1937, the domain is characterized as VWFA 8.
+At position 1965 to 2166, the domain is characterized as VWFA 9.
+At position 118 to 494, the domain is characterized as Protein kinase.
+At position 5 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 231 to 346, the domain is characterized as Calponin-homology (CH).
+At position 1421 to 1555, the domain is characterized as CKK.
+At position 222 to 391, the domain is characterized as tr-type G.
+At position 967 to 1109, the domain is characterized as Peptidase S59.
+At position 386 to 715, the domain is characterized as PDEase.
+At position 18 to 216, the domain is characterized as Lon N-terminal.
+At position 26 to 57, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 59 to 86, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 224 to 447, the domain is characterized as Helicase ATP-binding.
+At position 432 to 581, the domain is characterized as Helicase C-terminal.
+At position 358 to 527, the domain is characterized as tr-type G.
+At position 112 to 147, the domain is characterized as EF-hand 3.
+At position 343 to 422, the domain is characterized as Ubiquitin-like.
+At position 530 to 589, the domain is characterized as HTH myb-type.
+At position 9 to 192, the domain is characterized as Ku.
+At position 291 to 356, the domain is characterized as Mop.
+At position 194 to 428, the domain is characterized as Grh/CP2 DB.
+At position 16 to 146, the domain is characterized as RNase III.
+At position 183 to 409, the domain is characterized as NR LBD.
+At position 154 to 260, the domain is characterized as THUMP.
+At position 105 to 186, the domain is characterized as Core-binding (CB).
+At position 209 to 386, the domain is characterized as Tyr recombinase.
+At position 93 to 358, the domain is characterized as Peptidase S1.
+At position 475 to 548, the domain is characterized as HSA.
+At position 713 to 773, the domain is characterized as Myb-like.
+At position 1 to 129, the domain is characterized as BFN.
+At position 35 to 293, the domain is characterized as Protein kinase.
+At position 7 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 414 to 522, the domain is characterized as Fe2OG dioxygenase.
+At position 132 to 351, the domain is characterized as Radical SAM core.
+At position 224 to 425, the domain is characterized as Histidine kinase.
+At position 65 to 98, the domain is characterized as Orange.
+At position 148 to 304, the domain is characterized as Helicase ATP-binding.
+At position 405 to 577, the domain is characterized as Helicase C-terminal.
+At position 195 to 407, the domain is characterized as Helicase ATP-binding.
+At position 458 to 633, the domain is characterized as Helicase C-terminal.
+At position 442 to 533, the domain is characterized as GS beta-grasp.
+At position 540 to 865, the domain is characterized as GS catalytic.
+At position 525 to 620, the domain is characterized as SMC hinge.
+At position 219 to 291, the domain is characterized as Plastocyanin-like.
+At position 192 to 571, the domain is characterized as GRAS.
+At position 316 to 511, the domain is characterized as PCI.
+At position 74 to 352, the domain is characterized as Protein kinase.
+At position 59 to 186, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 366 to 526, the domain is characterized as Integrase catalytic.
+At position 450 to 728, the domain is characterized as Protein kinase.
+At position 76 to 268, the domain is characterized as ABC transmembrane type-1.
+At position 28 to 118, the domain is characterized as GOLD.
+At position 52 to 163, the domain is characterized as sHSP.
+At position 123 to 209, the domain is characterized as PDZ.
+At position 598 to 722, the domain is characterized as C2.
+At position 755 to 949, the domain is characterized as Rho-GAP.
+At position 102 to 307, the domain is characterized as ATP-grasp.
+At position 1 to 72, the domain is characterized as Ubiquitin-like 1.
+At position 73 to 148, the domain is characterized as Ubiquitin-like 2.
+At position 149 to 224, the domain is characterized as Ubiquitin-like 3.
+At position 225 to 300, the domain is characterized as Ubiquitin-like 4.
+At position 301 to 376, the domain is characterized as Ubiquitin-like 5.
+At position 43 to 107, the domain is characterized as J.
+At position 9 to 127, the domain is characterized as DMAP1-binding.
+At position 163 to 336, the domain is characterized as OBG-type G.
+At position 361 to 439, the domain is characterized as OCT.
+At position 1 to 262, the domain is characterized as Peptidase A1.
+At position 298 to 363, the domain is characterized as Mop.
+At position 370 to 437, the domain is characterized as BTB 1.
+At position 470 to 499, the domain is characterized as BTB 2.
+At position 24 to 248, the domain is characterized as Radical SAM core.
+At position 450 to 529, the domain is characterized as RRM 1.
+At position 551 to 628, the domain is characterized as RRM 2.
+At position 284 to 443, the domain is characterized as W2.
+At position 54 to 163, the domain is characterized as PA.
+At position 415 to 525, the domain is characterized as SET.
+At position 399 to 524, the domain is characterized as CRC.
+At position 41 to 338, the domain is characterized as GH10.
+At position 294 to 372, the domain is characterized as PUA.
+At position 110 to 169, the domain is characterized as CBS 1.
+At position 173 to 231, the domain is characterized as CBS 2.
+At position 94 to 162, the domain is characterized as PRC barrel.
+At position 22 to 381, the domain is characterized as GH18.
+At position 242 to 342, the domain is characterized as BTB.
+At position 29 to 141, the domain is characterized as Ig-like V-type 1.
+At position 149 to 235, the domain is characterized as Ig-like V-type 2.
+At position 286 to 480, the domain is characterized as B30.2/SPRY.
+At position 113 to 321, the domain is characterized as ATP-grasp.
+At position 239 to 252, the domain is characterized as CRIB.
+At position 147 to 409, the domain is characterized as Protein kinase.
+At position 757 to 870, the domain is characterized as VRR-NUC.
+At position 103 to 496, the domain is characterized as PPM-type phosphatase.
+At position 188 to 199, the domain is characterized as EGF-like 1.
+At position 219 to 230, the domain is characterized as EGF-like 2.
+At position 250 to 261, the domain is characterized as EGF-like 3.
+At position 281 to 292, the domain is characterized as EGF-like 4.
+At position 312 to 323, the domain is characterized as EGF-like 5.
+At position 328 to 420, the domain is characterized as Fibronectin type-III 1.
+At position 421 to 505, the domain is characterized as Fibronectin type-III 2.
+At position 506 to 595, the domain is characterized as Fibronectin type-III 3.
+At position 596 to 687, the domain is characterized as Fibronectin type-III 4.
+At position 688 to 777, the domain is characterized as Fibronectin type-III 5.
+At position 778 to 865, the domain is characterized as Fibronectin type-III 6.
+At position 866 to 955, the domain is characterized as Fibronectin type-III 7.
+At position 956 to 1042, the domain is characterized as Fibronectin type-III 8.
+At position 1043 to 1130, the domain is characterized as Fibronectin type-III 9.
+At position 1129 to 1344, the domain is characterized as Fibrinogen C-terminal.
+At position 22 to 123, the domain is characterized as Ig-like V-type.
+At position 39 to 114, the domain is characterized as H15.
+At position 347 to 381, the domain is characterized as SAP.
+At position 45 to 239, the domain is characterized as Helicase ATP-binding.
+At position 905 to 962, the domain is characterized as Tudor 1.
+At position 963 to 1019, the domain is characterized as Tudor 2.
+At position 150 to 202, the domain is characterized as bHLH.
+At position 56 to 313, the domain is characterized as Protein kinase.
+At position 14 to 121, the domain is characterized as PINc.
+At position 178 to 420, the domain is characterized as MHD.
+At position 109 to 370, the domain is characterized as GS catalytic.
+At position 6 to 295, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 300 to 371, the domain is characterized as ACT.
+At position 932 to 1067, the domain is characterized as MGS-like.
+At position 8 to 337, the domain is characterized as Kinesin motor.
+At position 71 to 154, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 105 to 182, the domain is characterized as RRM.
+At position 1 to 48, the domain is characterized as RRM.
+At position 115 to 271, the domain is characterized as PPIase cyclophilin-type.
+At position 63 to 166, the domain is characterized as THUMP.
+At position 51 to 361, the domain is characterized as AB hydrolase-1.
+At position 13 to 413, the domain is characterized as Kinesin motor.
+At position 54 to 200, the domain is characterized as Peptidase C51.
+At position 6 to 194, the domain is characterized as Flavodoxin-like.
+At position 357 to 396, the domain is characterized as Chitin-binding type-3.
+At position 145 to 655, the domain is characterized as USP.
+At position 657 to 750, the domain is characterized as DUSP 1.
+At position 759 to 862, the domain is characterized as DUSP 2.
+At position 27 to 244, the domain is characterized as Peptidase S1.
+At position 36 to 119, the domain is characterized as IGFBP N-terminal.
+At position 211 to 286, the domain is characterized as Thyroglobulin type-1.
+At position 11 to 137, the domain is characterized as RNase III.
+At position 164 to 233, the domain is characterized as DRBM.
+At position 158 to 470, the domain is characterized as Peptidase S8.
+At position 22 to 200, the domain is characterized as Guanylate kinase-like.
+At position 427 to 611, the domain is characterized as Senescence.
+At position 29 to 157, the domain is characterized as Ig-like V-type 1.
+At position 160 to 288, the domain is characterized as Ig-like V-type 2.
+At position 590 to 670, the domain is characterized as BRCT.
+At position 38 to 147, the domain is characterized as HTH APSES-type.
+At position 22 to 95, the domain is characterized as H15.
+At position 298 to 351, the domain is characterized as LRRCT.
+At position 405 to 442, the domain is characterized as EGF-like.
+At position 460 to 558, the domain is characterized as Fibronectin type-III.
+At position 50 to 77, the domain is characterized as IQ.
+At position 15 to 267, the domain is characterized as Pyruvate carboxyltransferase.
+At position 284 to 360, the domain is characterized as PUA.
+At position 174 to 329, the domain is characterized as Fibronectin type-III 1.
+At position 451 to 560, the domain is characterized as Fibronectin type-III 2.
+At position 141 to 201, the domain is characterized as MADS-box.
+At position 7 to 258, the domain is characterized as Nudix hydrolase.
+At position 1 to 128, the domain is characterized as Nudix hydrolase.
+At position 47 to 377, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 95 to 213, the domain is characterized as MTTase N-terminal.
+At position 236 to 466, the domain is characterized as Radical SAM core.
+At position 469 to 532, the domain is characterized as TRAM.
+At position 595 to 926, the domain is characterized as Reverse transcriptase.
+At position 32 to 182, the domain is characterized as FZ.
+At position 24 to 67, the domain is characterized as EGF-like.
+At position 70 to 225, the domain is characterized as F5/8 type C 1.
+At position 230 to 387, the domain is characterized as F5/8 type C 2.
+At position 70 to 411, the domain is characterized as Calpain catalytic.
+At position 906 to 935, the domain is characterized as IQ.
+At position 20 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 339 to 572, the domain is characterized as ABC transporter.
+At position 33 to 276, the domain is characterized as ABC transporter.
+At position 3 to 54, the domain is characterized as Myosin N-terminal SH3-like.
+At position 57 to 766, the domain is characterized as Myosin motor.
+At position 808 to 837, the domain is characterized as IQ.
+At position 11 to 223, the domain is characterized as Radical SAM core.
+At position 99 to 336, the domain is characterized as PABS.
+At position 84 to 190, the domain is characterized as PH 1.
+At position 506 to 605, the domain is characterized as PH 2.
+At position 520 to 595, the domain is characterized as RRM.
+At position 415 to 452, the domain is characterized as EF-hand 2.
+At position 453 to 488, the domain is characterized as EF-hand 3.
+At position 198 to 260, the domain is characterized as t-SNARE coiled-coil homology.
+At position 37 to 143, the domain is characterized as Cadherin 1.
+At position 144 to 249, the domain is characterized as Cadherin 2.
+At position 346 to 518, the domain is characterized as Helicase ATP-binding.
+At position 566 to 758, the domain is characterized as Helicase C-terminal.
+At position 96 to 155, the domain is characterized as LIM zinc-binding 1.
+At position 166 to 228, the domain is characterized as LIM zinc-binding 2.
+At position 149 to 208, the domain is characterized as SH3 1.
+At position 249 to 308, the domain is characterized as SH3 2.
+At position 445 to 504, the domain is characterized as SH3 3.
+At position 812 to 871, the domain is characterized as SH3 4.
+At position 1058 to 1119, the domain is characterized as SH3 5.
+At position 1 to 298, the domain is characterized as SPX.
+At position 557 to 750, the domain is characterized as EXS.
+At position 121 to 189, the domain is characterized as H15.
+At position 347 to 409, the domain is characterized as S4 RNA-binding.
+At position 221 to 401, the domain is characterized as PCI.
+At position 1 to 217, the domain is characterized as LXG.
+At position 202 to 512, the domain is characterized as USP.
+At position 344 to 404, the domain is characterized as S4 RNA-binding.
+At position 1 to 216, the domain is characterized as ABC transporter.
+At position 245 to 396, the domain is characterized as Cupin type-1.
+At position 276 to 468, the domain is characterized as B30.2/SPRY.
+At position 197 to 301, the domain is characterized as PpiC 1.
+At position 312 to 411, the domain is characterized as PpiC 2.
+At position 237 to 390, the domain is characterized as Cupin type-1.
+At position 217 to 248, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 222 to 292, the domain is characterized as PAS.
+At position 344 to 541, the domain is characterized as Histidine kinase.
+At position 643 to 702, the domain is characterized as S1 motif.
+At position 37 to 179, the domain is characterized as SIS.
+At position 205 to 264, the domain is characterized as CBS 1.
+At position 273 to 328, the domain is characterized as CBS 2.
+At position 15 to 137, the domain is characterized as MsrB.
+At position 195 to 272, the domain is characterized as PDZ 2.
+At position 380 to 446, the domain is characterized as PDZ 3.
+At position 475 to 549, the domain is characterized as SH3.
+At position 580 to 761, the domain is characterized as Guanylate kinase-like.
+At position 2 to 130, the domain is characterized as HTH rrf2-type.
+At position 22 to 244, the domain is characterized as Peptidase S1.
+At position 110 to 315, the domain is characterized as ATP-grasp.
+At position 69 to 255, the domain is characterized as NodB homology.
+At position 14 to 166, the domain is characterized as MPN.
+At position 392 to 427, the domain is characterized as EF-hand.
+At position 233 to 471, the domain is characterized as PABS.
+At position 13 to 98, the domain is characterized as Tudor-knot.
+At position 216 to 399, the domain is characterized as MRG.
+At position 210 to 295, the domain is characterized as RCK C-terminal 1.
+At position 296 to 379, the domain is characterized as RCK C-terminal 2.
+At position 20 to 94, the domain is characterized as Ubiquitin-like.
+At position 350 to 524, the domain is characterized as Helicase ATP-binding.
+At position 554 to 733, the domain is characterized as Helicase C-terminal.
+At position 277 to 363, the domain is characterized as PPIase FKBP-type.
+At position 18 to 55, the domain is characterized as EGF-like 1.
+At position 366 to 402, the domain is characterized as EGF-like 7.
+At position 443 to 562, the domain is characterized as Avidin-like.
+At position 7 to 154, the domain is characterized as N-acetyltransferase.
+At position 112 to 411, the domain is characterized as PPM-type phosphatase.
+At position 25 to 187, the domain is characterized as MAM.
+At position 189 to 274, the domain is characterized as Ig-like C2-type.
+At position 287 to 382, the domain is characterized as Fibronectin type-III 1.
+At position 385 to 483, the domain is characterized as Fibronectin type-III 2.
+At position 876 to 1132, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1164 to 1427, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 44 to 148, the domain is characterized as MaoC-like.
+At position 345 to 586, the domain is characterized as NR LBD.
+At position 144 to 225, the domain is characterized as RCK C-terminal 1.
+At position 368 to 448, the domain is characterized as RCK C-terminal 2.
+At position 20 to 190, the domain is characterized as PCI.
+At position 84 to 135, the domain is characterized as Chromo 1.
+At position 270 to 320, the domain is characterized as Chromo 2.
+At position 321 to 373, the domain is characterized as Chromo 3.
+At position 83 to 192, the domain is characterized as PX; atypical.
+At position 210 to 272, the domain is characterized as SH3.
+At position 339 to 534, the domain is characterized as Rho-GAP.
+At position 89 to 118, the domain is characterized as IQ.
+At position 51 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 416 to 503, the domain is characterized as Fibronectin type-III.
+At position 33 to 93, the domain is characterized as Sushi 1.
+At position 94 to 155, the domain is characterized as Sushi 2.
+At position 156 to 226, the domain is characterized as Sushi 3.
+At position 228 to 287, the domain is characterized as Sushi 4.
+At position 287 to 347, the domain is characterized as Sushi 5.
+At position 348 to 410, the domain is characterized as Sushi 6.
+At position 411 to 472, the domain is characterized as Sushi 7.
+At position 473 to 543, the domain is characterized as Sushi 8.
+At position 79 to 232, the domain is characterized as Ferritin-like diiron.
+At position 523 to 757, the domain is characterized as NR LBD.
+At position 9 to 269, the domain is characterized as tr-type G.
+At position 61 to 255, the domain is characterized as GH11.
+At position 77 to 132, the domain is characterized as CBS 1.
+At position 254 to 311, the domain is characterized as CBS 2.
+At position 103 to 174, the domain is characterized as SUI1.
+At position 8 to 138, the domain is characterized as B12-binding.
+At position 92 to 127, the domain is characterized as Tify.
+At position 28 to 215, the domain is characterized as GH16.
+At position 93 to 341, the domain is characterized as ABC transporter.
+At position 34 to 100, the domain is characterized as Importin N-terminal.
+At position 227 to 386, the domain is characterized as TrmE-type G.
+At position 124 to 243, the domain is characterized as Collagen-like 1.
+At position 251 to 305, the domain is characterized as Collagen-like 2.
+At position 321 to 380, the domain is characterized as Collagen-like 3.
+At position 412 to 460, the domain is characterized as Collagen-like 4.
+At position 463 to 522, the domain is characterized as Collagen-like 5.
+At position 217 to 367, the domain is characterized as TrmE-type G.
+At position 35 to 68, the domain is characterized as WW 1.
+At position 82 to 115, the domain is characterized as WW 2.
+At position 691 to 811, the domain is characterized as C2.
+At position 161 to 863, the domain is characterized as Lipoxygenase.
+At position 61 to 110, the domain is characterized as P-type 1.
+At position 932 to 978, the domain is characterized as P-type 2.
+At position 48 to 535, the domain is characterized as Sema.
+At position 661 to 740, the domain is characterized as Ig-like C2-type.
+At position 17 to 141, the domain is characterized as VOC 1.
+At position 147 to 274, the domain is characterized as VOC 2.
+At position 30 to 274, the domain is characterized as AB hydrolase-1.
+At position 265 to 394, the domain is characterized as RRM Nup35-type.
+At position 60 to 272, the domain is characterized as DCUN1.
+At position 561 to 623, the domain is characterized as KH.
+At position 633 to 702, the domain is characterized as S1 motif.
+At position 2 to 208, the domain is characterized as ABC transporter.
+At position 57 to 173, the domain is characterized as DOMON.
+At position 23 to 327, the domain is characterized as PPM-type phosphatase.
+At position 40 to 274, the domain is characterized as Radical SAM core.
+At position 327 to 459, the domain is characterized as ZU5 1.
+At position 460 to 601, the domain is characterized as ZU5 2.
+At position 793 to 878, the domain is characterized as Death.
+At position 246 to 346, the domain is characterized as Cadherin 3.
+At position 108 to 186, the domain is characterized as Cytochrome b5 heme-binding.
+At position 1 to 246, the domain is characterized as Radical SAM core.
+At position 189 to 266, the domain is characterized as TFIIS N-terminal.
+At position 226 to 574, the domain is characterized as Peptidase A1.
+At position 276 to 388, the domain is characterized as PAZ.
+At position 552 to 844, the domain is characterized as Piwi.
+At position 42 to 352, the domain is characterized as GH10.
+At position 375 to 484, the domain is characterized as CBM2.
+At position 17 to 217, the domain is characterized as YjeF N-terminal.
+At position 231 to 508, the domain is characterized as YjeF C-terminal.
+At position 172 to 224, the domain is characterized as BSD.
+At position 42 to 124, the domain is characterized as GOLD.
+At position 42 to 232, the domain is characterized as NodB homology.
+At position 566 to 715, the domain is characterized as uDENN.
+At position 737 to 870, the domain is characterized as cDENN.
+At position 872 to 969, the domain is characterized as dDENN.
+At position 32 to 110, the domain is characterized as RRM.
+At position 86 to 206, the domain is characterized as GST C-terminal.
+At position 38 to 329, the domain is characterized as Protein kinase.
+At position 1000 to 1198, the domain is characterized as Laminin G-like 4.
+At position 520 to 826, the domain is characterized as Protein kinase.
+At position 125 to 168, the domain is characterized as LysM.
+At position 746 to 907, the domain is characterized as TLDc.
+At position 41 to 81, the domain is characterized as Chaplin.
+At position 89 to 181, the domain is characterized as Ig-like V-type.
+At position 342 to 407, the domain is characterized as S4 RNA-binding.
+At position 108 to 135, the domain is characterized as IQ 1.
+At position 136 to 158, the domain is characterized as IQ 2.
+At position 22 to 394, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 29 to 133, the domain is characterized as Phytocyanin.
+At position 167 to 267, the domain is characterized as Fe2OG dioxygenase.
+At position 39 to 134, the domain is characterized as Link.
+At position 138 to 199, the domain is characterized as Sushi.
+At position 28 to 84, the domain is characterized as Cystatin.
+At position 49 to 153, the domain is characterized as FAD-binding FR-type.
+At position 307 to 594, the domain is characterized as Protein kinase.
+At position 21 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 208 to 297, the domain is characterized as Ig-like C2-type 3.
+At position 302 to 396, the domain is characterized as Ig-like C2-type 4.
+At position 401 to 491, the domain is characterized as Ig-like C2-type 5.
+At position 495 to 591, the domain is characterized as Fibronectin type-III 1.
+At position 593 to 688, the domain is characterized as Fibronectin type-III 2.
+At position 940 to 1003, the domain is characterized as Tudor.
+At position 25 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 5 to 70, the domain is characterized as HMA.
+At position 55 to 157, the domain is characterized as BMC circularly permuted 1.
+At position 158 to 256, the domain is characterized as BMC circularly permuted 2.
+At position 172 to 362, the domain is characterized as CheB-type methylesterase.
+At position 25 to 160, the domain is characterized as HTH marR-type.
+At position 5 to 198, the domain is characterized as Lon N-terminal.
+At position 588 to 769, the domain is characterized as Lon proteolytic.
+At position 63 to 168, the domain is characterized as THUMP.
+At position 212 to 581, the domain is characterized as GRAS.
+At position 98 to 201, the domain is characterized as Rieske.
+At position 24 to 169, the domain is characterized as MAM 1.
+At position 168 to 329, the domain is characterized as MAM 2.
+At position 340 to 498, the domain is characterized as MAM 3.
+At position 507 to 666, the domain is characterized as MAM 4.
+At position 89 to 392, the domain is characterized as Peptidase A1.
+At position 255 to 440, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 303, the domain is characterized as 5'-3' exonuclease.
+At position 304 to 592, the domain is characterized as 3'-5' exonuclease.
+At position 78 to 302, the domain is characterized as Radical SAM core.
+At position 607 to 653, the domain is characterized as F-box.
+At position 516 to 705, the domain is characterized as Helicase ATP-binding.
+At position 971 to 1125, the domain is characterized as Helicase C-terminal.
+At position 75 to 153, the domain is characterized as Core-binding (CB).
+At position 175 to 364, the domain is characterized as Tyr recombinase.
+At position 56 to 205, the domain is characterized as RUN.
+At position 42 to 115, the domain is characterized as SH3.
+At position 250 to 394, the domain is characterized as Helicase C-terminal.
+At position 141 to 337, the domain is characterized as B30.2/SPRY.
+At position 180 to 416, the domain is characterized as Methyl-accepting transducer.
+At position 287 to 543, the domain is characterized as CN hydrolase.
+At position 14 to 78, the domain is characterized as J.
+At position 2 to 45, the domain is characterized as LysM.
+At position 20 to 100, the domain is characterized as GS beta-grasp.
+At position 107 to 357, the domain is characterized as GS catalytic.
+At position 148 to 401, the domain is characterized as Protein kinase.
+At position 374 to 409, the domain is characterized as EF-hand 1.
+At position 410 to 445, the domain is characterized as EF-hand 2.
+At position 446 to 481, the domain is characterized as EF-hand 3.
+At position 485 to 516, the domain is characterized as EF-hand 4.
+At position 541 to 674, the domain is characterized as C1q.
+At position 38 to 125, the domain is characterized as Ig-like V-type 1.
+At position 156 to 222, the domain is characterized as Ig-like V-type 2.
+At position 253 to 359, the domain is characterized as Ig-like C2-type.
+At position 48 to 227, the domain is characterized as VWFA 1.
+At position 243 to 300, the domain is characterized as Collagen-like 1.
+At position 301 to 358, the domain is characterized as Collagen-like 2.
+At position 501 to 544, the domain is characterized as Collagen-like 3.
+At position 545 to 588, the domain is characterized as Collagen-like 4.
+At position 733 to 769, the domain is characterized as Collagen-like 5.
+At position 798 to 976, the domain is characterized as VWFA 2.
+At position 1088 to 1138, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 47 to 91, the domain is characterized as bZIP.
+At position 114 to 330, the domain is characterized as DOG1.
+At position 1 to 91, the domain is characterized as HIG1.
+At position 8 to 98, the domain is characterized as Acylphosphatase-like.
+At position 1 to 139, the domain is characterized as N-acetyltransferase.
+At position 1051 to 1111, the domain is characterized as SH3.
+At position 24 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 126 to 224, the domain is characterized as Ig-like C2-type 2.
+At position 236 to 318, the domain is characterized as Ig-like C2-type 3.
+At position 325 to 415, the domain is characterized as Fibronectin type-III 1.
+At position 420 to 516, the domain is characterized as Fibronectin type-III 2.
+At position 518 to 607, the domain is characterized as Fibronectin type-III 3.
+At position 612 to 709, the domain is characterized as Fibronectin type-III 4.
+At position 714 to 822, the domain is characterized as Fibronectin type-III 5.
+At position 823 to 916, the domain is characterized as Fibronectin type-III 6.
+At position 921 to 1016, the domain is characterized as Fibronectin type-III 7.
+At position 1020 to 1106, the domain is characterized as Fibronectin type-III 8.
+At position 1357 to 1612, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1644 to 1903, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 223 to 323, the domain is characterized as PKD.
+At position 23 to 148, the domain is characterized as Thioredoxin.
+At position 5 to 233, the domain is characterized as ABC transporter 1.
+At position 68 to 124, the domain is characterized as LIM zinc-binding 1.
+At position 127 to 187, the domain is characterized as LIM zinc-binding 2.
+At position 106 to 240, the domain is characterized as RUN.
+At position 597 to 844, the domain is characterized as Rab-GAP TBC.
+At position 20 to 89, the domain is characterized as PAS 1.
+At position 94 to 145, the domain is characterized as PAC 1.
+At position 185 to 256, the domain is characterized as PAS 2.
+At position 263 to 314, the domain is characterized as PAC 2.
+At position 334 to 548, the domain is characterized as Histidine kinase.
+At position 266 to 336, the domain is characterized as RRM.
+At position 678 to 960, the domain is characterized as Protein kinase.
+At position 206 to 332, the domain is characterized as Cyclin N-terminal.
+At position 1291 to 1411, the domain is characterized as N-terminal Ras-GEF.
+At position 1447 to 1676, the domain is characterized as Ras-GEF.
+At position 924 to 1271, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 339 to 575, the domain is characterized as ABC transporter.
+At position 114 to 230, the domain is characterized as C-type lectin.
+At position 312 to 358, the domain is characterized as LysM.
+At position 467 to 510, the domain is characterized as Chitin-binding type-1.
+At position 306 to 539, the domain is characterized as Glutamine amidotransferase type-1.
+At position 23 to 127, the domain is characterized as Ig-like V-type 1.
+At position 319 to 397, the domain is characterized as Ig-like C2-type 2.
+At position 28 to 115, the domain is characterized as KRAB.
+At position 99 to 185, the domain is characterized as Ras-associating.
+At position 228 to 341, the domain is characterized as PH.
+At position 434 to 530, the domain is characterized as SH2.
+At position 503 to 565, the domain is characterized as R3H.
+At position 51 to 255, the domain is characterized as Velvet.
+At position 605 to 669, the domain is characterized as DDT.
+At position 1352 to 1422, the domain is characterized as Bromo.
+At position 39 to 129, the domain is characterized as Ig-like C2-type 1.
+At position 17 to 120, the domain is characterized as Ig-like V-type.
+At position 145 to 228, the domain is characterized as Ig-like C2-type.
+At position 61 to 347, the domain is characterized as Protein kinase.
+At position 135 to 235, the domain is characterized as Fibronectin type-III.
+At position 284 to 414, the domain is characterized as Nop.
+At position 93 to 242, the domain is characterized as Exonuclease.
+At position 13 to 206, the domain is characterized as Lon N-terminal.
+At position 1 to 20, the domain is characterized as GMPS ATP-PPase.
+At position 22 to 93, the domain is characterized as S1 motif.
+At position 200 to 246, the domain is characterized as F-box.
+At position 41 to 158, the domain is characterized as PH.
+At position 149 to 267, the domain is characterized as C2.
+At position 327 to 519, the domain is characterized as Ras-GAP.
+At position 590 to 738, the domain is characterized as MOSC.
+At position 34 to 249, the domain is characterized as GB1/RHD3-type G.
+At position 168 to 225, the domain is characterized as KH.
+At position 36 to 89, the domain is characterized as TSP type-1 1.
+At position 94 to 131, the domain is characterized as LDL-receptor class A.
+At position 132 to 493, the domain is characterized as MACPF.
+At position 494 to 524, the domain is characterized as EGF-like.
+At position 543 to 585, the domain is characterized as TSP type-1 2.
+At position 159 to 244, the domain is characterized as PPIase FKBP-type.
+At position 7 to 327, the domain is characterized as Hcy-binding.
+At position 358 to 619, the domain is characterized as Pterin-binding.
+At position 652 to 746, the domain is characterized as B12-binding N-terminal.
+At position 748 to 883, the domain is characterized as B12-binding.
+At position 899 to 1226, the domain is characterized as AdoMet activation.
+At position 604 to 717, the domain is characterized as Cadherin 5.
+At position 175 to 219, the domain is characterized as DSL.
+At position 220 to 253, the domain is characterized as EGF-like 1.
+At position 257 to 284, the domain is characterized as EGF-like 2.
+At position 286 to 324, the domain is characterized as EGF-like 3.
+At position 326 to 362, the domain is characterized as EGF-like 4; calcium-binding.
+At position 441 to 477, the domain is characterized as EGF-like 7; calcium-binding.
+At position 479 to 515, the domain is characterized as EGF-like 8.
+At position 207 to 234, the domain is characterized as PLD phosphodiesterase 1.
+At position 421 to 447, the domain is characterized as PLD phosphodiesterase 2.
+At position 389 to 416, the domain is characterized as PLD phosphodiesterase 2.
+At position 112 to 305, the domain is characterized as Rho-GAP.
+At position 484 to 575, the domain is characterized as Ricin B-type lectin.
+At position 213 to 374, the domain is characterized as CP-type G.
+At position 69 to 103, the domain is characterized as SAP 2.
+At position 158 to 255, the domain is characterized as WGR.
+At position 286 to 404, the domain is characterized as PARP alpha-helical.
+At position 412 to 637, the domain is characterized as PARP catalytic.
+At position 33 to 111, the domain is characterized as Collagen-like.
+At position 112 to 247, the domain is characterized as C1q.
+At position 180 to 355, the domain is characterized as Helicase ATP-binding.
+At position 383 to 530, the domain is characterized as Helicase C-terminal.
+At position 294 to 353, the domain is characterized as AFP-like.
+At position 220 to 393, the domain is characterized as EngA-type G 2.
+At position 394 to 478, the domain is characterized as KH-like.
+At position 14 to 56, the domain is characterized as CHCH 1.
+At position 60 to 105, the domain is characterized as CHCH 2.
+At position 34 to 133, the domain is characterized as SRCR.
+At position 272 to 374, the domain is characterized as BACK.
+At position 25 to 152, the domain is characterized as Response regulatory.
+At position 45 to 135, the domain is characterized as PPIase FKBP-type.
+At position 135 to 170, the domain is characterized as EF-hand 1.
+At position 179 to 211, the domain is characterized as EF-hand 2.
+At position 17 to 132, the domain is characterized as Response regulatory.
+At position 18 to 167, the domain is characterized as Nudix hydrolase.
+At position 24 to 131, the domain is characterized as Ig-like V-type 1.
+At position 141 to 244, the domain is characterized as Ig-like V-type 2.
+At position 246 to 332, the domain is characterized as Ig-like C2-type 1.
+At position 337 to 426, the domain is characterized as Ig-like C2-type 2.
+At position 432 to 512, the domain is characterized as Ig-like C2-type 3.
+At position 96 to 152, the domain is characterized as CBS 1.
+At position 462 to 575, the domain is characterized as PAZ.
+At position 741 to 1032, the domain is characterized as Piwi.
+At position 137 to 189, the domain is characterized as bZIP.
+At position 46 to 133, the domain is characterized as GST N-terminal.
+At position 139 to 265, the domain is characterized as GST C-terminal.
+At position 34 to 716, the domain is characterized as Vitellogenin.
+At position 1340 to 1515, the domain is characterized as VWFD.
+At position 351 to 471, the domain is characterized as BRCT.
+At position 1 to 120, the domain is characterized as MGS-like.
+At position 95 to 200, the domain is characterized as sHSP 1.
+At position 216 to 314, the domain is characterized as sHSP 2.
+At position 268 to 417, the domain is characterized as Helicase ATP-binding.
+At position 469 to 621, the domain is characterized as Helicase C-terminal.
+At position 1425 to 1495, the domain is characterized as Bromo 1.
+At position 1547 to 1617, the domain is characterized as Bromo 2.
+At position 190 to 275, the domain is characterized as RCK C-terminal 1.
+At position 148 to 268, the domain is characterized as OmpA-like.
+At position 28 to 238, the domain is characterized as Brix.
+At position 36 to 76, the domain is characterized as Chaplin.
+At position 687 to 765, the domain is characterized as BRCT.
+At position 106 to 467, the domain is characterized as GS catalytic.
+At position 54 to 135, the domain is characterized as Ig-like V-type.
+At position 310 to 509, the domain is characterized as B30.2/SPRY.
+At position 297 to 512, the domain is characterized as Histidine kinase.
+At position 80 to 294, the domain is characterized as ABC transmembrane type-1.
+At position 34 to 266, the domain is characterized as ABC transporter.
+At position 159 to 376, the domain is characterized as MIF4G.
+At position 5 to 228, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 155, the domain is characterized as DHFR.
+At position 224 to 630, the domain is characterized as Myotubularin phosphatase.
+At position 320 to 374, the domain is characterized as MIR 1.
+At position 384 to 444, the domain is characterized as MIR 2.
+At position 454 to 510, the domain is characterized as MIR 3.
+At position 70 to 220, the domain is characterized as HD.
+At position 12 to 242, the domain is characterized as Radical SAM core.
+At position 839 to 895, the domain is characterized as WHEP-TRS.
+At position 511 to 635, the domain is characterized as STAS.
+At position 34 to 92, the domain is characterized as 4Fe-4S.
+At position 133 to 161, the domain is characterized as ITAM 3.
+At position 32 to 139, the domain is characterized as Calponin-homology (CH) 1.
+At position 187 to 291, the domain is characterized as Calponin-homology (CH) 2.
+At position 1060 to 1283, the domain is characterized as JmjC.
+At position 371 to 640, the domain is characterized as Radical SAM core.
+At position 30 to 95, the domain is characterized as VWFC 1.
+At position 108 to 174, the domain is characterized as VWFC 2.
+At position 253 to 318, the domain is characterized as VWFC 3.
+At position 36 to 97, the domain is characterized as Kazal-like.
+At position 2 to 130, the domain is characterized as CMP/dCMP-type deaminase.
+At position 242 to 415, the domain is characterized as SSD.
+At position 120 to 154, the domain is characterized as EF-hand 4.
+At position 170 to 285, the domain is characterized as Fe2OG dioxygenase.
+At position 1434 to 1723, the domain is characterized as Autotransporter.
+At position 171 to 351, the domain is characterized as Glutamine amidotransferase type-1.
+At position 28 to 414, the domain is characterized as Helicase ATP-binding.
+At position 653 to 688, the domain is characterized as UVR.
+At position 61 to 203, the domain is characterized as Thioredoxin.
+At position 38 to 142, the domain is characterized as PTS EIIA type-1.
+At position 16 to 363, the domain is characterized as Kinesin motor.
+At position 465 to 528, the domain is characterized as FHA.
+At position 285 to 364, the domain is characterized as PB1.
+At position 234 to 484, the domain is characterized as CN hydrolase.
+At position 45 to 70, the domain is characterized as Antistasin-like 1.
+At position 100 to 125, the domain is characterized as Antistasin-like 2.
+At position 1 to 131, the domain is characterized as DAGKc.
+At position 39 to 220, the domain is characterized as FAD-binding PCMH-type.
+At position 131 to 296, the domain is characterized as Helicase ATP-binding.
+At position 348 to 531, the domain is characterized as Helicase C-terminal.
+At position 951 to 1016, the domain is characterized as Tudor.
+At position 78 to 294, the domain is characterized as Radical SAM core.
+At position 24 to 122, the domain is characterized as Fibronectin type-III 1.
+At position 124 to 225, the domain is characterized as Fibronectin type-III 2.
+At position 223 to 315, the domain is characterized as Fibronectin type-III 3.
+At position 319 to 416, the domain is characterized as Fibronectin type-III 4.
+At position 421 to 515, the domain is characterized as Fibronectin type-III 5.
+At position 125 to 310, the domain is characterized as CP-type G.
+At position 8 to 227, the domain is characterized as Peptidase S1.
+At position 459 to 507, the domain is characterized as EGF-like 1.
+At position 608 to 652, the domain is characterized as EGF-like 2.
+At position 656 to 708, the domain is characterized as EGF-like 3.
+At position 1030 to 1145, the domain is characterized as Fibronectin type-III.
+At position 12 to 156, the domain is characterized as HTH marR-type.
+At position 93 to 248, the domain is characterized as CP-type G.
+At position 214 to 492, the domain is characterized as Protein kinase.
+At position 71 to 274, the domain is characterized as ABC transmembrane type-1.
+At position 471 to 730, the domain is characterized as Pterin-binding.
+At position 37 to 279, the domain is characterized as Peptidase S1.
+At position 3 to 68, the domain is characterized as Acylphosphatase-like.
+At position 445 to 632, the domain is characterized as VWFA.
+At position 1 to 62, the domain is characterized as Disintegrin.
+At position 475 to 596, the domain is characterized as RCK N-terminal.
+At position 136 to 226, the domain is characterized as Ig-like C2-type 2.
+At position 8 to 86, the domain is characterized as ACT 1.
+At position 102 to 174, the domain is characterized as ACT 2.
+At position 235 to 432, the domain is characterized as DH.
+At position 472 to 571, the domain is characterized as PH.
+At position 80 to 269, the domain is characterized as Protein kinase.
+At position 250 to 325, the domain is characterized as PUA.
+At position 216 to 293, the domain is characterized as BCNT-C.
+At position 109 to 312, the domain is characterized as ATP-grasp.
+At position 51 to 116, the domain is characterized as Cystatin.
+At position 204 to 282, the domain is characterized as RRM 2.
+At position 1219 to 1383, the domain is characterized as PNPLA.
+At position 154 to 426, the domain is characterized as ABC transporter 1.
+At position 846 to 1098, the domain is characterized as ABC transporter 2.
+At position 1171 to 1385, the domain is characterized as ABC transmembrane type-2 2.
+At position 10 to 203, the domain is characterized as Lon N-terminal.
+At position 1 to 17, the domain is characterized as Ig-like C2-type 1.
+At position 52 to 152, the domain is characterized as Ig-like C2-type 2.
+At position 10 to 81, the domain is characterized as PAS.
+At position 208 to 444, the domain is characterized as Methyl-accepting transducer.
+At position 72 to 106, the domain is characterized as EF-hand 1.
+At position 170 to 204, the domain is characterized as EF-hand 3.
+At position 755 to 915, the domain is characterized as C2.
+At position 70 to 112, the domain is characterized as CUE.
+At position 26 to 280, the domain is characterized as Alpha-carbonic anhydrase.
+At position 112 to 170, the domain is characterized as TCP.
+At position 17 to 71, the domain is characterized as TCP.
+At position 808 to 944, the domain is characterized as DAGKc.
+At position 279 to 478, the domain is characterized as MAGE.
+At position 26 to 107, the domain is characterized as Lipoyl-binding.
+At position 600 to 678, the domain is characterized as BRCT.
+At position 445 to 757, the domain is characterized as Piwi.
+At position 1575 to 1684, the domain is characterized as PH.
+At position 38 to 107, the domain is characterized as CSD.
+At position 21 to 241, the domain is characterized as Radical SAM core.
+At position 235 to 287, the domain is characterized as CpcD-like.
+At position 8 to 85, the domain is characterized as Ubiquitin-like.
+At position 108 to 194, the domain is characterized as BAG.
+At position 35 to 216, the domain is characterized as FAD-binding PCMH-type.
+At position 121 to 165, the domain is characterized as LysM.
+At position 10 to 91, the domain is characterized as GST N-terminal.
+At position 96 to 221, the domain is characterized as GST C-terminal.
+At position 111 to 230, the domain is characterized as FZ.
+At position 151 to 323, the domain is characterized as Helicase ATP-binding.
+At position 388 to 546, the domain is characterized as Helicase C-terminal.
+At position 14 to 68, the domain is characterized as bHLH.
+At position 7 to 97, the domain is characterized as Acylphosphatase-like.
+At position 211 to 277, the domain is characterized as J.
+At position 9 to 219, the domain is characterized as YjeF N-terminal.
+At position 264 to 283, the domain is characterized as UIM 1.
+At position 5 to 88, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 94 to 155, the domain is characterized as SH3.
+At position 161 to 258, the domain is characterized as SH2.
+At position 280 to 533, the domain is characterized as Protein kinase.
+At position 197 to 306, the domain is characterized as Fe2OG dioxygenase.
+At position 258 to 387, the domain is characterized as C2 2.
+At position 420 to 554, the domain is characterized as C2 3.
+At position 587 to 714, the domain is characterized as C2 4.
+At position 263 to 334, the domain is characterized as B5.
+At position 1 to 81, the domain is characterized as Acylphosphatase-like.
+At position 395 to 619, the domain is characterized as Roc.
+At position 1242 to 1546, the domain is characterized as Protein kinase.
+At position 511 to 618, the domain is characterized as Toprim.
+At position 25 to 265, the domain is characterized as SET.
+At position 247 to 455, the domain is characterized as Histidine kinase.
+At position 1057 to 1119, the domain is characterized as SH3.
+At position 255 to 449, the domain is characterized as PCI.
+At position 177 to 584, the domain is characterized as PPM-type phosphatase.
+At position 60 to 284, the domain is characterized as Radical SAM core.
+At position 186 to 279, the domain is characterized as 5'-3' exonuclease.
+At position 317 to 493, the domain is characterized as 3'-5' exonuclease.
+At position 109 to 165, the domain is characterized as BRX 1.
+At position 267 to 322, the domain is characterized as BRX 2.
+At position 262 to 378, the domain is characterized as RGS.
+At position 278 to 370, the domain is characterized as PI3K-RBD.
+At position 540 to 688, the domain is characterized as C2 PI3K-type.
+At position 703 to 879, the domain is characterized as PIK helical.
+At position 948 to 1226, the domain is characterized as PI3K/PI4K catalytic.
+At position 1259 to 1371, the domain is characterized as PX.
+At position 1384 to 1505, the domain is characterized as C2.
+At position 52 to 293, the domain is characterized as ABC transporter.
+At position 388 to 645, the domain is characterized as ABC transmembrane type-2.
+At position 25 to 54, the domain is characterized as LRRNT.
+At position 255 to 306, the domain is characterized as LRRCT.
+At position 391 to 588, the domain is characterized as PCI.
+At position 93 to 256, the domain is characterized as Helicase ATP-binding.
+At position 640 to 803, the domain is characterized as Toprim.
+At position 1107 to 1222, the domain is characterized as DOD-type homing endonuclease.
+At position 60 to 123, the domain is characterized as Pre-SET.
+At position 126 to 250, the domain is characterized as SET.
+At position 270 to 286, the domain is characterized as Post-SET.
+At position 73 to 119, the domain is characterized as F-box; degenerate.
+At position 1 to 148, the domain is characterized as RPW8.
+At position 74 to 180, the domain is characterized as Thioredoxin.
+At position 96 to 186, the domain is characterized as SUEL-type lectin 1.
+At position 193 to 280, the domain is characterized as SUEL-type lectin 2.
+At position 21 to 64, the domain is characterized as CHCH.
+At position 36 to 201, the domain is characterized as Cohesin 1.
+At position 207 to 370, the domain is characterized as Cohesin 2.
+At position 453 to 520, the domain is characterized as SLH 1.
+At position 521 to 584, the domain is characterized as SLH 2.
+At position 585 to 648, the domain is characterized as SLH 3.
+At position 649 to 669, the domain is characterized as SLH 4; truncated.
+At position 128 to 232, the domain is characterized as PilZ.
+At position 125 to 157, the domain is characterized as EF-hand 3.
+At position 83 to 344, the domain is characterized as Protein kinase.
+At position 345 to 415, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 65, the domain is characterized as Myosin motor.
+At position 7 to 85, the domain is characterized as Carrier.
+At position 84 to 399, the domain is characterized as Peptidase A1.
+At position 15 to 63, the domain is characterized as F-box.
+At position 4 to 32, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 57 to 89, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 21 to 214, the domain is characterized as NodB homology.
+At position 122 to 309, the domain is characterized as ATP-grasp.
+At position 16 to 67, the domain is characterized as F-box.
+At position 149 to 221, the domain is characterized as Bromo.
+At position 280 to 361, the domain is characterized as NET.
+At position 290 to 442, the domain is characterized as GAF 1.
+At position 474 to 658, the domain is characterized as GAF 2.
+At position 688 to 1119, the domain is characterized as PDEase.
+At position 120 to 295, the domain is characterized as Helicase ATP-binding.
+At position 321 to 468, the domain is characterized as Helicase C-terminal.
+At position 1178 to 1248, the domain is characterized as Bromo 1.
+At position 1332 to 1402, the domain is characterized as Bromo 2.
+At position 352 to 407, the domain is characterized as EGF-like.
+At position 318 to 402, the domain is characterized as RCK C-terminal 2.
+At position 407 to 492, the domain is characterized as RCK C-terminal 3.
+At position 498 to 584, the domain is characterized as RCK C-terminal 4.
+At position 650 to 720, the domain is characterized as Bromo.
+At position 9 to 99, the domain is characterized as HTH arsR-type.
+At position 52 to 154, the domain is characterized as THUMP.
+At position 211 to 287, the domain is characterized as PUA.
+At position 6 to 99, the domain is characterized as HTH asnC-type.
+At position 21 to 206, the domain is characterized as Ku.
+At position 82 to 153, the domain is characterized as POTRA.
+At position 132 to 312, the domain is characterized as EngB-type G.
+At position 41 to 80, the domain is characterized as SCP.
+At position 7 to 84, the domain is characterized as Carrier.
+At position 47 to 107, the domain is characterized as v-SNARE coiled-coil homology.
+At position 7 to 456, the domain is characterized as Hexokinase.
+At position 5 to 187, the domain is characterized as UmuC.
+At position 373 to 440, the domain is characterized as TRAM.
+At position 5 to 78, the domain is characterized as BTB.
+At position 11 to 269, the domain is characterized as Protein kinase.
+At position 1233 to 1520, the domain is characterized as Autotransporter.
+At position 305 to 423, the domain is characterized as Rhodanese.
+At position 34 to 75, the domain is characterized as JmjN.
+At position 162 to 333, the domain is characterized as JmjC.
+At position 548 to 567, the domain is characterized as WH2.
+At position 290 to 396, the domain is characterized as ERCC4.
+At position 37 to 139, the domain is characterized as Ig-like C2-type.
+At position 398 to 473, the domain is characterized as RRM 1.
+At position 496 to 571, the domain is characterized as RRM 2.
+At position 191 to 295, the domain is characterized as IRS-type PTB.
+At position 77 to 251, the domain is characterized as Helicase ATP-binding.
+At position 31 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 58 to 205, the domain is characterized as SCP.
+At position 51 to 91, the domain is characterized as Fibronectin type-I 1.
+At position 96 to 139, the domain is characterized as Fibronectin type-I 2.
+At position 140 to 183, the domain is characterized as Fibronectin type-I 3.
+At position 185 to 229, the domain is characterized as Fibronectin type-I 4.
+At position 230 to 274, the domain is characterized as Fibronectin type-I 5.
+At position 306 to 343, the domain is characterized as Fibronectin type-I 6.
+At position 468 to 516, the domain is characterized as Fibronectin type-I 7.
+At position 610 to 717, the domain is characterized as Fibronectin type-III 1.
+At position 721 to 811, the domain is characterized as Fibronectin type-III 2.
+At position 812 to 903, the domain is characterized as Fibronectin type-III 3.
+At position 908 to 997, the domain is characterized as Fibronectin type-III 4.
+At position 998 to 1087, the domain is characterized as Fibronectin type-III 5.
+At position 1088 to 1174, the domain is characterized as Fibronectin type-III 6.
+At position 1175 to 1269, the domain is characterized as Fibronectin type-III 7.
+At position 1270 to 1358, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1359 to 1451, the domain is characterized as Fibronectin type-III 9.
+At position 1452 to 1539, the domain is characterized as Fibronectin type-III 10.
+At position 1540 to 1633, the domain is characterized as Fibronectin type-III 11.
+At position 1634 to 1725, the domain is characterized as Fibronectin type-III 12.
+At position 1726 to 1813, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1814 to 1907, the domain is characterized as Fibronectin type-III 14.
+At position 1908 to 1994, the domain is characterized as Fibronectin type-III 15.
+At position 1995 to 2085, the domain is characterized as Fibronectin type-III 16.
+At position 2193 to 2287, the domain is characterized as Fibronectin type-III 17.
+At position 2294 to 2338, the domain is characterized as Fibronectin type-I 10.
+At position 2339 to 2381, the domain is characterized as Fibronectin type-I 11.
+At position 2383 to 2426, the domain is characterized as Fibronectin type-I 12.
+At position 278 to 341, the domain is characterized as bZIP.
+At position 98 to 464, the domain is characterized as GBD/FH3.
+At position 549 to 623, the domain is characterized as FH1.
+At position 628 to 1028, the domain is characterized as FH2.
+At position 1051 to 1081, the domain is characterized as DAD.
+At position 87 to 198, the domain is characterized as C-type lectin.
+At position 251 to 331, the domain is characterized as BCNT-C.
+At position 285 to 487, the domain is characterized as Pentraxin (PTX).
+At position 439 to 634, the domain is characterized as PNPLA.
+At position 119 to 189, the domain is characterized as PAH 1.
+At position 300 to 383, the domain is characterized as PAH 2.
+At position 457 to 526, the domain is characterized as PAH 3.
+At position 10 to 128, the domain is characterized as MTTase N-terminal.
+At position 151 to 382, the domain is characterized as Radical SAM core.
+At position 384 to 447, the domain is characterized as TRAM.
+At position 28 to 308, the domain is characterized as Deacetylase sirtuin-type.
+At position 23 to 83, the domain is characterized as HTH iclR-type.
+At position 98 to 271, the domain is characterized as IclR-ED.
+At position 17 to 139, the domain is characterized as MsrB.
+At position 55 to 370, the domain is characterized as USP.
+At position 220 to 339, the domain is characterized as PAZ.
+At position 501 to 800, the domain is characterized as Piwi.
+At position 194 to 283, the domain is characterized as BRCT 2.
+At position 354 to 444, the domain is characterized as BRCT 3.
+At position 538 to 611, the domain is characterized as BRCT 4.
+At position 629 to 726, the domain is characterized as BRCT 5.
+At position 892 to 984, the domain is characterized as BRCT 6.
+At position 1253 to 1344, the domain is characterized as BRCT 7.
+At position 1383 to 1480, the domain is characterized as BRCT 8.
+At position 104 to 421, the domain is characterized as Kinesin motor.
+At position 44 to 230, the domain is characterized as BPL/LPL catalytic.
+At position 197 to 358, the domain is characterized as SUN.
+At position 375 to 572, the domain is characterized as DH.
+At position 593 to 696, the domain is characterized as PH.
+At position 138 to 312, the domain is characterized as CRAL-TRIO.
+At position 591 to 692, the domain is characterized as tRNA-binding.
+At position 141 to 328, the domain is characterized as Helicase ATP-binding.
+At position 353 to 503, the domain is characterized as Helicase C-terminal.
+At position 6 to 212, the domain is characterized as tr-type G.
+At position 162 to 224, the domain is characterized as Dockerin.
+At position 44 to 203, the domain is characterized as MABP.
+At position 195 to 369, the domain is characterized as uDENN.
+At position 390 to 526, the domain is characterized as cDENN.
+At position 528 to 644, the domain is characterized as dDENN.
+At position 594 to 747, the domain is characterized as STAS.
+At position 508 to 612, the domain is characterized as Calponin-homology (CH).
+At position 695 to 757, the domain is characterized as LIM zinc-binding.
+At position 921 to 1070, the domain is characterized as bMERB.
+At position 169 to 358, the domain is characterized as Helicase ATP-binding.
+At position 386 to 529, the domain is characterized as Helicase C-terminal.
+At position 414 to 475, the domain is characterized as LIM zinc-binding 1.
+At position 479 to 539, the domain is characterized as LIM zinc-binding 2.
+At position 540 to 608, the domain is characterized as LIM zinc-binding 3.
+At position 1256 to 1370, the domain is characterized as PH.
+At position 48 to 77, the domain is characterized as HhH.
+At position 440 to 572, the domain is characterized as Ricin B-type lectin.
+At position 48 to 104, the domain is characterized as FHA.
+At position 10 to 194, the domain is characterized as Ku.
+At position 93 to 164, the domain is characterized as RRM 2.
+At position 22 to 270, the domain is characterized as Deacetylase sirtuin-type.
+At position 1 to 50, the domain is characterized as HTH lysR-type.
+At position 1 to 244, the domain is characterized as KaiC 1.
+At position 258 to 516, the domain is characterized as KaiC 2.
+At position 212 to 387, the domain is characterized as EXS.
+At position 116 to 333, the domain is characterized as ATP-grasp.
+At position 129 to 378, the domain is characterized as Radical SAM core.
+At position 240 to 315, the domain is characterized as MIT.
+At position 179 to 262, the domain is characterized as 5'-3' exonuclease.
+At position 157 to 190, the domain is characterized as WW 1.
+At position 251 to 284, the domain is characterized as WW 2.
+At position 297 to 330, the domain is characterized as WW 3.
+At position 431 to 765, the domain is characterized as HECT.
+At position 78 to 145, the domain is characterized as ACT.
+At position 132 to 186, the domain is characterized as HTH cro/C1-type.
+At position 80 to 198, the domain is characterized as MTTase N-terminal.
+At position 221 to 451, the domain is characterized as Radical SAM core.
+At position 454 to 517, the domain is characterized as TRAM.
+At position 2 to 21, the domain is characterized as UIM.
+At position 362 to 453, the domain is characterized as PI3K-RBD.
+At position 598 to 766, the domain is characterized as C2 PI3K-type.
+At position 776 to 953, the domain is characterized as PIK helical.
+At position 1029 to 1303, the domain is characterized as PI3K/PI4K catalytic.
+At position 1344 to 1458, the domain is characterized as PX.
+At position 1472 to 1601, the domain is characterized as C2.
+At position 206 to 403, the domain is characterized as GMPS ATP-PPase.
+At position 325 to 654, the domain is characterized as PDEase.
+At position 28 to 302, the domain is characterized as Pyruvate carboxyltransferase.
+At position 8 to 64, the domain is characterized as CBS 1.
+At position 72 to 127, the domain is characterized as CBS 2.
+At position 175 to 262, the domain is characterized as 5'-3' exonuclease.
+At position 48 to 300, the domain is characterized as AB hydrolase-1.
+At position 10 to 244, the domain is characterized as SET.
+At position 404 to 469, the domain is characterized as KH 3.
+At position 486 to 552, the domain is characterized as KH 4.
+At position 102 to 202, the domain is characterized as SRCR 1.
+At position 234 to 334, the domain is characterized as SRCR 2.
+At position 363 to 463, the domain is characterized as SRCR 3.
+At position 494 to 594, the domain is characterized as SRCR 4.
+At position 733 to 833, the domain is characterized as SRCR 6.
+At position 862 to 962, the domain is characterized as SRCR 7.
+At position 993 to 1093, the domain is characterized as SRCR 8.
+At position 1122 to 1222, the domain is characterized as SRCR 9.
+At position 1251 to 1351, the domain is characterized as SRCR 10.
+At position 1380 to 1480, the domain is characterized as SRCR 11.
+At position 1509 to 1609, the domain is characterized as SRCR 12.
+At position 1640 to 1740, the domain is characterized as SRCR 13.
+At position 1766 to 1877, the domain is characterized as CUB 1.
+At position 1883 to 1986, the domain is characterized as SRCR 14.
+At position 2008 to 2117, the domain is characterized as CUB 2.
+At position 2126 to 2381, the domain is characterized as ZP.
+At position 25 to 92, the domain is characterized as Importin N-terminal.
+At position 25 to 121, the domain is characterized as SH2.
+At position 1198 to 1260, the domain is characterized as SAM.
+At position 219 to 379, the domain is characterized as PCI.
+At position 1 to 123, the domain is characterized as CBM20.
+At position 155 to 322, the domain is characterized as Tyrosine-protein phosphatase.
+At position 49 to 86, the domain is characterized as EF-hand 1.
+At position 163 to 195, the domain is characterized as EF-hand 3.
+At position 15 to 193, the domain is characterized as Helicase ATP-binding.
+At position 366 to 536, the domain is characterized as Helicase C-terminal.
+At position 571 to 673, the domain is characterized as Dicer dsRNA-binding fold.
+At position 875 to 929, the domain is characterized as PAZ.
+At position 1177 to 1382, the domain is characterized as RNase III 1.
+At position 1433 to 1628, the domain is characterized as RNase III 2.
+At position 1697 to 1719, the domain is characterized as DRBM.
+At position 18 to 275, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 371 to 466, the domain is characterized as Rhodanese.
+At position 82 to 299, the domain is characterized as RNase H type-2.
+At position 107 to 468, the domain is characterized as GS catalytic.
+At position 43 to 111, the domain is characterized as BIG2 1.
+At position 134 to 205, the domain is characterized as BIG2 2.
+At position 221 to 288, the domain is characterized as BIG2 3.
+At position 306 to 386, the domain is characterized as BIG2 4.
+At position 392 to 471, the domain is characterized as BIG2 5.
+At position 478 to 558, the domain is characterized as BIG2 6.
+At position 565 to 638, the domain is characterized as BIG2 7.
+At position 38 to 143, the domain is characterized as HPt.
+At position 222 to 371, the domain is characterized as N-acetyltransferase.
+At position 472 to 543, the domain is characterized as Bromo.
+At position 29 to 150, the domain is characterized as FZ.
+At position 58 to 164, the domain is characterized as HD.
+At position 102 to 164, the domain is characterized as S4 RNA-binding.
+At position 131 to 301, the domain is characterized as Helicase ATP-binding.
+At position 312 to 479, the domain is characterized as Helicase C-terminal.
+At position 29 to 148, the domain is characterized as Bulb-type lectin.
+At position 283 to 319, the domain is characterized as EGF-like.
+At position 338 to 422, the domain is characterized as PAN.
+At position 505 to 792, the domain is characterized as Protein kinase.
+At position 411 to 506, the domain is characterized as ERCC4.
+At position 15 to 92, the domain is characterized as PABC.
+At position 98 to 156, the domain is characterized as S4 RNA-binding.
+At position 196 to 863, the domain is characterized as USP.
+At position 43 to 99, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 5 to 481, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 526 to 824, the domain is characterized as UvrD-like helicase C-terminal.
+At position 292 to 351, the domain is characterized as SH3 1.
+At position 354 to 411, the domain is characterized as SH3 2.
+At position 12 to 185, the domain is characterized as Ku.
+At position 25 to 88, the domain is characterized as bZIP.
+At position 132 to 219, the domain is characterized as PNT.
+At position 123 to 304, the domain is characterized as Helicase ATP-binding.
+At position 444 to 617, the domain is characterized as Helicase C-terminal.
+At position 640 to 730, the domain is characterized as Dicer dsRNA-binding fold.
+At position 879 to 1007, the domain is characterized as PAZ.
+At position 1031 to 1190, the domain is characterized as RNase III 1.
+At position 1241 to 1392, the domain is characterized as RNase III 2.
+At position 1426 to 1494, the domain is characterized as DRBM.
+At position 486 to 515, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 520 to 544, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 699 to 792, the domain is characterized as FDX-ACB.
+At position 57 to 113, the domain is characterized as Clip.
+At position 151 to 404, the domain is characterized as Peptidase S1.
+At position 557 to 586, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 4 to 241, the domain is characterized as PABS.
+At position 249 to 441, the domain is characterized as GATase cobBQ-type.
+At position 45 to 322, the domain is characterized as ABC transmembrane type-1.
+At position 354 to 585, the domain is characterized as ABC transporter.
+At position 38 to 321, the domain is characterized as AB hydrolase-1.
+At position 20 to 62, the domain is characterized as SMB 1.
+At position 86 to 130, the domain is characterized as SMB 2.
+At position 137 to 410, the domain is characterized as EndoU.
+At position 221 to 339, the domain is characterized as OmpA-like.
+At position 23 to 94, the domain is characterized as IGFBP N-terminal.
+At position 59 to 87, the domain is characterized as EF-hand 2.
+At position 1 to 78, the domain is characterized as Core-binding (CB).
+At position 106 to 313, the domain is characterized as Tyr recombinase.
+At position 125 to 216, the domain is characterized as Fibronectin type-III 1.
+At position 224 to 324, the domain is characterized as Fibronectin type-III 2.
+At position 329 to 424, the domain is characterized as Fibronectin type-III 3.
+At position 426 to 517, the domain is characterized as Fibronectin type-III 4.
+At position 518 to 613, the domain is characterized as Fibronectin type-III 5.
+At position 1 to 27, the domain is characterized as EF-hand 1.
+At position 28 to 63, the domain is characterized as EF-hand 2.
+At position 214 to 249, the domain is characterized as EF-hand 4.
+At position 321 to 356, the domain is characterized as EF-hand 5.
+At position 357 to 392, the domain is characterized as EF-hand 6.
+At position 468 to 503, the domain is characterized as EF-hand 7.
+At position 504 to 539, the domain is characterized as EF-hand 8.
+At position 579 to 614, the domain is characterized as EF-hand 9.
+At position 615 to 646, the domain is characterized as EF-hand 10.
+At position 7 to 121, the domain is characterized as NTF2.
+At position 22 to 343, the domain is characterized as Kinesin motor.
+At position 548 to 714, the domain is characterized as C2 DOCK-type.
+At position 1587 to 2023, the domain is characterized as DOCKER.
+At position 58 to 122, the domain is characterized as CSD.
+At position 446 to 482, the domain is characterized as EF-hand 1.
+At position 483 to 518, the domain is characterized as EF-hand 2.
+At position 519 to 558, the domain is characterized as EF-hand 3.
+At position 559 to 588, the domain is characterized as EF-hand 4.
+At position 7 to 82, the domain is characterized as Carrier.
+At position 295 to 519, the domain is characterized as CHASE.
+At position 587 to 862, the domain is characterized as Histidine kinase.
+At position 886 to 1017, the domain is characterized as Response regulatory 1.
+At position 1041 to 1178, the domain is characterized as Response regulatory 2.
+At position 268 to 516, the domain is characterized as EAL.
+At position 577 to 678, the domain is characterized as tRNA-binding.
+At position 133 to 234, the domain is characterized as C-type lectin.
+At position 74 to 325, the domain is characterized as Calpain catalytic.
+At position 213 to 247, the domain is characterized as PKD 1.
+At position 436 to 503, the domain is characterized as PKD 2.
+At position 724 to 806, the domain is characterized as PKD 3.
+At position 822 to 886, the domain is characterized as PKD 4.
+At position 925 to 962, the domain is characterized as PKD 5.
+At position 4 to 54, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 56 to 106, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 115 to 165, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 133 to 163, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 3 to 364, the domain is characterized as Kinesin motor.
+At position 1129 to 1259, the domain is characterized as PX.
+At position 290 to 349, the domain is characterized as LIM zinc-binding.
+At position 242 to 262, the domain is characterized as ELK.
+At position 39 to 306, the domain is characterized as CN hydrolase.
+At position 366 to 794, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1263 to 1569, the domain is characterized as PKS/mFAS DH.
+At position 1620 to 1697, the domain is characterized as Carrier.
+At position 39 to 167, the domain is characterized as SCP.
+At position 126 to 250, the domain is characterized as C2 1.
+At position 163 to 394, the domain is characterized as Radical SAM core.
+At position 112 to 321, the domain is characterized as TLC.
+At position 17 to 146, the domain is characterized as C-type lysozyme.
+At position 249 to 416, the domain is characterized as TrmE-type G.
+At position 28 to 577, the domain is characterized as PLA2c.
+At position 383 to 444, the domain is characterized as SH3 3.
+At position 19 to 81, the domain is characterized as LCN-type CS-alpha/beta.
+At position 143 to 212, the domain is characterized as BTB.
+At position 266 to 358, the domain is characterized as BACK.
+At position 402 to 478, the domain is characterized as B5.
+At position 710 to 739, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 767 to 796, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1288 to 1438, the domain is characterized as Flavodoxin-like.
+At position 1501 to 1759, the domain is characterized as FAD-binding FR-type.
+At position 233 to 332, the domain is characterized as CBM20.
+At position 88 to 346, the domain is characterized as Protein kinase.
+At position 389 to 424, the domain is characterized as EF-hand 1.
+At position 461 to 496, the domain is characterized as EF-hand 3.
+At position 497 to 530, the domain is characterized as EF-hand 4.
+At position 23 to 215, the domain is characterized as RNase H type-2.
+At position 394 to 510, the domain is characterized as PAZ.
+At position 677 to 1009, the domain is characterized as Piwi.
+At position 97 to 217, the domain is characterized as MTTase N-terminal.
+At position 241 to 495, the domain is characterized as Radical SAM core.
+At position 498 to 573, the domain is characterized as TRAM.
+At position 346 to 553, the domain is characterized as MCM.
+At position 1 to 97, the domain is characterized as CRM.
+At position 56 to 107, the domain is characterized as HTH psq-type.
+At position 121 to 194, the domain is characterized as HTH CENPB-type.
+At position 239 to 364, the domain is characterized as DDE-1.
+At position 222 to 270, the domain is characterized as bHLH.
+At position 94 to 216, the domain is characterized as C2 1.
+At position 256 to 389, the domain is characterized as C2 2.
+At position 41 to 159, the domain is characterized as Rhodanese.
+At position 195 to 336, the domain is characterized as Tyrosine-protein phosphatase.
+At position 21 to 703, the domain is characterized as Myosin motor.
+At position 696 to 728, the domain is characterized as IQ 1.
+At position 729 to 751, the domain is characterized as IQ 2.
+At position 752 to 779, the domain is characterized as IQ 3.
+At position 857 to 1035, the domain is characterized as TH1.
+At position 596 to 873, the domain is characterized as Protein kinase.
+At position 81 to 301, the domain is characterized as Peptidase S1.
+At position 8 to 427, the domain is characterized as PTS EIIC type-3.
+At position 212 to 349, the domain is characterized as ZU5.
+At position 549 to 619, the domain is characterized as SH3.
+At position 327 to 488, the domain is characterized as PH.
+At position 509 to 629, the domain is characterized as Arf-GAP.
+At position 4 to 89, the domain is characterized as Core-binding (CB).
+At position 158 to 349, the domain is characterized as Tyr recombinase.
+At position 39 to 214, the domain is characterized as Helicase ATP-binding.
+At position 402 to 563, the domain is characterized as Helicase C-terminal.
+At position 587 to 677, the domain is characterized as Dicer dsRNA-binding fold.
+At position 879 to 1006, the domain is characterized as PAZ.
+At position 1413 to 1481, the domain is characterized as DRBM.
+At position 1333 to 1486, the domain is characterized as VPS9.
+At position 10 to 142, the domain is characterized as Response regulatory.
+At position 36 to 76, the domain is characterized as LRRNT.
+At position 416 to 505, the domain is characterized as LRRCT.
+At position 334 to 856, the domain is characterized as USP.
+At position 650 to 691, the domain is characterized as UBA 1.
+At position 184 to 385, the domain is characterized as Helicase ATP-binding.
+At position 411 to 625, the domain is characterized as Helicase C-terminal.
+At position 50 to 128, the domain is characterized as RRM 1.
+At position 138 to 215, the domain is characterized as RRM 2.
+At position 231 to 308, the domain is characterized as RRM 3.
+At position 334 to 411, the domain is characterized as RRM 4.
+At position 507 to 586, the domain is characterized as PABC.
+At position 306 to 474, the domain is characterized as tr-type G.
+At position 3 to 150, the domain is characterized as bMERB.
+At position 299 to 362, the domain is characterized as bZIP.
+At position 65 to 118, the domain is characterized as bHLH.
+At position 137 to 208, the domain is characterized as PAS 1.
+At position 325 to 395, the domain is characterized as PAS 2.
+At position 400 to 443, the domain is characterized as PAC.
+At position 12 to 132, the domain is characterized as Calponin-homology (CH).
+At position 30 to 304, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1 to 216, the domain is characterized as N-acetyltransferase.
+At position 488 to 731, the domain is characterized as ABC transmembrane type-2 1.
+At position 423 to 645, the domain is characterized as ABC transporter 1.
+At position 37 to 113, the domain is characterized as H15.
+At position 595 to 683, the domain is characterized as BRCT.
+At position 25 to 73, the domain is characterized as F-box.
+At position 105 to 169, the domain is characterized as S4 RNA-binding.
+At position 355 to 695, the domain is characterized as Protein kinase.
+At position 765 to 895, the domain is characterized as Guanylate cyclase.
+At position 116 to 243, the domain is characterized as NlpC/P60.
+At position 118 to 501, the domain is characterized as Protein kinase.
+At position 4 to 187, the domain is characterized as KARI N-terminal Rossmann.
+At position 309 to 499, the domain is characterized as NTF2.
+At position 565 to 617, the domain is characterized as TAP-C.
+At position 10 to 186, the domain is characterized as NAC.
+At position 151 to 242, the domain is characterized as TonB C-terminal.
+At position 126 to 278, the domain is characterized as Nudix hydrolase.
+At position 103 to 132, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 29 to 222, the domain is characterized as GH11.
+At position 2 to 52, the domain is characterized as Kazal-like.
+At position 39 to 74, the domain is characterized as EF-hand 2.
+At position 223 to 242, the domain is characterized as UIM.
+At position 366 to 573, the domain is characterized as MCM.
+At position 279 to 443, the domain is characterized as SUN.
+At position 5 to 289, the domain is characterized as CN hydrolase.
+At position 397 to 566, the domain is characterized as tr-type G.
+At position 49 to 332, the domain is characterized as ABC transmembrane type-1.
+At position 366 to 600, the domain is characterized as ABC transporter.
+At position 9 to 229, the domain is characterized as DOG1.
+At position 132 to 390, the domain is characterized as Protein kinase.
+At position 433 to 468, the domain is characterized as EF-hand 1.
+At position 469 to 505, the domain is characterized as EF-hand 2; degenerate.
+At position 663 to 831, the domain is characterized as MOSC.
+At position 65 to 133, the domain is characterized as J.
+At position 124 to 520, the domain is characterized as GRAS.
+At position 187 to 263, the domain is characterized as RRM.
+At position 98 to 304, the domain is characterized as Rho-GAP.
+At position 492 to 550, the domain is characterized as SH3.
+At position 2 to 120, the domain is characterized as Thioredoxin.
+At position 106 to 353, the domain is characterized as GS catalytic.
+At position 8 to 212, the domain is characterized as DPCK.
+At position 47 to 140, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 185 to 215, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 7 to 139, the domain is characterized as MATH.
+At position 240 to 267, the domain is characterized as KOW 1.
+At position 415 to 442, the domain is characterized as KOW 2.
+At position 45 to 156, the domain is characterized as Expansin-like EG45.
+At position 166 to 246, the domain is characterized as Expansin-like CBD.
+At position 8 to 126, the domain is characterized as TsaA-like.
+At position 54 to 345, the domain is characterized as ABC transmembrane type-1 1.
+At position 378 to 667, the domain is characterized as ABC transporter 1.
+At position 735 to 1024, the domain is characterized as ABC transmembrane type-1 2.
+At position 1060 to 1296, the domain is characterized as ABC transporter 2.
+At position 96 to 159, the domain is characterized as bZIP.
+At position 167 to 379, the domain is characterized as DOG1.
+At position 26 to 87, the domain is characterized as CSD 1.
+At position 136 to 179, the domain is characterized as CSD 2; truncated.
+At position 186 to 245, the domain is characterized as CSD 3.
+At position 297 to 337, the domain is characterized as CSD 4; truncated.
+At position 349 to 410, the domain is characterized as CSD 5.
+At position 447 to 507, the domain is characterized as CSD 6.
+At position 519 to 579, the domain is characterized as CSD 7.
+At position 610 to 670, the domain is characterized as CSD 8.
+At position 674 to 735, the domain is characterized as CSD 9.
+At position 748 to 789, the domain is characterized as SUZ-C.
+At position 8 to 131, the domain is characterized as Longin.
+At position 48 to 168, the domain is characterized as Expansin-like EG45.
+At position 190 to 412, the domain is characterized as RMT2.
+At position 1 to 68, the domain is characterized as UmuC.
+At position 14 to 193, the domain is characterized as Guanylate kinase-like.
+At position 58 to 272, the domain is characterized as Radical SAM core.
+At position 25 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 26 to 281, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 17 to 146, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 2 to 191, the domain is characterized as RNase H type-2.
+At position 1 to 44, the domain is characterized as Peptidase S1.
+At position 91 to 335, the domain is characterized as ABC transporter.
+At position 436 to 684, the domain is characterized as ABC transmembrane type-2.
+At position 1 to 365, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 107 to 350, the domain is characterized as Radical SAM core.
+At position 35 to 156, the domain is characterized as FZ.
+At position 24 to 162, the domain is characterized as Ig-like V-type.
+At position 325 to 403, the domain is characterized as RRM 2.
+At position 512 to 584, the domain is characterized as RRM 3.
+At position 640 to 723, the domain is characterized as RRM 4.
+At position 738 to 815, the domain is characterized as RRM 5.
+At position 38 to 99, the domain is characterized as S4 RNA-binding.
+At position 137 to 218, the domain is characterized as VPS37 C-terminal.
+At position 900 to 1054, the domain is characterized as Guanylate cyclase.
+At position 23 to 57, the domain is characterized as ShKT 1.
+At position 59 to 93, the domain is characterized as ShKT 2.
+At position 103 to 392, the domain is characterized as Protein kinase.
+At position 27 to 218, the domain is characterized as Albumin 1.
+At position 223 to 415, the domain is characterized as Albumin 2.
+At position 416 to 609, the domain is characterized as Albumin 3.
+At position 78 to 156, the domain is characterized as RRM 1.
+At position 164 to 244, the domain is characterized as RRM 2.
+At position 73 to 124, the domain is characterized as bHLH.
+At position 49 to 307, the domain is characterized as Protein kinase.
+At position 350 to 385, the domain is characterized as EF-hand 1.
+At position 386 to 421, the domain is characterized as EF-hand 2.
+At position 422 to 457, the domain is characterized as EF-hand 3.
+At position 460 to 491, the domain is characterized as EF-hand 4.
+At position 182 to 223, the domain is characterized as LDL-receptor class A 1.
+At position 225 to 334, the domain is characterized as CUB 1.
+At position 342 to 504, the domain is characterized as MAM.
+At position 524 to 634, the domain is characterized as CUB 2.
+At position 641 to 679, the domain is characterized as LDL-receptor class A 2.
+At position 678 to 771, the domain is characterized as SRCR.
+At position 785 to 1019, the domain is characterized as Peptidase S1.
+At position 36 to 112, the domain is characterized as Lipoyl-binding.
+At position 179 to 216, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 91 to 153, the domain is characterized as S4 RNA-binding.
+At position 137 to 293, the domain is characterized as PPIase cyclophilin-type.
+At position 339 to 417, the domain is characterized as OCT.
+At position 135 to 345, the domain is characterized as TRUD.
+At position 532 to 685, the domain is characterized as Helicase C-terminal.
+At position 1 to 164, the domain is characterized as DHFR.
+At position 73 to 156, the domain is characterized as Biotinyl-binding.
+At position 349 to 425, the domain is characterized as UBX.
+At position 52 to 299, the domain is characterized as Peptidase S1.
+At position 311 to 421, the domain is characterized as CUB 1.
+At position 431 to 543, the domain is characterized as CUB 2.
+At position 36 to 116, the domain is characterized as Ig-like.
+At position 49 to 242, the domain is characterized as PIK helical.
+At position 102 to 313, the domain is characterized as Lon N-terminal.
+At position 811 to 995, the domain is characterized as Lon proteolytic.
+At position 39 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 122 to 204, the domain is characterized as Ig-like C2-type 2.
+At position 371 to 539, the domain is characterized as tr-type G.
+At position 424 to 487, the domain is characterized as SAM.
+At position 372 to 507, the domain is characterized as DAGKc.
+At position 278 to 329, the domain is characterized as SOCS box.
+At position 506 to 694, the domain is characterized as Rho-GAP.
+At position 743 to 802, the domain is characterized as SH3.
+At position 508 to 802, the domain is characterized as NACHT.
+At position 822 to 965, the domain is characterized as SET.
+At position 1 to 28, the domain is characterized as Chitin-binding type-1.
+At position 4 to 79, the domain is characterized as Ubiquitin-like.
+At position 72 to 141, the domain is characterized as Bromo 1.
+At position 205 to 275, the domain is characterized as Bromo 2.
+At position 367 to 399, the domain is characterized as EGF-like 1.
+At position 402 to 438, the domain is characterized as EGF-like 2.
+At position 473 to 510, the domain is characterized as EGF-like 3.
+At position 701 to 880, the domain is characterized as ABC transmembrane type-2.
+At position 215 to 282, the domain is characterized as BTB.
+At position 269 to 478, the domain is characterized as NEL.
+At position 123 to 189, the domain is characterized as PQ-loop 1.
+At position 263 to 328, the domain is characterized as PQ-loop 2.
+At position 29 to 139, the domain is characterized as Ig-like V-type.
+At position 145 to 238, the domain is characterized as Ig-like C2-type.
+At position 367 to 538, the domain is characterized as tr-type G.
+At position 108 to 260, the domain is characterized as Nudix hydrolase.
+At position 489 to 568, the domain is characterized as PABC.
+At position 122 to 160, the domain is characterized as LDL-receptor class A 1.
+At position 161 to 213, the domain is characterized as LDL-receptor class A 2.
+At position 215 to 252, the domain is characterized as LDL-receptor class A 3.
+At position 253 to 288, the domain is characterized as LDL-receptor class A 4.
+At position 291 to 328, the domain is characterized as LDL-receptor class A 5.
+At position 370 to 412, the domain is characterized as LDL-receptor class A 6.
+At position 416 to 454, the domain is characterized as LDL-receptor class A 7.
+At position 455 to 492, the domain is characterized as LDL-receptor class A 8.
+At position 60 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 104 to 133, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 299, the domain is characterized as Deacetylase sirtuin-type.
+At position 50 to 275, the domain is characterized as Radical SAM core.
+At position 33 to 207, the domain is characterized as Exonuclease.
+At position 73 to 195, the domain is characterized as GST C-terminal.
+At position 684 to 764, the domain is characterized as ERCC4.
+At position 8 to 256, the domain is characterized as ABC transporter.
+At position 111 to 187, the domain is characterized as Lipoyl-binding.
+At position 248 to 285, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 8 to 84, the domain is characterized as KRAB.
+At position 76 to 417, the domain is characterized as Peptidase A1.
+At position 35 to 169, the domain is characterized as MPN.
+At position 1 to 447, the domain is characterized as Biotin carboxylation.
+At position 121 to 318, the domain is characterized as ATP-grasp.
+At position 22 to 81, the domain is characterized as LIM zinc-binding 1.
+At position 81 to 141, the domain is characterized as LIM zinc-binding 2.
+At position 151 to 210, the domain is characterized as LIM zinc-binding 3.
+At position 210 to 270, the domain is characterized as LIM zinc-binding 4.
+At position 543 to 611, the domain is characterized as HP.
+At position 296 to 546, the domain is characterized as Glutamine amidotransferase type-1.
+At position 35 to 151, the domain is characterized as Plastocyanin-like 1.
+At position 161 to 314, the domain is characterized as Plastocyanin-like 2.
+At position 424 to 558, the domain is characterized as Plastocyanin-like 3.
+At position 395 to 474, the domain is characterized as Albumin 3.
+At position 54 to 294, the domain is characterized as ABC transporter.
+At position 371 to 550, the domain is characterized as Rab-GAP TBC.
+At position 17 to 100, the domain is characterized as Rhodanese.
+At position 42 to 112, the domain is characterized as SH3.
+At position 224 to 384, the domain is characterized as TrmE-type G.
+At position 60 to 230, the domain is characterized as Helicase ATP-binding.
+At position 1 to 122, the domain is characterized as PH.
+At position 722 to 902, the domain is characterized as Rho-GAP.
+At position 126 to 176, the domain is characterized as DHHC.
+At position 162 to 247, the domain is characterized as APO 1.
+At position 332 to 417, the domain is characterized as APO 2.
+At position 226 to 404, the domain is characterized as Helicase ATP-binding.
+At position 592 to 742, the domain is characterized as Helicase C-terminal.
+At position 9 to 194, the domain is characterized as Miro 1.
+At position 210 to 245, the domain is characterized as EF-hand 1.
+At position 444 to 607, the domain is characterized as Miro 2.
+At position 1 to 286, the domain is characterized as CN hydrolase.
+At position 13 to 91, the domain is characterized as GST N-terminal.
+At position 92 to 236, the domain is characterized as GST C-terminal.
+At position 47 to 282, the domain is characterized as ABC transmembrane type-2.
+At position 126 to 240, the domain is characterized as sHSP.
+At position 100 to 149, the domain is characterized as G-patch.
+At position 1 to 361, the domain is characterized as PTS EIIC type-1.
+At position 375 to 452, the domain is characterized as PTS EIIB type-1.
+At position 40 to 127, the domain is characterized as PPIase FKBP-type.
+At position 7 to 80, the domain is characterized as PAS 1.
+At position 81 to 135, the domain is characterized as PAC 1.
+At position 200 to 273, the domain is characterized as PAS 2.
+At position 274 to 328, the domain is characterized as PAC 2.
+At position 404 to 712, the domain is characterized as Protein kinase.
+At position 713 to 749, the domain is characterized as AGC-kinase C-terminal.
+At position 5 to 151, the domain is characterized as Flavodoxin-like.
+At position 202 to 439, the domain is characterized as FAD-binding FR-type.
+At position 288 to 331, the domain is characterized as EGF-like.
+At position 65 to 301, the domain is characterized as NR LBD.
+At position 8 to 76, the domain is characterized as TRAM.
+At position 4 to 100, the domain is characterized as Rieske.
+At position 93 to 221, the domain is characterized as FAD-binding FR-type.
+At position 27 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 31 to 60, the domain is characterized as IQ 1.
+At position 220 to 251, the domain is characterized as IQ 2.
+At position 270 to 299, the domain is characterized as IQ 3.
+At position 293 to 322, the domain is characterized as IQ 4.
+At position 366 to 395, the domain is characterized as IQ 5.
+At position 389 to 420, the domain is characterized as IQ 6.
+At position 439 to 468, the domain is characterized as IQ 7.
+At position 462 to 491, the domain is characterized as IQ 8.
+At position 512 to 541, the domain is characterized as IQ 9.
+At position 535 to 566, the domain is characterized as IQ 10.
+At position 608 to 639, the domain is characterized as IQ 11.
+At position 658 to 687, the domain is characterized as IQ 12.
+At position 681 to 712, the domain is characterized as IQ 13.
+At position 731 to 762, the domain is characterized as IQ 14.
+At position 754 to 785, the domain is characterized as IQ 15.
+At position 804 to 835, the domain is characterized as IQ 16.
+At position 827 to 856, the domain is characterized as IQ 17.
+At position 877 to 908, the domain is characterized as IQ 18.
+At position 900 to 931, the domain is characterized as IQ 19.
+At position 949 to 980, the domain is characterized as IQ 20.
+At position 972 to 1003, the domain is characterized as IQ 21.
+At position 1022 to 1053, the domain is characterized as IQ 22.
+At position 1045 to 1076, the domain is characterized as IQ 23.
+At position 1095 to 1126, the domain is characterized as IQ 24.
+At position 1168 to 1199, the domain is characterized as IQ 25.
+At position 1304 to 1333, the domain is characterized as IQ 26.
+At position 1327 to 1358, the domain is characterized as IQ 27.
+At position 1377 to 1406, the domain is characterized as IQ 28.
+At position 1452 to 1483, the domain is characterized as IQ 29.
+At position 1474 to 1503, the domain is characterized as IQ 30.
+At position 1500 to 1531, the domain is characterized as IQ 31.
+At position 59 to 274, the domain is characterized as Radical SAM core.
+At position 49 to 350, the domain is characterized as Protein kinase.
+At position 28 to 85, the domain is characterized as Chitin-binding type-2 1.
+At position 88 to 146, the domain is characterized as Chitin-binding type-2 2.
+At position 147 to 201, the domain is characterized as Chitin-binding type-2 3.
+At position 220 to 283, the domain is characterized as Chitin-binding type-2 4.
+At position 286 to 355, the domain is characterized as Chitin-binding type-2 5.
+At position 120 to 324, the domain is characterized as ATP-grasp.
+At position 26 to 105, the domain is characterized as RRM 1.
+At position 174 to 247, the domain is characterized as RRM 2.
+At position 24 to 249, the domain is characterized as ABC transporter.
+At position 28 to 50, the domain is characterized as LRRNT.
+At position 180 to 234, the domain is characterized as LRRCT.
+At position 431 to 518, the domain is characterized as Rieske.
+At position 18 to 172, the domain is characterized as Thioredoxin 1.
+At position 178 to 321, the domain is characterized as Thioredoxin 2.
+At position 325 to 485, the domain is characterized as Thioredoxin 3.
+At position 33 to 163, the domain is characterized as VHS.
+At position 188 to 315, the domain is characterized as GAT.
+At position 484 to 605, the domain is characterized as GAE.
+At position 30 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 16 to 252, the domain is characterized as Radical SAM core.
+At position 58 to 158, the domain is characterized as THUMP.
+At position 173 to 206, the domain is characterized as EF-hand 1.
+At position 203 to 238, the domain is characterized as EF-hand 2.
+At position 268 to 302, the domain is characterized as EF-hand 3.
+At position 136 to 481, the domain is characterized as Peptidase S8.
+At position 489 to 625, the domain is characterized as P/Homo B.
+At position 20 to 84, the domain is characterized as S4 RNA-binding.
+At position 33 to 260, the domain is characterized as RNase H type-2.
+At position 39 to 157, the domain is characterized as MTTase N-terminal.
+At position 180 to 410, the domain is characterized as Radical SAM core.
+At position 149 to 246, the domain is characterized as HD.
+At position 503 to 564, the domain is characterized as TGS.
+At position 768 to 842, the domain is characterized as ACT.
+At position 38 to 141, the domain is characterized as Glutaredoxin.
+At position 148 to 219, the domain is characterized as LRRCT.
+At position 196 to 285, the domain is characterized as Ig-like C2-type 1.
+At position 295 to 368, the domain is characterized as Ig-like C2-type 2.
+At position 513 to 784, the domain is characterized as Protein kinase.
+At position 46 to 172, the domain is characterized as SCP.
+At position 208 to 241, the domain is characterized as ShKT.
+At position 287 to 329, the domain is characterized as CCT.
+At position 580 to 686, the domain is characterized as tRNA-binding.
+At position 35 to 141, the domain is characterized as PINc.
+At position 286 to 345, the domain is characterized as SH3 1.
+At position 348 to 403, the domain is characterized as SH3 2.
+At position 57 to 324, the domain is characterized as Protein kinase.
+At position 371 to 406, the domain is characterized as EF-hand 1.
+At position 415 to 450, the domain is characterized as EF-hand 2.
+At position 451 to 486, the domain is characterized as EF-hand 3.
+At position 487 to 520, the domain is characterized as EF-hand 4.
+At position 147 to 213, the domain is characterized as KH 2.
+At position 397 to 464, the domain is characterized as KH 3.
+At position 96 to 171, the domain is characterized as PRC barrel.
+At position 3 to 224, the domain is characterized as ABC transporter.
+At position 27 to 216, the domain is characterized as FAD-binding PCMH-type.
+At position 139 to 262, the domain is characterized as RNase III.
+At position 285 to 356, the domain is characterized as DRBM.
+At position 37 to 147, the domain is characterized as HTH APSES-type.
+At position 86 to 210, the domain is characterized as GST C-terminal.
+At position 26 to 88, the domain is characterized as R3H.
+At position 70 to 169, the domain is characterized as Cytochrome b5 heme-binding.
+At position 3 to 92, the domain is characterized as CS.
+At position 12 to 292, the domain is characterized as Protein kinase.
+At position 703 to 786, the domain is characterized as BRCT.
+At position 5 to 162, the domain is characterized as UBC core.
+At position 174 to 374, the domain is characterized as CheB-type methylesterase.
+At position 76 to 226, the domain is characterized as PPIase cyclophilin-type.
+At position 128 to 377, the domain is characterized as Radical SAM core.
+At position 235 to 360, the domain is characterized as GAF.
+At position 360 to 577, the domain is characterized as Histidine kinase.
+At position 36 to 182, the domain is characterized as FAS1.
+At position 41 to 158, the domain is characterized as RabBD.
+At position 16 to 274, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 54 to 255, the domain is characterized as ABC transmembrane type-1 1.
+At position 315 to 496, the domain is characterized as ABC transmembrane type-1 2.
+At position 387 to 724, the domain is characterized as Kinesin motor.
+At position 28 to 107, the domain is characterized as GS beta-grasp.
+At position 114 to 359, the domain is characterized as GS catalytic.
+At position 301 to 366, the domain is characterized as SAM.
+At position 1088 to 1483, the domain is characterized as Protein kinase.
+At position 92 to 214, the domain is characterized as C2 1.
+At position 254 to 387, the domain is characterized as C2 2.
+At position 441 to 926, the domain is characterized as USP.
+At position 43 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 214 to 256, the domain is characterized as EGF-like 1.
+At position 258 to 303, the domain is characterized as EGF-like 2.
+At position 305 to 345, the domain is characterized as EGF-like 3.
+At position 372 to 426, the domain is characterized as Ig-like C2-type 2.
+At position 446 to 545, the domain is characterized as Fibronectin type-III 1.
+At position 548 to 642, the domain is characterized as Fibronectin type-III 2.
+At position 646 to 739, the domain is characterized as Fibronectin type-III 3.
+At position 839 to 1118, the domain is characterized as Protein kinase.
+At position 47 to 106, the domain is characterized as TSP type-1 1.
+At position 570 to 624, the domain is characterized as TSP type-1 2.
+At position 628 to 692, the domain is characterized as TSP type-1 3.
+At position 694 to 742, the domain is characterized as TSP type-1 4.
+At position 743 to 801, the domain is characterized as TSP type-1 5.
+At position 803 to 857, the domain is characterized as TSP type-1 6.
+At position 859 to 914, the domain is characterized as TSP type-1 7.
+At position 918 to 956, the domain is characterized as PLAC.
+At position 391 to 817, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1306 to 1613, the domain is characterized as PKS/mFAS DH.
+At position 1659 to 1734, the domain is characterized as Carrier 1.
+At position 1844 to 1921, the domain is characterized as Carrier 2.
+At position 36 to 207, the domain is characterized as FAD-binding PCMH-type.
+At position 29 to 102, the domain is characterized as CSD.
+At position 90 to 166, the domain is characterized as RRM 2.
+At position 96 to 262, the domain is characterized as Helicase ATP-binding.
+At position 625 to 789, the domain is characterized as Toprim.
+At position 156 to 267, the domain is characterized as FAD-binding FR-type.
+At position 69 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 434 to 549, the domain is characterized as PH 1.
+At position 765 to 832, the domain is characterized as RBD.
+At position 845 to 908, the domain is characterized as PDZ.
+At position 1040 to 1234, the domain is characterized as DH.
+At position 1261 to 1397, the domain is characterized as PH 2.
+At position 15 to 176, the domain is characterized as Exonuclease.
+At position 97 to 471, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 90, the domain is characterized as Ubiquitin-like.
+At position 214 to 337, the domain is characterized as SET.
+At position 10 to 62, the domain is characterized as HTH myb-type 1.
+At position 27 to 98, the domain is characterized as Ig-like.
+At position 163 to 190, the domain is characterized as ITAM.
+At position 16 to 146, the domain is characterized as VHS.
+At position 589 to 710, the domain is characterized as GAE.
+At position 20 to 242, the domain is characterized as Peptidase S1.
+At position 37 to 503, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 532 to 816, the domain is characterized as UvrD-like helicase C-terminal.
+At position 208 to 268, the domain is characterized as KH.
+At position 254 to 366, the domain is characterized as PAZ.
+At position 535 to 844, the domain is characterized as Piwi.
+At position 21 to 287, the domain is characterized as Protein kinase.
+At position 15 to 293, the domain is characterized as CNH.
+At position 160 to 348, the domain is characterized as Helicase ATP-binding.
+At position 379 to 568, the domain is characterized as Helicase C-terminal.
+At position 15 to 342, the domain is characterized as Peptidase A1.
+At position 104 to 183, the domain is characterized as PRC barrel.
+At position 73 to 271, the domain is characterized as Peptidase M12A.
+At position 287 to 325, the domain is characterized as ShKT 1.
+At position 348 to 384, the domain is characterized as ShKT 2.
+At position 203 to 280, the domain is characterized as BCNT-C.
+At position 44 to 171, the domain is characterized as RNase III.
+At position 196 to 265, the domain is characterized as DRBM.
+At position 7 to 74, the domain is characterized as NAC-A/B.
+At position 22 to 135, the domain is characterized as Ig-like C2-type.
+At position 142 to 235, the domain is characterized as Fibronectin type-III 1.
+At position 240 to 335, the domain is characterized as Fibronectin type-III 2.
+At position 337 to 438, the domain is characterized as Fibronectin type-III 3.
+At position 439 to 538, the domain is characterized as Fibronectin type-III 4.
+At position 643 to 903, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 888 to 1153, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 95 to 300, the domain is characterized as ABC transmembrane type-1.
+At position 38 to 121, the domain is characterized as Apple.
+At position 338 to 398, the domain is characterized as S4 RNA-binding.
+At position 2 to 80, the domain is characterized as BRCT 1.
+At position 121 to 199, the domain is characterized as BRCT 2.
+At position 337 to 446, the domain is characterized as BRCT.
+At position 253 to 484, the domain is characterized as NR LBD.
+At position 40 to 115, the domain is characterized as DEP.
+At position 261 to 330, the domain is characterized as G protein gamma.
+At position 336 to 441, the domain is characterized as RGS.
+At position 21 to 73, the domain is characterized as Kazal-like.
+At position 938 to 1061, the domain is characterized as PINc.
+At position 163 to 332, the domain is characterized as OBG-type G.
+At position 80 to 380, the domain is characterized as AB hydrolase-1.
+At position 215 to 338, the domain is characterized as DEUBAD.
+At position 44 to 163, the domain is characterized as Bulb-type lectin.
+At position 371 to 386, the domain is characterized as EF-hand 2.
+At position 72 to 157, the domain is characterized as PB1.
+At position 70 to 145, the domain is characterized as HTH CENPB-type.
+At position 172 to 384, the domain is characterized as DDE-1.
+At position 162 to 246, the domain is characterized as GST N-terminal.
+At position 255 to 404, the domain is characterized as GST C-terminal.
+At position 704 to 782, the domain is characterized as RRM 1.
+At position 801 to 878, the domain is characterized as RRM 2.
+At position 21 to 129, the domain is characterized as Ig-like V-type.
+At position 1307 to 1360, the domain is characterized as AWS.
+At position 1362 to 1479, the domain is characterized as SET.
+At position 1486 to 1502, the domain is characterized as Post-SET.
+At position 1963 to 1996, the domain is characterized as WW.
+At position 211 to 287, the domain is characterized as Carrier.
+At position 7 to 64, the domain is characterized as HTH lysR-type 1.
+At position 99 to 156, the domain is characterized as HTH lysR-type 2.
+At position 38 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 203, the domain is characterized as Ig-like C2-type 2.
+At position 486 to 669, the domain is characterized as Helicase ATP-binding 1.
+At position 728 to 914, the domain is characterized as Helicase C-terminal 1.
+At position 978 to 1287, the domain is characterized as SEC63 1.
+At position 1336 to 1511, the domain is characterized as Helicase ATP-binding 2.
+At position 1544 to 1739, the domain is characterized as Helicase C-terminal 2.
+At position 1812 to 2176, the domain is characterized as SEC63 2.
+At position 274 to 357, the domain is characterized as PUA.
+At position 22 to 286, the domain is characterized as Protein kinase.
+At position 16 to 58, the domain is characterized as CUE.
+At position 213 to 283, the domain is characterized as PAS.
+At position 287 to 329, the domain is characterized as PAC.
+At position 480 to 820, the domain is characterized as PDEase.
+At position 46 to 228, the domain is characterized as Macro.
+At position 397 to 553, the domain is characterized as CRAL-TRIO.
+At position 287 to 381, the domain is characterized as BRCT.
+At position 665 to 926, the domain is characterized as Protein kinase.
+At position 267 to 343, the domain is characterized as ACT 1.
+At position 13 to 217, the domain is characterized as Cytochrome b561.
+At position 208 to 474, the domain is characterized as Protein kinase.
+At position 226 to 383, the domain is characterized as TrmE-type G.
+At position 16 to 196, the domain is characterized as Guanylate kinase-like.
+At position 62 to 286, the domain is characterized as SET.
+At position 68 to 350, the domain is characterized as Protein kinase.
+At position 82 to 245, the domain is characterized as CRAL-TRIO.
+At position 90 to 395, the domain is characterized as BRO1.
+At position 227 to 288, the domain is characterized as CBS 1.
+At position 302 to 361, the domain is characterized as CBS 2.
+At position 374 to 431, the domain is characterized as CBS 3.
+At position 435 to 502, the domain is characterized as CBS 4.
+At position 33 to 352, the domain is characterized as ABC transporter.
+At position 538 to 638, the domain is characterized as tRNA-binding.
+At position 220 to 320, the domain is characterized as Fe2OG dioxygenase.
+At position 12 to 153, the domain is characterized as N-acetyltransferase.
+At position 1021 to 1054, the domain is characterized as WW.
+At position 652 to 825, the domain is characterized as MOSC.
+At position 3 to 218, the domain is characterized as Glutamine amidotransferase type-1.
+At position 255 to 349, the domain is characterized as OTU.
+At position 27 to 150, the domain is characterized as Bulb-type lectin.
+At position 290 to 326, the domain is characterized as EGF-like; atypical.
+At position 345 to 425, the domain is characterized as PAN.
+At position 509 to 788, the domain is characterized as Protein kinase.
+At position 205 to 243, the domain is characterized as LDL-receptor class A 1.
+At position 244 to 296, the domain is characterized as LDL-receptor class A 2.
+At position 298 to 335, the domain is characterized as LDL-receptor class A 3.
+At position 336 to 375, the domain is characterized as LDL-receptor class A 4.
+At position 378 to 415, the domain is characterized as LDL-receptor class A 5.
+At position 457 to 499, the domain is characterized as LDL-receptor class A 6.
+At position 503 to 541, the domain is characterized as LDL-receptor class A 7.
+At position 542 to 579, the domain is characterized as LDL-receptor class A 8.
+At position 284 to 303, the domain is characterized as UIM.
+At position 424 to 500, the domain is characterized as UBX.
+At position 185 to 285, the domain is characterized as Glutaredoxin.
+At position 43 to 97, the domain is characterized as HTH myb-type.
+At position 4 to 232, the domain is characterized as ABC transporter.
+At position 186 to 235, the domain is characterized as bHLH.
+At position 32 to 101, the domain is characterized as POTRA.
+At position 173 to 224, the domain is characterized as F-box.
+At position 195 to 417, the domain is characterized as Histidine kinase.
+At position 463 to 581, the domain is characterized as Response regulatory.
+At position 618 to 711, the domain is characterized as HPt.
+At position 145 to 334, the domain is characterized as CheB-type methylesterase.
+At position 267 to 376, the domain is characterized as PH.
+At position 527 to 625, the domain is characterized as SH2.
+At position 136 to 396, the domain is characterized as Protein kinase.
+At position 8 to 74, the domain is characterized as HTH gntR-type.
+At position 22 to 71, the domain is characterized as F-box.
+At position 156 to 360, the domain is characterized as ATP-grasp.
+At position 1 to 390, the domain is characterized as PIPK.
+At position 28 to 114, the domain is characterized as IGFBP N-terminal.
+At position 105 to 158, the domain is characterized as Kazal-like.
+At position 160 to 264, the domain is characterized as Ig-like C2-type.
+At position 276 to 465, the domain is characterized as B30.2/SPRY.
+At position 4 to 197, the domain is characterized as DPCK.
+At position 335 to 383, the domain is characterized as RPE1 insert.
+At position 11 to 120, the domain is characterized as Rieske.
+At position 6 to 215, the domain is characterized as ABC transporter.
+At position 461 to 494, the domain is characterized as PLD phosphodiesterase 2.
+At position 11 to 202, the domain is characterized as Albumin 1.
+At position 203 to 395, the domain is characterized as Albumin 2.
+At position 396 to 593, the domain is characterized as Albumin 3.
+At position 49 to 126, the domain is characterized as PTS EIIB type-1.
+At position 1 to 75, the domain is characterized as Peptidase S1.
+At position 333 to 610, the domain is characterized as BEACH.
+At position 113 to 138, the domain is characterized as IQ 1.
+At position 139 to 161, the domain is characterized as IQ 2.
+At position 260 to 436, the domain is characterized as TR mART core.
+At position 406 to 489, the domain is characterized as PPIase FKBP-type.
+At position 22 to 62, the domain is characterized as CHCH.
+At position 200 to 389, the domain is characterized as GMPS ATP-PPase.
+At position 28 to 327, the domain is characterized as ABC transmembrane type-1.
+At position 358 to 410, the domain is characterized as FBD.
+At position 40 to 190, the domain is characterized as CBM-cenC 1.
+At position 193 to 342, the domain is characterized as CBM-cenC 2.
+At position 350 to 678, the domain is characterized as GH10.
+At position 3 to 2230, the domain is characterized as Zinc-hook.
+At position 70 to 324, the domain is characterized as Chorismate mutase.
+At position 18 to 228, the domain is characterized as Radical SAM core.
+At position 482 to 591, the domain is characterized as DOD-type homing endonuclease.
+At position 656 to 966, the domain is characterized as Protein kinase.
+At position 27 to 122, the domain is characterized as Ig-like.
+At position 3 to 113, the domain is characterized as HIT.
+At position 61 to 168, the domain is characterized as THUMP.
+At position 53 to 270, the domain is characterized as ABC transmembrane type-1.
+At position 146 to 201, the domain is characterized as AWS.
+At position 203 to 320, the domain is characterized as SET.
+At position 327 to 343, the domain is characterized as Post-SET.
+At position 604 to 635, the domain is characterized as WW.
+At position 319 to 691, the domain is characterized as Protein kinase 1.
+At position 894 to 1482, the domain is characterized as Protein kinase 2.
+At position 257 to 306, the domain is characterized as RPE1 insert.
+At position 791 to 974, the domain is characterized as DH.
+At position 1015 to 1224, the domain is characterized as BAR.
+At position 1292 to 1355, the domain is characterized as SH3 5.
+At position 1519 to 1582, the domain is characterized as SH3 6.
+At position 7 to 60, the domain is characterized as bHLH.
+At position 24 to 204, the domain is characterized as Chitin-binding type-4.
+At position 443 to 484, the domain is characterized as Chitin-binding type-3.
+At position 75 to 370, the domain is characterized as Deacetylase sirtuin-type.
+At position 151 to 412, the domain is characterized as SMP-LTD.
+At position 8 to 119, the domain is characterized as PH.
+At position 28 to 251, the domain is characterized as AB hydrolase-1.
+At position 143 to 453, the domain is characterized as NB-ARC.
+At position 415 to 590, the domain is characterized as Helicase ATP-binding.
+At position 602 to 763, the domain is characterized as Helicase C-terminal.
+At position 1 to 106, the domain is characterized as SSB.
+At position 92 to 182, the domain is characterized as Ig-like C1-type.
+At position 493 to 642, the domain is characterized as CBM3.
+At position 653 to 743, the domain is characterized as Fibronectin type-III 1.
+At position 751 to 840, the domain is characterized as Fibronectin type-III 2.
+At position 849 to 940, the domain is characterized as Fibronectin type-III 3.
+At position 939 to 1045, the domain is characterized as CBM2.
+At position 30 to 82, the domain is characterized as Myosin N-terminal SH3-like.
+At position 86 to 759, the domain is characterized as Myosin motor.
+At position 762 to 791, the domain is characterized as IQ.
+At position 122 to 189, the domain is characterized as BTB.
+At position 1081 to 1101, the domain is characterized as WH2.
+At position 314 to 499, the domain is characterized as VWFA.
+At position 1752 to 1850, the domain is characterized as Calx-beta 1.
+At position 1863 to 1974, the domain is characterized as Calx-beta 2.
+At position 1989 to 2095, the domain is characterized as Calx-beta 3.
+At position 208 to 395, the domain is characterized as Glutamine amidotransferase type-1.
+At position 147 to 174, the domain is characterized as EF-hand 2.
+At position 19 to 230, the domain is characterized as SEC7.
+At position 362 to 508, the domain is characterized as PH.
+At position 193 to 434, the domain is characterized as RMT2.
+At position 102 to 259, the domain is characterized as Nudix hydrolase.
+At position 1394 to 1546, the domain is characterized as Nudix hydrolase.
+At position 17 to 117, the domain is characterized as AB hydrolase-1.
+At position 158 to 226, the domain is characterized as BTB.
+At position 141 to 414, the domain is characterized as ABC transporter 1.
+At position 492 to 704, the domain is characterized as ABC transmembrane type-2 1.
+At position 808 to 1053, the domain is characterized as ABC transporter 2.
+At position 1125 to 1339, the domain is characterized as ABC transmembrane type-2 2.
+At position 69 to 388, the domain is characterized as Kinesin motor.
+At position 27 to 52, the domain is characterized as LRRNT.
+At position 360 to 514, the domain is characterized as Helicase C-terminal.
+At position 26 to 101, the domain is characterized as IGFBP N-terminal.
+At position 87 to 145, the domain is characterized as Kazal-like.
+At position 147 to 251, the domain is characterized as Ig-like C2-type.
+At position 5 to 114, the domain is characterized as MTTase N-terminal.
+At position 160 to 390, the domain is characterized as Radical SAM core.
+At position 213 to 245, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 23 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 161 to 332, the domain is characterized as OBG-type G.
+At position 1 to 40, the domain is characterized as S1 motif; truncated.
+At position 34 to 84, the domain is characterized as CAP-Gly.
+At position 80 to 175, the domain is characterized as Fe2OG dioxygenase.
+At position 157 to 299, the domain is characterized as PPC.
+At position 12 to 52, the domain is characterized as LDL-receptor class A 1.
+At position 53 to 93, the domain is characterized as LDL-receptor class A 2.
+At position 94 to 132, the domain is characterized as LDL-receptor class A 3.
+At position 133 to 173, the domain is characterized as LDL-receptor class A 4.
+At position 182 to 220, the domain is characterized as LDL-receptor class A 5.
+At position 221 to 259, the domain is characterized as LDL-receptor class A 6.
+At position 261 to 300, the domain is characterized as LDL-receptor class A 7.
+At position 301 to 340, the domain is characterized as EGF-like 1.
+At position 341 to 380, the domain is characterized as EGF-like 2; calcium-binding.
+At position 650 to 699, the domain is characterized as EGF-like 3.
+At position 4 to 216, the domain is characterized as N-acetyltransferase.
+At position 1 to 155, the domain is characterized as Reticulon.
+At position 41 to 178, the domain is characterized as Nudix hydrolase.
+At position 226 to 494, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 3 to 282, the domain is characterized as Deacetylase sirtuin-type.
+At position 400 to 460, the domain is characterized as Dockerin.
+At position 186 to 264, the domain is characterized as PDZ.
+At position 744 to 857, the domain is characterized as VRR-NUC.
+At position 236 to 538, the domain is characterized as CN hydrolase.
+At position 107 to 167, the domain is characterized as TRAM.
+At position 57 to 248, the domain is characterized as Reverse transcriptase.
+At position 463 to 593, the domain is characterized as RNase H type-1.
+At position 645 to 806, the domain is characterized as Integrase catalytic.
+At position 5 to 113, the domain is characterized as PINc.
+At position 19 to 112, the domain is characterized as PPIase FKBP-type.
+At position 74 to 299, the domain is characterized as Radical SAM core.
+At position 234 to 359, the domain is characterized as Cyclin N-terminal.
+At position 610 to 792, the domain is characterized as Lon proteolytic.
+At position 148 to 516, the domain is characterized as GRAS.
+At position 4 to 101, the domain is characterized as PH 1.
+At position 136 to 221, the domain is characterized as DEP.
+At position 244 to 347, the domain is characterized as PH 2.
+At position 30 to 145, the domain is characterized as Plastocyanin-like 1.
+At position 154 to 318, the domain is characterized as Plastocyanin-like 2.
+At position 423 to 545, the domain is characterized as Plastocyanin-like 3.
+At position 264 to 510, the domain is characterized as ABC transporter 2.
+At position 54 to 217, the domain is characterized as EngA-type G 1.
+At position 229 to 402, the domain is characterized as EngA-type G 2.
+At position 403 to 485, the domain is characterized as KH-like.
+At position 179 to 251, the domain is characterized as PUB.
+At position 332 to 409, the domain is characterized as UBX.
+At position 8 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 374 to 627, the domain is characterized as Protein kinase.
+At position 96 to 177, the domain is characterized as PRC barrel.
+At position 17 to 77, the domain is characterized as v-SNARE coiled-coil homology.
+At position 244 to 487, the domain is characterized as CN hydrolase.
+At position 160 to 507, the domain is characterized as PPM-type phosphatase.
+At position 1 to 106, the domain is characterized as Ig-like.
+At position 1094 to 1530, the domain is characterized as CBP/p300-type HAT.
+At position 233 to 480, the domain is characterized as NR LBD.
+At position 32 to 116, the domain is characterized as GST N-terminal.
+At position 121 to 241, the domain is characterized as GST C-terminal.
+At position 208 to 261, the domain is characterized as HAMP.
+At position 269 to 487, the domain is characterized as Histidine kinase.
+At position 5 to 63, the domain is characterized as CpcD-like.
+At position 132 to 424, the domain is characterized as Peptidase S8.
+At position 157 to 388, the domain is characterized as NR LBD.
+At position 412 to 622, the domain is characterized as Histidine kinase.
+At position 425 to 488, the domain is characterized as SAM.
+At position 216 to 241, the domain is characterized as EF-hand 1.
+At position 243 to 278, the domain is characterized as EF-hand 2.
+At position 329 to 364, the domain is characterized as EF-hand 3.
+At position 437 to 472, the domain is characterized as EF-hand 4.
+At position 530 to 621, the domain is characterized as BRCT 4.
+At position 83 to 241, the domain is characterized as Flavodoxin-like.
+At position 403 to 649, the domain is characterized as Radical SAM core.
+At position 1 to 107, the domain is characterized as MTTase N-terminal.
+At position 131 to 360, the domain is characterized as Radical SAM core.
+At position 205 to 238, the domain is characterized as ShKT.
+At position 11 to 40, the domain is characterized as IQ 1.
+At position 67 to 96, the domain is characterized as IQ 2.
+At position 302 to 377, the domain is characterized as B5.
+At position 210 to 290, the domain is characterized as G5.
+At position 126 to 170, the domain is characterized as bZIP.
+At position 191 to 405, the domain is characterized as DOG1.
+At position 150 to 358, the domain is characterized as ATP-grasp.
+At position 793 to 963, the domain is characterized as Helicase ATP-binding.
+At position 1237 to 1391, the domain is characterized as Helicase C-terminal.
+At position 205 to 435, the domain is characterized as SMP-LTD.
+At position 221 to 315, the domain is characterized as PH.
+At position 7 to 94, the domain is characterized as Phosphagen kinase N-terminal.
+At position 120 to 362, the domain is characterized as Phosphagen kinase C-terminal.
+At position 194 to 374, the domain is characterized as PCI.
+At position 278 to 355, the domain is characterized as PUA.
+At position 18 to 203, the domain is characterized as RNase H type-2.
+At position 19 to 122, the domain is characterized as Cadherin 1.
+At position 123 to 250, the domain is characterized as Cadherin 2.
+At position 251 to 358, the domain is characterized as Cadherin 3.
+At position 359 to 463, the domain is characterized as Cadherin 4.
+At position 464 to 574, the domain is characterized as Cadherin 5.
+At position 582 to 690, the domain is characterized as Cadherin 6.
+At position 357 to 421, the domain is characterized as S4 RNA-binding.
+At position 128 to 207, the domain is characterized as RRM.
+At position 1194 to 1258, the domain is characterized as SAM.
+At position 5 to 457, the domain is characterized as ADPK.
+At position 316 to 351, the domain is characterized as EF-hand 2.
+At position 425 to 599, the domain is characterized as Miro 2.
+At position 44 to 294, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 299 to 569, the domain is characterized as Protein kinase.
+At position 48 to 102, the domain is characterized as HTH cro/C1-type.
+At position 34 to 274, the domain is characterized as ABC transporter.
+At position 209 to 263, the domain is characterized as PAP-associated.
+At position 385 to 419, the domain is characterized as SAP.
+At position 434 to 596, the domain is characterized as Helicase C-terminal.
+At position 42 to 242, the domain is characterized as Lon N-terminal.
+At position 629 to 809, the domain is characterized as Lon proteolytic.
+At position 139 to 174, the domain is characterized as EF-hand 4.
+At position 378 to 417, the domain is characterized as LIM interaction domain (LID).
+At position 5 to 274, the domain is characterized as PTS EIID.
+At position 226 to 378, the domain is characterized as TrmE-type G.
+At position 86 to 205, the domain is characterized as GST C-terminal.
+At position 157 to 245, the domain is characterized as EH 1.
+At position 189 to 224, the domain is characterized as EF-hand 1.
+At position 438 to 527, the domain is characterized as EH 2.
+At position 471 to 506, the domain is characterized as EF-hand 2.
+At position 1453 to 1470, the domain is characterized as WH2.
+At position 614 to 954, the domain is characterized as PUM-HD.
+At position 165 to 228, the domain is characterized as KH.
+At position 291 to 384, the domain is characterized as HD.
+At position 5 to 142, the domain is characterized as N-acetyltransferase 1.
+At position 171 to 328, the domain is characterized as N-acetyltransferase 2.
+At position 27 to 283, the domain is characterized as SET.
+At position 136 to 337, the domain is characterized as ATP-grasp.
+At position 65 to 236, the domain is characterized as Helicase ATP-binding.
+At position 247 to 408, the domain is characterized as Helicase C-terminal.
+At position 80 to 155, the domain is characterized as ACT.
+At position 518 to 620, the domain is characterized as ASD1.
+At position 1150 to 1419, the domain is characterized as ASD2.
+At position 306 to 319, the domain is characterized as CRIB.
+At position 634 to 885, the domain is characterized as Protein kinase.
+At position 301 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 41, the domain is characterized as Gla.
+At position 179 to 445, the domain is characterized as SF4 helicase.
+At position 4 to 196, the domain is characterized as RNase H type-2.
+At position 5 to 203, the domain is characterized as tr-type G.
+At position 1307 to 1614, the domain is characterized as PKS/mFAS DH.
+At position 1660 to 1735, the domain is characterized as Carrier 1.
+At position 165 to 215, the domain is characterized as DHHC.
+At position 549 to 826, the domain is characterized as Protein kinase.
+At position 2 to 81, the domain is characterized as Core-binding (CB).
+At position 102 to 283, the domain is characterized as Tyr recombinase.
+At position 62 to 224, the domain is characterized as Laminin G-like.
+At position 391 to 440, the domain is characterized as Collagen-like 1.
+At position 482 to 538, the domain is characterized as Collagen-like 2.
+At position 824 to 877, the domain is characterized as Collagen-like 3.
+At position 905 to 950, the domain is characterized as Collagen-like 4.
+At position 951 to 989, the domain is characterized as Collagen-like 5.
+At position 1430 to 1488, the domain is characterized as Collagen-like 6.
+At position 1514 to 1744, the domain is characterized as Fibrillar collagen NC1.
+At position 63 to 124, the domain is characterized as SH3.
+At position 130 to 222, the domain is characterized as SH2.
+At position 248 to 504, the domain is characterized as Protein kinase.
+At position 45 to 163, the domain is characterized as Rhodanese.
+At position 199 to 340, the domain is characterized as Tyrosine-protein phosphatase.
+At position 112 to 201, the domain is characterized as RRM.
+At position 239 to 297, the domain is characterized as F-box.
+At position 18 to 125, the domain is characterized as PH.
+At position 172 to 371, the domain is characterized as Rho-GAP.
+At position 30 to 221, the domain is characterized as ABC transmembrane type-1.
+At position 72 to 170, the domain is characterized as Plastocyanin-like.
+At position 24 to 123, the domain is characterized as Expansin-like EG45.
+At position 26 to 142, the domain is characterized as Ig-like V-type.
+At position 86 to 146, the domain is characterized as Tudor.
+At position 23 to 317, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 38 to 133, the domain is characterized as SCAN box.
+At position 120 to 364, the domain is characterized as Radical SAM core.
+At position 91 to 183, the domain is characterized as PRC barrel.
+At position 28 to 185, the domain is characterized as DAC.
+At position 13 to 65, the domain is characterized as F-box.
+At position 112 to 397, the domain is characterized as ABC transmembrane type-1 1.
+At position 474 to 700, the domain is characterized as ABC transporter 1.
+At position 777 to 1060, the domain is characterized as ABC transmembrane type-1 2.
+At position 1101 to 1336, the domain is characterized as ABC transporter 2.
+At position 331 to 491, the domain is characterized as Helicase C-terminal.
+At position 41 to 91, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 38 to 121, the domain is characterized as KRAB.
+At position 236 to 464, the domain is characterized as CN hydrolase.
+At position 1 to 56, the domain is characterized as HTH lysR-type.
+At position 50 to 161, the domain is characterized as sHSP.
+At position 345 to 425, the domain is characterized as OCT.
+At position 1137 to 1301, the domain is characterized as PNPLA.
+At position 1 to 82, the domain is characterized as Ras-associating.
+At position 68 to 139, the domain is characterized as HTH CENPB-type.
+At position 169 to 399, the domain is characterized as DDE-1.
+At position 142 to 279, the domain is characterized as PPC.
+At position 42 to 248, the domain is characterized as BPL/LPL catalytic.
+At position 539 to 641, the domain is characterized as tRNA-binding.
+At position 30 to 140, the domain is characterized as Ig-like V-type.
+At position 76 to 400, the domain is characterized as A to I editase.
+At position 3 to 100, the domain is characterized as BMC circularly permuted 1.
+At position 106 to 205, the domain is characterized as BMC circularly permuted 2.
+At position 6 to 114, the domain is characterized as Cadherin 1.
+At position 115 to 227, the domain is characterized as Cadherin 2.
+At position 228 to 339, the domain is characterized as Cadherin 3.
+At position 340 to 443, the domain is characterized as Cadherin 4.
+At position 444 to 554, the domain is characterized as Cadherin 5.
+At position 58 to 353, the domain is characterized as GH16.
+At position 147 to 226, the domain is characterized as Ig-like C2-type.
+At position 29 to 141, the domain is characterized as Thioredoxin 1.
+At position 356 to 485, the domain is characterized as Thioredoxin 2.
+At position 36 to 225, the domain is characterized as FZ.
+At position 236 to 310, the domain is characterized as Kringle.
+At position 410 to 677, the domain is characterized as Protein kinase.
+At position 18 to 142, the domain is characterized as Response regulatory.
+At position 67 to 167, the domain is characterized as THUMP.
+At position 70 to 323, the domain is characterized as ZP.
+At position 414 to 520, the domain is characterized as HTH APSES-type.
+At position 411 to 625, the domain is characterized as BURP.
+At position 15 to 158, the domain is characterized as N-acetyltransferase 1.
+At position 164 to 307, the domain is characterized as N-acetyltransferase 2.
+At position 298 to 476, the domain is characterized as Helicase ATP-binding.
+At position 505 to 659, the domain is characterized as Helicase C-terminal.
+At position 57 to 197, the domain is characterized as CBM-cenC 1.
+At position 227 to 362, the domain is characterized as CBM-cenC 2.
+At position 397 to 541, the domain is characterized as CBM-cenC 3.
+At position 589 to 884, the domain is characterized as GH10.
+At position 263 to 347, the domain is characterized as RCK C-terminal.
+At position 164 to 411, the domain is characterized as Radical SAM core.
+At position 44 to 145, the domain is characterized as SRCR 1.
+At position 169 to 282, the domain is characterized as SRCR 2.
+At position 307 to 407, the domain is characterized as SRCR 3.
+At position 417 to 525, the domain is characterized as SRCR 4.
+At position 380 to 493, the domain is characterized as PAZ.
+At position 669 to 990, the domain is characterized as Piwi.
+At position 115 to 229, the domain is characterized as C-type lectin.
+At position 10 to 153, the domain is characterized as N-acetyltransferase 1.
+At position 22 to 128, the domain is characterized as WAC.
+At position 422 to 487, the domain is characterized as DDT.
+At position 1446 to 1516, the domain is characterized as Bromo.
+At position 22 to 147, the domain is characterized as WIF.
+At position 281 to 583, the domain is characterized as Protein kinase.
+At position 24 to 90, the domain is characterized as SAM.
+At position 134 to 393, the domain is characterized as Protein kinase.
+At position 386 to 458, the domain is characterized as Bromo 2.
+At position 624 to 708, the domain is characterized as NET.
+At position 220 to 453, the domain is characterized as Grh/CP2 DB.
+At position 651 to 1079, the domain is characterized as PDEase.
+At position 63 to 329, the domain is characterized as Septin-type G.
+At position 22 to 140, the domain is characterized as Response regulatory.
+At position 221 to 417, the domain is characterized as CheB-type methylesterase.
+At position 228 to 453, the domain is characterized as Collagen IV NC1.
+At position 17 to 329, the domain is characterized as Protein kinase.
+At position 330 to 421, the domain is characterized as AGC-kinase C-terminal.
+At position 13 to 149, the domain is characterized as MARVEL 1.
+At position 154 to 298, the domain is characterized as MARVEL 2.
+At position 300 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 102, the domain is characterized as Acylphosphatase-like.
+At position 1085 to 1163, the domain is characterized as BRCT 1.
+At position 1184 to 1275, the domain is characterized as BRCT 2.
+At position 34 to 234, the domain is characterized as GH11.
+At position 449 to 484, the domain is characterized as CBM1.
+At position 302 to 420, the domain is characterized as CobW C-terminal.
+At position 303 to 381, the domain is characterized as RRM.
+At position 29 to 99, the domain is characterized as Chitin-binding type R&R.
+At position 128 to 313, the domain is characterized as ATP-grasp.
+At position 591 to 712, the domain is characterized as MHD1.
+At position 786 to 906, the domain is characterized as C2.
+At position 1014 to 1130, the domain is characterized as MHD2.
+At position 19 to 168, the domain is characterized as Reelin.
+At position 356 to 470, the domain is characterized as PLAT.
+At position 290 to 510, the domain is characterized as Helicase ATP-binding.
+At position 717 to 891, the domain is characterized as Helicase C-terminal.
+At position 6 to 63, the domain is characterized as F-box.
+At position 278 to 358, the domain is characterized as PDZ.
+At position 23 to 97, the domain is characterized as Ig-like C2-type 1.
+At position 102 to 183, the domain is characterized as Ig-like C2-type 2.
+At position 193 to 271, the domain is characterized as Ig-like C2-type 3.
+At position 275 to 374, the domain is characterized as Ig-like C2-type 4.
+At position 33 to 291, the domain is characterized as AB hydrolase-1.
+At position 420 to 533, the domain is characterized as PAZ.
+At position 709 to 1030, the domain is characterized as Piwi.
+At position 47 to 294, the domain is characterized as GB1/RHD3-type G.
+At position 47 to 477, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 982 to 1286, the domain is characterized as PKS/mFAS DH.
+At position 2286 to 2364, the domain is characterized as Carrier.
+At position 29 to 237, the domain is characterized as MIF4G.
+At position 328 to 460, the domain is characterized as MI.
+At position 216 to 365, the domain is characterized as Thioredoxin.
+At position 5 to 128, the domain is characterized as RNase III.
+At position 8 to 247, the domain is characterized as ABC transporter 1.
+At position 258 to 504, the domain is characterized as ABC transporter 2.
+At position 158 to 559, the domain is characterized as GH18.
+At position 76 to 275, the domain is characterized as OTU.
+At position 264 to 427, the domain is characterized as MAM 1.
+At position 437 to 473, the domain is characterized as LDL-receptor class A.
+At position 478 to 636, the domain is characterized as MAM 2.
+At position 1116 to 1392, the domain is characterized as Protein kinase.
+At position 29 to 159, the domain is characterized as C-type lectin.
+At position 1 to 87, the domain is characterized as Barwin.
+At position 57 to 191, the domain is characterized as SCP.
+At position 39 to 151, the domain is characterized as MTTase N-terminal.
+At position 170 to 407, the domain is characterized as Radical SAM core.
+At position 410 to 476, the domain is characterized as TRAM.
+At position 23 to 139, the domain is characterized as AB hydrolase-1.
+At position 252 to 443, the domain is characterized as GATase cobBQ-type.
+At position 38 to 142, the domain is characterized as FAD-binding FR-type.
+At position 79 to 174, the domain is characterized as Pre-SET.
+At position 177 to 312, the domain is characterized as SET.
+At position 328 to 344, the domain is characterized as Post-SET.
+At position 26 to 66, the domain is characterized as Saposin A-type.
+At position 66 to 148, the domain is characterized as Saposin B-type 1.
+At position 188 to 265, the domain is characterized as Saposin B-type 2.
+At position 284 to 359, the domain is characterized as Saposin B-type 3.
+At position 5 to 169, the domain is characterized as Exonuclease.
+At position 104 to 522, the domain is characterized as GBD/FH3.
+At position 868 to 1278, the domain is characterized as FH2.
+At position 78 to 190, the domain is characterized as sHSP.
+At position 749 to 835, the domain is characterized as SUEL-type lectin.
+At position 460 to 588, the domain is characterized as RNase H type-1.
+At position 640 to 801, the domain is characterized as Integrase catalytic.
+At position 3 to 70, the domain is characterized as SH3 1.
+At position 71 to 132, the domain is characterized as SH3 2.
+At position 380 to 442, the domain is characterized as SH3 3.
+At position 303 to 539, the domain is characterized as NR LBD.
+At position 403 to 476, the domain is characterized as Death.
+At position 254 to 455, the domain is characterized as GATase cobBQ-type.
+At position 340 to 399, the domain is characterized as COS.
+At position 398 to 531, the domain is characterized as Fibronectin type-III.
+At position 516 to 709, the domain is characterized as B30.2/SPRY.
+At position 28 to 197, the domain is characterized as GH16.
+At position 393 to 650, the domain is characterized as Olfactomedin-like.
+At position 344 to 461, the domain is characterized as Rhodanese.
+At position 237 to 449, the domain is characterized as Helicase ATP-binding.
+At position 489 to 657, the domain is characterized as Helicase C-terminal.
+At position 1063 to 1155, the domain is characterized as ELM2.
+At position 1170 to 1221, the domain is characterized as SANT.
+At position 2 to 188, the domain is characterized as Glutamine amidotransferase type-1.
+At position 247 to 438, the domain is characterized as GATase cobBQ-type.
+At position 1535 to 1759, the domain is characterized as Collagen IV NC1.
+At position 7 to 104, the domain is characterized as Glutaredoxin.
+At position 95 to 271, the domain is characterized as Collagen-like 1.
+At position 279 to 293, the domain is characterized as Collagen-like 2.
+At position 11 to 73, the domain is characterized as GST C-terminal.
+At position 160 to 341, the domain is characterized as FCP1 homology.
+At position 486 to 579, the domain is characterized as BRCT.
+At position 24 to 100, the domain is characterized as Importin N-terminal.
+At position 7 to 299, the domain is characterized as Protein kinase.
+At position 384 to 533, the domain is characterized as MATH.
+At position 52 to 238, the domain is characterized as Helicase ATP-binding.
+At position 249 to 487, the domain is characterized as Helicase C-terminal.
+At position 56 to 103, the domain is characterized as F-box.
+At position 222 to 281, the domain is characterized as SH3.
+At position 171 to 251, the domain is characterized as RRM 2.
+At position 153 to 352, the domain is characterized as VWFA.
+At position 338 to 522, the domain is characterized as PCI.
+At position 164 to 340, the domain is characterized as PX.
+At position 191 to 381, the domain is characterized as Helicase ATP-binding.
+At position 392 to 552, the domain is characterized as Helicase C-terminal.
+At position 245 to 425, the domain is characterized as PCI.
+At position 17 to 87, the domain is characterized as BTB.
+At position 1069 to 1131, the domain is characterized as SH3.
+At position 148 to 319, the domain is characterized as Helicase ATP-binding.
+At position 348 to 497, the domain is characterized as Helicase C-terminal.
+At position 46 to 206, the domain is characterized as SIS 1.
+At position 217 to 365, the domain is characterized as SIS 2.
+At position 90 to 211, the domain is characterized as MI 1.
+At position 254 to 375, the domain is characterized as MI 2.
+At position 389 to 510, the domain is characterized as MI 3.
+At position 560 to 681, the domain is characterized as MI 4.
+At position 50 to 248, the domain is characterized as Cupin type-1 1.
+At position 318 to 467, the domain is characterized as Cupin type-1 2.
+At position 171 to 336, the domain is characterized as CMP/dCMP-type deaminase.
+At position 167 to 359, the domain is characterized as CheB-type methylesterase.
+At position 136 to 186, the domain is characterized as DHHC.
+At position 214 to 333, the domain is characterized as PAZ.
+At position 492 to 790, the domain is characterized as Piwi.
+At position 4 to 481, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 531 to 839, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 230, the domain is characterized as Radical SAM core.
+At position 46 to 297, the domain is characterized as ABC transporter.
+At position 1 to 183, the domain is characterized as Macro.
+At position 498 to 591, the domain is characterized as Fibronectin type-III 1.
+At position 3 to 187, the domain is characterized as UmuC.
+At position 18 to 166, the domain is characterized as TNase-like 1.
+At position 193 to 328, the domain is characterized as TNase-like 2.
+At position 341 to 496, the domain is characterized as TNase-like 3.
+At position 525 to 660, the domain is characterized as TNase-like 4.
+At position 729 to 787, the domain is characterized as Tudor.
+At position 108 to 240, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 59 to 147, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 190 to 220, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 201 to 296, the domain is characterized as HTH araC/xylS-type.
+At position 51 to 148, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 238, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 346, the domain is characterized as Ig-like C2-type 3.
+At position 352 to 438, the domain is characterized as Ig-like C2-type 4.
+At position 467 to 573, the domain is characterized as Fibronectin type-III 1.
+At position 581 to 676, the domain is characterized as Fibronectin type-III 2.
+At position 41 to 145, the domain is characterized as Calponin-homology (CH) 1.
+At position 154 to 260, the domain is characterized as Calponin-homology (CH) 2.
+At position 756 to 791, the domain is characterized as EF-hand 1.
+At position 792 to 827, the domain is characterized as EF-hand 2.
+At position 14 to 109, the domain is characterized as BRCT.
+At position 62 to 181, the domain is characterized as AB hydrolase-1.
+At position 26 to 160, the domain is characterized as Ephrin RBD.
+At position 43 to 282, the domain is characterized as Laminin N-terminal.
+At position 283 to 346, the domain is characterized as Laminin EGF-like 1.
+At position 410 to 469, the domain is characterized as Laminin EGF-like 3.
+At position 470 to 521, the domain is characterized as Laminin EGF-like 4.
+At position 522 to 552, the domain is characterized as Laminin EGF-like 5; truncated.
+At position 561 to 777, the domain is characterized as Laminin IV type B.
+At position 783 to 830, the domain is characterized as Laminin EGF-like 6.
+At position 831 to 876, the domain is characterized as Laminin EGF-like 7.
+At position 877 to 926, the domain is characterized as Laminin EGF-like 8.
+At position 927 to 985, the domain is characterized as Laminin EGF-like 9.
+At position 986 to 1037, the domain is characterized as Laminin EGF-like 10.
+At position 1038 to 1094, the domain is characterized as Laminin EGF-like 11.
+At position 1095 to 1142, the domain is characterized as Laminin EGF-like 12.
+At position 1143 to 1189, the domain is characterized as Laminin EGF-like 13.
+At position 5 to 194, the domain is characterized as Glutamine amidotransferase type-1.
+At position 49 to 178, the domain is characterized as VOC.
+At position 111 to 182, the domain is characterized as SUI1.
+At position 276 to 311, the domain is characterized as EF-hand 1.
+At position 315 to 347, the domain is characterized as EF-hand 2.
+At position 22 to 56, the domain is characterized as ShKT.
+At position 75 to 325, the domain is characterized as Radical SAM core 1.
+At position 534 to 769, the domain is characterized as Radical SAM core 2.
+At position 50 to 300, the domain is characterized as GB1/RHD3-type G.
+At position 257 to 315, the domain is characterized as PWWP.
+At position 263 to 446, the domain is characterized as Tyr recombinase.
+At position 4 to 146, the domain is characterized as SIS.
+At position 17 to 238, the domain is characterized as Radical SAM core.
+At position 102 to 274, the domain is characterized as CP-type G.
+At position 232 to 267, the domain is characterized as EF-hand 1.
+At position 470 to 505, the domain is characterized as EF-hand 3.
+At position 231 to 349, the domain is characterized as OmpA-like.
+At position 1635 to 1843, the domain is characterized as Rap-GAP.
+At position 825 to 1096, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1127 to 1387, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 174 to 186, the domain is characterized as EGF-like 1; incomplete.
+At position 186 to 217, the domain is characterized as EGF-like 2.
+At position 217 to 248, the domain is characterized as EGF-like 3.
+At position 248 to 280, the domain is characterized as EGF-like 4.
+At position 280 to 311, the domain is characterized as EGF-like 5.
+At position 311 to 342, the domain is characterized as EGF-like 6.
+At position 342 to 373, the domain is characterized as EGF-like 7.
+At position 373 to 404, the domain is characterized as EGF-like 8.
+At position 404 to 435, the domain is characterized as EGF-like 9.
+At position 435 to 466, the domain is characterized as EGF-like 10.
+At position 466 to 497, the domain is characterized as EGF-like 11.
+At position 497 to 528, the domain is characterized as EGF-like 12.
+At position 528 to 559, the domain is characterized as EGF-like 13.
+At position 559 to 590, the domain is characterized as EGF-like 14.
+At position 590 to 621, the domain is characterized as EGF-like 15.
+At position 625 to 715, the domain is characterized as Fibronectin type-III 1.
+At position 716 to 804, the domain is characterized as Fibronectin type-III 2.
+At position 805 to 894, the domain is characterized as Fibronectin type-III 3.
+At position 895 to 990, the domain is characterized as Fibronectin type-III 4.
+At position 991 to 1075, the domain is characterized as Fibronectin type-III 5.
+At position 1076 to 1165, the domain is characterized as Fibronectin type-III 6.
+At position 1167 to 1256, the domain is characterized as Fibronectin type-III 7.
+At position 1258 to 1350, the domain is characterized as Fibronectin type-III 8.
+At position 1351 to 1439, the domain is characterized as Fibronectin type-III 9.
+At position 1440 to 1531, the domain is characterized as Fibronectin type-III 10.
+At position 1533 to 1621, the domain is characterized as Fibronectin type-III 11.
+At position 1622 to 1711, the domain is characterized as Fibronectin type-III 12.
+At position 1712 to 1801, the domain is characterized as Fibronectin type-III 13.
+At position 1802 to 1888, the domain is characterized as Fibronectin type-III 14.
+At position 1889 to 1977, the domain is characterized as Fibronectin type-III 15.
+At position 1975 to 2190, the domain is characterized as Fibrinogen C-terminal.
+At position 656 to 985, the domain is characterized as PDEase.
+At position 332 to 611, the domain is characterized as Radical SAM core.
+At position 59 to 239, the domain is characterized as BPL/LPL catalytic.
+At position 73 to 183, the domain is characterized as THUMP.
+At position 73 to 184, the domain is characterized as PH.
+At position 685 to 940, the domain is characterized as Protein kinase.
+At position 2168 to 2215, the domain is characterized as GRIP.
+At position 102 to 335, the domain is characterized as Radical SAM core.
+At position 42 to 284, the domain is characterized as ABC transporter.
+At position 371 to 581, the domain is characterized as ABC transmembrane type-2.
+At position 164 to 229, the domain is characterized as BTB.
+At position 335 to 497, the domain is characterized as Helicase ATP-binding.
+At position 551 to 705, the domain is characterized as Helicase C-terminal.
+At position 7 to 169, the domain is characterized as PPIase cyclophilin-type.
+At position 414 to 498, the domain is characterized as B5.
+At position 15 to 222, the domain is characterized as Glutamine amidotransferase type-1.
+At position 508 to 604, the domain is characterized as EH.
+At position 129 to 301, the domain is characterized as Helicase ATP-binding.
+At position 327 to 471, the domain is characterized as Helicase C-terminal.
+At position 53 to 299, the domain is characterized as ABC transporter 1.
+At position 388 to 665, the domain is characterized as ABC transmembrane type-2 1.
+At position 721 to 960, the domain is characterized as ABC transporter 2.
+At position 1049 to 1286, the domain is characterized as ABC transmembrane type-2 2.
+At position 8 to 320, the domain is characterized as Kinesin motor.
+At position 7 to 51, the domain is characterized as SpoVT-AbrB 1.
+At position 89 to 132, the domain is characterized as SpoVT-AbrB 2.
+At position 75 to 150, the domain is characterized as Smr.
+At position 152 to 359, the domain is characterized as ATP-grasp.
+At position 3 to 76, the domain is characterized as RRM 1.
+At position 82 to 157, the domain is characterized as RRM 2.
+At position 193 to 258, the domain is characterized as KH 1.
+At position 274 to 341, the domain is characterized as KH 2.
+At position 384 to 449, the domain is characterized as KH 3.
+At position 466 to 532, the domain is characterized as KH 4.
+At position 542 to 672, the domain is characterized as CheW-like.
+At position 153 to 192, the domain is characterized as UBA.
+At position 37 to 174, the domain is characterized as Thioredoxin.
+At position 380 to 458, the domain is characterized as RRM 3.
+At position 33 to 190, the domain is characterized as PPIase cyclophilin-type.
+At position 328 to 357, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 368 to 396, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 122 to 200, the domain is characterized as RRM 2.
+At position 5 to 257, the domain is characterized as Protein kinase.
+At position 66 to 374, the domain is characterized as IF rod.
+At position 128 to 191, the domain is characterized as GRAM.
+At position 24 to 196, the domain is characterized as Laminin G-like.
+At position 277 to 318, the domain is characterized as EGF-like 1.
+At position 319 to 358, the domain is characterized as EGF-like 2; calcium-binding.
+At position 373 to 412, the domain is characterized as EGF-like 3; calcium-binding.
+At position 416 to 458, the domain is characterized as EGF-like 4.
+At position 732 to 946, the domain is characterized as TSP C-terminal.
+At position 253 to 333, the domain is characterized as Toprim.
+At position 523 to 636, the domain is characterized as SMC hinge.
+At position 271 to 466, the domain is characterized as B30.2/SPRY.
+At position 983 to 1286, the domain is characterized as PKS/mFAS DH.
+At position 2289 to 2368, the domain is characterized as Carrier.
+At position 37 to 488, the domain is characterized as Hexokinase.
+At position 51 to 102, the domain is characterized as bHLH.
+At position 157 to 189, the domain is characterized as EF-hand 4.
+At position 513 to 626, the domain is characterized as CRC.
+At position 15 to 112, the domain is characterized as PH.
+At position 397 to 841, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1326 to 1631, the domain is characterized as PKS/mFAS DH.
+At position 1692 to 1766, the domain is characterized as Carrier 1.
+At position 1807 to 1884, the domain is characterized as Carrier 2.
+At position 45 to 260, the domain is characterized as GB1/RHD3-type G.
+At position 229 to 412, the domain is characterized as FAD-binding PCMH-type.
+At position 324 to 394, the domain is characterized as Bromo.
+At position 399 to 429, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 440 to 469, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 101 to 224, the domain is characterized as Rhodanese.
+At position 98 to 207, the domain is characterized as PA.
+At position 155 to 268, the domain is characterized as Fe2OG dioxygenase.
+At position 104 to 177, the domain is characterized as RRM 2.
+At position 956 to 1157, the domain is characterized as Helicase ATP-binding.
+At position 1447 to 1606, the domain is characterized as Helicase C-terminal.
+At position 187 to 250, the domain is characterized as bZIP.
+At position 21 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 340 to 573, the domain is characterized as ABC transporter.
+At position 93 to 181, the domain is characterized as RRM.
+At position 1827 to 1944, the domain is characterized as SET.
+At position 1950 to 1966, the domain is characterized as Post-SET.
+At position 334 to 592, the domain is characterized as Protein kinase.
+At position 6 to 193, the domain is characterized as RNase H type-2.
+At position 186 to 360, the domain is characterized as Letm1 RBD.
+At position 148 to 342, the domain is characterized as CheB-type methylesterase.
+At position 30 to 67, the domain is characterized as EGF-like 1; atypical.
+At position 69 to 107, the domain is characterized as EGF-like 2.
+At position 109 to 145, the domain is characterized as EGF-like 3.
+At position 147 to 183, the domain is characterized as EGF-like 4; calcium-binding.
+At position 185 to 221, the domain is characterized as EGF-like 5; calcium-binding.
+At position 223 to 259, the domain is characterized as EGF-like 6; calcium-binding.
+At position 261 to 298, the domain is characterized as EGF-like 7.
+At position 300 to 336, the domain is characterized as EGF-like 8.
+At position 338 to 394, the domain is characterized as EGF-like 9.
+At position 396 to 438, the domain is characterized as EGF-like 10.
+At position 440 to 480, the domain is characterized as EGF-like 11.
+At position 482 to 669, the domain is characterized as Laminin G-like 1.
+At position 671 to 707, the domain is characterized as EGF-like 12.
+At position 713 to 884, the domain is characterized as Laminin G-like 2.
+At position 886 to 922, the domain is characterized as EGF-like 13.
+At position 923 to 959, the domain is characterized as EGF-like 14.
+At position 950 to 1136, the domain is characterized as Laminin G-like 3.
+At position 1138 to 1174, the domain is characterized as EGF-like 15.
+At position 1176 to 1211, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1213 to 1249, the domain is characterized as EGF-like 17.
+At position 1254 to 1294, the domain is characterized as EGF-like 18.
+At position 1296 to 1332, the domain is characterized as EGF-like 19; calcium-binding.
+At position 393 to 504, the domain is characterized as EH.
+At position 48 to 356, the domain is characterized as PPM-type phosphatase.
+At position 1 to 56, the domain is characterized as TGS.
+At position 224 to 367, the domain is characterized as FCP1 homology.
+At position 62 to 125, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 49 to 110, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 84 to 265, the domain is characterized as tr-type G.
+At position 89 to 158, the domain is characterized as S1 motif.
+At position 311 to 370, the domain is characterized as CBS 1.
+At position 374 to 434, the domain is characterized as CBS 2.
+At position 245 to 404, the domain is characterized as JmjC.
+At position 3 to 80, the domain is characterized as GIY-YIG.
+At position 169 to 373, the domain is characterized as ATP-grasp.
+At position 636 to 930, the domain is characterized as Autotransporter.
+At position 88 to 131, the domain is characterized as LysM 2.
+At position 152 to 195, the domain is characterized as LysM 3.
+At position 205 to 329, the domain is characterized as Peptidase C51.
+At position 7 to 200, the domain is characterized as Lon N-terminal.
+At position 587 to 768, the domain is characterized as Lon proteolytic.
+At position 28 to 289, the domain is characterized as Protein kinase.
+At position 695 to 950, the domain is characterized as Roc.
+At position 1308 to 1389, the domain is characterized as Death.
+At position 170 to 414, the domain is characterized as NR LBD.
+At position 74 to 146, the domain is characterized as Bromo 1.
+At position 385 to 457, the domain is characterized as Bromo 2.
+At position 623 to 707, the domain is characterized as NET.
+At position 13 to 92, the domain is characterized as U-box.
+At position 124 to 199, the domain is characterized as Sm.
+At position 24 to 126, the domain is characterized as CMP/dCMP-type deaminase.
+At position 62 to 103, the domain is characterized as LDL-receptor class A.
+At position 787 to 977, the domain is characterized as TH1.
+At position 1080 to 1141, the domain is characterized as SH3.
+At position 500 to 604, the domain is characterized as PTS EIIA type-1.
+At position 123 to 385, the domain is characterized as Protein kinase.
+At position 427 to 463, the domain is characterized as EF-hand 1.
+At position 464 to 499, the domain is characterized as EF-hand 2.
+At position 500 to 539, the domain is characterized as EF-hand 3.
+At position 542 to 571, the domain is characterized as EF-hand 4.
+At position 5 to 60, the domain is characterized as HTH cro/C1-type.
+At position 21 to 109, the domain is characterized as Rhodanese.
+At position 34 to 180, the domain is characterized as YEATS.
+At position 1 to 95, the domain is characterized as SH2.
+At position 117 to 522, the domain is characterized as Tyrosine-protein phosphatase.
+At position 20 to 190, the domain is characterized as FAD-binding PCMH-type.
+At position 33 to 201, the domain is characterized as VWFD 1.
+At position 294 to 347, the domain is characterized as TIL 1.
+At position 385 to 559, the domain is characterized as VWFD 2.
+At position 651 to 706, the domain is characterized as TIL 2.
+At position 864 to 937, the domain is characterized as VWFD 3.
+At position 100 to 186, the domain is characterized as Ras-associating.
+At position 229 to 338, the domain is characterized as PH.
+At position 431 to 527, the domain is characterized as SH2.
+At position 98 to 166, the domain is characterized as POTRA.
+At position 429 to 548, the domain is characterized as FAD-binding FR-type.
+At position 716 to 793, the domain is characterized as Cytochrome b5 heme-binding.
+At position 19 to 51, the domain is characterized as LRRNT.
+At position 181 to 232, the domain is characterized as LRRCT.
+At position 233 to 371, the domain is characterized as Ig-like.
+At position 437 to 495, the domain is characterized as Kazal-like.
+At position 500 to 557, the domain is characterized as Kazal-like.
+At position 399 to 480, the domain is characterized as B5.
+At position 714 to 808, the domain is characterized as FDX-ACB.
+At position 218 to 335, the domain is characterized as BAH.
+At position 23 to 37, the domain is characterized as EF-hand 1; degenerate.
+At position 86 to 239, the domain is characterized as Ferritin-like diiron.
+At position 371 to 423, the domain is characterized as bHLH.
+At position 512 to 611, the domain is characterized as Zinc-hook.
+At position 688 to 1004, the domain is characterized as Protein kinase.
+At position 88 to 152, the domain is characterized as BTB.
+At position 8 to 141, the domain is characterized as N-acetyltransferase 1.
+At position 625 to 888, the domain is characterized as MHD.
+At position 281 to 341, the domain is characterized as LIM zinc-binding.
+At position 146 to 259, the domain is characterized as THUMP.
+At position 238 to 370, the domain is characterized as FAD-binding FR-type.
+At position 19 to 86, the domain is characterized as PAS.
+At position 535 to 748, the domain is characterized as Histidine kinase.
+At position 265 to 360, the domain is characterized as PH.
+At position 405 to 527, the domain is characterized as Arf-GAP.
+At position 529 to 763, the domain is characterized as NR LBD.
+At position 558 to 607, the domain is characterized as FHA.
+At position 74 to 109, the domain is characterized as EF-hand 2.
+At position 600 to 667, the domain is characterized as CBS 1.
+At position 710 to 757, the domain is characterized as CBS 2.
+At position 98 to 141, the domain is characterized as LysM.
+At position 212 to 268, the domain is characterized as GRAM.
+At position 711 to 872, the domain is characterized as TLDc.
+At position 5 to 200, the domain is characterized as tr-type G.
+At position 4 to 400, the domain is characterized as BRO1.
+At position 741 to 766, the domain is characterized as IQ 2.
+At position 772 to 962, the domain is characterized as TH1.
+At position 1083 to 1145, the domain is characterized as SH3.
+At position 106 to 419, the domain is characterized as IF rod.
+At position 408 to 502, the domain is characterized as Ig-like C2-type 5.
+At position 500 to 587, the domain is characterized as Ig-like C2-type 6.
+At position 401 to 452, the domain is characterized as GRIP.
+At position 1105 to 1159, the domain is characterized as PAP-associated.
+At position 686 to 992, the domain is characterized as Protein kinase.
+At position 36 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 850 to 1133, the domain is characterized as FIIND.
+At position 1143 to 1226, the domain is characterized as CARD.
+At position 283 to 346, the domain is characterized as bZIP.
+At position 31 to 144, the domain is characterized as Ig-like V-type.
+At position 32 to 64, the domain is characterized as LisH.
+At position 70 to 127, the domain is characterized as CTLH.
+At position 138 to 361, the domain is characterized as GB1/RHD3-type G.
+At position 50 to 96, the domain is characterized as F-box.
+At position 621 to 667, the domain is characterized as Kazal-like 1.
+At position 692 to 746, the domain is characterized as Kazal-like 2.
+At position 749 to 783, the domain is characterized as Kazal-like 3.
+At position 211 to 394, the domain is characterized as PCI.
+At position 85 to 342, the domain is characterized as Protein kinase.
+At position 343 to 418, the domain is characterized as AGC-kinase C-terminal.
+At position 4 to 252, the domain is characterized as CN hydrolase.
+At position 37 to 170, the domain is characterized as N-terminal Ras-GEF.
+At position 1121 to 1361, the domain is characterized as Ras-GEF.
+At position 141 to 254, the domain is characterized as SCP.
+At position 1 to 118, the domain is characterized as THUMP.
+At position 1 to 164, the domain is characterized as PXA.
+At position 287 to 401, the domain is characterized as RGS.
+At position 508 to 628, the domain is characterized as PX.
+At position 150 to 209, the domain is characterized as CHORD 2.
+At position 216 to 305, the domain is characterized as CS.
+At position 130 to 216, the domain is characterized as RWP-RK.
+At position 225 to 281, the domain is characterized as bZIP.
+At position 44 to 154, the domain is characterized as sHSP.
+At position 26 to 112, the domain is characterized as Ig-like C2-type.
+At position 113 to 217, the domain is characterized as Fibronectin type-III 1.
+At position 218 to 316, the domain is characterized as Fibronectin type-III 2.
+At position 15 to 219, the domain is characterized as DPCK.
+At position 126 to 159, the domain is characterized as EF-hand 4.
+At position 35 to 177, the domain is characterized as GAF.
+At position 210 to 439, the domain is characterized as Sigma-54 factor interaction.
+At position 15 to 68, the domain is characterized as ClpX-type ZB.
+At position 285 to 356, the domain is characterized as KRAB.
+At position 20 to 199, the domain is characterized as UmuC.
+At position 46 to 175, the domain is characterized as VOC.
+At position 17 to 85, the domain is characterized as KH type-2.
+At position 323 to 487, the domain is characterized as VPS9.
+At position 41 to 76, the domain is characterized as EF-hand.
+At position 95 to 294, the domain is characterized as ATP-grasp.
+At position 1 to 160, the domain is characterized as DHFR.
+At position 291 to 350, the domain is characterized as SH3.
+At position 62 to 243, the domain is characterized as tr-type G.
+At position 131 to 362, the domain is characterized as Histidine kinase.
+At position 64 to 244, the domain is characterized as tr-type G.
+At position 195 to 384, the domain is characterized as GMPS ATP-PPase.
+At position 121 to 245, the domain is characterized as G8.
+At position 676 to 865, the domain is characterized as ATP-grasp 2.
+At position 937 to 1047, the domain is characterized as MGS-like.
+At position 425 to 539, the domain is characterized as Response regulatory.
+At position 30 to 167, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 24 to 99, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 142 to 172, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 27, the domain is characterized as Anaphylatoxin-like 2.
+At position 28 to 60, the domain is characterized as Anaphylatoxin-like 3.
+At position 92 to 131, the domain is characterized as EGF-like 1.
+At position 132 to 177, the domain is characterized as EGF-like 2; calcium-binding.
+At position 178 to 223, the domain is characterized as EGF-like 3; calcium-binding.
+At position 224 to 270, the domain is characterized as EGF-like 4; calcium-binding.
+At position 271 to 313, the domain is characterized as EGF-like 5; calcium-binding.
+At position 314 to 355, the domain is characterized as EGF-like 6; calcium-binding.
+At position 356 to 395, the domain is characterized as EGF-like 7; calcium-binding.
+At position 396 to 439, the domain is characterized as EGF-like 8; calcium-binding.
+At position 440 to 484, the domain is characterized as EGF-like 9; calcium-binding.
+At position 181 to 464, the domain is characterized as NB-ARC.
+At position 30 to 356, the domain is characterized as G-alpha.
+At position 316 to 345, the domain is characterized as LRRCT.
+At position 247 to 440, the domain is characterized as B30.2/SPRY.
+At position 183 to 296, the domain is characterized as PAZ.
+At position 472 to 770, the domain is characterized as Piwi.
+At position 57 to 144, the domain is characterized as PPIase FKBP-type.
+At position 272 to 498, the domain is characterized as tr-type G.
+At position 822 to 888, the domain is characterized as KHA.
+At position 108 to 224, the domain is characterized as PX.
+At position 133 to 332, the domain is characterized as ATP-grasp.
+At position 295 to 373, the domain is characterized as RRM.
+At position 214 to 342, the domain is characterized as OmpA-like.
+At position 1026 to 1131, the domain is characterized as Calponin-homology (CH).
+At position 76 to 146, the domain is characterized as HMA.
+At position 134 to 370, the domain is characterized as Radical SAM core.
+At position 1 to 234, the domain is characterized as VWFA.
+At position 62 to 139, the domain is characterized as Cytochrome b5 heme-binding.
+At position 309 to 476, the domain is characterized as Helicase ATP-binding.
+At position 564 to 738, the domain is characterized as Helicase C-terminal.
+At position 28 to 264, the domain is characterized as Peptidase S1.
+At position 35 to 164, the domain is characterized as RNase III.
+At position 190 to 259, the domain is characterized as DRBM.
+At position 31 to 241, the domain is characterized as ThyX.
+At position 7 to 125, the domain is characterized as PINc.
+At position 17 to 289, the domain is characterized as Protein kinase.
+At position 583 to 669, the domain is characterized as Death.
+At position 100 to 171, the domain is characterized as SUI1.
+At position 31 to 159, the domain is characterized as SCP.
+At position 195 to 228, the domain is characterized as ShKT.
+At position 107 to 176, the domain is characterized as COMM.
+At position 4 to 220, the domain is characterized as ABC transporter.
+At position 8 to 123, the domain is characterized as Response regulatory.
+At position 151 to 344, the domain is characterized as CheB-type methylesterase.
+At position 271 to 388, the domain is characterized as PH.
+At position 402 to 589, the domain is characterized as Rho-GAP.
+At position 963 to 1023, the domain is characterized as SH3.
+At position 39 to 121, the domain is characterized as SCAN box.
+At position 274 to 351, the domain is characterized as B5.
+At position 66 to 285, the domain is characterized as ABC transporter.
+At position 76 to 139, the domain is characterized as S5 DRBM.
+At position 397 to 597, the domain is characterized as Helicase ATP-binding.
+At position 608 to 771, the domain is characterized as Helicase C-terminal.
+At position 209 to 595, the domain is characterized as Peptidase S53.
+At position 112 to 606, the domain is characterized as Peptidase S8.
+At position 390 to 464, the domain is characterized as PA.
+At position 113 to 280, the domain is characterized as JmjC.
+At position 429 to 471, the domain is characterized as EGF-like.
+At position 344 to 539, the domain is characterized as Helicase ATP-binding.
+At position 566 to 710, the domain is characterized as Helicase C-terminal.
+At position 421 to 546, the domain is characterized as CBM6 1.
+At position 748 to 871, the domain is characterized as CBM6 2.
+At position 371 to 408, the domain is characterized as ShKT.
+At position 71 to 245, the domain is characterized as FAD-binding PCMH-type.
+At position 35 to 173, the domain is characterized as FAS1 1.
+At position 257 to 400, the domain is characterized as FAS1 2.
+At position 9 to 271, the domain is characterized as Protein kinase.
+At position 25 to 221, the domain is characterized as Laminin G-like.
+At position 324 to 381, the domain is characterized as VWFC.
+At position 387 to 437, the domain is characterized as TSP type-1 1.
+At position 443 to 498, the domain is characterized as TSP type-1 2.
+At position 500 to 555, the domain is characterized as TSP type-1 3.
+At position 555 to 595, the domain is characterized as EGF-like 1.
+At position 654 to 698, the domain is characterized as EGF-like 2.
+At position 966 to 1178, the domain is characterized as TSP C-terminal.
+At position 1 to 38, the domain is characterized as F-box.
+At position 212 to 480, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 411 to 478, the domain is characterized as TRAM.
+At position 244 to 258, the domain is characterized as UIM 2.
+At position 42 to 141, the domain is characterized as Expansin-like EG45.
+At position 96 to 148, the domain is characterized as LIM zinc-binding 1.
+At position 157 to 210, the domain is characterized as LIM zinc-binding 2.
+At position 95 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 786 to 860, the domain is characterized as Carrier 1.
+At position 1872 to 1948, the domain is characterized as Carrier 2.
+At position 2404 to 2480, the domain is characterized as Carrier 3.
+At position 6 to 108, the domain is characterized as Response regulatory.
+At position 140 to 395, the domain is characterized as ABC transporter 1.
+At position 840 to 1083, the domain is characterized as ABC transporter 2.
+At position 70 to 152, the domain is characterized as PTS EIIB type-1.
+At position 12 to 122, the domain is characterized as AB hydrolase-1.
+At position 74 to 305, the domain is characterized as PABS.
+At position 285 to 352, the domain is characterized as Dockerin.
+At position 174 to 221, the domain is characterized as LysM.
+At position 317 to 591, the domain is characterized as Protein kinase.
+At position 15 to 137, the domain is characterized as Arf-GAP.
+At position 162 to 280, the domain is characterized as C2.
+At position 159 to 501, the domain is characterized as USP.
+At position 44 to 498, the domain is characterized as Hexokinase.
+At position 89 to 212, the domain is characterized as GST C-terminal.
+At position 499 to 741, the domain is characterized as ABC transporter.
+At position 859 to 1056, the domain is characterized as ABC transmembrane type-2.
+At position 546 to 714, the domain is characterized as tr-type G.
+At position 103 to 263, the domain is characterized as PA14.
+At position 129 to 297, the domain is characterized as CRAL-TRIO.
+At position 1 to 214, the domain is characterized as START.
+At position 631 to 677, the domain is characterized as F-box.
+At position 40 to 98, the domain is characterized as SANT.
+At position 23 to 114, the domain is characterized as Core-binding (CB).
+At position 137 to 319, the domain is characterized as Tyr recombinase.
+At position 191 to 407, the domain is characterized as Rap-GAP.
+At position 489 to 800, the domain is characterized as CNH.
+At position 280 to 496, the domain is characterized as Fibrinogen C-terminal.
+At position 2 to 260, the domain is characterized as Glutamine amidotransferase type-2.
+At position 100 to 504, the domain is characterized as Glutamine amidotransferase type-2.
+At position 340 to 477, the domain is characterized as NYN.
+At position 779 to 858, the domain is characterized as RRM.
+At position 863 to 937, the domain is characterized as HTH OST-type 1.
+At position 991 to 1067, the domain is characterized as HTH OST-type 2.
+At position 1087 to 1161, the domain is characterized as HTH OST-type 3.
+At position 1163 to 1238, the domain is characterized as HTH OST-type 4.
+At position 1247 to 1321, the domain is characterized as HTH OST-type 5.
+At position 1323 to 1398, the domain is characterized as HTH OST-type 6.
+At position 1399 to 1472, the domain is characterized as HTH OST-type 7.
+At position 1474 to 1548, the domain is characterized as HTH OST-type 8.
+At position 42 to 97, the domain is characterized as F-box.
+At position 85 to 336, the domain is characterized as ABC transporter.
+At position 60 to 144, the domain is characterized as RRM.
+At position 100 to 174, the domain is characterized as RRM.
+At position 24 to 103, the domain is characterized as GS beta-grasp.
+At position 110 to 372, the domain is characterized as GS catalytic.
+At position 29 to 61, the domain is characterized as LisH.
+At position 94 to 174, the domain is characterized as PRC barrel.
+At position 89 to 330, the domain is characterized as Dynamin-type G.
+At position 187 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 684 to 917, the domain is characterized as Helicase C-terminal 1.
+At position 981 to 1286, the domain is characterized as SEC63 1.
+At position 1337 to 1511, the domain is characterized as Helicase ATP-binding 2.
+At position 1544 to 1752, the domain is characterized as Helicase C-terminal 2.
+At position 1811 to 2128, the domain is characterized as SEC63 2.
+At position 27 to 513, the domain is characterized as Sema.
+At position 561 to 654, the domain is characterized as IPT/TIG 1.
+At position 656 to 738, the domain is characterized as IPT/TIG 2.
+At position 741 to 835, the domain is characterized as IPT/TIG 3.
+At position 1077 to 1344, the domain is characterized as Protein kinase.
+At position 289 to 361, the domain is characterized as PAS.
+At position 365 to 417, the domain is characterized as PAC.
+At position 437 to 652, the domain is characterized as Histidine kinase.
+At position 489 to 677, the domain is characterized as Helicase C-terminal.
+At position 39 to 70, the domain is characterized as LRRNT.
+At position 151 to 204, the domain is characterized as LRRCT.
+At position 9 to 209, the domain is characterized as ThyX.
+At position 39 to 222, the domain is characterized as NodB homology.
+At position 256 to 298, the domain is characterized as Chitin-binding type-1.
+At position 63 to 98, the domain is characterized as EGF-like 1.
+At position 100 to 139, the domain is characterized as EGF-like 2; calcium-binding.
+At position 144 to 178, the domain is characterized as EGF-like 3.
+At position 180 to 218, the domain is characterized as EGF-like 4; calcium-binding.
+At position 225 to 265, the domain is characterized as EGF-like 5; calcium-binding.
+At position 399 to 543, the domain is characterized as MAM.
+At position 22 to 313, the domain is characterized as Protein kinase.
+At position 81 to 157, the domain is characterized as Biotinyl-binding.
+At position 1 to 59, the domain is characterized as 4Fe-4S.
+At position 38 to 75, the domain is characterized as LRRNT.
+At position 205 to 259, the domain is characterized as LRRCT.
+At position 103 to 343, the domain is characterized as Radical SAM core.
+At position 181 to 272, the domain is characterized as SH2 1.
+At position 279 to 341, the domain is characterized as SH3.
+At position 351 to 441, the domain is characterized as SH2 2.
+At position 474 to 577, the domain is characterized as PH.
+At position 577 to 690, the domain is characterized as C2.
+At position 748 to 942, the domain is characterized as Ras-GAP.
+At position 93 to 149, the domain is characterized as HTH myb-type.
+At position 250 to 441, the domain is characterized as GATase cobBQ-type.
+At position 259 to 552, the domain is characterized as Letm1 RBD.
+At position 680 to 715, the domain is characterized as EF-hand.
+At position 89 to 339, the domain is characterized as Obg.
+At position 340 to 512, the domain is characterized as OBG-type G.
+At position 316 to 444, the domain is characterized as PH.
+At position 464 to 725, the domain is characterized as Protein kinase.
+At position 45 to 133, the domain is characterized as SCP2.
+At position 280 to 355, the domain is characterized as PUA.
+At position 213 to 273, the domain is characterized as KRAB.
+At position 513 to 637, the domain is characterized as STAS.
+At position 53 to 126, the domain is characterized as MBD.
+At position 9 to 102, the domain is characterized as RWD.
+At position 28 to 127, the domain is characterized as Fibronectin type-III 1.
+At position 128 to 229, the domain is characterized as Fibronectin type-III 2.
+At position 142 to 370, the domain is characterized as Radical SAM core.
+At position 383 to 415, the domain is characterized as EGF-like 2.
+At position 538 to 590, the domain is characterized as TB 1.
+At position 608 to 648, the domain is characterized as EGF-like 3; calcium-binding.
+At position 658 to 710, the domain is characterized as TB 2.
+At position 834 to 876, the domain is characterized as EGF-like 4.
+At position 877 to 919, the domain is characterized as EGF-like 5; calcium-binding.
+At position 920 to 959, the domain is characterized as EGF-like 6; calcium-binding.
+At position 960 to 999, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1000 to 1040, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1041 to 1082, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1083 to 1124, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1125 to 1165, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1166 to 1207, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1208 to 1248, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1249 to 1290, the domain is characterized as EGF-like 15; calcium-binding.
+At position 1291 to 1333, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1357 to 1409, the domain is characterized as TB 3.
+At position 1431 to 1473, the domain is characterized as EGF-like 17; calcium-binding.
+At position 1474 to 1513, the domain is characterized as EGF-like 18; calcium-binding.
+At position 1530 to 1582, the domain is characterized as TB 4.
+At position 1676 to 1716, the domain is characterized as EGF-like 19; calcium-binding.
+At position 1717 to 1761, the domain is characterized as EGF-like 20; calcium-binding.
+At position 5 to 192, the domain is characterized as UmuC.
+At position 356 to 440, the domain is characterized as KH-like.
+At position 11 to 100, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 26 to 277, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 7 to 90, the domain is characterized as GIY-YIG.
+At position 27 to 142, the domain is characterized as Response regulatory.
+At position 37 to 135, the domain is characterized as Rieske.
+At position 5 to 80, the domain is characterized as BTB.
+At position 207 to 465, the domain is characterized as NPH3.
+At position 35 to 153, the domain is characterized as C-type lectin.
+At position 161 to 252, the domain is characterized as SUEL-type lectin.
+At position 422 to 1123, the domain is characterized as REJ.
+At position 1279 to 1328, the domain is characterized as GPS.
+At position 1390 to 1507, the domain is characterized as PLAT.
+At position 18 to 87, the domain is characterized as KH type-2.
+At position 43 to 731, the domain is characterized as Myosin motor.
+At position 735 to 755, the domain is characterized as IQ 1.
+At position 756 to 781, the domain is characterized as IQ 2.
+At position 789 to 981, the domain is characterized as TH1.
+At position 1156 to 1216, the domain is characterized as SH3.
+At position 615 to 676, the domain is characterized as SH3.
+At position 688 to 824, the domain is characterized as PID.
+At position 154 to 245, the domain is characterized as Ig-like C2-type 1.
+At position 266 to 371, the domain is characterized as Ig-like C2-type 2.
+At position 385 to 480, the domain is characterized as Fibronectin type-III 1.
+At position 513 to 608, the domain is characterized as Fibronectin type-III 2.
+At position 614 to 707, the domain is characterized as Fibronectin type-III 3.
+At position 710 to 812, the domain is characterized as Fibronectin type-III 4.
+At position 815 to 912, the domain is characterized as Fibronectin type-III 5.
+At position 904 to 1002, the domain is characterized as Ig-like C2-type 3.
+At position 1130 to 1211, the domain is characterized as Ig-like C2-type 4.
+At position 1345 to 1434, the domain is characterized as Ig-like C2-type 5.
+At position 4 to 72, the domain is characterized as HMA.
+At position 1 to 59, the domain is characterized as SH3 1; truncated.
+At position 108 to 167, the domain is characterized as SH3 2.
+At position 269 to 330, the domain is characterized as SH3 3.
+At position 85 to 393, the domain is characterized as IF rod.
+At position 20 to 127, the domain is characterized as VPS28 N-terminal.
+At position 131 to 227, the domain is characterized as VPS28 C-terminal.
+At position 192 to 252, the domain is characterized as DDT.
+At position 135 to 205, the domain is characterized as BTB.
+At position 52 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 56 to 185, the domain is characterized as VIT.
+At position 308 to 468, the domain is characterized as VWFA.
+At position 8 to 228, the domain is characterized as Radical SAM core.
+At position 130 to 304, the domain is characterized as CRAL-TRIO.
+At position 358 to 413, the domain is characterized as SOCS box.
+At position 1 to 188, the domain is characterized as PPM-type phosphatase.
+At position 394 to 457, the domain is characterized as BTB.
+At position 246 to 401, the domain is characterized as RNase NYN.
+At position 228 to 460, the domain is characterized as Peptidase S1.
+At position 129 to 362, the domain is characterized as Radical SAM core.
+At position 97 to 404, the domain is characterized as Peptidase A1.
+At position 107 to 253, the domain is characterized as PI-PLC X-box.
+At position 265 to 385, the domain is characterized as PI-PLC Y-box.
+At position 386 to 513, the domain is characterized as C2.
+At position 147 to 419, the domain is characterized as ABC transporter 1.
+At position 497 to 710, the domain is characterized as ABC transmembrane type-2 1.
+At position 821 to 1073, the domain is characterized as ABC transporter 2.
+At position 1146 to 1360, the domain is characterized as ABC transmembrane type-2 2.
+At position 2 to 42, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 43 to 81, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 87 to 126, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 26 to 259, the domain is characterized as AB hydrolase-1.
+At position 188 to 356, the domain is characterized as PCI.
+At position 92 to 310, the domain is characterized as IF rod.
+At position 30 to 130, the domain is characterized as CBM2.
+At position 180 to 209, the domain is characterized as CBM10.
+At position 339 to 574, the domain is characterized as NR LBD.
+At position 1 to 142, the domain is characterized as Jacalin-type lectin 1.
+At position 154 to 296, the domain is characterized as Jacalin-type lectin 2.
+At position 306 to 449, the domain is characterized as Jacalin-type lectin 3.
+At position 68 to 213, the domain is characterized as Cupin type-1.
+At position 150 to 264, the domain is characterized as C-type lectin.
+At position 4 to 170, the domain is characterized as 3'-5' exonuclease.
+At position 208 to 289, the domain is characterized as HRDC.
+At position 43 to 257, the domain is characterized as ThyX.
+At position 35 to 180, the domain is characterized as UBC core.
+At position 26 to 147, the domain is characterized as MTTase N-terminal.
+At position 156 to 390, the domain is characterized as Radical SAM core.
+At position 393 to 453, the domain is characterized as TRAM.
+At position 600 to 666, the domain is characterized as CBS 1.
+At position 697 to 755, the domain is characterized as CBS 2.
+At position 624 to 724, the domain is characterized as tRNA-binding.
+At position 17 to 351, the domain is characterized as tr-type G.
+At position 628 to 728, the domain is characterized as tRNA-binding.
+At position 29 to 122, the domain is characterized as Ig-like 1.
+At position 132 to 214, the domain is characterized as Ig-like 2.
+At position 219 to 304, the domain is characterized as Ig-like 3.
+At position 189 to 384, the domain is characterized as EXS.
+At position 128 to 262, the domain is characterized as Fatty acid hydroxylase.
+At position 286 to 306, the domain is characterized as ELK.
+At position 33 to 318, the domain is characterized as IF rod.
+At position 71 to 148, the domain is characterized as PDZ.
+At position 247 to 423, the domain is characterized as PID.
+At position 827 to 943, the domain is characterized as RGS.
+At position 1072 to 1142, the domain is characterized as RBD 1.
+At position 1143 to 1213, the domain is characterized as RBD 2.
+At position 1354 to 1376, the domain is characterized as GoLoco.
+At position 587 to 696, the domain is characterized as Peptidase S74.
+At position 2 to 42, the domain is characterized as LEM.
+At position 34 to 263, the domain is characterized as Peptidase S1.
+At position 20 to 139, the domain is characterized as PX.
+At position 72 to 155, the domain is characterized as Ig-like C2-type 1.
+At position 261 to 355, the domain is characterized as Ig-like C2-type 2.
+At position 359 to 445, the domain is characterized as Ig-like C2-type 3.
+At position 455 to 541, the domain is characterized as Ig-like C2-type 4.
+At position 546 to 636, the domain is characterized as Ig-like C2-type 5.
+At position 643 to 753, the domain is characterized as Fibronectin type-III 1.
+At position 758 to 855, the domain is characterized as Fibronectin type-III 2.
+At position 860 to 967, the domain is characterized as Fibronectin type-III 3.
+At position 971 to 1065, the domain is characterized as Fibronectin type-III 4.
+At position 1069 to 1164, the domain is characterized as Fibronectin type-III 5.
+At position 1169 to 1270, the domain is characterized as Fibronectin type-III 6.
+At position 1275 to 1372, the domain is characterized as Fibronectin type-III 7.
+At position 1376 to 1469, the domain is characterized as Fibronectin type-III 8.
+At position 1474 to 1570, the domain is characterized as Fibronectin type-III 9.
+At position 1575 to 1677, the domain is characterized as Fibronectin type-III 10.
+At position 1682 to 1785, the domain is characterized as Fibronectin type-III 11.
+At position 1789 to 1883, the domain is characterized as Fibronectin type-III 12.
+At position 1885 to 1984, the domain is characterized as Fibronectin type-III 13.
+At position 1 to 241, the domain is characterized as Deacetylase sirtuin-type.
+At position 115 to 264, the domain is characterized as MOSC.
+At position 289 to 369, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 60 to 329, the domain is characterized as AB hydrolase-1.
+At position 169 to 481, the domain is characterized as Calpain catalytic.
+At position 9 to 141, the domain is characterized as ENTH.
+At position 2 to 239, the domain is characterized as Glutamine amidotransferase type-2.
+At position 3 to 228, the domain is characterized as ABC transporter.
+At position 30 to 377, the domain is characterized as FERM.
+At position 177 to 218, the domain is characterized as P-type.
+At position 223 to 496, the domain is characterized as ZP.
+At position 26 to 62, the domain is characterized as ATP-grasp.
+At position 1 to 326, the domain is characterized as SPX.
+At position 585 to 785, the domain is characterized as EXS.
+At position 251 to 415, the domain is characterized as DOD-type homing endonuclease.
+At position 53 to 178, the domain is characterized as MATH.
+At position 198 to 522, the domain is characterized as USP.
+At position 10 to 138, the domain is characterized as VOC 1.
+At position 160 to 282, the domain is characterized as VOC 2.
+At position 251 to 330, the domain is characterized as KH.
+At position 319 to 412, the domain is characterized as BRCT.
+At position 85 to 215, the domain is characterized as C-type lectin.
+At position 1 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 123 to 340, the domain is characterized as GB1/RHD3-type G.
+At position 289 to 350, the domain is characterized as SH3.
+At position 34 to 142, the domain is characterized as PpiC.
+At position 36 to 221, the domain is characterized as SIS.
+At position 55 to 346, the domain is characterized as ABC transmembrane type-1.
+At position 380 to 617, the domain is characterized as ABC transporter.
+At position 35 to 206, the domain is characterized as Helicase ATP-binding.
+At position 236 to 386, the domain is characterized as Helicase C-terminal.
+At position 367 to 502, the domain is characterized as DAGKc.
+At position 237 to 527, the domain is characterized as Deacetylase sirtuin-type.
+At position 324 to 385, the domain is characterized as SH3.
+At position 74 to 383, the domain is characterized as Peptidase A1.
+At position 59 to 150, the domain is characterized as WGR.
+At position 182 to 300, the domain is characterized as PARP alpha-helical.
+At position 313 to 533, the domain is characterized as PARP catalytic.
+At position 1 to 125, the domain is characterized as C2 1.
+At position 132 to 255, the domain is characterized as C2 2.
+At position 299 to 500, the domain is characterized as VWFA.
+At position 450 to 507, the domain is characterized as Kazal-like.
+At position 162 to 349, the domain is characterized as B30.2/SPRY.
+At position 86 to 307, the domain is characterized as Fibrinogen C-terminal.
+At position 28 to 61, the domain is characterized as LRRNT.
+At position 208 to 272, the domain is characterized as LRRCT.
+At position 269 to 352, the domain is characterized as Ig-like C2-type.
+At position 146 to 255, the domain is characterized as Gnk2-homologous 2.
+At position 16 to 276, the domain is characterized as Protein kinase.
+At position 66 to 213, the domain is characterized as Cupin type-1.
+At position 156 to 253, the domain is characterized as Fe2OG dioxygenase.
+At position 441 to 610, the domain is characterized as tr-type G.
+At position 229 to 334, the domain is characterized as HD.
+At position 12 to 92, the domain is characterized as GIY-YIG.
+At position 265 to 336, the domain is characterized as S1 motif.
+At position 575 to 738, the domain is characterized as Helicase ATP-binding.
+At position 756 to 936, the domain is characterized as Helicase C-terminal.
+At position 266 to 440, the domain is characterized as NodB homology.
+At position 17 to 214, the domain is characterized as PNPLA.
+At position 250 to 389, the domain is characterized as Flavodoxin-like.
+At position 1 to 202, the domain is characterized as SMP-LTD.
+At position 438 to 864, the domain is characterized as FH2.
+At position 102 to 168, the domain is characterized as MaoC-like.
+At position 10 to 128, the domain is characterized as NTF2.
+At position 4 to 394, the domain is characterized as Kinesin motor.
+At position 850 to 911, the domain is characterized as SH3 4.
+At position 18 to 104, the domain is characterized as LBH.
+At position 287 to 351, the domain is characterized as KH 3.
+At position 1 to 303, the domain is characterized as SPX.
+At position 606 to 815, the domain is characterized as EXS.
+At position 72 to 425, the domain is characterized as Peptidase A1.
+At position 455 to 505, the domain is characterized as DHHC.
+At position 866 to 1011, the domain is characterized as TIR.
+At position 83 to 96, the domain is characterized as CRIB.
+At position 430 to 681, the domain is characterized as Protein kinase.
+At position 229 to 306, the domain is characterized as PUA.
+At position 26 to 277, the domain is characterized as AB hydrolase-1.
+At position 385 to 468, the domain is characterized as PDZ.
+At position 198 to 578, the domain is characterized as GRAS.
+At position 106 to 188, the domain is characterized as PDZ.
+At position 476 to 676, the domain is characterized as FtsK.
+At position 119 to 338, the domain is characterized as Radical SAM core.
+At position 16 to 214, the domain is characterized as GATase cobBQ-type.
+At position 77 to 190, the domain is characterized as C-type lectin 1.
+At position 210 to 324, the domain is characterized as C-type lectin 2.
+At position 468 to 1187, the domain is characterized as REJ.
+At position 1353 to 1403, the domain is characterized as GPS.
+At position 269 to 508, the domain is characterized as NR LBD.
+At position 184 to 410, the domain is characterized as NR LBD.
+At position 419 to 494, the domain is characterized as B5.
+At position 263 to 324, the domain is characterized as PAS.
+At position 325 to 379, the domain is characterized as PAC.
+At position 383 to 602, the domain is characterized as Histidine kinase.
+At position 4 to 306, the domain is characterized as Protein kinase.
+At position 14 to 112, the domain is characterized as SH2.
+At position 113 to 173, the domain is characterized as SH3 1.
+At position 214 to 275, the domain is characterized as SH3 2.
+At position 88 to 158, the domain is characterized as POTRA.
+At position 7 to 59, the domain is characterized as SANT.
+At position 50 to 212, the domain is characterized as SIS.
+At position 614 to 837, the domain is characterized as JmjC.
+At position 369 to 518, the domain is characterized as MATH.
+At position 12 to 264, the domain is characterized as Protein kinase.
+At position 291 to 315, the domain is characterized as NAF.
+At position 149 to 327, the domain is characterized as Rho-GAP.
+At position 217 to 341, the domain is characterized as Fatty acid hydroxylase.
+At position 433 to 576, the domain is characterized as Thioredoxin.
+At position 94 to 129, the domain is characterized as EF-hand 1.
+At position 107 to 286, the domain is characterized as Helicase ATP-binding.
+At position 314 to 472, the domain is characterized as Helicase C-terminal.
+At position 129 to 202, the domain is characterized as PDZ.
+At position 174 to 411, the domain is characterized as PPM-type phosphatase.
+At position 23 to 69, the domain is characterized as Kazal-like 1.
+At position 137 to 181, the domain is characterized as Kazal-like 2.
+At position 651 to 778, the domain is characterized as MOSC.
+At position 16 to 276, the domain is characterized as Pyruvate carboxyltransferase.
+At position 461 to 548, the domain is characterized as SWIRM.
+At position 157 to 272, the domain is characterized as Glutaredoxin.
+At position 25 to 204, the domain is characterized as Eph LBD.
+At position 326 to 434, the domain is characterized as Fibronectin type-III 1.
+At position 438 to 529, the domain is characterized as Fibronectin type-III 2.
+At position 613 to 897, the domain is characterized as Protein kinase.
+At position 906 to 970, the domain is characterized as SAM.
+At position 404 to 486, the domain is characterized as RCK C-terminal.
+At position 5 to 355, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 364 to 690, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 311 to 465, the domain is characterized as 3'-5' exonuclease.
+At position 15 to 124, the domain is characterized as FAD-binding FR-type.
+At position 295 to 577, the domain is characterized as ABC transmembrane type-1.
+At position 609 to 842, the domain is characterized as ABC transporter.
+At position 347 to 482, the domain is characterized as PLAT.
+At position 203 to 431, the domain is characterized as Sigma-54 factor interaction.
+At position 29 to 120, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 341 to 402, the domain is characterized as S4 RNA-binding.
+At position 13 to 242, the domain is characterized as AB hydrolase-1.
+At position 11 to 129, the domain is characterized as VOC 1.
+At position 143 to 257, the domain is characterized as VOC 2.
+At position 362 to 480, the domain is characterized as Rhodanese.
+At position 150 to 459, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 108 to 173, the domain is characterized as CBS 1.
+At position 199 to 258, the domain is characterized as CBS 2.
+At position 276 to 333, the domain is characterized as CBS 3.
+At position 336 to 394, the domain is characterized as CBS 4.
+At position 579 to 709, the domain is characterized as B12-binding.
+At position 16 to 125, the domain is characterized as Bulb-type lectin.
+At position 41 to 75, the domain is characterized as SAP.
+At position 338 to 413, the domain is characterized as RRM.
+At position 55 to 95, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 83 to 340, the domain is characterized as Protein kinase.
+At position 1 to 118, the domain is characterized as WH1.
+At position 81 to 214, the domain is characterized as GST C-terminal.
+At position 25 to 272, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 106 to 455, the domain is characterized as Protein kinase.
+At position 214 to 504, the domain is characterized as Protein kinase.
+At position 13 to 209, the domain is characterized as ABC transmembrane type-1.
+At position 537 to 808, the domain is characterized as Protein kinase.
+At position 462 to 741, the domain is characterized as Protein kinase.
+At position 112 to 620, the domain is characterized as Peptidase S8.
+At position 382 to 474, the domain is characterized as PA.
+At position 375 to 426, the domain is characterized as FBD.
+At position 33 to 102, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 212 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 370 to 516, the domain is characterized as TIR.
+At position 371 to 637, the domain is characterized as ZP.
+At position 4 to 129, the domain is characterized as VOC.
+At position 33 to 270, the domain is characterized as ABC transporter.
+At position 516 to 742, the domain is characterized as NB-ARC.
+At position 2 to 30, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 85 to 243, the domain is characterized as Tyr recombinase.
+At position 394 to 788, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1278 to 1591, the domain is characterized as PKS/mFAS DH.
+At position 1651 to 1727, the domain is characterized as Carrier.
+At position 317 to 682, the domain is characterized as Protein kinase.
+At position 307 to 581, the domain is characterized as Protein kinase.
+At position 11 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 130, the domain is characterized as VOC 1.
+At position 137 to 258, the domain is characterized as VOC 2.
+At position 92 to 251, the domain is characterized as CP-type G.
+At position 16 to 515, the domain is characterized as Biotin carboxylation.
+At position 170 to 360, the domain is characterized as ATP-grasp.
+At position 646 to 720, the domain is characterized as Biotinyl-binding.
+At position 1495 to 1851, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1852 to 2178, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 156 to 389, the domain is characterized as Radical SAM core.
+At position 3 to 236, the domain is characterized as ABC transporter.
+At position 6 to 58, the domain is characterized as HTH myb-type 1.
+At position 59 to 113, the domain is characterized as HTH myb-type 2.
+At position 363 to 397, the domain is characterized as EGF-like 1.
+At position 398 to 429, the domain is characterized as EGF-like 2.
+At position 432 to 470, the domain is characterized as EGF-like 3.
+At position 9 to 51, the domain is characterized as JmjN.
+At position 140 to 306, the domain is characterized as JmjC.
+At position 8 to 286, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 287 to 564, the domain is characterized as UvrD-like helicase C-terminal.
+At position 146 to 186, the domain is characterized as UBA 1.
+At position 355 to 395, the domain is characterized as UBA 2.
+At position 256 to 460, the domain is characterized as Peptidase M12B.
+At position 470 to 550, the domain is characterized as Disintegrin.
+At position 551 to 606, the domain is characterized as TSP type-1 1.
+At position 845 to 905, the domain is characterized as TSP type-1 2.
+At position 906 to 965, the domain is characterized as TSP type-1 3.
+At position 966 to 1014, the domain is characterized as TSP type-1 4.
+At position 1015 to 1054, the domain is characterized as PLAC.
+At position 240 to 421, the domain is characterized as PCI.
+At position 28 to 290, the domain is characterized as Protein kinase.
+At position 332 to 367, the domain is characterized as EF-hand 1.
+At position 368 to 403, the domain is characterized as EF-hand 2.
+At position 404 to 439, the domain is characterized as EF-hand 3.
+At position 444 to 474, the domain is characterized as EF-hand 4.
+At position 225 to 302, the domain is characterized as RRM 1.
+At position 326 to 406, the domain is characterized as RRM 2.
+At position 445 to 525, the domain is characterized as RRM 3.
+At position 28 to 282, the domain is characterized as Pterin-binding.
+At position 78 to 142, the domain is characterized as TGS.
+At position 219 to 351, the domain is characterized as Nudix hydrolase.
+At position 72 to 259, the domain is characterized as RNase H type-2.
+At position 356 to 446, the domain is characterized as IPT/TIG.
+At position 33 to 62, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 314 to 492, the domain is characterized as DUSP.
+At position 677 to 1675, the domain is characterized as USP.
+At position 406 to 840, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1730 to 1807, the domain is characterized as Carrier.
+At position 1 to 125, the domain is characterized as PX.
+At position 44 to 205, the domain is characterized as PCI.
+At position 1 to 144, the domain is characterized as PTS EIIA type-2.
+At position 168 to 491, the domain is characterized as DOT1.
+At position 44 to 186, the domain is characterized as Thioredoxin.
+At position 266 to 357, the domain is characterized as Link 2.
+At position 170 to 268, the domain is characterized as PpiC 1.
+At position 277 to 377, the domain is characterized as PpiC 2.
+At position 52 to 372, the domain is characterized as Peptidase A1.
+At position 152 to 266, the domain is characterized as Fe2OG dioxygenase.
+At position 55 to 216, the domain is characterized as TNase-like.
+At position 499 to 656, the domain is characterized as Helicase ATP-binding.
+At position 677 to 833, the domain is characterized as Helicase C-terminal.
+At position 3 to 153, the domain is characterized as Nudix hydrolase.
+At position 10 to 85, the domain is characterized as REM-1.
+At position 296 to 403, the domain is characterized as PH.
+At position 28 to 78, the domain is characterized as LIM zinc-binding 1.
+At position 87 to 141, the domain is characterized as LIM zinc-binding 2.
+At position 54 to 79, the domain is characterized as Antistasin-like 2.
+At position 91 to 117, the domain is characterized as Antistasin-like 3.
+At position 120 to 145, the domain is characterized as Antistasin-like 4.
+At position 154 to 180, the domain is characterized as Antistasin-like 5.
+At position 183 to 208, the domain is characterized as Antistasin-like 6.
+At position 217 to 396, the domain is characterized as Helicase ATP-binding.
+At position 32 to 166, the domain is characterized as FZ.
+At position 190 to 342, the domain is characterized as Tyrosine-protein phosphatase.
+At position 314 to 412, the domain is characterized as Fibronectin type-III.
+At position 9 to 295, the domain is characterized as Protein kinase.
+At position 589 to 669, the domain is characterized as BRCT.
+At position 37 to 380, the domain is characterized as FERM.
+At position 401 to 482, the domain is characterized as SH2; atypical.
+At position 545 to 809, the domain is characterized as Protein kinase 1.
+At position 849 to 1126, the domain is characterized as Protein kinase 2.
+At position 9 to 110, the domain is characterized as CUB.
+At position 801 to 884, the domain is characterized as SWIB/MDM2.
+At position 944 to 1076, the domain is characterized as Plus3.
+At position 1307 to 1361, the domain is characterized as GYF.
+At position 401 to 818, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1259 to 1562, the domain is characterized as PKS/mFAS DH.
+At position 1588 to 1662, the domain is characterized as Carrier.
+At position 2 to 70, the domain is characterized as EamA.
+At position 28 to 166, the domain is characterized as ENTH.
+At position 64 to 110, the domain is characterized as F-box.
+At position 27 to 127, the domain is characterized as Cystatin.
+At position 33 to 60, the domain is characterized as CBM1.
+At position 30 to 78, the domain is characterized as MADS-box.
+At position 47 to 175, the domain is characterized as Thioredoxin.
+At position 42 to 120, the domain is characterized as RRM 1.
+At position 130 to 207, the domain is characterized as RRM 2.
+At position 223 to 300, the domain is characterized as RRM 3.
+At position 326 to 454, the domain is characterized as RRM 4.
+At position 630 to 707, the domain is characterized as PABC.
+At position 497 to 533, the domain is characterized as EGF-like.
+At position 5 to 179, the domain is characterized as Thioredoxin.
+At position 119 to 405, the domain is characterized as ABC transmembrane type-1 1.
+At position 439 to 662, the domain is characterized as ABC transporter 1.
+At position 735 to 1025, the domain is characterized as ABC transmembrane type-1 2.
+At position 1062 to 1296, the domain is characterized as ABC transporter 2.
+At position 489 to 752, the domain is characterized as ATP-grasp.
+At position 157 to 305, the domain is characterized as GAF.
+At position 348 to 585, the domain is characterized as Histidine kinase.
+At position 613 to 730, the domain is characterized as Response regulatory.
+At position 12 to 141, the domain is characterized as VHS.
+At position 403 to 546, the domain is characterized as RCK N-terminal.
+At position 483 to 723, the domain is characterized as NR LBD.
+At position 201 to 275, the domain is characterized as POU-specific.
+At position 102 to 173, the domain is characterized as PRC barrel.
+At position 262 to 325, the domain is characterized as bZIP.
+At position 625 to 813, the domain is characterized as PCI.
+At position 146 to 208, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 15 to 202, the domain is characterized as FHA; atypical.
+At position 225 to 299, the domain is characterized as CVC.
+At position 587 to 645, the domain is characterized as RAP.
+At position 175 to 765, the domain is characterized as Peptidase M2.
+At position 266 to 405, the domain is characterized as DAGKc.
+At position 231 to 396, the domain is characterized as TrmE-type G.
+At position 5 to 319, the domain is characterized as Protein kinase.
+At position 175 to 263, the domain is characterized as GAT.
+At position 33 to 355, the domain is characterized as Kinesin motor.
+At position 31 to 101, the domain is characterized as Chitin-binding type R&R.
+At position 164 to 326, the domain is characterized as DIPSY.
+At position 13 to 144, the domain is characterized as Galectin 1.
+At position 152 to 279, the domain is characterized as Galectin 2.
+At position 110 to 160, the domain is characterized as LysM 1.
+At position 179 to 222, the domain is characterized as LysM 2.
+At position 522 to 635, the domain is characterized as SMC hinge.
+At position 84 to 201, the domain is characterized as SET.
+At position 194 to 322, the domain is characterized as EamA 2.
+At position 46 to 129, the domain is characterized as ACT.
+At position 7 to 88, the domain is characterized as GST N-terminal.
+At position 93 to 221, the domain is characterized as GST C-terminal.
+At position 521 to 596, the domain is characterized as RRM.
+At position 398 to 603, the domain is characterized as Helicase C-terminal.
+At position 313 to 365, the domain is characterized as bHLH.
+At position 449 to 661, the domain is characterized as FtsK.
+At position 109 to 166, the domain is characterized as S4 RNA-binding.
+At position 29 to 230, the domain is characterized as MurNAc-LAA.
+At position 22 to 273, the domain is characterized as Protein kinase.
+At position 110 to 411, the domain is characterized as USP.
+At position 91 to 142, the domain is characterized as bHLH.
+At position 52 to 167, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 232 to 528, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 560 to 818, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 175 to 351, the domain is characterized as CP-type G.
+At position 3 to 132, the domain is characterized as RNase III.
+At position 158 to 227, the domain is characterized as DRBM.
+At position 27 to 131, the domain is characterized as Cystatin kininogen-type 1.
+At position 73 to 407, the domain is characterized as G-alpha.
+At position 18 to 247, the domain is characterized as Chitin-binding type-4.
+At position 293 to 400, the domain is characterized as CBM20.
+At position 32 to 166, the domain is characterized as Nudix hydrolase.
+At position 236 to 283, the domain is characterized as GRAM 1.
+At position 287 to 384, the domain is characterized as PH.
+At position 774 to 840, the domain is characterized as GRAM 2.
+At position 222 to 282, the domain is characterized as KH.
+At position 348 to 441, the domain is characterized as HD.
+At position 269 to 431, the domain is characterized as Flavodoxin-like.
+At position 95 to 298, the domain is characterized as ATP-grasp.
+At position 32 to 262, the domain is characterized as AB hydrolase-1.
+At position 25 to 130, the domain is characterized as Phytocyanin.
+At position 164 to 445, the domain is characterized as CP-type G.
+At position 131 to 333, the domain is characterized as GST C-terminal.
+At position 31 to 274, the domain is characterized as Peptidase S1.
+At position 85 to 395, the domain is characterized as Peptidase A1.
+At position 22 to 219, the domain is characterized as RNase H type-2.
+At position 521 to 627, the domain is characterized as SMC hinge.
+At position 532 to 589, the domain is characterized as LIM zinc-binding 2.
+At position 590 to 660, the domain is characterized as LIM zinc-binding 3.
+At position 123 to 368, the domain is characterized as PPM-type phosphatase.
+At position 3 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 462, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 928 to 1223, the domain is characterized as PKS/mFAS DH.
+At position 2069 to 2145, the domain is characterized as Carrier.
+At position 187 to 261, the domain is characterized as POU-specific.
+At position 182 to 270, the domain is characterized as TonB C-terminal.
+At position 374 to 538, the domain is characterized as Helicase ATP-binding.
+At position 563 to 737, the domain is characterized as Helicase C-terminal.
+At position 194 to 408, the domain is characterized as SMP-LTD.
+At position 279 to 370, the domain is characterized as Ig-like 1.
+At position 1476 to 1564, the domain is characterized as Ig-like 2.
+At position 1592 to 1827, the domain is characterized as Alpha-type protein kinase.
+At position 184 to 347, the domain is characterized as NIDO.
+At position 638 to 818, the domain is characterized as AMOP.
+At position 166 to 222, the domain is characterized as BTB.
+At position 3 to 93, the domain is characterized as Acylphosphatase-like.
+At position 329 to 421, the domain is characterized as PH 1.
+At position 442 to 531, the domain is characterized as PH 2.
+At position 537 to 662, the domain is characterized as Arf-GAP.
+At position 745 to 852, the domain is characterized as PH 3.
+At position 956 to 1141, the domain is characterized as Rho-GAP.
+At position 1174 to 1263, the domain is characterized as Ras-associating.
+At position 1276 to 1398, the domain is characterized as PH 4.
+At position 32 to 86, the domain is characterized as HTH cro/C1-type.
+At position 23 to 362, the domain is characterized as USP.
+At position 1 to 41, the domain is characterized as Chitin-binding type-1.
+At position 79 to 189, the domain is characterized as PH.
+At position 246 to 404, the domain is characterized as PID.
+At position 800 to 994, the domain is characterized as Rab-GAP TBC.
+At position 8 to 179, the domain is characterized as Josephin.
+At position 242 to 261, the domain is characterized as UIM 2.
+At position 75 to 204, the domain is characterized as PH.
+At position 35 to 261, the domain is characterized as Laminin N-terminal.
+At position 262 to 317, the domain is characterized as Laminin EGF-like 1.
+At position 318 to 380, the domain is characterized as Laminin EGF-like 2.
+At position 381 to 430, the domain is characterized as Laminin EGF-like 3.
+At position 449 to 578, the domain is characterized as NTR.
+At position 224 to 314, the domain is characterized as PDZ 1.
+At position 402 to 486, the domain is characterized as PDZ 2.
+At position 2 to 84, the domain is characterized as Phosphagen kinase N-terminal.
+At position 112 to 350, the domain is characterized as Phosphagen kinase C-terminal.
+At position 345 to 405, the domain is characterized as S4 RNA-binding.
+At position 393 to 445, the domain is characterized as DHHC.
+At position 349 to 465, the domain is characterized as PI-PLC Y-box.
+At position 465 to 589, the domain is characterized as C2.
+At position 29 to 287, the domain is characterized as Protein kinase.
+At position 769 to 850, the domain is characterized as PKD.
+At position 20 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 208 to 295, the domain is characterized as Ig-like C2-type 3.
+At position 303 to 397, the domain is characterized as Ig-like C2-type 4.
+At position 400 to 489, the domain is characterized as Ig-like C2-type 5.
+At position 493 to 592, the domain is characterized as Fibronectin type-III 1.
+At position 595 to 691, the domain is characterized as Fibronectin type-III 2.
+At position 28 to 121, the domain is characterized as LCCL.
+At position 165 to 350, the domain is characterized as VWFA 1.
+At position 367 to 537, the domain is characterized as VWFA 2.
+At position 55 to 131, the domain is characterized as EMI.
+At position 12 to 59, the domain is characterized as SpoVT-AbrB.
+At position 294 to 591, the domain is characterized as Protein kinase.
+At position 54 to 227, the domain is characterized as DH.
+At position 153 to 199, the domain is characterized as G-patch.
+At position 13 to 179, the domain is characterized as Reelin.
+At position 216 to 331, the domain is characterized as DOMON.
+At position 335 to 534, the domain is characterized as Cytochrome b561.
+At position 23 to 283, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 31 to 124, the domain is characterized as UPAR/Ly6.
+At position 254 to 414, the domain is characterized as EF-1-gamma C-terminal.
+At position 17 to 100, the domain is characterized as MtN3/slv 1.
+At position 136 to 219, the domain is characterized as MtN3/slv 2.
+At position 103 to 178, the domain is characterized as PRC barrel.
+At position 48 to 145, the domain is characterized as Ig-like.
+At position 246 to 300, the domain is characterized as TSP type-1 1.
+At position 302 to 354, the domain is characterized as TSP type-1 2.
+At position 543 to 686, the domain is characterized as ZU5.
+At position 865 to 943, the domain is characterized as Death.
+At position 24 to 276, the domain is characterized as Protein kinase.
+At position 21 to 74, the domain is characterized as Clip.
+At position 121 to 370, the domain is characterized as Peptidase S1.
+At position 14 to 94, the domain is characterized as KRAB.
+At position 220 to 286, the domain is characterized as SCA7.
+At position 38 to 194, the domain is characterized as VOC 1.
+At position 210 to 370, the domain is characterized as VOC 2.
+At position 34 to 107, the domain is characterized as EMI.
+At position 115 to 159, the domain is characterized as WAP.
+At position 265 to 306, the domain is characterized as EGF-like 1; calcium-binding.
+At position 307 to 391, the domain is characterized as Fibronectin type-III 1.
+At position 389 to 503, the domain is characterized as SEA 1.
+At position 500 to 545, the domain is characterized as EGF-like 2; calcium-binding.
+At position 709 to 795, the domain is characterized as Fibronectin type-III 2.
+At position 792 to 904, the domain is characterized as SEA 2.
+At position 901 to 945, the domain is characterized as EGF-like 3; calcium-binding.
+At position 995 to 1238, the domain is characterized as ZP.
+At position 242 to 452, the domain is characterized as Histidine kinase.
+At position 336 to 488, the domain is characterized as N-acetyltransferase.
+At position 283 to 346, the domain is characterized as LRRCT.
+At position 118 to 285, the domain is characterized as Nudix hydrolase.
+At position 168 to 390, the domain is characterized as START.
+At position 5 to 232, the domain is characterized as tr-type G.
+At position 1549 to 1661, the domain is characterized as MaoC-like.
+At position 4 to 168, the domain is characterized as Flavodoxin-like.
+At position 212 to 272, the domain is characterized as HTH myb-type.
+At position 171 to 356, the domain is characterized as Glutamine amidotransferase type-1.
+At position 317 to 551, the domain is characterized as ABC transporter 2.
+At position 558 to 754, the domain is characterized as VWFA.
+At position 18 to 99, the domain is characterized as Exonuclease.
+At position 3 to 369, the domain is characterized as BRO1.
+At position 23 to 276, the domain is characterized as Protein kinase.
+At position 88 to 147, the domain is characterized as KID.
+At position 286 to 345, the domain is characterized as bZIP.
+At position 404 to 755, the domain is characterized as FERM.
+At position 7 to 150, the domain is characterized as ADF-H.
+At position 11 to 105, the domain is characterized as PH.
+At position 86 to 203, the domain is characterized as sHSP.
+At position 96 to 155, the domain is characterized as KH; atypical.
+At position 51 to 141, the domain is characterized as YebF/Cmi.
+At position 14 to 107, the domain is characterized as HTH arsR-type.
+At position 98 to 172, the domain is characterized as PA.
+At position 134 to 232, the domain is characterized as Rhodanese.
+At position 86 to 160, the domain is characterized as PRC barrel.
+At position 9 to 323, the domain is characterized as Hcy-binding.
+At position 161 to 245, the domain is characterized as Ras-associating.
+At position 285 to 394, the domain is characterized as PH.
+At position 488 to 584, the domain is characterized as SH2.
+At position 188 to 312, the domain is characterized as Fatty acid hydroxylase.
+At position 67 to 347, the domain is characterized as Protein kinase.
+At position 189 to 249, the domain is characterized as FHA.
+At position 166 to 254, the domain is characterized as EH 1.
+At position 1440 to 1457, the domain is characterized as WH2.
+At position 269 to 355, the domain is characterized as Ras-associating.
+At position 396 to 505, the domain is characterized as PH.
+At position 8 to 94, the domain is characterized as Disintegrin.
+At position 50 to 109, the domain is characterized as HTH myb-type 1.
+At position 135 to 193, the domain is characterized as HTH myb-type 2.
+At position 114 to 663, the domain is characterized as Lipoxygenase.
+At position 236 to 433, the domain is characterized as DH.
+At position 473 to 572, the domain is characterized as PH.
+At position 144 to 363, the domain is characterized as Radical SAM core.
+At position 1 to 144, the domain is characterized as N-acetyltransferase.
+At position 33 to 119, the domain is characterized as PNT.
+At position 207 to 287, the domain is characterized as RCK C-terminal 1.
+At position 295 to 375, the domain is characterized as RCK C-terminal 2.
+At position 135 to 269, the domain is characterized as Thioredoxin.
+At position 712 to 1095, the domain is characterized as ACD.
+At position 238 to 429, the domain is characterized as SMP-LTD.
+At position 2 to 258, the domain is characterized as OBG-type G.
+At position 671 to 860, the domain is characterized as ATP-grasp 2.
+At position 929 to 1067, the domain is characterized as MGS-like.
+At position 6 to 81, the domain is characterized as Ubiquitin-like 1.
+At position 90 to 163, the domain is characterized as Ubiquitin-like 2.
+At position 247 to 463, the domain is characterized as Rap-GAP.
+At position 563 to 621, the domain is characterized as RAP.
+At position 37 to 138, the domain is characterized as Gnk2-homologous 1.
+At position 144 to 256, the domain is characterized as Gnk2-homologous 2.
+At position 4 to 116, the domain is characterized as Response regulatory.
+At position 332 to 607, the domain is characterized as MYST-type HAT.
+At position 250 to 294, the domain is characterized as RPE1 insert.
+At position 291 to 567, the domain is characterized as Dynamin-type G.
+At position 19 to 141, the domain is characterized as VIT.
+At position 353 to 532, the domain is characterized as VWFA.
+At position 291 to 540, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 272, the domain is characterized as S4 RNA-binding.
+At position 223 to 321, the domain is characterized as HTH araC/xylS-type.
+At position 5 to 91, the domain is characterized as KRAB.
+At position 120 to 147, the domain is characterized as EF-hand 4.
+At position 168 to 457, the domain is characterized as USP.
+At position 752 to 919, the domain is characterized as Helicase ATP-binding.
+At position 1205 to 1354, the domain is characterized as Helicase C-terminal.
+At position 232 to 267, the domain is characterized as Tify.
+At position 76 to 221, the domain is characterized as Nudix hydrolase.
+At position 53 to 308, the domain is characterized as Protein kinase.
+At position 1 to 257, the domain is characterized as YjeF C-terminal.
+At position 23 to 83, the domain is characterized as S4 RNA-binding.
+At position 338 to 496, the domain is characterized as Helicase ATP-binding.
+At position 638 to 815, the domain is characterized as Helicase C-terminal.
+At position 47 to 125, the domain is characterized as GIY-YIG.
+At position 235 to 270, the domain is characterized as UVR.
+At position 356 to 421, the domain is characterized as Death.
+At position 580 to 758, the domain is characterized as Helicase ATP-binding.
+At position 785 to 935, the domain is characterized as Helicase C-terminal.
+At position 13 to 248, the domain is characterized as ABC transporter 1.
+At position 277 to 507, the domain is characterized as ABC transporter 2.
+At position 683 to 909, the domain is characterized as ABC transmembrane type-2.
+At position 274 to 348, the domain is characterized as POU-specific.
+At position 186 to 375, the domain is characterized as Rho-GAP.
+At position 55 to 87, the domain is characterized as LisH.
+At position 92 to 137, the domain is characterized as F-box-like.
+At position 25 to 72, the domain is characterized as F-box.
+At position 364 to 423, the domain is characterized as SH3.
+At position 244 to 508, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 144 to 222, the domain is characterized as RRM 2.
+At position 265 to 340, the domain is characterized as RRM 3.
+At position 502 to 798, the domain is characterized as JmjC.
+At position 147 to 339, the domain is characterized as RHD.
+At position 24 to 101, the domain is characterized as UPAR/Ly6.
+At position 73 to 203, the domain is characterized as AB hydrolase-1.
+At position 434 to 608, the domain is characterized as Helicase C-terminal.
+At position 170 to 295, the domain is characterized as NlpC/P60.
+At position 99 to 163, the domain is characterized as J.
+At position 33 to 294, the domain is characterized as Protein kinase.
+At position 211 to 324, the domain is characterized as Calponin-homology (CH).
+At position 1321 to 1455, the domain is characterized as CKK.
+At position 692 to 773, the domain is characterized as ACT 1.
+At position 799 to 872, the domain is characterized as ACT 2.
+At position 186 to 218, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 310 to 593, the domain is characterized as ABC transmembrane type-1 1.
+At position 626 to 850, the domain is characterized as ABC transporter 1.
+At position 967 to 1248, the domain is characterized as ABC transmembrane type-1 2.
+At position 1287 to 1519, the domain is characterized as ABC transporter 2.
+At position 217 to 306, the domain is characterized as Kringle.
+At position 369 to 611, the domain is characterized as Peptidase S1.
+At position 68 to 174, the domain is characterized as Expansin-like EG45.
+At position 187 to 270, the domain is characterized as Expansin-like CBD.
+At position 9 to 91, the domain is characterized as DIX.
+At position 226 to 294, the domain is characterized as PDZ.
+At position 427 to 501, the domain is characterized as DEP.
+At position 19 to 289, the domain is characterized as Protein kinase.
+At position 112 to 235, the domain is characterized as Fatty acid hydroxylase.
+At position 240 to 462, the domain is characterized as PE-PPE.
+At position 97 to 359, the domain is characterized as Protein kinase.
+At position 360 to 430, the domain is characterized as AGC-kinase C-terminal.
+At position 1469 to 1589, the domain is characterized as PH.
+At position 1617 to 1907, the domain is characterized as CNH.
+At position 41 to 109, the domain is characterized as POTRA.
+At position 347 to 458, the domain is characterized as Rhodanese.
+At position 400 to 457, the domain is characterized as HTH myb-type.
+At position 13 to 97, the domain is characterized as J.
+At position 120 to 184, the domain is characterized as DPH-type MB.
+At position 892 to 1049, the domain is characterized as F5/8 type C 1.
+At position 1061 to 1157, the domain is characterized as PKD.
+At position 1142 to 1302, the domain is characterized as F5/8 type C 2.
+At position 1678 to 1716, the domain is characterized as FIVAR 1.
+At position 1746 to 1790, the domain is characterized as FIVAR 2.
+At position 1823 to 1864, the domain is characterized as FIVAR 3.
+At position 68 to 99, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 22 to 149, the domain is characterized as ALOG.
+At position 528 to 707, the domain is characterized as Helicase ATP-binding.
+At position 728 to 876, the domain is characterized as Helicase C-terminal.
+At position 1115 to 1195, the domain is characterized as HRDC.
+At position 27 to 260, the domain is characterized as ABC transporter.
+At position 272 to 340, the domain is characterized as S1 motif.
+At position 636 to 670, the domain is characterized as SAP.
+At position 70 to 247, the domain is characterized as Helicase ATP-binding.
+At position 412 to 582, the domain is characterized as Helicase C-terminal.
+At position 603 to 704, the domain is characterized as Dicer dsRNA-binding fold.
+At position 968 to 1111, the domain is characterized as RNase III 1.
+At position 1153 to 1351, the domain is characterized as RNase III 2.
+At position 164 to 444, the domain is characterized as CP-type G.
+At position 825 to 927, the domain is characterized as Fibronectin type-III 1.
+At position 928 to 1026, the domain is characterized as Fibronectin type-III 2.
+At position 1210 to 1305, the domain is characterized as Fibronectin type-III 3.
+At position 1371 to 1659, the domain is characterized as Protein kinase.
+At position 244 to 429, the domain is characterized as GATase cobBQ-type.
+At position 68 to 119, the domain is characterized as bHLH.
+At position 517 to 589, the domain is characterized as PDZ.
+At position 655 to 911, the domain is characterized as Tyrosine-protein phosphatase.
+At position 22 to 203, the domain is characterized as KIND.
+At position 248 to 262, the domain is characterized as WH2 1.
+At position 278 to 296, the domain is characterized as WH2 2.
+At position 342 to 359, the domain is characterized as WH2 3.
+At position 33 to 270, the domain is characterized as PABS.
+At position 1 to 50, the domain is characterized as Ferritin-like diiron.
+At position 10 to 67, the domain is characterized as CBS 1.
+At position 90 to 146, the domain is characterized as CBS 2.
+At position 154 to 209, the domain is characterized as CBS 3.
+At position 229 to 280, the domain is characterized as CBS 4.
+At position 27 to 185, the domain is characterized as Nudix hydrolase.
+At position 576 to 605, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 13 to 144, the domain is characterized as C2.
+At position 173 to 430, the domain is characterized as Protein kinase.
+At position 431 to 503, the domain is characterized as AGC-kinase C-terminal.
+At position 568 to 645, the domain is characterized as UBX.
+At position 23 to 283, the domain is characterized as Protein kinase.
+At position 170 to 212, the domain is characterized as LRRCT.
+At position 120 to 174, the domain is characterized as AWS.
+At position 176 to 293, the domain is characterized as SET.
+At position 300 to 316, the domain is characterized as Post-SET.
+At position 564 to 596, the domain is characterized as WW.
+At position 39 to 179, the domain is characterized as N-acetyltransferase.
+At position 575 to 673, the domain is characterized as tRNA-binding.
+At position 17 to 113, the domain is characterized as PH.
+At position 135 to 421, the domain is characterized as Tyr recombinase Flp-type.
+At position 1 to 199, the domain is characterized as Protein kinase.
+At position 329 to 498, the domain is characterized as tr-type G.
+At position 82 to 154, the domain is characterized as PAS 1.
+At position 227 to 297, the domain is characterized as PAS 2.
+At position 26 to 207, the domain is characterized as KIND.
+At position 251 to 265, the domain is characterized as WH2 1.
+At position 281 to 299, the domain is characterized as WH2 2.
+At position 345 to 362, the domain is characterized as WH2 3.
+At position 190 to 574, the domain is characterized as GRAS.
+At position 34 to 74, the domain is characterized as Chaplin.
+At position 332 to 476, the domain is characterized as VWFA.
+At position 2 to 217, the domain is characterized as DPCK.
+At position 100 to 317, the domain is characterized as ThyX.
+At position 52 to 400, the domain is characterized as IF rod.
+At position 508 to 621, the domain is characterized as LTD.
+At position 104 to 389, the domain is characterized as PPM-type phosphatase.
+At position 259 to 497, the domain is characterized as ABC transporter 2.
+At position 84 to 234, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 37 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 190 to 232, the domain is characterized as CCT.
+At position 259 to 341, the domain is characterized as Toprim.
+At position 62 to 316, the domain is characterized as Chorismate mutase.
+At position 504 to 626, the domain is characterized as HD.
+At position 742 to 818, the domain is characterized as ACT 1.
+At position 852 to 927, the domain is characterized as ACT 2.
+At position 361 to 431, the domain is characterized as J.
+At position 410 to 499, the domain is characterized as Ig-like C2-type.
+At position 114 to 232, the domain is characterized as sHSP.
+At position 17 to 177, the domain is characterized as UBC core.
+At position 202 to 320, the domain is characterized as C-type lectin.
+At position 2 to 95, the domain is characterized as Stress-response A/B barrel.
+At position 314 to 423, the domain is characterized as ERCC4.
+At position 9 to 126, the domain is characterized as VOC 1.
+At position 169 to 285, the domain is characterized as VOC 2.
+At position 123 to 190, the domain is characterized as GRAM.
+At position 245 to 346, the domain is characterized as SWIRM.
+At position 6 to 203, the domain is characterized as DPCK.
+At position 135 to 252, the domain is characterized as RGS.
+At position 175 to 496, the domain is characterized as PDEase.
+At position 96 to 326, the domain is characterized as Radical SAM core.
+At position 363 to 467, the domain is characterized as tRNA-binding.
+At position 11 to 99, the domain is characterized as Cystatin.
+At position 5 to 139, the domain is characterized as Jacalin-type lectin.
+At position 23 to 103, the domain is characterized as Importin N-terminal.
+At position 113 to 343, the domain is characterized as ATP-grasp.
+At position 273 to 414, the domain is characterized as VPS9.
+At position 61 to 149, the domain is characterized as PPIase FKBP-type 1.
+At position 173 to 261, the domain is characterized as PPIase FKBP-type 2.
+At position 285 to 373, the domain is characterized as PPIase FKBP-type 3.
+At position 398 to 485, the domain is characterized as PPIase FKBP-type 4.
+At position 541 to 576, the domain is characterized as EF-hand 2.
+At position 1 to 170, the domain is characterized as PRELI/MSF1.
+At position 127 to 239, the domain is characterized as PilZ.
+At position 110 to 269, the domain is characterized as N-acetyltransferase.
+At position 59 to 348, the domain is characterized as PPM-type phosphatase.
+At position 12 to 239, the domain is characterized as Glutamine amidotransferase type-1.
+At position 72 to 176, the domain is characterized as FAD-binding FR-type.
+At position 19 to 111, the domain is characterized as Ig-like.
+At position 262 to 376, the domain is characterized as C2 2.
+At position 411 to 551, the domain is characterized as C2 3.
+At position 585 to 710, the domain is characterized as C2 4.
+At position 104 to 237, the domain is characterized as C2.
+At position 439 to 474, the domain is characterized as PLD phosphodiesterase 1.
+At position 773 to 800, the domain is characterized as PLD phosphodiesterase 2.
+At position 13 to 143, the domain is characterized as uDENN.
+At position 47 to 169, the domain is characterized as Arf-GAP.
+At position 212 to 326, the domain is characterized as C2.
+At position 86 to 401, the domain is characterized as IF rod.
+At position 30 to 80, the domain is characterized as Myb-like.
+At position 74 to 224, the domain is characterized as Nudix hydrolase.
+At position 30 to 142, the domain is characterized as SSB.
+At position 38 to 406, the domain is characterized as GBD/FH3.
+At position 527 to 611, the domain is characterized as FH1.
+At position 612 to 1011, the domain is characterized as FH2.
+At position 1071 to 1100, the domain is characterized as DAD.
+At position 163 to 465, the domain is characterized as Peptidase S8.
+At position 44 to 143, the domain is characterized as Cytochrome b5 heme-binding.
+At position 529 to 695, the domain is characterized as N-acetyltransferase.
+At position 7 to 47, the domain is characterized as F-box.
+At position 16 to 131, the domain is characterized as SET.
+At position 417 to 739, the domain is characterized as Kinesin motor.
+At position 7 to 95, the domain is characterized as Acylphosphatase-like.
+At position 120 to 341, the domain is characterized as Fibrinogen C-terminal.
+At position 424 to 580, the domain is characterized as Exonuclease.
+At position 34 to 135, the domain is characterized as Rhodanese.
+At position 29 to 277, the domain is characterized as Zn-dependent PLC.
+At position 283 to 399, the domain is characterized as PLAT.
+At position 161 to 199, the domain is characterized as UBA.
+At position 55 to 297, the domain is characterized as Peptidase S1.
+At position 10 to 128, the domain is characterized as Response regulatory.
+At position 18 to 174, the domain is characterized as VOC 1.
+At position 229 to 408, the domain is characterized as VOC 2.
+At position 295 to 347, the domain is characterized as BSD.
+At position 173 to 367, the domain is characterized as CheB-type methylesterase.
+At position 46 to 146, the domain is characterized as SRCR 1.
+At position 153 to 253, the domain is characterized as SRCR 2.
+At position 260 to 360, the domain is characterized as SRCR 3.
+At position 367 to 467, the domain is characterized as SRCR 4.
+At position 472 to 572, the domain is characterized as SRCR 5.
+At position 577 to 677, the domain is characterized as SRCR 6.
+At position 713 to 813, the domain is characterized as SRCR 7.
+At position 818 to 920, the domain is characterized as SRCR 8.
+At position 923 to 1023, the domain is characterized as SRCR 9.
+At position 13 to 330, the domain is characterized as Hcy-binding.
+At position 3 to 165, the domain is characterized as Flavodoxin-like.
+At position 56 to 143, the domain is characterized as PPIase FKBP-type.
+At position 42 to 161, the domain is characterized as FZ.
+At position 143 to 214, the domain is characterized as KRAB.
+At position 102 to 416, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 66 to 209, the domain is characterized as SCP.
+At position 302 to 370, the domain is characterized as KH.
+At position 160 to 336, the domain is characterized as DH.
+At position 348 to 466, the domain is characterized as PH.
+At position 28 to 237, the domain is characterized as MARVEL.
+At position 171 to 209, the domain is characterized as LRRCT.
+At position 63 to 135, the domain is characterized as MBD.
+At position 384 to 491, the domain is characterized as SH2.
+At position 486 to 535, the domain is characterized as SOCS box.
+At position 60 to 142, the domain is characterized as Cytochrome c.
+At position 167 to 377, the domain is characterized as Peptidase M12B.
+At position 1321 to 1396, the domain is characterized as DEP.
+At position 210 to 468, the domain is characterized as NPH3.
+At position 1 to 159, the domain is characterized as DHFR.
+At position 246 to 434, the domain is characterized as GATase cobBQ-type.
+At position 702 to 1068, the domain is characterized as HECT.
+At position 649 to 716, the domain is characterized as SH3 1.
+At position 787 to 878, the domain is characterized as Fibronectin type-III 1.
+At position 880 to 972, the domain is characterized as Fibronectin type-III 2.
+At position 977 to 1075, the domain is characterized as Fibronectin type-III 3.
+At position 1616 to 1684, the domain is characterized as SH3 2.
+At position 1755 to 1822, the domain is characterized as SH3 3.
+At position 13 to 360, the domain is characterized as Protein kinase.
+At position 705 to 789, the domain is characterized as PB1.
+At position 269 to 324, the domain is characterized as Collagen-like 1.
+At position 325 to 356, the domain is characterized as Collagen-like 2.
+At position 358 to 403, the domain is characterized as Collagen-like 3.
+At position 416 to 472, the domain is characterized as Collagen-like 4.
+At position 473 to 516, the domain is characterized as Collagen-like 5.
+At position 587 to 643, the domain is characterized as Collagen-like 6.
+At position 655 to 712, the domain is characterized as Collagen-like 7.
+At position 713 to 755, the domain is characterized as Collagen-like 8.
+At position 790 to 847, the domain is characterized as Collagen-like 9.
+At position 848 to 899, the domain is characterized as Collagen-like 10.
+At position 31 to 80, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 324 to 607, the domain is characterized as ABC transmembrane type-1 1.
+At position 641 to 865, the domain is characterized as ABC transporter 1.
+At position 969 to 1250, the domain is characterized as ABC transmembrane type-1 2.
+At position 1289 to 1521, the domain is characterized as ABC transporter 2.
+At position 75 to 111, the domain is characterized as F-box; degenerate.
+At position 295 to 436, the domain is characterized as ApaG.
+At position 4 to 241, the domain is characterized as Radical SAM core.
+At position 10 to 301, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 302 to 553, the domain is characterized as UvrD-like helicase C-terminal.
+At position 626 to 700, the domain is characterized as HRDC.
+At position 40 to 736, the domain is characterized as Myosin motor.
+At position 739 to 768, the domain is characterized as IQ.
+At position 870 to 1069, the domain is characterized as TH1.
+At position 629 to 697, the domain is characterized as KHA.
+At position 80 to 144, the domain is characterized as HTH iclR-type.
+At position 473 to 534, the domain is characterized as SAM.
+At position 132 to 195, the domain is characterized as CBS 1.
+At position 225 to 282, the domain is characterized as CBS 2.
+At position 302 to 360, the domain is characterized as CBS 3.
+At position 382 to 468, the domain is characterized as CBS 4.
+At position 17 to 254, the domain is characterized as BAR.
+At position 382 to 440, the domain is characterized as SH3.
+At position 19 to 55, the domain is characterized as Pacifastin 1.
+At position 58 to 93, the domain is characterized as Pacifastin 2.
+At position 106 to 139, the domain is characterized as Pacifastin 3.
+At position 23 to 99, the domain is characterized as Ubiquitin-like.
+At position 200 to 439, the domain is characterized as PABS.
+At position 457 to 508, the domain is characterized as Rubredoxin-like.
+At position 66 to 247, the domain is characterized as tr-type G.
+At position 992 to 1205, the domain is characterized as FtsK.
+At position 63 to 145, the domain is characterized as Lipoyl-binding.
+At position 40 to 309, the domain is characterized as GP-PDE.
+At position 155 to 637, the domain is characterized as Myotubularin phosphatase.
+At position 224 to 381, the domain is characterized as TrmE-type G.
+At position 169 to 356, the domain is characterized as Glutamine amidotransferase type-1.
+At position 308 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 416 to 501, the domain is characterized as Ig-like C2-type 5.
+At position 509 to 608, the domain is characterized as Fibronectin type-III 1.
+At position 33 to 269, the domain is characterized as Alpha-carbonic anhydrase.
+At position 125 to 158, the domain is characterized as EF-hand 2.
+At position 12 to 48, the domain is characterized as F-box.
+At position 92 to 263, the domain is characterized as Helicase ATP-binding.
+At position 290 to 434, the domain is characterized as Helicase C-terminal.
+At position 851 to 870, the domain is characterized as UIM.
+At position 123 to 383, the domain is characterized as Protein kinase.
+At position 386 to 446, the domain is characterized as SH3.
+At position 1029 to 1072, the domain is characterized as UBA.
+At position 19 to 281, the domain is characterized as Glutamine amidotransferase type-1.
+At position 139 to 174, the domain is characterized as RPE1 insert.
+At position 79 to 171, the domain is characterized as Ig-like C1-type.
+At position 84 to 336, the domain is characterized as Radical SAM core 1.
+At position 544 to 785, the domain is characterized as Radical SAM core 2.
+At position 124 to 303, the domain is characterized as Helicase ATP-binding.
+At position 335 to 492, the domain is characterized as Helicase C-terminal.
+At position 4 to 444, the domain is characterized as Helicase ATP-binding.
+At position 493 to 702, the domain is characterized as Roc.
+At position 103 to 303, the domain is characterized as ATP-grasp.
+At position 144 to 361, the domain is characterized as Helicase ATP-binding.
+At position 395 to 555, the domain is characterized as Helicase C-terminal.
+At position 12 to 213, the domain is characterized as RNase H type-2.
+At position 400 to 450, the domain is characterized as bHLH.
+At position 150 to 199, the domain is characterized as bHLH.
+At position 98 to 161, the domain is characterized as S5 DRBM.
+At position 131 to 244, the domain is characterized as PilZ.
+At position 106 to 176, the domain is characterized as BTB.
+At position 311 to 509, the domain is characterized as B30.2/SPRY.
+At position 40 to 119, the domain is characterized as H15.
+At position 867 to 937, the domain is characterized as R3H.
+At position 776 to 793, the domain is characterized as WH2.
+At position 191 to 812, the domain is characterized as USP.
+At position 122 to 387, the domain is characterized as GH16.
+At position 607 to 820, the domain is characterized as FtsK.
+At position 1 to 63, the domain is characterized as Sm.
+At position 93 to 129, the domain is characterized as DFDF.
+At position 288 to 527, the domain is characterized as YjeF N-terminal.
+At position 421 to 602, the domain is characterized as RUN.
+At position 127 to 419, the domain is characterized as NR LBD.
+At position 5 to 635, the domain is characterized as PFL.
+At position 642 to 770, the domain is characterized as Glycine radical.
+At position 4 to 79, the domain is characterized as Saposin B-type.
+At position 5 to 95, the domain is characterized as EH 1.
+At position 171 to 206, the domain is characterized as EF-hand 2.
+At position 1 to 23, the domain is characterized as IF rod.
+At position 4 to 130, the domain is characterized as CMP/dCMP-type deaminase.
+At position 39 to 123, the domain is characterized as KH type-2.
+At position 67 to 399, the domain is characterized as PPM-type phosphatase.
+At position 211 to 320, the domain is characterized as RRM 1.
+At position 328 to 432, the domain is characterized as RRM 2.
+At position 213 to 392, the domain is characterized as Helicase ATP-binding.
+At position 425 to 569, the domain is characterized as Helicase C-terminal.
+At position 105 to 181, the domain is characterized as S4 RNA-binding.
+At position 3 to 437, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 965 to 1259, the domain is characterized as PKS/mFAS DH.
+At position 2409 to 2487, the domain is characterized as Carrier.
+At position 530 to 627, the domain is characterized as PI3K-ABD.
+At position 700 to 789, the domain is characterized as PI3K-RBD.
+At position 851 to 1020, the domain is characterized as C2 PI3K-type.
+At position 1040 to 1216, the domain is characterized as PIK helical.
+At position 1280 to 1558, the domain is characterized as PI3K/PI4K catalytic.
+At position 27 to 74, the domain is characterized as SERTA.
+At position 91 to 234, the domain is characterized as GAF 1.
+At position 266 to 412, the domain is characterized as GAF 2.
+At position 442 to 759, the domain is characterized as PDEase.
+At position 20 to 96, the domain is characterized as IGFBP N-terminal.
+At position 106 to 192, the domain is characterized as Ras-associating.
+At position 234 to 342, the domain is characterized as PH.
+At position 439 to 535, the domain is characterized as SH2.
+At position 153 to 236, the domain is characterized as KH.
+At position 229 to 273, the domain is characterized as PCI.
+At position 643 to 737, the domain is characterized as PH 1.
+At position 751 to 859, the domain is characterized as PH 2.
+At position 896 to 1050, the domain is characterized as MyTH4.
+At position 1061 to 1392, the domain is characterized as FERM.
+At position 107 to 246, the domain is characterized as DOD-type homing endonuclease.
+At position 38 to 337, the domain is characterized as GH18.
+At position 31 to 181, the domain is characterized as F5/8 type C.
+At position 606 to 901, the domain is characterized as Protein kinase.
+At position 80 to 192, the domain is characterized as sHSP.
+At position 31 to 355, the domain is characterized as GP-PDE.
+At position 36 to 176, the domain is characterized as Thioredoxin.
+At position 61 to 248, the domain is characterized as HD.
+At position 584 to 654, the domain is characterized as BRCT.
+At position 135 to 184, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 42 to 157, the domain is characterized as DOMON.
+At position 94 to 159, the domain is characterized as J.
+At position 6 to 35, the domain is characterized as IQ.
+At position 29 to 78, the domain is characterized as F-box.
+At position 88 to 280, the domain is characterized as B30.2/SPRY.
+At position 357 to 423, the domain is characterized as J.
+At position 42 to 296, the domain is characterized as Protein kinase.
+At position 54 to 143, the domain is characterized as PPIase FKBP-type.
+At position 228 to 428, the domain is characterized as Peptidase M12B.
+At position 101 to 165, the domain is characterized as S4 RNA-binding.
+At position 24 to 198, the domain is characterized as Exonuclease.
+At position 342 to 421, the domain is characterized as OCT.
+At position 343 to 661, the domain is characterized as Peptidase S8.
+At position 1 to 89, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 96 to 193, the domain is characterized as FAD-binding FR-type.
+At position 1 to 267, the domain is characterized as F-BAR.
+At position 352 to 429, the domain is characterized as REM-1.
+At position 547 to 610, the domain is characterized as SH3.
+At position 5 to 83, the domain is characterized as GST N-terminal.
+At position 88 to 203, the domain is characterized as GST C-terminal.
+At position 287 to 365, the domain is characterized as PDZ 2.
+At position 489 to 570, the domain is characterized as PDZ 3.
+At position 584 to 649, the domain is characterized as SH3.
+At position 660 to 858, the domain is characterized as Guanylate kinase-like.
+At position 115 to 249, the domain is characterized as SET.
+At position 138 to 346, the domain is characterized as ATP-grasp.
+At position 243 to 274, the domain is characterized as EGF-like 3.
+At position 37 to 161, the domain is characterized as RGS.
+At position 154 to 345, the domain is characterized as CheB-type methylesterase.
+At position 38 to 83, the domain is characterized as WRC.
+At position 621 to 873, the domain is characterized as JmjC.
+At position 381 to 523, the domain is characterized as GOLD.
+At position 1 to 36, the domain is characterized as Ig-like.
+At position 85 to 144, the domain is characterized as KID.
+At position 267 to 325, the domain is characterized as bZIP.
+At position 232 to 293, the domain is characterized as KH 1.
+At position 326 to 387, the domain is characterized as KH 2.
+At position 218 to 485, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 3 to 85, the domain is characterized as Phosphagen kinase N-terminal.
+At position 113 to 349, the domain is characterized as Phosphagen kinase C-terminal.
+At position 335 to 371, the domain is characterized as CBM1.
+At position 1 to 275, the domain is characterized as CheR-type methyltransferase.
+At position 223 to 268, the domain is characterized as TSP type-1.
+At position 281 to 355, the domain is characterized as CTCK.
+At position 446 to 528, the domain is characterized as G5 1.
+At position 574 to 656, the domain is characterized as G5 2.
+At position 702 to 784, the domain is characterized as G5 3.
+At position 830 to 912, the domain is characterized as G5 4.
+At position 958 to 1040, the domain is characterized as G5 5.
+At position 1086 to 1168, the domain is characterized as G5 6.
+At position 1211 to 1296, the domain is characterized as G5 7.
+At position 1854 to 1917, the domain is characterized as SAM.
+At position 24 to 305, the domain is characterized as PPM-type phosphatase.
+At position 46 to 224, the domain is characterized as Helicase ATP-binding.
+At position 235 to 455, the domain is characterized as Helicase C-terminal.
+At position 59 to 152, the domain is characterized as Ig-like C2-type 1.
+At position 161 to 261, the domain is characterized as Ig-like C2-type 2.
+At position 379 to 667, the domain is characterized as Protein kinase.
+At position 71 to 169, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 318 to 483, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 12 to 154, the domain is characterized as Jacalin-type lectin.
+At position 10 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 200 to 398, the domain is characterized as GMPS ATP-PPase.
+At position 54 to 169, the domain is characterized as C-type lectin.
+At position 261 to 504, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 45 to 74, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 27 to 110, the domain is characterized as Disintegrin.
+At position 287 to 468, the domain is characterized as Helicase ATP-binding.
+At position 44 to 290, the domain is characterized as CN hydrolase.
+At position 43 to 158, the domain is characterized as TBDR plug.
+At position 163 to 663, the domain is characterized as TBDR beta-barrel.
+At position 26 to 187, the domain is characterized as FZ.
+At position 1 to 254, the domain is characterized as CN hydrolase.
+At position 578 to 656, the domain is characterized as SH3.
+At position 281 to 337, the domain is characterized as AFP-like.
+At position 24 to 94, the domain is characterized as BTB.
+At position 45 to 141, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 1 to 280, the domain is characterized as Hcy-binding.
+At position 366 to 457, the domain is characterized as Fibronectin type-III 1.
+At position 1808 to 1898, the domain is characterized as Fibronectin type-III 2.
+At position 1900 to 2016, the domain is characterized as Fibronectin type-III 3.
+At position 4 to 168, the domain is characterized as N-acetyltransferase.
+At position 12 to 251, the domain is characterized as Peptidase S1.
+At position 58 to 88, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 2 to 193, the domain is characterized as Glutamine amidotransferase type-1.
+At position 78 to 172, the domain is characterized as Toprim.
+At position 184 to 251, the domain is characterized as DRBM 2.
+At position 286 to 354, the domain is characterized as DRBM 3.
+At position 30 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 221 to 384, the domain is characterized as TrmE-type G.
+At position 449 to 551, the domain is characterized as CBM20.
+At position 13 to 168, the domain is characterized as N-acetyltransferase 1.
+At position 159 to 292, the domain is characterized as N-acetyltransferase 2.
+At position 340 to 415, the domain is characterized as RRM.
+At position 161 to 233, the domain is characterized as MBD.
+At position 294 to 367, the domain is characterized as Pre-SET.
+At position 370 to 688, the domain is characterized as SET.
+At position 3 to 83, the domain is characterized as KRAB.
+At position 139 to 273, the domain is characterized as Fatty acid hydroxylase.
+At position 161 to 335, the domain is characterized as Helicase ATP-binding.
+At position 364 to 541, the domain is characterized as Helicase C-terminal.
+At position 42 to 151, the domain is characterized as tRNA-binding.
+At position 720 to 813, the domain is characterized as FDX-ACB.
+At position 2 to 68, the domain is characterized as LCN-type CS-alpha/beta.
+At position 224 to 264, the domain is characterized as P-type.
+At position 269 to 540, the domain is characterized as ZP.
+At position 1761 to 1912, the domain is characterized as BEACH-type PH.
+At position 1936 to 2226, the domain is characterized as BEACH.
+At position 155 to 325, the domain is characterized as Helicase ATP-binding.
+At position 238 to 306, the domain is characterized as Death.
+At position 106 to 170, the domain is characterized as J.
+At position 2 to 137, the domain is characterized as Flavodoxin-like.
+At position 25 to 143, the domain is characterized as DOMON.
+At position 284 to 493, the domain is characterized as Ku.
+At position 618 to 652, the domain is characterized as SAP.
+At position 1 to 245, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 27 to 41, the domain is characterized as CRIB.
+At position 24 to 103, the domain is characterized as U-box.
+At position 55 to 145, the domain is characterized as UPAR/Ly6.
+At position 30 to 110, the domain is characterized as sHSP.
+At position 85 to 297, the domain is characterized as ABC transmembrane type-1.
+At position 9 to 193, the domain is characterized as DOC.
+At position 287 to 590, the domain is characterized as ABC transmembrane type-1 1.
+At position 951 to 1235, the domain is characterized as ABC transmembrane type-1 2.
+At position 1272 to 1507, the domain is characterized as ABC transporter 2.
+At position 30 to 160, the domain is characterized as Response regulatory.
+At position 545 to 718, the domain is characterized as tr-type G.
+At position 21 to 307, the domain is characterized as Septin-type G.
+At position 7 to 55, the domain is characterized as EF-hand 1.
+At position 123 to 240, the domain is characterized as Calponin-homology (CH) 1.
+At position 268 to 371, the domain is characterized as Calponin-homology (CH) 2.
+At position 392 to 498, the domain is characterized as Calponin-homology (CH) 3.
+At position 607 to 634, the domain is characterized as EGF-like 1.
+At position 635 to 667, the domain is characterized as EGF-like 2.
+At position 331 to 501, the domain is characterized as tr-type G.
+At position 22 to 70, the domain is characterized as FHA.
+At position 91 to 168, the domain is characterized as BRCT.
+At position 273 to 292, the domain is characterized as UIM 1.
+At position 314 to 333, the domain is characterized as UIM 2.
+At position 45 to 146, the domain is characterized as Rhodanese.
+At position 5 to 185, the domain is characterized as VWFA.
+At position 205 to 224, the domain is characterized as UIM.
+At position 290 to 464, the domain is characterized as Helicase ATP-binding.
+At position 475 to 641, the domain is characterized as Helicase C-terminal.
+At position 74 to 141, the domain is characterized as BTB.
+At position 176 to 278, the domain is characterized as BACK.
+At position 532 to 606, the domain is characterized as RRM 1.
+At position 891 to 960, the domain is characterized as RRM 2.
+At position 157 to 245, the domain is characterized as HPr.
+At position 233 to 374, the domain is characterized as YDG.
+At position 20 to 131, the domain is characterized as Ig-like V-type.
+At position 136 to 223, the domain is characterized as Ig-like C2-type.
+At position 25 to 312, the domain is characterized as Protein kinase.
+At position 23 to 131, the domain is characterized as Thioredoxin 1.
+At position 132 to 250, the domain is characterized as Thioredoxin 2.
+At position 28 to 253, the domain is characterized as ABC transporter.
+At position 68 to 103, the domain is characterized as QLQ.
+At position 135 to 179, the domain is characterized as WRC.
+At position 305 to 394, the domain is characterized as Rhodanese.
+At position 56 to 106, the domain is characterized as HTH myb-type 2.
+At position 104 to 167, the domain is characterized as BTB.
+At position 408 to 494, the domain is characterized as B5.
+At position 1 to 273, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 282 to 578, the domain is characterized as UvrD-like helicase C-terminal.
+At position 24 to 293, the domain is characterized as GH18.
+At position 50 to 163, the domain is characterized as PINc.
+At position 57 to 399, the domain is characterized as Kinesin motor.
+At position 1 to 89, the domain is characterized as Core-binding (CB).
+At position 110 to 290, the domain is characterized as Tyr recombinase.
+At position 39 to 290, the domain is characterized as Protein kinase.
+At position 85 to 148, the domain is characterized as S4 RNA-binding.
+At position 223 to 385, the domain is characterized as W2.
+At position 43 to 106, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 202, the domain is characterized as Ig-like C2-type 2.
+At position 220 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 320 to 405, the domain is characterized as Ig-like C2-type 4.
+At position 412 to 534, the domain is characterized as Ig-like C2-type 5.
+At position 540 to 651, the domain is characterized as Ig-like C2-type 6.
+At position 658 to 744, the domain is characterized as Ig-like C2-type 7.
+At position 825 to 1155, the domain is characterized as Protein kinase.
+At position 242 to 504, the domain is characterized as Protein kinase.
+At position 168 to 505, the domain is characterized as Kinesin motor.
+At position 37 to 159, the domain is characterized as THUMP.
+At position 186 to 292, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 26 to 660, the domain is characterized as Vitellogenin.
+At position 292 to 475, the domain is characterized as Helicase ATP-binding.
+At position 506 to 651, the domain is characterized as Helicase C-terminal.
+At position 262 to 506, the domain is characterized as ABC transporter 2.
+At position 2 to 142, the domain is characterized as Tyrosine-protein phosphatase.
+At position 80 to 394, the domain is characterized as GH18.
+At position 10 to 71, the domain is characterized as TRAM.
+At position 23 to 125, the domain is characterized as Gnk2-homologous 1.
+At position 131 to 240, the domain is characterized as Gnk2-homologous 2.
+At position 337 to 614, the domain is characterized as Protein kinase.
+At position 373 to 455, the domain is characterized as KH-like.
+At position 640 to 703, the domain is characterized as SAM.
+At position 777 to 987, the domain is characterized as DDHD.
+At position 4 to 273, the domain is characterized as PTS EIID.
+At position 136 to 230, the domain is characterized as BRICHOS.
+At position 204 to 418, the domain is characterized as SMP-LTD.
+At position 320 to 387, the domain is characterized as SCA7.
+At position 117 to 293, the domain is characterized as Helicase ATP-binding.
+At position 329 to 481, the domain is characterized as Helicase C-terminal.
+At position 61 to 432, the domain is characterized as Peptidase A1.
+At position 109 to 273, the domain is characterized as CP-type G.
+At position 235 to 318, the domain is characterized as KRAB.
+At position 492 to 659, the domain is characterized as tr-type G.
+At position 596 to 676, the domain is characterized as BRCT.
+At position 126 to 408, the domain is characterized as tr-type G.
+At position 166 to 528, the domain is characterized as SAC.
+At position 50 to 160, the domain is characterized as Cadherin 1.
+At position 161 to 273, the domain is characterized as Cadherin 2.
+At position 274 to 388, the domain is characterized as Cadherin 3.
+At position 389 to 503, the domain is characterized as Cadherin 4.
+At position 8 to 20, the domain is characterized as ATP-grasp.
+At position 4 to 44, the domain is characterized as EGF-like.
+At position 21 to 123, the domain is characterized as AB hydrolase-1.
+At position 458 to 528, the domain is characterized as Bromo.
+At position 224 to 278, the domain is characterized as FAF.
+At position 79 to 347, the domain is characterized as Protein kinase.
+At position 289 to 529, the domain is characterized as Glutamine amidotransferase type-1.
+At position 115 to 298, the domain is characterized as Helicase ATP-binding.
+At position 439 to 607, the domain is characterized as Helicase C-terminal.
+At position 639 to 729, the domain is characterized as Dicer dsRNA-binding fold.
+At position 888 to 1012, the domain is characterized as PAZ.
+At position 1050 to 1190, the domain is characterized as RNase III 1.
+At position 1243 to 1406, the domain is characterized as RNase III 2.
+At position 1440 to 1514, the domain is characterized as DRBM.
+At position 67 to 99, the domain is characterized as LisH.
+At position 100 to 184, the domain is characterized as CTLH.
+At position 286 to 328, the domain is characterized as CCT.
+At position 37 to 50, the domain is characterized as CRIB.
+At position 9 to 42, the domain is characterized as WW 1.
+At position 56 to 89, the domain is characterized as WW 2.
+At position 684 to 806, the domain is characterized as C2.
+At position 34 to 123, the domain is characterized as Fibronectin type-III 1.
+At position 128 to 226, the domain is characterized as Fibronectin type-III 2.
+At position 227 to 339, the domain is characterized as Fibronectin type-III 3.
+At position 239 to 456, the domain is characterized as FAD-binding FR-type.
+At position 47 to 136, the domain is characterized as C-type lectin.
+At position 587 to 668, the domain is characterized as BRCT.
+At position 607 to 638, the domain is characterized as IQ.
+At position 8 to 452, the domain is characterized as Biotin carboxylation.
+At position 127 to 324, the domain is characterized as ATP-grasp.
+At position 522 to 598, the domain is characterized as Biotinyl-binding.
+At position 352 to 434, the domain is characterized as PDZ.
+At position 112 to 262, the domain is characterized as Thioredoxin.
+At position 22 to 124, the domain is characterized as Inhibitor I9.
+At position 120 to 672, the domain is characterized as Peptidase S8.
+At position 418 to 492, the domain is characterized as PA.
+At position 304 to 328, the domain is characterized as NAF.
+At position 92 to 429, the domain is characterized as Peptidase A1.
+At position 11 to 55, the domain is characterized as F-box.
+At position 135 to 236, the domain is characterized as HTH LytTR-type.
+At position 547 to 608, the domain is characterized as SH3.
+At position 626 to 690, the domain is characterized as SAM 1.
+At position 1160 to 1224, the domain is characterized as SAM 2.
+At position 169 to 307, the domain is characterized as Flavodoxin-like.
+At position 307 to 542, the domain is characterized as Glutamine amidotransferase type-1.
+At position 59 to 158, the domain is characterized as Rieske.
+At position 139 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 243 to 348, the domain is characterized as Ig-like C2-type 3.
+At position 125 to 192, the domain is characterized as SUI1.
+At position 18 to 67, the domain is characterized as F-box.
+At position 14 to 274, the domain is characterized as Protein kinase.
+At position 466 to 539, the domain is characterized as PASTA 1.
+At position 545 to 614, the domain is characterized as PASTA 2.
+At position 615 to 681, the domain is characterized as PASTA 3.
+At position 33 to 141, the domain is characterized as sHSP.
+At position 2 to 131, the domain is characterized as C-type lysozyme.
+At position 193 to 297, the domain is characterized as Fe2OG dioxygenase.
+At position 26 to 169, the domain is characterized as ENTH.
+At position 174 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 10 to 84, the domain is characterized as ACT.
+At position 203 to 389, the domain is characterized as Glutamine amidotransferase type-1.
+At position 29 to 96, the domain is characterized as HTH gntR-type.
+At position 155 to 237, the domain is characterized as Ubiquitin-like 3.
+At position 238 to 318, the domain is characterized as Ubiquitin-like 4.
+At position 319 to 392, the domain is characterized as Ubiquitin-like 5.
+At position 393 to 468, the domain is characterized as Ubiquitin-like 6.
+At position 469 to 551, the domain is characterized as Ubiquitin-like 7.
+At position 552 to 627, the domain is characterized as Ubiquitin-like 8.
+At position 54 to 323, the domain is characterized as GP-PDE.
+At position 4 to 247, the domain is characterized as CN hydrolase.
+At position 78 to 267, the domain is characterized as RNase H type-2.
+At position 404 to 504, the domain is characterized as Fibronectin type-III.
+At position 486 to 679, the domain is characterized as B30.2/SPRY.
+At position 197 to 287, the domain is characterized as PpiC.
+At position 1350 to 1501, the domain is characterized as Nudix hydrolase.
+At position 92 to 338, the domain is characterized as ABC transporter.
+At position 141 to 427, the domain is characterized as Protein kinase.
+At position 102 to 158, the domain is characterized as HTH myb-type.
+At position 10 to 228, the domain is characterized as ABC transporter.
+At position 365 to 656, the domain is characterized as Protein kinase.
+At position 89 to 194, the domain is characterized as Thioredoxin.
+At position 211 to 509, the domain is characterized as NPH3.
+At position 49 to 163, the domain is characterized as Expansin-like EG45.
+At position 144 to 341, the domain is characterized as HIN-200.
+At position 170 to 205, the domain is characterized as EF-hand 1.
+At position 423 to 558, the domain is characterized as DAGKc.
+At position 761 to 873, the domain is characterized as GAE.
+At position 471 to 498, the domain is characterized as KOW 1.
+At position 520 to 547, the domain is characterized as KOW 2.
+At position 727 to 754, the domain is characterized as KOW 3.
+At position 1140 to 1203, the domain is characterized as SAM.
+At position 366 to 427, the domain is characterized as Tudor 1.
+At position 573 to 630, the domain is characterized as Tudor 2.
+At position 45 to 286, the domain is characterized as Peptidase S1.
+At position 140 to 368, the domain is characterized as Sigma-54 factor interaction.
+At position 31 to 400, the domain is characterized as GRAS.
+At position 17 to 53, the domain is characterized as Oxidoreductase-like.
+At position 76 to 178, the domain is characterized as FAD-binding FR-type.
+At position 20 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 216 to 413, the domain is characterized as GMPS ATP-PPase.
+At position 296 to 361, the domain is characterized as Mop.
+At position 309 to 418, the domain is characterized as SH2.
+At position 90 to 388, the domain is characterized as PPM-type phosphatase.
+At position 264 to 381, the domain is characterized as PH.
+At position 94 to 150, the domain is characterized as CBS 1.
+At position 154 to 215, the domain is characterized as CBS 2.
+At position 44 to 311, the domain is characterized as Protein kinase.
+At position 386 to 491, the domain is characterized as PH.
+At position 243 to 402, the domain is characterized as JmjC.
+At position 226 to 322, the domain is characterized as RRM.
+At position 32 to 204, the domain is characterized as VWFD 1.
+At position 292 to 348, the domain is characterized as TIL.
+At position 350 to 410, the domain is characterized as VWFC.
+At position 386 to 561, the domain is characterized as VWFD 2.
+At position 856 to 1025, the domain is characterized as VWFD 3.
+At position 452 to 671, the domain is characterized as FtsK.
+At position 112 to 360, the domain is characterized as GS catalytic.
+At position 972 to 1035, the domain is characterized as Pre-SET.
+At position 1038 to 1155, the domain is characterized as SET.
+At position 1164 to 1180, the domain is characterized as Post-SET.
+At position 1 to 147, the domain is characterized as NR LBD.
+At position 14 to 168, the domain is characterized as N-acetyltransferase.
+At position 35 to 127, the domain is characterized as PpiC.
+At position 40 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 569 to 842, the domain is characterized as Protein kinase.
+At position 1 to 64, the domain is characterized as HMA.
+At position 300 to 357, the domain is characterized as FHA.
+At position 188 to 364, the domain is characterized as EngA-type G 2.
+At position 23 to 72, the domain is characterized as Kazal-like 1.
+At position 90 to 127, the domain is characterized as Kazal-like 2.
+At position 156 to 210, the domain is characterized as Kazal-like 3.
+At position 19 to 366, the domain is characterized as Lon N-terminal.
+At position 924 to 1163, the domain is characterized as Lon proteolytic.
+At position 31 to 168, the domain is characterized as Chitin-binding type-4.
+At position 55 to 247, the domain is characterized as PIK helical.
+At position 525 to 791, the domain is characterized as PI3K/PI4K catalytic.
+At position 254 to 485, the domain is characterized as Helicase ATP-binding.
+At position 533 to 698, the domain is characterized as Helicase C-terminal.
+At position 219 to 347, the domain is characterized as OmpA-like.
+At position 175 to 364, the domain is characterized as TRUD.
+At position 73 to 159, the domain is characterized as Lipoyl-binding.
+At position 142 to 298, the domain is characterized as Exonuclease.
+At position 720 to 1019, the domain is characterized as Protein kinase.
+At position 4 to 159, the domain is characterized as N-acetyltransferase.
+At position 566 to 664, the domain is characterized as tRNA-binding.
+At position 133 to 328, the domain is characterized as ATP-grasp.
+At position 70 to 114, the domain is characterized as LysM.
+At position 346 to 453, the domain is characterized as Calponin-homology (CH).
+At position 424 to 499, the domain is characterized as F-box.
+At position 13 to 87, the domain is characterized as U-box.
+At position 55 to 499, the domain is characterized as Trm1 methyltransferase.
+At position 572 to 859, the domain is characterized as Protein kinase.
+At position 917 to 1047, the domain is characterized as Guanylate cyclase.
+At position 144 to 227, the domain is characterized as PPIase FKBP-type.
+At position 20 to 207, the domain is characterized as RNase H type-2.
+At position 198 to 245, the domain is characterized as F-box.
+At position 14 to 184, the domain is characterized as Phosphatase tensin-type.
+At position 189 to 349, the domain is characterized as C2 tensin-type.
+At position 4 to 80, the domain is characterized as CIDE-N.
+At position 36 to 304, the domain is characterized as Protein kinase.
+At position 25 to 66, the domain is characterized as EGF-like 1.
+At position 67 to 118, the domain is characterized as EGF-like 2; calcium-binding.
+At position 119 to 162, the domain is characterized as EGF-like 3; calcium-binding.
+At position 163 to 211, the domain is characterized as EGF-like 4; calcium-binding.
+At position 212 to 260, the domain is characterized as EGF-like 5; calcium-binding.
+At position 479 to 529, the domain is characterized as GPS.
+At position 60 to 309, the domain is characterized as Radical SAM core.
+At position 324 to 619, the domain is characterized as Protein kinase.
+At position 38 to 160, the domain is characterized as MPN.
+At position 4 to 131, the domain is characterized as Galectin.
+At position 23 to 308, the domain is characterized as FERM.
+At position 898 to 1169, the domain is characterized as Tyrosine-protein phosphatase.
+At position 19 to 221, the domain is characterized as uDENN.
+At position 249 to 397, the domain is characterized as cDENN.
+At position 399 to 490, the domain is characterized as dDENN.
+At position 1 to 136, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 46 to 136, the domain is characterized as Fibronectin type-III 1.
+At position 142 to 234, the domain is characterized as Fibronectin type-III 2.
+At position 237 to 337, the domain is characterized as Fibronectin type-III 3.
+At position 338 to 444, the domain is characterized as Fibronectin type-III 4.
+At position 448 to 542, the domain is characterized as Fibronectin type-III 5.
+At position 247 to 435, the domain is characterized as GATase cobBQ-type.
+At position 83 to 315, the domain is characterized as Radical SAM core.
+At position 260 to 323, the domain is characterized as bZIP.
+At position 260 to 312, the domain is characterized as VWFC.
+At position 317 to 490, the domain is characterized as VWFD 1.
+At position 578 to 620, the domain is characterized as TIL 1.
+At position 690 to 865, the domain is characterized as VWFD 2.
+At position 963 to 1013, the domain is characterized as TIL 2.
+At position 1066 to 1250, the domain is characterized as VWFD 3.
+At position 1345 to 1398, the domain is characterized as TIL 3.
+At position 1458 to 1633, the domain is characterized as VWFD 4.
+At position 1772 to 2026, the domain is characterized as ZP.
+At position 72 to 144, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 340, the domain is characterized as Ig-like C2-type 2.
+At position 341 to 431, the domain is characterized as Ig-like C2-type 3.
+At position 432 to 520, the domain is characterized as Ig-like C2-type 4.
+At position 522 to 619, the domain is characterized as Ig-like C2-type 5.
+At position 622 to 721, the domain is characterized as Fibronectin type-III 1.
+At position 722 to 833, the domain is characterized as Fibronectin type-III 2.
+At position 837 to 931, the domain is characterized as Ig-like C2-type 6.
+At position 934 to 1029, the domain is characterized as Fibronectin type-III 3.
+At position 1047 to 1141, the domain is characterized as Ig-like C2-type 7.
+At position 25 to 143, the domain is characterized as CUB 1.
+At position 144 to 187, the domain is characterized as EGF-like; calcium-binding.
+At position 190 to 302, the domain is characterized as CUB 2.
+At position 304 to 369, the domain is characterized as Sushi 1.
+At position 370 to 439, the domain is characterized as Sushi 2.
+At position 454 to 701, the domain is characterized as Peptidase S1.
+At position 923 to 1103, the domain is characterized as FCP1 homology.
+At position 1146 to 1239, the domain is characterized as BRCT.
+At position 393 to 479, the domain is characterized as PPIase FKBP-type.
+At position 16 to 129, the domain is characterized as MaoC-like.
+At position 27 to 127, the domain is characterized as Phytocyanin.
+At position 555 to 724, the domain is characterized as N-acetyltransferase.
+At position 58 to 242, the domain is characterized as ABC transmembrane type-1.
+At position 16 to 244, the domain is characterized as AB hydrolase-1.
+At position 105 to 157, the domain is characterized as F-box.
+At position 505 to 763, the domain is characterized as Histidine kinase.
+At position 1045 to 1196, the domain is characterized as Response regulatory.
+At position 65 to 100, the domain is characterized as Tify.
+At position 45 to 142, the domain is characterized as THUMP.
+At position 163 to 264, the domain is characterized as PpiC 1.
+At position 273 to 372, the domain is characterized as PpiC 2.
+At position 284 to 424, the domain is characterized as SIS 1.
+At position 453 to 600, the domain is characterized as SIS 2.
+At position 151 to 391, the domain is characterized as AB hydrolase-1.
+At position 218 to 383, the domain is characterized as TrmE-type G.
+At position 439 to 486, the domain is characterized as RPE1 insert.
+At position 1 to 129, the domain is characterized as C2.
+At position 576 to 638, the domain is characterized as FIP-RBD.
+At position 20 to 150, the domain is characterized as VHS.
+At position 103 to 163, the domain is characterized as CBS 1.
+At position 167 to 228, the domain is characterized as CBS 2.
+At position 431 to 543, the domain is characterized as PH.
+At position 17 to 43, the domain is characterized as LRRNT 1.
+At position 195 to 243, the domain is characterized as LRRCT 1.
+At position 259 to 286, the domain is characterized as LRRNT 2.
+At position 417 to 466, the domain is characterized as LRRCT 2.
+At position 484 to 511, the domain is characterized as LRRNT 3.
+At position 619 to 671, the domain is characterized as LRRCT 3.
+At position 677 to 703, the domain is characterized as LRRNT 4.
+At position 810 to 859, the domain is characterized as LRRCT 4.
+At position 871 to 906, the domain is characterized as EGF-like 1.
+At position 908 to 945, the domain is characterized as EGF-like 2.
+At position 947 to 983, the domain is characterized as EGF-like 1; calcium-binding.
+At position 985 to 1023, the domain is characterized as EGF-like 3.
+At position 1025 to 1061, the domain is characterized as EGF-like 2; calcium-binding.
+At position 1072 to 1109, the domain is characterized as EGF-like 4.
+At position 1112 to 1285, the domain is characterized as Laminin G-like.
+At position 1288 to 1326, the domain is characterized as EGF-like 5.
+At position 1332 to 1406, the domain is characterized as CTCK.
+At position 71 to 110, the domain is characterized as EGF-like 1.
+At position 122 to 163, the domain is characterized as EGF-like 2.
+At position 175 to 213, the domain is characterized as EGF-like 3.
+At position 220 to 265, the domain is characterized as WR1.
+At position 278 to 315, the domain is characterized as EGF-like 4.
+At position 327 to 360, the domain is characterized as EGF-like 5.
+At position 377 to 416, the domain is characterized as EGF-like 6.
+At position 437 to 612, the domain is characterized as VWFA.
+At position 728 to 772, the domain is characterized as EGF-like 7.
+At position 819 to 857, the domain is characterized as EGF-like 8.
+At position 869 to 907, the domain is characterized as EGF-like 9; calcium-binding.
+At position 919 to 958, the domain is characterized as EGF-like 10.
+At position 968 to 1007, the domain is characterized as EGF-like 11.
+At position 1016 to 1058, the domain is characterized as EGF-like 12.
+At position 1071 to 1110, the domain is characterized as EGF-like 13.
+At position 1121 to 1160, the domain is characterized as EGF-like 14.
+At position 1169 to 1208, the domain is characterized as EGF-like 15.
+At position 1215 to 1254, the domain is characterized as EGF-like 16.
+At position 1322 to 1444, the domain is characterized as SEA 1.
+At position 1495 to 1620, the domain is characterized as SEA 2.
+At position 1622 to 1658, the domain is characterized as EGF-like 17.
+At position 1669 to 1705, the domain is characterized as EGF-like 18.
+At position 1717 to 1754, the domain is characterized as EGF-like 19.
+At position 1772 to 1810, the domain is characterized as EGF-like 20; calcium-binding.
+At position 1817 to 1853, the domain is characterized as EGF-like 21.
+At position 103 to 283, the domain is characterized as BAH.
+At position 284 to 387, the domain is characterized as ELM2.
+At position 391 to 443, the domain is characterized as SANT.
+At position 18 to 101, the domain is characterized as PB1.
+At position 246 to 514, the domain is characterized as Protein kinase.
+At position 515 to 586, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 43, the domain is characterized as CHCH.
+At position 159 to 266, the domain is characterized as Cadherin 1.
+At position 267 to 379, the domain is characterized as Cadherin 2.
+At position 380 to 490, the domain is characterized as Cadherin 3.
+At position 491 to 597, the domain is characterized as Cadherin 4.
+At position 598 to 701, the domain is characterized as Cadherin 5.
+At position 783 to 872, the domain is characterized as EH.
+At position 816 to 851, the domain is characterized as EF-hand.
+At position 308 to 371, the domain is characterized as WWE 1.
+At position 374 to 468, the domain is characterized as WWE 2.
+At position 494 to 708, the domain is characterized as PARP catalytic.
+At position 269 to 346, the domain is characterized as PUA.
+At position 261 to 338, the domain is characterized as POU-specific.
+At position 55 to 290, the domain is characterized as GB1/RHD3-type G.
+At position 590 to 671, the domain is characterized as BRCT.
+At position 210 to 441, the domain is characterized as Peptidase S1.
+At position 282 to 345, the domain is characterized as bZIP.
+At position 299 to 334, the domain is characterized as EF-hand 1.
+At position 339 to 374, the domain is characterized as EF-hand 2.
+At position 147 to 182, the domain is characterized as EF-hand 2.
+At position 184 to 219, the domain is characterized as EF-hand 3.
+At position 228 to 263, the domain is characterized as EF-hand 4.
+At position 87 to 465, the domain is characterized as Protein kinase.
+At position 466 to 525, the domain is characterized as AGC-kinase C-terminal.
+At position 152 to 326, the domain is characterized as CRAL-TRIO.
+At position 4 to 69, the domain is characterized as Tudor 1.
+At position 83 to 147, the domain is characterized as Tudor 2.
+At position 273 to 468, the domain is characterized as GATase cobBQ-type.
+At position 208 to 485, the domain is characterized as Protein kinase.
+At position 48 to 115, the domain is characterized as BTB.
+At position 522 to 636, the domain is characterized as SMC hinge.
+At position 63 to 86, the domain is characterized as BRCT.
+At position 257 to 530, the domain is characterized as AB hydrolase-1.
+At position 34 to 174, the domain is characterized as Ephrin RBD.
+At position 460 to 549, the domain is characterized as SH2.
+At position 561 to 822, the domain is characterized as Protein kinase.
+At position 270 to 353, the domain is characterized as PUA.
+At position 290 to 522, the domain is characterized as START.
+At position 27 to 112, the domain is characterized as Ig-like C2-type.
+At position 82 to 160, the domain is characterized as GIY-YIG.
+At position 270 to 305, the domain is characterized as UVR.
+At position 24 to 88, the domain is characterized as SH3.
+At position 110 to 390, the domain is characterized as Protein kinase.
+At position 186 to 306, the domain is characterized as Fe2OG dioxygenase.
+At position 75 to 257, the domain is characterized as tr-type G.
+At position 257 to 347, the domain is characterized as BRCT.
+At position 370 to 635, the domain is characterized as ZP.
+At position 329 to 399, the domain is characterized as Bromo.
+At position 40 to 141, the domain is characterized as tRNA-binding.
+At position 389 to 467, the domain is characterized as B5.
+At position 676 to 768, the domain is characterized as FDX-ACB.
+At position 91 to 152, the domain is characterized as SH3.
+At position 158 to 255, the domain is characterized as SH2.
+At position 277 to 530, the domain is characterized as Protein kinase.
+At position 1945 to 2040, the domain is characterized as Peptidase C50.
+At position 144 to 459, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 117 to 296, the domain is characterized as Helicase ATP-binding.
+At position 324 to 486, the domain is characterized as Helicase C-terminal.
+At position 286 to 384, the domain is characterized as Fe2OG dioxygenase.
+At position 157 to 385, the domain is characterized as Radical SAM core.
+At position 388 to 458, the domain is characterized as TRAM.
+At position 21 to 125, the domain is characterized as Calponin-homology (CH).
+At position 1011 to 1077, the domain is characterized as LIM zinc-binding.
+At position 248 to 437, the domain is characterized as GATase cobBQ-type.
+At position 237 to 331, the domain is characterized as Fibronectin type-III 1.
+At position 637 to 730, the domain is characterized as Fibronectin type-III 3.
+At position 198 to 359, the domain is characterized as CP-type G.
+At position 15 to 286, the domain is characterized as CheR-type methyltransferase.
+At position 5 to 158, the domain is characterized as UBC core.
+At position 248 to 364, the domain is characterized as C2.
+At position 9 to 465, the domain is characterized as Trm1 methyltransferase.
+At position 19 to 271, the domain is characterized as Protein kinase.
+At position 292 to 332, the domain is characterized as UBA.
+At position 131 to 372, the domain is characterized as AB hydrolase-1.
+At position 280 to 543, the domain is characterized as Tyrosine-protein phosphatase.
+At position 300 to 435, the domain is characterized as Fido.
+At position 1140 to 1648, the domain is characterized as WAPL.
+At position 26 to 73, the domain is characterized as SERTA.
+At position 43 to 196, the domain is characterized as SIS.
+At position 39 to 115, the domain is characterized as ACT 1.
+At position 130 to 207, the domain is characterized as ACT 2.
+At position 271 to 347, the domain is characterized as ACT 3.
+At position 349 to 432, the domain is characterized as ACT 4.
+At position 197 to 376, the domain is characterized as CNNM transmembrane.
+At position 394 to 456, the domain is characterized as CBS 1.
+At position 462 to 530, the domain is characterized as CBS 2.
+At position 60 to 183, the domain is characterized as C2.
+At position 332 to 875, the domain is characterized as PLA2c.
+At position 19 to 220, the domain is characterized as Cytochrome b561.
+At position 218 to 302, the domain is characterized as RCK C-terminal 1.
+At position 316 to 403, the domain is characterized as RCK C-terminal 2.
+At position 17 to 87, the domain is characterized as S1 motif 1.
+At position 107 to 173, the domain is characterized as S1 motif 2.
+At position 194 to 262, the domain is characterized as S1 motif 3.
+At position 279 to 348, the domain is characterized as S1 motif 4.
+At position 143 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 453, the domain is characterized as TRAM.
+At position 346 to 607, the domain is characterized as Protein kinase.
+At position 128 to 765, the domain is characterized as USP.
+At position 28 to 162, the domain is characterized as MATH.
+At position 198 to 264, the domain is characterized as BTB.
+At position 1 to 215, the domain is characterized as NR LBD.
+At position 676 to 910, the domain is characterized as PH.
+At position 931 to 1051, the domain is characterized as Arf-GAP.
+At position 30 to 174, the domain is characterized as UBC core.
+At position 65 to 228, the domain is characterized as Laminin G-like.
+At position 121 to 212, the domain is characterized as ARID.
+At position 408 to 574, the domain is characterized as JmjC.
+At position 168 to 253, the domain is characterized as CTCK.
+At position 16 to 118, the domain is characterized as AB hydrolase-1.
+At position 9 to 341, the domain is characterized as Kinesin motor.
+At position 1 to 137, the domain is characterized as Pentraxin (PTX).
+At position 47 to 159, the domain is characterized as Expansin-like EG45.
+At position 143 to 246, the domain is characterized as Ig-like C1-type.
+At position 297 to 399, the domain is characterized as RAMA.
+At position 2 to 80, the domain is characterized as Carrier.
+At position 25 to 111, the domain is characterized as Ig-like C1-type.
+At position 22 to 126, the domain is characterized as Gnk2-homologous 1.
+At position 132 to 240, the domain is characterized as Gnk2-homologous 2.
+At position 5 to 87, the domain is characterized as GIY-YIG.
+At position 10 to 288, the domain is characterized as Protein kinase.
+At position 276 to 382, the domain is characterized as PRD.
+At position 490 to 640, the domain is characterized as PTS EIIA type-2.
+At position 1749 to 1845, the domain is characterized as BRCT 1.
+At position 1861 to 1961, the domain is characterized as BRCT 2.
+At position 565 to 624, the domain is characterized as CBS 1.
+At position 640 to 702, the domain is characterized as CBS 2.
+At position 29 to 226, the domain is characterized as GH11.
+At position 398 to 574, the domain is characterized as NodB homology.
+At position 616 to 645, the domain is characterized as CBM10.
+At position 106 to 172, the domain is characterized as J.
+At position 540 to 666, the domain is characterized as STAS.
+At position 79 to 163, the domain is characterized as RCK C-terminal.
+At position 1 to 401, the domain is characterized as SMP-LTD.
+At position 4 to 198, the domain is characterized as DPCK.
+At position 401 to 782, the domain is characterized as USP.
+At position 48 to 327, the domain is characterized as AB hydrolase-1.
+At position 15 to 115, the domain is characterized as FAD-binding FR-type.
+At position 152 to 255, the domain is characterized as FAD-binding FR-type.
+At position 162 to 484, the domain is characterized as Protein kinase.
+At position 107 to 178, the domain is characterized as SCAN box.
+At position 11 to 358, the domain is characterized as Protein kinase.
+At position 26 to 374, the domain is characterized as MACPF.
+At position 375 to 407, the domain is characterized as EGF-like.
+At position 395 to 513, the domain is characterized as C2.
+At position 498 to 691, the domain is characterized as DH.
+At position 708 to 866, the domain is characterized as PH.
+At position 893 to 1020, the domain is characterized as C2.
+At position 1054 to 1248, the domain is characterized as Rho-GAP.
+At position 356 to 408, the domain is characterized as FBD.
+At position 94 to 406, the domain is characterized as IF rod.
+At position 224 to 287, the domain is characterized as KH.
+At position 350 to 443, the domain is characterized as HD.
+At position 250 to 432, the domain is characterized as GATase cobBQ-type.
+At position 12 to 193, the domain is characterized as Exonuclease.
+At position 202 to 349, the domain is characterized as ExoI SH3-like.
+At position 350 to 413, the domain is characterized as ExoI C-terminal.
+At position 146 to 460, the domain is characterized as IF rod.
+At position 31 to 86, the domain is characterized as Kazal-like.
+At position 10 to 247, the domain is characterized as ABC transporter.
+At position 18 to 156, the domain is characterized as DAC.
+At position 282 to 328, the domain is characterized as F-box.
+At position 720 to 885, the domain is characterized as Helicase ATP-binding.
+At position 1185 to 1324, the domain is characterized as Helicase C-terminal.
+At position 23 to 270, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 1 to 90, the domain is characterized as HTH arsR-type.
+At position 125 to 220, the domain is characterized as Ig-like 2.
+At position 228 to 330, the domain is characterized as Ig-like 3.
+At position 372 to 521, the domain is characterized as Helicase C-terminal.
+At position 226 to 461, the domain is characterized as Grh/CP2 DB.
+At position 46 to 280, the domain is characterized as GB1/RHD3-type G.
+At position 23 to 77, the domain is characterized as HTH cro/C1-type.
+At position 2 to 70, the domain is characterized as Carrier.
+At position 6 to 127, the domain is characterized as CMP/dCMP-type deaminase.
+At position 62 to 211, the domain is characterized as N-acetyltransferase.
+At position 194 to 364, the domain is characterized as Hflx-type G.
+At position 85 to 367, the domain is characterized as Tyr recombinase Flp-type.
+At position 5 to 182, the domain is characterized as KARI N-terminal Rossmann.
+At position 106 to 248, the domain is characterized as SIS.
+At position 31 to 103, the domain is characterized as BTB.
+At position 104 to 206, the domain is characterized as C-type lectin.
+At position 319 to 596, the domain is characterized as ABC transporter 1.
+At position 616 to 945, the domain is characterized as ABC transporter 2.
+At position 873 to 908, the domain is characterized as UVR.
+At position 25 to 104, the domain is characterized as Ig-like C2-type 1.
+At position 108 to 190, the domain is characterized as Ig-like C2-type 2.
+At position 6 to 103, the domain is characterized as Ig-like.
+At position 364 to 442, the domain is characterized as EGF-like.
+At position 175 to 263, the domain is characterized as Ras-associating.
+At position 271 to 318, the domain is characterized as SARAH.
+At position 349 to 485, the domain is characterized as DAGKc.
+At position 1832 to 1895, the domain is characterized as SAM.
+At position 447 to 498, the domain is characterized as Rubredoxin-like.
+At position 71 to 144, the domain is characterized as U-box.
+At position 768 to 951, the domain is characterized as PCI.
+At position 51 to 169, the domain is characterized as Response regulatory.
+At position 509 to 551, the domain is characterized as CCT.
+At position 45 to 123, the domain is characterized as H15.
+At position 751 to 809, the domain is characterized as Tudor 1.
+At position 985 to 1044, the domain is characterized as Tudor 2.
+At position 1246 to 1303, the domain is characterized as Tudor 3.
+At position 1496 to 1556, the domain is characterized as Tudor 4.
+At position 242 to 275, the domain is characterized as WW.
+At position 338 to 671, the domain is characterized as HECT.
+At position 1 to 202, the domain is characterized as Protein kinase.
+At position 5 to 169, the domain is characterized as EngA-type G 1.
+At position 352 to 439, the domain is characterized as KH-like.
+At position 161 to 271, the domain is characterized as MaoC-like.
+At position 217 to 375, the domain is characterized as Cupin type-1 1.
+At position 434 to 594, the domain is characterized as Cupin type-1 2.
+At position 1 to 40, the domain is characterized as Ubiquitin-like.
+At position 444 to 642, the domain is characterized as MAGE.
+At position 113 to 202, the domain is characterized as CS 1.
+At position 282 to 384, the domain is characterized as CS 2.
+At position 497 to 1214, the domain is characterized as USP.
+At position 61 to 274, the domain is characterized as HD.
+At position 419 to 490, the domain is characterized as ACT-like 1.
+At position 512 to 583, the domain is characterized as ACT-like 2.
+At position 211 to 883, the domain is characterized as Peptidase M13.
+At position 3 to 358, the domain is characterized as SAM-dependent MTase C5-type.
+At position 366 to 640, the domain is characterized as Protein kinase.
+At position 258 to 340, the domain is characterized as UBX.
+At position 128 to 379, the domain is characterized as SMP-LTD.
+At position 339 to 401, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 493 to 555, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 744 to 819, the domain is characterized as Smr.
+At position 26 to 282, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 96 to 325, the domain is characterized as ABC transmembrane type-1.
+At position 11 to 102, the domain is characterized as HIG1.
+At position 71 to 125, the domain is characterized as HTH myb-type.
+At position 90 to 176, the domain is characterized as KRAB.
+At position 195 to 472, the domain is characterized as Rho-GAP.
+At position 219 to 306, the domain is characterized as Ig-like C2-type 3.
+At position 865 to 907, the domain is characterized as Bromo.
+At position 51 to 112, the domain is characterized as LIM zinc-binding 1.
+At position 113 to 175, the domain is characterized as LIM zinc-binding 2.
+At position 137 to 281, the domain is characterized as PI-PLC X-box.
+At position 466 to 595, the domain is characterized as C2.
+At position 34 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 125 to 208, the domain is characterized as Ig-like C2-type 2.
+At position 221 to 310, the domain is characterized as Ig-like C2-type 3.
+At position 329 to 407, the domain is characterized as Ig-like C2-type 4.
+At position 404 to 513, the domain is characterized as Ig-like C2-type 5.
+At position 584 to 918, the domain is characterized as Protein kinase.
+At position 31 to 130, the domain is characterized as Cadherin 1.
+At position 240 to 347, the domain is characterized as Cadherin 3.
+At position 455 to 563, the domain is characterized as Cadherin 5.
+At position 569 to 676, the domain is characterized as Cadherin 6.
+At position 111 to 157, the domain is characterized as F-box.
+At position 16 to 121, the domain is characterized as Ig-like V-type.
+At position 26 to 161, the domain is characterized as RanBD1.
+At position 26 to 87, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 13 to 164, the domain is characterized as CheW-like.
+At position 182 to 308, the domain is characterized as Response regulatory.
+At position 124 to 193, the domain is characterized as KRAB.
+At position 59 to 357, the domain is characterized as Protein kinase.
+At position 10 to 102, the domain is characterized as SH2 1.
+At position 163 to 254, the domain is characterized as SH2 2.
+At position 338 to 600, the domain is characterized as Protein kinase.
+At position 408 to 479, the domain is characterized as B5.
+At position 707 to 804, the domain is characterized as FDX-ACB.
+At position 409 to 740, the domain is characterized as Kinesin motor.
+At position 32 to 267, the domain is characterized as GB1/RHD3-type G.
+At position 635 to 726, the domain is characterized as Fe2OG dioxygenase.
+At position 571 to 631, the domain is characterized as KH.
+At position 657 to 724, the domain is characterized as S1 motif.
+At position 590 to 777, the domain is characterized as Reticulon.
+At position 12 to 136, the domain is characterized as EamA 1.
+At position 154 to 274, the domain is characterized as EamA 2.
+At position 57 to 172, the domain is characterized as DOMON.
+At position 179 to 380, the domain is characterized as Cytochrome b561.
+At position 153 to 256, the domain is characterized as Ig-like C2-type 1.
+At position 362 to 452, the domain is characterized as Ig-like C2-type 2.
+At position 453 to 543, the domain is characterized as Ig-like C2-type 3.
+At position 544 to 633, the domain is characterized as Ig-like C2-type 4.
+At position 645 to 771, the domain is characterized as Ig-like C2-type 5.
+At position 971 to 1065, the domain is characterized as Ig-like C2-type 6.
+At position 1181 to 1274, the domain is characterized as Ig-like C2-type 7.
+At position 35 to 131, the domain is characterized as Glutaredoxin.
+At position 23 to 143, the domain is characterized as C2 1.
+At position 182 to 305, the domain is characterized as C2 2.
+At position 346 to 472, the domain is characterized as C2 3.
+At position 250 to 315, the domain is characterized as Laminin EGF-like 1.
+At position 316 to 378, the domain is characterized as Laminin EGF-like 2.
+At position 379 to 430, the domain is characterized as Laminin EGF-like 3.
+At position 431 to 480, the domain is characterized as Laminin EGF-like 4.
+At position 481 to 533, the domain is characterized as Laminin EGF-like 5.
+At position 534 to 580, the domain is characterized as Laminin EGF-like 6.
+At position 305 to 557, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 143, the domain is characterized as Ig-like C2-type 1.
+At position 166 to 256, the domain is characterized as Ig-like C2-type 2.
+At position 216 to 477, the domain is characterized as NR LBD.
+At position 86 to 266, the domain is characterized as JmjC.
+At position 116 to 617, the domain is characterized as Biotin carboxylation.
+At position 274 to 465, the domain is characterized as ATP-grasp.
+At position 744 to 818, the domain is characterized as Biotinyl-binding.
+At position 1575 to 1913, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1917 to 2233, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 210 to 380, the domain is characterized as Helicase ATP-binding.
+At position 470 to 640, the domain is characterized as Helicase C-terminal.
+At position 30 to 243, the domain is characterized as tr-type G.
+At position 466 to 651, the domain is characterized as Rab-GAP TBC.
+At position 790 to 889, the domain is characterized as Rhodanese.
+At position 484 to 545, the domain is characterized as SH3.
+At position 557 to 696, the domain is characterized as PID.
+At position 653 to 907, the domain is characterized as Protein kinase.
+At position 173 to 253, the domain is characterized as RRM Nup35-type.
+At position 203 to 261, the domain is characterized as CTLH.
+At position 674 to 850, the domain is characterized as PCI.
+At position 29 to 294, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 172 to 342, the domain is characterized as Helicase ATP-binding.
+At position 370 to 514, the domain is characterized as Helicase C-terminal.
+At position 173 to 244, the domain is characterized as bHLH.
+At position 27 to 464, the domain is characterized as GBD/FH3.
+At position 627 to 1018, the domain is characterized as FH2.
+At position 1049 to 1082, the domain is characterized as DAD.
+At position 7 to 261, the domain is characterized as Protein kinase.
+At position 262 to 322, the domain is characterized as AGC-kinase C-terminal.
+At position 26 to 223, the domain is characterized as GH16.
+At position 1 to 85, the domain is characterized as HIG1.
+At position 39 to 91, the domain is characterized as bHLH.
+At position 1 to 256, the domain is characterized as CheR-type methyltransferase.
+At position 876 to 1024, the domain is characterized as JmjC.
+At position 159 to 323, the domain is characterized as OBG-type G.
+At position 61 to 110, the domain is characterized as bHLH.
+At position 459 to 548, the domain is characterized as Toprim.
+At position 59 to 92, the domain is characterized as Collagen-like.
+At position 231 to 514, the domain is characterized as ABC transmembrane type-1 1.
+At position 634 to 855, the domain is characterized as ABC transporter 1.
+At position 940 to 1221, the domain is characterized as ABC transmembrane type-1 2.
+At position 1286 to 1521, the domain is characterized as ABC transporter 2.
+At position 244 to 665, the domain is characterized as PPM-type phosphatase.
+At position 94 to 401, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 133 to 249, the domain is characterized as C-type lectin.
+At position 29 to 138, the domain is characterized as CMP/dCMP-type deaminase.
+At position 22 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 40 to 147, the domain is characterized as Ig-like C2-type 1.
+At position 244 to 336, the domain is characterized as Ig-like C2-type 3.
+At position 342 to 429, the domain is characterized as Ig-like C2-type 4.
+At position 462 to 571, the domain is characterized as Fibronectin type-III 1.
+At position 579 to 674, the domain is characterized as Fibronectin type-III 2.
+At position 6 to 157, the domain is characterized as HTH marR-type.
+At position 426 to 654, the domain is characterized as ABC transporter 1.
+At position 680 to 995, the domain is characterized as ABC transporter 2.
+At position 51 to 136, the domain is characterized as Ig-like V-type.
+At position 138 to 229, the domain is characterized as Ig-like C2-type.
+At position 47 to 274, the domain is characterized as Radical SAM core.
+At position 47 to 97, the domain is characterized as Tudor-knot.
+At position 196 to 529, the domain is characterized as MYST-type HAT.
+At position 47 to 104, the domain is characterized as S4 RNA-binding.
+At position 266 to 376, the domain is characterized as PX.
+At position 411 to 614, the domain is characterized as BAR.
+At position 636 to 812, the domain is characterized as PCI.
+At position 116 to 238, the domain is characterized as TBDR plug.
+At position 243 to 1003, the domain is characterized as TBDR beta-barrel.
+At position 9 to 139, the domain is characterized as CMP/dCMP-type deaminase.
+At position 35 to 94, the domain is characterized as KID.
+At position 191 to 249, the domain is characterized as bZIP.
+At position 126 to 504, the domain is characterized as Myotubularin phosphatase.
+At position 397 to 470, the domain is characterized as Histone-fold.
+At position 55 to 145, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 143 to 211, the domain is characterized as POTRA.
+At position 98 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 203 to 300, the domain is characterized as Ig-like C2-type 3.
+At position 311 to 395, the domain is characterized as Ig-like C2-type 4.
+At position 398 to 498, the domain is characterized as Ig-like C2-type 5.
+At position 579 to 926, the domain is characterized as Protein kinase.
+At position 3 to 121, the domain is characterized as VOC.
+At position 13 to 205, the domain is characterized as DPCK.
+At position 289 to 344, the domain is characterized as MIR 1.
+At position 359 to 418, the domain is characterized as MIR 2.
+At position 432 to 488, the domain is characterized as MIR 3.
+At position 317 to 695, the domain is characterized as Protein kinase.
+At position 173 to 349, the domain is characterized as EngA-type G 2.
+At position 26 to 64, the domain is characterized as LDL-receptor class A 1.
+At position 69 to 107, the domain is characterized as LDL-receptor class A 2.
+At position 122 to 163, the domain is characterized as LDL-receptor class A 3.
+At position 166 to 204, the domain is characterized as LDL-receptor class A 4.
+At position 222 to 285, the domain is characterized as Sushi 1.
+At position 300 to 356, the domain is characterized as Sushi 2.
+At position 369 to 621, the domain is characterized as Peptidase S1.
+At position 32 to 102, the domain is characterized as BTB.
+At position 137 to 239, the domain is characterized as BACK.
+At position 117 to 147, the domain is characterized as EF-hand 4.
+At position 70 to 181, the domain is characterized as Thioredoxin.
+At position 118 to 273, the domain is characterized as N-acetyltransferase.
+At position 360 to 430, the domain is characterized as Bromo.
+At position 71 to 229, the domain is characterized as Flavodoxin-like.
+At position 389 to 635, the domain is characterized as Radical SAM core.
+At position 20 to 351, the domain is characterized as SET.
+At position 142 to 171, the domain is characterized as HhH 1.
+At position 172 to 201, the domain is characterized as HhH 2.
+At position 242 to 282, the domain is characterized as EGF-like 1.
+At position 285 to 325, the domain is characterized as EGF-like 2.
+At position 326 to 364, the domain is characterized as EGF-like 3; calcium-binding.
+At position 366 to 406, the domain is characterized as EGF-like 4.
+At position 405 to 441, the domain is characterized as EGF-like 5.
+At position 442 to 481, the domain is characterized as EGF-like 6; calcium-binding.
+At position 78 to 391, the domain is characterized as GH18.
+At position 9 to 331, the domain is characterized as DhaK.
+At position 103 to 333, the domain is characterized as Radical SAM core.
+At position 56 to 128, the domain is characterized as Histone-fold.
+At position 1 to 177, the domain is characterized as TCTP.
+At position 46 to 195, the domain is characterized as Tyrosine-protein phosphatase.
+At position 86 to 791, the domain is characterized as Myosin motor.
+At position 794 to 823, the domain is characterized as IQ.
+At position 93 to 183, the domain is characterized as PpiC.
+At position 205 to 297, the domain is characterized as Rhodanese.
+At position 55 to 95, the domain is characterized as bZIP.
+At position 1 to 56, the domain is characterized as F-box.
+At position 11 to 208, the domain is characterized as YjeF N-terminal.
+At position 135 to 228, the domain is characterized as Ig-like C2-type.
+At position 8 to 87, the domain is characterized as GRAM.
+At position 49 to 149, the domain is characterized as Ig-like V-type.
+At position 167 to 263, the domain is characterized as Ig-like C2-type.
+At position 226 to 288, the domain is characterized as t-SNARE coiled-coil homology.
+At position 27 to 64, the domain is characterized as LDL-receptor class A.
+At position 48 to 317, the domain is characterized as Protein kinase 1.
+At position 318 to 386, the domain is characterized as AGC-kinase C-terminal.
+At position 428 to 675, the domain is characterized as Protein kinase 2.
+At position 120 to 206, the domain is characterized as RRM.
+At position 16 to 194, the domain is characterized as RNase H type-2.
+At position 39 to 84, the domain is characterized as Clip.
+At position 128 to 375, the domain is characterized as Peptidase S1.
+At position 25 to 163, the domain is characterized as Helicase ATP-binding.
+At position 111 to 140, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 150 to 179, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 232 to 621, the domain is characterized as GRAS.
+At position 598 to 719, the domain is characterized as GAE.
+At position 39 to 68, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 66 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 308 to 569, the domain is characterized as Protein kinase.
+At position 309 to 375, the domain is characterized as Thyroglobulin type-1.
+At position 10 to 111, the domain is characterized as LOB.
+At position 11 to 273, the domain is characterized as Protein kinase.
+At position 352 to 418, the domain is characterized as PASTA 1.
+At position 419 to 486, the domain is characterized as PASTA 2.
+At position 487 to 553, the domain is characterized as PASTA 3.
+At position 554 to 622, the domain is characterized as PASTA 4.
+At position 246 to 548, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 549 to 860, the domain is characterized as UvrD-like helicase C-terminal.
+At position 182 to 354, the domain is characterized as C2.
+At position 392 to 653, the domain is characterized as Protein kinase.
+At position 654 to 729, the domain is characterized as AGC-kinase C-terminal.
+At position 296 to 543, the domain is characterized as Olfactomedin-like.
+At position 253 to 472, the domain is characterized as B30.2/SPRY.
+At position 63 to 288, the domain is characterized as Radical SAM core.
+At position 50 to 91, the domain is characterized as Gla.
+At position 113 to 151, the domain is characterized as EGF-like 1; calcium-binding.
+At position 153 to 193, the domain is characterized as EGF-like 2; calcium-binding.
+At position 194 to 234, the domain is characterized as EGF-like 3; calcium-binding.
+At position 235 to 275, the domain is characterized as EGF-like 4; calcium-binding.
+At position 295 to 467, the domain is characterized as Laminin G-like 1.
+At position 474 to 666, the domain is characterized as Laminin G-like 2.
+At position 406 to 622, the domain is characterized as Helicase ATP-binding.
+At position 864 to 1029, the domain is characterized as Helicase C-terminal.
+At position 1489 to 1712, the domain is characterized as Collagen IV NC1.
+At position 24 to 106, the domain is characterized as KRAB.
+At position 28 to 55, the domain is characterized as H15.
+At position 242 to 294, the domain is characterized as TSP type-1.
+At position 441 to 584, the domain is characterized as ZU5.
+At position 761 to 841, the domain is characterized as Death.
+At position 14 to 178, the domain is characterized as Helicase ATP-binding.
+At position 200 to 377, the domain is characterized as Helicase C-terminal.
+At position 219 to 359, the domain is characterized as MPN.
+At position 27 to 427, the domain is characterized as Glutamine amidotransferase type-2.
+At position 319 to 585, the domain is characterized as ZP.
+At position 74 to 141, the domain is characterized as GRAM.
+At position 4 to 243, the domain is characterized as Protein kinase.
+At position 67 to 124, the domain is characterized as HTH myb-type.
+At position 126 to 305, the domain is characterized as FAD-binding PCMH-type.
+At position 163 to 331, the domain is characterized as OBG-type G.
+At position 54 to 181, the domain is characterized as ALOG.
+At position 26 to 532, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 615 to 920, the domain is characterized as UvrD-like helicase C-terminal.
+At position 35 to 157, the domain is characterized as FZ.
+At position 243 to 393, the domain is characterized as Helicase C-terminal.
+At position 56 to 144, the domain is characterized as BTB.
+At position 50 to 204, the domain is characterized as PX.
+At position 477 to 504, the domain is characterized as PLD phosphodiesterase 1.
+At position 892 to 919, the domain is characterized as PLD phosphodiesterase 2.
+At position 93 to 173, the domain is characterized as RRM.
+At position 460 to 602, the domain is characterized as SIS 2.
+At position 13 to 141, the domain is characterized as EamA.
+At position 108 to 174, the domain is characterized as S4 RNA-binding.
+At position 136 to 225, the domain is characterized as EH 2.
+At position 97 to 337, the domain is characterized as Radical SAM core.
+At position 3 to 72, the domain is characterized as PAS.
+At position 528 to 877, the domain is characterized as Protein kinase.
+At position 6 to 320, the domain is characterized as Hcy-binding.
+At position 378 to 484, the domain is characterized as Calponin-homology (CH).
+At position 1 to 416, the domain is characterized as PTS EIIC type-1.
+At position 450 to 529, the domain is characterized as PTS EIIB type-1.
+At position 33 to 251, the domain is characterized as ABC transmembrane type-2.
+At position 18 to 364, the domain is characterized as GH16.
+At position 321 to 381, the domain is characterized as HTH myb-type.
+At position 32 to 131, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 224, the domain is characterized as Ig-like C2-type 2.
+At position 248 to 345, the domain is characterized as Fibronectin type-III 1.
+At position 347 to 442, the domain is characterized as Fibronectin type-III 2.
+At position 33 to 280, the domain is characterized as PPM-type phosphatase.
+At position 394 to 485, the domain is characterized as PDZ 2.
+At position 1 to 399, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 868 to 1144, the domain is characterized as PKS/mFAS DH.
+At position 1644 to 1718, the domain is characterized as Carrier.
+At position 62 to 491, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 988 to 1298, the domain is characterized as PKS/mFAS DH.
+At position 2382 to 2462, the domain is characterized as Carrier.
+At position 280 to 559, the domain is characterized as ABC transmembrane type-1 1.
+At position 639 to 884, the domain is characterized as ABC transporter 1.
+At position 963 to 1241, the domain is characterized as ABC transmembrane type-1 2.
+At position 1295 to 1538, the domain is characterized as ABC transporter 2.
+At position 30 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 15 to 61, the domain is characterized as F-box.
+At position 30 to 143, the domain is characterized as CUB 1.
+At position 145 to 255, the domain is characterized as CUB 2.
+At position 257 to 373, the domain is characterized as CUB 3.
+At position 48 to 494, the domain is characterized as Biotin carboxylation.
+At position 643 to 715, the domain is characterized as Biotinyl-binding.
+At position 47 to 289, the domain is characterized as ABC transmembrane type-2.
+At position 1 to 101, the domain is characterized as WH1.
+At position 47 to 215, the domain is characterized as Helicase ATP-binding.
+At position 236 to 385, the domain is characterized as Helicase C-terminal.
+At position 544 to 624, the domain is characterized as HRDC.
+At position 196 to 286, the domain is characterized as GIY-YIG.
+At position 1 to 103, the domain is characterized as C2 1.
+At position 253 to 426, the domain is characterized as VASt 1.
+At position 516 to 639, the domain is characterized as C2 2.
+At position 693 to 756, the domain is characterized as GRAM.
+At position 855 to 1018, the domain is characterized as VASt 2.
+At position 281 to 353, the domain is characterized as RRM 1.
+At position 355 to 441, the domain is characterized as RRM 2.
+At position 5 to 129, the domain is characterized as TIR.
+At position 262 to 486, the domain is characterized as NR LBD.
+At position 242 to 461, the domain is characterized as Histidine kinase.
+At position 484 to 601, the domain is characterized as Response regulatory.
+At position 164 to 445, the domain is characterized as Protein kinase.
+At position 97 to 290, the domain is characterized as ATP-grasp.
+At position 167 to 379, the domain is characterized as Ras-GAP.
+At position 131 to 308, the domain is characterized as Prephenate dehydratase.
+At position 321 to 412, the domain is characterized as ACT.
+At position 8 to 82, the domain is characterized as PAS.
+At position 79 to 133, the domain is characterized as PAC.
+At position 139 to 334, the domain is characterized as Histidine kinase.
+At position 21 to 137, the domain is characterized as MTTase N-terminal.
+At position 160 to 389, the domain is characterized as Radical SAM core.
+At position 392 to 453, the domain is characterized as TRAM.
+At position 142 to 400, the domain is characterized as Tyrosine-protein phosphatase.
+At position 16 to 162, the domain is characterized as PPIase cyclophilin-type.
+At position 134 to 177, the domain is characterized as CHCH.
+At position 58 to 408, the domain is characterized as SAM-dependent MTase C5-type.
+At position 133 to 366, the domain is characterized as Radical SAM core.
+At position 367 to 431, the domain is characterized as TRAM.
+At position 29 to 105, the domain is characterized as Importin N-terminal.
+At position 365 to 586, the domain is characterized as Protein kinase.
+At position 589 to 723, the domain is characterized as KEN.
+At position 40 to 168, the domain is characterized as tRNA-binding.
+At position 426 to 501, the domain is characterized as B5.
+At position 753 to 846, the domain is characterized as FDX-ACB.
+At position 99 to 177, the domain is characterized as GAF.
+At position 126 to 139, the domain is characterized as CRIB.
+At position 16 to 88, the domain is characterized as S1 motif.
+At position 376 to 481, the domain is characterized as PAZ.
+At position 650 to 977, the domain is characterized as Piwi.
+At position 386 to 421, the domain is characterized as EF-hand 1.
+At position 422 to 457, the domain is characterized as EF-hand 2.
+At position 458 to 493, the domain is characterized as EF-hand 3.
+At position 603 to 728, the domain is characterized as DBINO.
+At position 853 to 1025, the domain is characterized as Helicase ATP-binding.
+At position 1426 to 1586, the domain is characterized as Helicase C-terminal.
+At position 20 to 101, the domain is characterized as Core-binding (CB).
+At position 122 to 302, the domain is characterized as Tyr recombinase.
+At position 2 to 78, the domain is characterized as GIY-YIG.
+At position 32 to 148, the domain is characterized as GOLD.
+At position 525 to 631, the domain is characterized as PH.
+At position 757 to 835, the domain is characterized as DEP.
+At position 8 to 248, the domain is characterized as ABC transporter.
+At position 14 to 99, the domain is characterized as Acylphosphatase-like.
+At position 167 to 489, the domain is characterized as ABC transmembrane type-1.
+At position 521 to 767, the domain is characterized as ABC transporter.
+At position 304 to 577, the domain is characterized as NR LBD.
+At position 667 to 702, the domain is characterized as UVR.
+At position 234 to 537, the domain is characterized as Protein kinase.
+At position 15 to 244, the domain is characterized as ABC transporter.
+At position 489 to 717, the domain is characterized as ABC transmembrane type-2.
+At position 101 to 152, the domain is characterized as FBD.
+At position 107 to 182, the domain is characterized as REM-1 2.
+At position 189 to 315, the domain is characterized as C2.
+At position 664 to 923, the domain is characterized as Protein kinase.
+At position 924 to 988, the domain is characterized as AGC-kinase C-terminal.
+At position 32 to 121, the domain is characterized as PPIase FKBP-type.
+At position 135 to 321, the domain is characterized as CP-type G.
+At position 26 to 118, the domain is characterized as Ig-like C2-type.
+At position 126 to 231, the domain is characterized as Fibronectin type-III 1.
+At position 236 to 331, the domain is characterized as Fibronectin type-III 2.
+At position 334 to 433, the domain is characterized as Fibronectin type-III 3.
+At position 434 to 529, the domain is characterized as Fibronectin type-III 4.
+At position 530 to 624, the domain is characterized as Fibronectin type-III 5.
+At position 608 to 691, the domain is characterized as BRCT.
+At position 660 to 751, the domain is characterized as Big-1 2.
+At position 79 to 203, the domain is characterized as OTU.
+At position 17 to 225, the domain is characterized as AIG1-type G.
+At position 613 to 707, the domain is characterized as BRCT.
+At position 51 to 140, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 16 to 370, the domain is characterized as PTS EIIC type-2.
+At position 31 to 232, the domain is characterized as Brix.
+At position 178 to 276, the domain is characterized as HTH araC/xylS-type.
+At position 233 to 307, the domain is characterized as PUA.
+At position 26 to 144, the domain is characterized as AB hydrolase-1.
+At position 14 to 216, the domain is characterized as Lon N-terminal.
+At position 605 to 786, the domain is characterized as Lon proteolytic.
+At position 339 to 533, the domain is characterized as Protein kinase.
+At position 27 to 165, the domain is characterized as MPN.
+At position 714 to 807, the domain is characterized as FDX-ACB.
+At position 1 to 121, the domain is characterized as Ig-like.
+At position 181 to 225, the domain is characterized as bZIP.
+At position 245 to 460, the domain is characterized as DOG1.
+At position 62 to 228, the domain is characterized as 3'-5' exonuclease.
+At position 587 to 665, the domain is characterized as BRCT.
+At position 31 to 252, the domain is characterized as Peptidase S1.
+At position 53 to 128, the domain is characterized as EMI.
+At position 815 to 865, the domain is characterized as Collagen-like.
+At position 866 to 1012, the domain is characterized as C1q.
+At position 23 to 87, the domain is characterized as TRAM.
+At position 16 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 148 to 220, the domain is characterized as ACT.
+At position 206 to 296, the domain is characterized as Ig-like.
+At position 79 to 337, the domain is characterized as Protein kinase.
+At position 380 to 415, the domain is characterized as EF-hand 1.
+At position 416 to 451, the domain is characterized as EF-hand 2; degenerate.
+At position 38 to 78, the domain is characterized as ShKT.
+At position 175 to 264, the domain is characterized as Ras-associating.
+At position 21 to 150, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 6 to 189, the domain is characterized as YrdC-like.
+At position 19 to 106, the domain is characterized as GIY-YIG.
+At position 15 to 289, the domain is characterized as Protein kinase.
+At position 180 to 255, the domain is characterized as RRM.
+At position 59 to 243, the domain is characterized as TNase-like.
+At position 481 to 716, the domain is characterized as ABC transporter 1.
+At position 1287 to 1520, the domain is characterized as ABC transporter 2.
+At position 5 to 220, the domain is characterized as AMMECR1.
+At position 100 to 164, the domain is characterized as S4 RNA-binding.
+At position 211 to 588, the domain is characterized as PDEase.
+At position 22 to 402, the domain is characterized as TTL.
+At position 499 to 668, the domain is characterized as N-acetyltransferase.
+At position 144 to 187, the domain is characterized as CUE.
+At position 255 to 317, the domain is characterized as t-SNARE coiled-coil homology.
+At position 173 to 221, the domain is characterized as bZIP.
+At position 37 to 116, the domain is characterized as GIY-YIG.
+At position 226 to 261, the domain is characterized as UVR.
+At position 374 to 499, the domain is characterized as MATH.
+At position 936 to 1073, the domain is characterized as MGS-like.
+At position 6 to 285, the domain is characterized as tr-type G.
+At position 7 to 234, the domain is characterized as ABC transporter.
+At position 269 to 531, the domain is characterized as FAD-binding FR-type.
+At position 5 to 131, the domain is characterized as C2 1.
+At position 21 to 190, the domain is characterized as Era-type G.
+At position 221 to 297, the domain is characterized as KH type-2.
+At position 157 to 361, the domain is characterized as Helicase ATP-binding.
+At position 407 to 563, the domain is characterized as Helicase C-terminal.
+At position 40 to 115, the domain is characterized as RRM 1.
+At position 205 to 280, the domain is characterized as RRM 2.
+At position 370 to 445, the domain is characterized as RRM 3.
+At position 497 to 520, the domain is characterized as DAZ 1.
+At position 521 to 544, the domain is characterized as DAZ 2.
+At position 545 to 568, the domain is characterized as DAZ 3.
+At position 569 to 592, the domain is characterized as DAZ 4.
+At position 593 to 616, the domain is characterized as DAZ 5.
+At position 617 to 640, the domain is characterized as DAZ 6.
+At position 641 to 664, the domain is characterized as DAZ 7.
+At position 665 to 688, the domain is characterized as DAZ 8.
+At position 689 to 712, the domain is characterized as DAZ 9.
+At position 118 to 177, the domain is characterized as Myb-like 1.
+At position 422 to 479, the domain is characterized as Myb-like 2.
+At position 107 to 159, the domain is characterized as bHLH.
+At position 33 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 265 to 440, the domain is characterized as DH.
+At position 159 to 299, the domain is characterized as cDENN.
+At position 96 to 173, the domain is characterized as RRM 2.
+At position 26 to 344, the domain is characterized as Kinesin motor.
+At position 305 to 549, the domain is characterized as START.
+At position 280 to 449, the domain is characterized as tr-type G.
+At position 70 to 273, the domain is characterized as ABC transmembrane type-1.
+At position 162 to 551, the domain is characterized as SAC.
+At position 80 to 145, the domain is characterized as NAC-A/B.
+At position 180 to 479, the domain is characterized as Protein kinase.
+At position 98 to 174, the domain is characterized as PRC barrel.
+At position 67 to 241, the domain is characterized as FAD-binding PCMH-type.
+At position 26 to 691, the domain is characterized as Vitellogenin.
+At position 1346 to 1514, the domain is characterized as VWFD.
+At position 166 to 234, the domain is characterized as KH.
+At position 293 to 385, the domain is characterized as HD.
+At position 2 to 205, the domain is characterized as CNNM transmembrane.
+At position 224 to 285, the domain is characterized as CBS 1.
+At position 286 to 346, the domain is characterized as CBS 2.
+At position 125 to 275, the domain is characterized as Exonuclease.
+At position 7 to 414, the domain is characterized as BRO1.
+At position 1 to 111, the domain is characterized as HPt.
+At position 418 to 661, the domain is characterized as Histidine kinase.
+At position 663 to 798, the domain is characterized as CheW-like.
+At position 125 to 189, the domain is characterized as PWWP.
+At position 55 to 170, the domain is characterized as Expansin-like EG45.
+At position 180 to 261, the domain is characterized as Expansin-like CBD.
+At position 531 to 586, the domain is characterized as SOCS box.
+At position 1210 to 1279, the domain is characterized as Sushi 1.
+At position 1280 to 1341, the domain is characterized as Sushi 2.
+At position 1342 to 1409, the domain is characterized as Sushi 3.
+At position 1410 to 1470, the domain is characterized as Sushi 4.
+At position 1473 to 1553, the domain is characterized as Sushi 5.
+At position 604 to 778, the domain is characterized as PCI.
+At position 595 to 675, the domain is characterized as BRCT.
+At position 2197 to 2307, the domain is characterized as PH.
+At position 108 to 351, the domain is characterized as Radical SAM core.
+At position 285 to 361, the domain is characterized as SPOR.
+At position 12 to 184, the domain is characterized as N-acetyltransferase.
+At position 34 to 259, the domain is characterized as SET.
+At position 342 to 768, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 64 to 127, the domain is characterized as bZIP.
+At position 250 to 460, the domain is characterized as Peptidase M12B.
+At position 469 to 548, the domain is characterized as Disintegrin.
+At position 546 to 601, the domain is characterized as TSP type-1 1.
+At position 827 to 887, the domain is characterized as TSP type-1 2.
+At position 891 to 947, the domain is characterized as TSP type-1 3.
+At position 948 to 1001, the domain is characterized as TSP type-1 4.
+At position 1318 to 1371, the domain is characterized as TSP type-1 5.
+At position 1373 to 1428, the domain is characterized as TSP type-1 6.
+At position 1429 to 1477, the domain is characterized as TSP type-1 7.
+At position 57 to 147, the domain is characterized as Cystatin.
+At position 14 to 163, the domain is characterized as NAC.
+At position 293 to 377, the domain is characterized as PDZ.
+At position 59 to 98, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 99 to 143, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 149 to 190, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 191 to 233, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 48 to 142, the domain is characterized as Ig-like V-type.
+At position 147 to 241, the domain is characterized as Ig-like C2-type 1.
+At position 246 to 332, the domain is characterized as Ig-like C2-type 2.
+At position 306 to 369, the domain is characterized as bZIP.
+At position 111 to 124, the domain is characterized as CRIB.
+At position 139 to 390, the domain is characterized as Protein kinase.
+At position 770 to 903, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1222 to 1361, the domain is characterized as DOD-type homing endonuclease 2.
+At position 1 to 502, the domain is characterized as GRAD1.
+At position 273 to 678, the domain is characterized as USP.
+At position 39 to 163, the domain is characterized as CUB.
+At position 165 to 230, the domain is characterized as Sushi.
+At position 245 to 484, the domain is characterized as Peptidase S1.
+At position 443 to 566, the domain is characterized as Ricin B-type lectin.
+At position 303 to 552, the domain is characterized as Glutamine amidotransferase type-1.
+At position 122 to 439, the domain is characterized as Peptidase S8.
+At position 28 to 99, the domain is characterized as BTB.
+At position 218 to 507, the domain is characterized as NPH3.
+At position 214 to 304, the domain is characterized as Fibronectin type-III 1.
+At position 334 to 427, the domain is characterized as Fibronectin type-III 2.
+At position 162 to 227, the domain is characterized as HTH luxR-type.
+At position 56 to 91, the domain is characterized as EF-hand.
+At position 8 to 69, the domain is characterized as TRAM.
+At position 49 to 274, the domain is characterized as Peptidase S1.
+At position 32 to 91, the domain is characterized as Ig-like C2-type 1.
+At position 103 to 180, the domain is characterized as Ig-like C2-type 2.
+At position 189 to 282, the domain is characterized as Ig-like C2-type 3.
+At position 293 to 380, the domain is characterized as Ig-like C2-type 4.
+At position 389 to 477, the domain is characterized as Ig-like C2-type 5.
+At position 568 to 942, the domain is characterized as Protein kinase.
+At position 138 to 187, the domain is characterized as bHLH.
+At position 14 to 199, the domain is characterized as YrdC-like.
+At position 1 to 237, the domain is characterized as ThyX.
+At position 252 to 429, the domain is characterized as VWFA.
+At position 445 to 536, the domain is characterized as Cache.
+At position 145 to 316, the domain is characterized as Helicase ATP-binding.
+At position 339 to 487, the domain is characterized as Helicase C-terminal.
+At position 24 to 72, the domain is characterized as TSP type-1 0.
+At position 73 to 130, the domain is characterized as TSP type-1 1.
+At position 132 to 187, the domain is characterized as TSP type-1 2.
+At position 189 to 251, the domain is characterized as TSP type-1 3.
+At position 253 to 309, the domain is characterized as TSP type-1 4.
+At position 311 to 372, the domain is characterized as TSP type-1 5.
+At position 374 to 457, the domain is characterized as TSP type-1 6.
+At position 151 to 250, the domain is characterized as Fe2OG dioxygenase.
+At position 344 to 419, the domain is characterized as OCT.
+At position 43 to 297, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 649 to 738, the domain is characterized as BRCT.
+At position 2 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 282, the domain is characterized as Protein kinase.
+At position 365 to 432, the domain is characterized as PASTA 1.
+At position 433 to 499, the domain is characterized as PASTA 2.
+At position 500 to 566, the domain is characterized as PASTA 3.
+At position 410 to 477, the domain is characterized as TRAM.
+At position 1 to 339, the domain is characterized as MACPF.
+At position 25 to 145, the domain is characterized as MTTase N-terminal.
+At position 168 to 397, the domain is characterized as Radical SAM core.
+At position 538 to 814, the domain is characterized as Protein kinase.
+At position 649 to 836, the domain is characterized as Rho-GAP.
+At position 851 to 983, the domain is characterized as N-terminal Ras-GEF.
+At position 1021 to 1255, the domain is characterized as Ras-GEF.
+At position 24 to 80, the domain is characterized as Kazal-like.
+At position 30 to 115, the domain is characterized as Cystatin.
+At position 7 to 235, the domain is characterized as ABC transporter.
+At position 288 to 323, the domain is characterized as EF-hand 1.
+At position 59 to 309, the domain is characterized as Protein kinase.
+At position 750 to 843, the domain is characterized as PWI.
+At position 775 to 893, the domain is characterized as GAE.
+At position 46 to 237, the domain is characterized as RNase H type-2.
+At position 685 to 919, the domain is characterized as NR LBD.
+At position 1 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 27 to 148, the domain is characterized as Rhodanese.
+At position 575 to 629, the domain is characterized as 3'-5' exonuclease.
+At position 2 to 56, the domain is characterized as F-box.
+At position 79 to 179, the domain is characterized as Fe2OG dioxygenase.
+At position 350 to 540, the domain is characterized as Rho-GAP.
+At position 111 to 229, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 314, the domain is characterized as Ig-like C2-type 3.
+At position 338 to 419, the domain is characterized as Ig-like C2-type 4.
+At position 187 to 648, the domain is characterized as Trm1 methyltransferase.
+At position 455 to 586, the domain is characterized as AXH.
+At position 146 to 341, the domain is characterized as ATP-grasp.
+At position 194 to 340, the domain is characterized as Ricin B-type lectin.
+At position 70 to 408, the domain is characterized as G-alpha.
+At position 66 to 127, the domain is characterized as SoHo.
+At position 863 to 922, the domain is characterized as SH3 1.
+At position 938 to 999, the domain is characterized as SH3 2.
+At position 1041 to 1100, the domain is characterized as SH3 3.
+At position 141 to 289, the domain is characterized as Tyrosine-protein phosphatase.
+At position 30 to 58, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 283 to 457, the domain is characterized as Helicase C-terminal.
+At position 19 to 249, the domain is characterized as Radical SAM core.
+At position 35 to 224, the domain is characterized as RHD.
+At position 764 to 851, the domain is characterized as Death.
+At position 1 to 110, the domain is characterized as Tyrosine-protein phosphatase.
+At position 2 to 309, the domain is characterized as Hcy-binding.
+At position 76 to 234, the domain is characterized as OTU.
+At position 47 to 225, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 111, the domain is characterized as SSB.
+At position 34 to 236, the domain is characterized as Cupin type-1 1.
+At position 289 to 438, the domain is characterized as Cupin type-1 2.
+At position 336 to 560, the domain is characterized as NR LBD.
+At position 101 to 393, the domain is characterized as ABC transmembrane type-1.
+At position 482 to 708, the domain is characterized as ABC transporter.
+At position 195 to 233, the domain is characterized as LDL-receptor class A 5.
+At position 234 to 272, the domain is characterized as LDL-receptor class A 6.
+At position 274 to 313, the domain is characterized as LDL-receptor class A 7.
+At position 314 to 353, the domain is characterized as EGF-like 1.
+At position 354 to 393, the domain is characterized as EGF-like 2; calcium-binding.
+At position 663 to 712, the domain is characterized as EGF-like 3.
+At position 114 to 219, the domain is characterized as Fe2OG dioxygenase.
+At position 45 to 111, the domain is characterized as KRAB.
+At position 27 to 369, the domain is characterized as GH10.
+At position 542 to 596, the domain is characterized as LRRCT.
+At position 648 to 791, the domain is characterized as TIR.
+At position 155 to 378, the domain is characterized as NR LBD.
+At position 37 to 314, the domain is characterized as Pyruvate carboxyltransferase.
+At position 8 to 432, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 973 to 1283, the domain is characterized as PKS/mFAS DH.
+At position 2472 to 2549, the domain is characterized as Carrier.
+At position 776 to 887, the domain is characterized as MaoC-like.
+At position 143 to 468, the domain is characterized as Peptidase S8.
+At position 478 to 603, the domain is characterized as P/Homo B.
+At position 43 to 116, the domain is characterized as S4 RNA-binding.
+At position 19 to 136, the domain is characterized as MTTase N-terminal.
+At position 258 to 428, the domain is characterized as CRAL-TRIO.
+At position 433 to 534, the domain is characterized as GOLD.
+At position 139 to 168, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 23 to 91, the domain is characterized as BON.
+At position 97 to 146, the domain is characterized as LysM.
+At position 636 to 717, the domain is characterized as BRCT.
+At position 159 to 351, the domain is characterized as CheB-type methylesterase.
+At position 23 to 206, the domain is characterized as Integrase catalytic.
+At position 408 to 532, the domain is characterized as SET.
+At position 38 to 197, the domain is characterized as SIS.
+At position 24 to 235, the domain is characterized as Ch-type lysozyme.
+At position 25 to 282, the domain is characterized as Protein kinase.
+At position 804 to 1091, the domain is characterized as Protein kinase.
+At position 346 to 453, the domain is characterized as SH2.
+At position 8 to 259, the domain is characterized as ABC transporter.
+At position 21 to 234, the domain is characterized as RNase H type-2.
+At position 116 to 230, the domain is characterized as C-type lectin.
+At position 1 to 171, the domain is characterized as PPIase cyclophilin-type.
+At position 248 to 326, the domain is characterized as RRM.
+At position 174 to 299, the domain is characterized as Fatty acid hydroxylase.
+At position 37 to 99, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 170 to 232, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 39 to 131, the domain is characterized as PpiC.
+At position 143 to 176, the domain is characterized as EF-hand 4.
+At position 245 to 319, the domain is characterized as POU-specific.
+At position 7 to 70, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 30 to 163, the domain is characterized as ENTH.
+At position 17 to 45, the domain is characterized as LRRNT.
+At position 346 to 438, the domain is characterized as Ig-like C2-type 1.
+At position 445 to 532, the domain is characterized as Ig-like C2-type 2.
+At position 228 to 379, the domain is characterized as Exonuclease.
+At position 4 to 163, the domain is characterized as Jacalin-type lectin.
+At position 197 to 456, the domain is characterized as Protein kinase.
+At position 7 to 119, the domain is characterized as MTTase N-terminal.
+At position 15 to 261, the domain is characterized as ABC transporter.
+At position 163 to 327, the domain is characterized as Helicase ATP-binding.
+At position 424 to 620, the domain is characterized as Helicase C-terminal.
+At position 59 to 248, the domain is characterized as PID.
+At position 114 to 255, the domain is characterized as PA14.
+At position 89 to 215, the domain is characterized as GST C-terminal.
+At position 254 to 415, the domain is characterized as EF-1-gamma C-terminal.
+At position 718 to 793, the domain is characterized as Smr.
+At position 197 to 290, the domain is characterized as PPIase FKBP-type.
+At position 45 to 175, the domain is characterized as SCP.
+At position 211 to 244, the domain is characterized as ShKT.
+At position 5 to 285, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 21 to 177, the domain is characterized as PPIase cyclophilin-type.
+At position 17 to 69, the domain is characterized as HTH myb-type 1.
+At position 70 to 124, the domain is characterized as HTH myb-type 2.
+At position 483 to 666, the domain is characterized as MIF4G.
+At position 776 to 892, the domain is characterized as MI.
+At position 105 to 396, the domain is characterized as Protein kinase.
+At position 315 to 596, the domain is characterized as ABC transporter 1.
+At position 1 to 262, the domain is characterized as Deacetylase sirtuin-type.
+At position 10 to 88, the domain is characterized as Ubiquitin-like.
+At position 207 to 273, the domain is characterized as J.
+At position 130 to 380, the domain is characterized as SMP-LTD.
+At position 5 to 54, the domain is characterized as CSD.
+At position 49 to 279, the domain is characterized as ABC transporter.
+At position 175 to 349, the domain is characterized as EngA-type G 2.
+At position 3 to 77, the domain is characterized as Tudor-knot.
+At position 163 to 353, the domain is characterized as MRG.
+At position 19 to 69, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 392 to 646, the domain is characterized as Tyrosine-protein phosphatase.
+At position 15 to 263, the domain is characterized as Nudix hydrolase.
+At position 39 to 213, the domain is characterized as Helicase ATP-binding.
+At position 241 to 398, the domain is characterized as Helicase C-terminal.
+At position 276 to 404, the domain is characterized as G8.
+At position 19 to 106, the domain is characterized as Ig-like.
+At position 75 to 125, the domain is characterized as DHHC.
+At position 117 to 393, the domain is characterized as PPM-type phosphatase.
+At position 9 to 70, the domain is characterized as HTH myb-type 1.
+At position 71 to 125, the domain is characterized as HTH myb-type 2.
+At position 118 to 346, the domain is characterized as OTU.
+At position 662 to 739, the domain is characterized as BRCT.
+At position 14 to 179, the domain is characterized as CP-type G.
+At position 38 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 165, the domain is characterized as Nudix hydrolase.
+At position 99 to 326, the domain is characterized as Radical SAM core.
+At position 6 to 93, the domain is characterized as ASCH.
+At position 106 to 171, the domain is characterized as CBS 1.
+At position 199 to 256, the domain is characterized as CBS 2.
+At position 274 to 331, the domain is characterized as CBS 3.
+At position 253 to 438, the domain is characterized as Helicase ATP-binding.
+At position 449 to 609, the domain is characterized as Helicase C-terminal.
+At position 91 to 167, the domain is characterized as Lipoyl-binding 1.
+At position 218 to 294, the domain is characterized as Lipoyl-binding 2.
+At position 356 to 393, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 5 to 59, the domain is characterized as bHLH.
+At position 77 to 185, the domain is characterized as AB hydrolase-1.
+At position 31 to 242, the domain is characterized as BPL/LPL catalytic.
+At position 45 to 80, the domain is characterized as ShKT.
+At position 933 to 978, the domain is characterized as UBA.
+At position 1565 to 1632, the domain is characterized as RRM.
+At position 27 to 514, the domain is characterized as Sema.
+At position 562 to 654, the domain is characterized as IPT/TIG 1.
+At position 1076 to 1343, the domain is characterized as Protein kinase.
+At position 233 to 391, the domain is characterized as SSD.
+At position 23 to 258, the domain is characterized as ABC transporter.
+At position 1040 to 1545, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 885 to 1152, the domain is characterized as Protein kinase.
+At position 147 to 701, the domain is characterized as RINT1/TIP20.
+At position 16 to 271, the domain is characterized as Protein kinase.
+At position 89 to 419, the domain is characterized as USP.
+At position 457 to 552, the domain is characterized as DUSP 1.
+At position 567 to 690, the domain is characterized as DUSP 2.
+At position 710 to 823, the domain is characterized as DUSP 3.
+At position 931 to 1007, the domain is characterized as Ubiquitin-like.
+At position 52 to 181, the domain is characterized as CMP/dCMP-type deaminase.
+At position 184 to 395, the domain is characterized as Helicase ATP-binding.
+At position 444 to 615, the domain is characterized as Helicase C-terminal.
+At position 181 to 381, the domain is characterized as Helicase ATP-binding.
+At position 421 to 566, the domain is characterized as Helicase C-terminal.
+At position 56 to 85, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 30 to 113, the domain is characterized as Core-binding (CB).
+At position 142 to 332, the domain is characterized as Tyr recombinase.
+At position 935 to 979, the domain is characterized as UBA.
+At position 635 to 731, the domain is characterized as ERCC4.
+At position 109 to 261, the domain is characterized as Nudix hydrolase.
+At position 4 to 122, the domain is characterized as CMP/dCMP-type deaminase.
+At position 262 to 519, the domain is characterized as KaiC 2.
+At position 1053 to 1535, the domain is characterized as FAT.
+At position 1754 to 2099, the domain is characterized as PI3K/PI4K catalytic.
+At position 2290 to 2322, the domain is characterized as FATC.
+At position 572 to 647, the domain is characterized as PUA.
+At position 95 to 156, the domain is characterized as S4 RNA-binding.
+At position 258 to 444, the domain is characterized as GATase cobBQ-type.
+At position 78 to 185, the domain is characterized as sHSP.
+At position 61 to 319, the domain is characterized as Protein kinase.
+At position 362 to 397, the domain is characterized as EF-hand 1.
+At position 398 to 433, the domain is characterized as EF-hand 2.
+At position 434 to 469, the domain is characterized as EF-hand 3.
+At position 473 to 504, the domain is characterized as EF-hand 4.
+At position 12 to 127, the domain is characterized as VOC.
+At position 41 to 162, the domain is characterized as tRNA-binding.
+At position 443 to 519, the domain is characterized as B5.
+At position 776 to 868, the domain is characterized as FDX-ACB.
+At position 47 to 159, the domain is characterized as CUB 1.
+At position 165 to 201, the domain is characterized as LDL-receptor class A 1.
+At position 214 to 255, the domain is characterized as LDL-receptor class A 2.
+At position 259 to 372, the domain is characterized as CUB 2.
+At position 374 to 411, the domain is characterized as LDL-receptor class A 3.
+At position 412 to 449, the domain is characterized as LDL-receptor class A 4.
+At position 450 to 486, the domain is characterized as LDL-receptor class A 5.
+At position 36 to 385, the domain is characterized as GH18.
+At position 15 to 281, the domain is characterized as Protein kinase.
+At position 1 to 198, the domain is characterized as Glutamine amidotransferase type-1.
+At position 574 to 784, the domain is characterized as Helicase ATP-binding.
+At position 1060 to 1216, the domain is characterized as Helicase C-terminal.
+At position 191 to 300, the domain is characterized as Guanylate cyclase.
+At position 38 to 395, the domain is characterized as PIPK.
+At position 155 to 287, the domain is characterized as TIR.
+At position 222 to 491, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 13 to 288, the domain is characterized as CN hydrolase.
+At position 249 to 411, the domain is characterized as PCI.
+At position 567 to 646, the domain is characterized as KIX.
+At position 1066 to 1138, the domain is characterized as Bromo.
+At position 1286 to 1662, the domain is characterized as CBP/p300-type HAT.
+At position 311 to 378, the domain is characterized as DRBM 1.
+At position 490 to 557, the domain is characterized as DRBM 2.
+At position 711 to 781, the domain is characterized as DRBM 4.
+At position 951 to 1018, the domain is characterized as DRBM 5.
+At position 27 to 106, the domain is characterized as Death.
+At position 212 to 521, the domain is characterized as Protein kinase.
+At position 33 to 459, the domain is characterized as Velvet.
+At position 2 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 18 to 145, the domain is characterized as Nudix hydrolase.
+At position 131 to 232, the domain is characterized as BACK.
+At position 70 to 316, the domain is characterized as ABC transporter.
+At position 392 to 603, the domain is characterized as ABC transmembrane type-2.
+At position 13 to 152, the domain is characterized as Jacalin-type lectin.
+At position 35 to 136, the domain is characterized as Ig-like C2-type 1.
+At position 146 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 249 to 357, the domain is characterized as Ig-like C2-type 3.
+At position 698 to 792, the domain is characterized as FDX-ACB.
+At position 1120 to 1355, the domain is characterized as Fibrillar collagen NC1.
+At position 96 to 419, the domain is characterized as Calpain catalytic.
+At position 1 to 18, the domain is characterized as Ubiquitin-like 1.
+At position 19 to 94, the domain is characterized as Ubiquitin-like 2.
+At position 95 to 170, the domain is characterized as Ubiquitin-like 3.
+At position 41 to 236, the domain is characterized as Helicase ATP-binding.
+At position 266 to 444, the domain is characterized as Helicase C-terminal.
+At position 453 to 566, the domain is characterized as STAS.
+At position 383 to 498, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 657 to 736, the domain is characterized as POLO box.
+At position 33 to 145, the domain is characterized as BTB.
+At position 197 to 440, the domain is characterized as START.
+At position 20 to 135, the domain is characterized as Cytochrome c.
+At position 121 to 408, the domain is characterized as Protein kinase.
+At position 411 to 554, the domain is characterized as KEN.
+At position 65 to 154, the domain is characterized as FAR1.
+At position 275 to 371, the domain is characterized as MULE.
+At position 76 to 559, the domain is characterized as GBD/FH3.
+At position 687 to 1088, the domain is characterized as FH2.
+At position 1136 to 1169, the domain is characterized as DAD.
+At position 2 to 45, the domain is characterized as Chitin-binding type-1.
+At position 526 to 617, the domain is characterized as SH2.
+At position 166 to 457, the domain is characterized as Protein kinase.
+At position 170 to 416, the domain is characterized as Fibrinogen C-terminal.
+At position 299 to 355, the domain is characterized as RRM 1.
+At position 409 to 482, the domain is characterized as RRM 2.
+At position 500 to 571, the domain is characterized as RRM 3.
+At position 31 to 165, the domain is characterized as Nudix hydrolase.
+At position 205 to 398, the domain is characterized as CheB-type methylesterase.
+At position 259 to 309, the domain is characterized as DHHC.
+At position 47 to 211, the domain is characterized as BUB1 N-terminal.
+At position 953 to 1298, the domain is characterized as Protein kinase.
+At position 30 to 97, the domain is characterized as BTB.
+At position 229 to 414, the domain is characterized as FAD-binding PCMH-type.
+At position 394 to 450, the domain is characterized as CBS 1.
+At position 455 to 509, the domain is characterized as CBS 2.
+At position 310 to 558, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 133, the domain is characterized as Response regulatory.
+At position 41 to 154, the domain is characterized as C-type lectin 1.
+At position 562 to 687, the domain is characterized as C-type lectin 2.
+At position 716 to 828, the domain is characterized as C-type lectin 3.
+At position 114 to 269, the domain is characterized as N-acetyltransferase.
+At position 359 to 429, the domain is characterized as Bromo.
+At position 6 to 415, the domain is characterized as Helicase ATP-binding.
+At position 36 to 234, the domain is characterized as VWFA 1.
+At position 614 to 802, the domain is characterized as VWFA 2.
+At position 826 to 1018, the domain is characterized as VWFA 3.
+At position 164 to 407, the domain is characterized as Radical SAM core.
+At position 410 to 480, the domain is characterized as TRAM.
+At position 81 to 136, the domain is characterized as AWS.
+At position 138 to 255, the domain is characterized as SET.
+At position 262 to 278, the domain is characterized as Post-SET.
+At position 479 to 511, the domain is characterized as WW.
+At position 283 to 439, the domain is characterized as W2.
+At position 109 to 217, the domain is characterized as C-type lectin.
+At position 150 to 248, the domain is characterized as PH.
+At position 785 to 1033, the domain is characterized as PPM-type phosphatase.
+At position 40 to 349, the domain is characterized as GH10.
+At position 354 to 457, the domain is characterized as CBM2.
+At position 79 to 202, the domain is characterized as PX.
+At position 317 to 396, the domain is characterized as PB1.
+At position 74 to 255, the domain is characterized as FAD-binding PCMH-type.
+At position 45 to 283, the domain is characterized as Radical SAM core.
+At position 81 to 242, the domain is characterized as Bms1-type G.
+At position 90 to 243, the domain is characterized as N-acetyltransferase.
+At position 3 to 392, the domain is characterized as BRO1.
+At position 74 to 255, the domain is characterized as Macro.
+At position 40 to 341, the domain is characterized as Protein kinase.
+At position 547 to 680, the domain is characterized as C1q.
+At position 90 to 150, the domain is characterized as S4 RNA-binding.
+At position 18 to 131, the domain is characterized as EamA 1.
+At position 199 to 310, the domain is characterized as EamA 2.
+At position 72 to 201, the domain is characterized as SEC7.
+At position 259 to 376, the domain is characterized as PH.
+At position 330 to 473, the domain is characterized as DAGKc.
+At position 153 to 208, the domain is characterized as HTH myb-type 1.
+At position 209 to 259, the domain is characterized as HTH myb-type 2.
+At position 125 to 363, the domain is characterized as Radical SAM core.
+At position 119 to 151, the domain is characterized as EF-hand 4.
+At position 226 to 365, the domain is characterized as Helicase ATP-binding.
+At position 390 to 546, the domain is characterized as Helicase C-terminal.
+At position 24 to 123, the domain is characterized as Phytocyanin.
+At position 91 to 421, the domain is characterized as Asparaginase/glutaminase.
+At position 72 to 382, the domain is characterized as IF rod.
+At position 1109 to 1303, the domain is characterized as Rap-GAP.
+At position 570 to 665, the domain is characterized as SH2.
+At position 123 to 231, the domain is characterized as CBM21.
+At position 170 to 202, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 221 to 251, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 61 to 144, the domain is characterized as RRM.
+At position 16 to 177, the domain is characterized as NAC.
+At position 357 to 645, the domain is characterized as Protein kinase.
+At position 29 to 143, the domain is characterized as sHSP.
+At position 25 to 162, the domain is characterized as C1q 1.
+At position 172 to 317, the domain is characterized as C1q 2.
+At position 22 to 296, the domain is characterized as Dynamin-type G.
+At position 762 to 853, the domain is characterized as GED.
+At position 86 to 170, the domain is characterized as GST N-terminal.
+At position 179 to 328, the domain is characterized as GST C-terminal.
+At position 185 to 509, the domain is characterized as Protein kinase.
+At position 510 to 577, the domain is characterized as AGC-kinase C-terminal.
+At position 212 to 485, the domain is characterized as ABC transporter 1.
+At position 563 to 775, the domain is characterized as ABC transmembrane type-2 1.
+At position 877 to 1129, the domain is characterized as ABC transporter 2.
+At position 1202 to 1418, the domain is characterized as ABC transmembrane type-2 2.
+At position 89 to 192, the domain is characterized as Glutaredoxin.
+At position 262 to 376, the domain is characterized as GST C-terminal.
+At position 6 to 163, the domain is characterized as Thioredoxin.
+At position 15 to 96, the domain is characterized as MIT.
+At position 325 to 509, the domain is characterized as Senescence.
+At position 556 to 867, the domain is characterized as CNH.
+At position 139 to 357, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 299 to 473, the domain is characterized as Helicase ATP-binding.
+At position 503 to 682, the domain is characterized as Helicase C-terminal.
+At position 344 to 394, the domain is characterized as FBD.
+At position 15 to 202, the domain is characterized as RNase H type-2.
+At position 14 to 144, the domain is characterized as ADF-H.
+At position 22 to 67, the domain is characterized as LRRNT 1.
+At position 218 to 269, the domain is characterized as LRRCT 1.
+At position 319 to 360, the domain is characterized as LRRNT 2.
+At position 516 to 567, the domain is characterized as LRRCT 2.
+At position 53 to 149, the domain is characterized as Glutaredoxin.
+At position 38 to 140, the domain is characterized as Glutaredoxin.
+At position 34 to 223, the domain is characterized as GH11.
+At position 17 to 274, the domain is characterized as Alpha-carbonic anhydrase.
+At position 83 to 248, the domain is characterized as CP-type G.
+At position 289 to 359, the domain is characterized as Mop.
+At position 97 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 11 to 96, the domain is characterized as Sm.
+At position 82 to 147, the domain is characterized as DPH-type MB.
+At position 1036 to 1172, the domain is characterized as RanBD1 1.
+At position 1333 to 1469, the domain is characterized as RanBD1 2.
+At position 1702 to 1752, the domain is characterized as GRIP.
+At position 136 to 230, the domain is characterized as Rhodanese.
+At position 55 to 235, the domain is characterized as tr-type G.
+At position 39 to 166, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 27 to 320, the domain is characterized as Protein kinase.
+At position 88 to 221, the domain is characterized as GST C-terminal.
+At position 275 to 436, the domain is characterized as EF-1-gamma C-terminal.
+At position 112 to 319, the domain is characterized as ATP-grasp.
+At position 172 to 296, the domain is characterized as Rhodanese.
+At position 488 to 849, the domain is characterized as USP.
+At position 1 to 386, the domain is characterized as SMP-LTD.
+At position 369 to 524, the domain is characterized as Helicase ATP-binding.
+At position 673 to 838, the domain is characterized as Helicase C-terminal.
+At position 46 to 345, the domain is characterized as GH10.
+At position 511 to 572, the domain is characterized as SH3 1.
+At position 700 to 768, the domain is characterized as SH3 2.
+At position 170 to 363, the domain is characterized as FCP1 homology.
+At position 499 to 593, the domain is characterized as BRCT.
+At position 1062 to 1285, the domain is characterized as JmjC.
+At position 86 to 342, the domain is characterized as Glutamine amidotransferase type-1.
+At position 8 to 59, the domain is characterized as L27 1.
+At position 60 to 118, the domain is characterized as L27 2.
+At position 140 to 219, the domain is characterized as PDZ.
+At position 225 to 293, the domain is characterized as SH3.
+At position 350 to 537, the domain is characterized as Guanylate kinase-like.
+At position 135 to 192, the domain is characterized as Chitin-binding type-2 2.
+At position 244 to 301, the domain is characterized as Chitin-binding type-2 3.
+At position 306 to 361, the domain is characterized as Chitin-binding type-2 4.
+At position 400 to 456, the domain is characterized as Chitin-binding type-2 5.
+At position 469 to 524, the domain is characterized as Chitin-binding type-2 6.
+At position 6 to 117, the domain is characterized as PH.
+At position 65 to 242, the domain is characterized as DHFR.
+At position 678 to 825, the domain is characterized as bMERB.
+At position 3 to 96, the domain is characterized as Cystatin 1.
+At position 97 to 191, the domain is characterized as Cystatin 2.
+At position 192 to 285, the domain is characterized as Cystatin 3.
+At position 286 to 380, the domain is characterized as Cystatin 4.
+At position 381 to 474, the domain is characterized as Cystatin 5.
+At position 475 to 568, the domain is characterized as Cystatin 6.
+At position 569 to 662, the domain is characterized as Cystatin 7.
+At position 663 to 756, the domain is characterized as Cystatin 8.
+At position 52 to 89, the domain is characterized as LDL-receptor class A 1.
+At position 120 to 157, the domain is characterized as LDL-receptor class A 2.
+At position 154 to 195, the domain is characterized as JmjN.
+At position 348 to 514, the domain is characterized as JmjC.
+At position 1019 to 1077, the domain is characterized as FYR N-terminal.
+At position 1079 to 1169, the domain is characterized as FYR C-terminal.
+At position 81 to 143, the domain is characterized as CBS 1.
+At position 12 to 86, the domain is characterized as UPAR/Ly6.
+At position 113 to 206, the domain is characterized as PRC barrel.
+At position 72 to 107, the domain is characterized as EF-hand.
+At position 4 to 124, the domain is characterized as PINc.
+At position 347 to 457, the domain is characterized as PLAT.
+At position 129 to 571, the domain is characterized as Urease.
+At position 191 to 280, the domain is characterized as TonB C-terminal.
+At position 113 to 197, the domain is characterized as GST N-terminal.
+At position 206 to 355, the domain is characterized as GST C-terminal.
+At position 5 to 249, the domain is characterized as ABC transporter 1.
+At position 265 to 487, the domain is characterized as ABC transporter 2.
+At position 2 to 61, the domain is characterized as LCN-type CS-alpha/beta.
+At position 133 to 308, the domain is characterized as Helicase ATP-binding.
+At position 336 to 483, the domain is characterized as Helicase C-terminal.
+At position 1 to 172, the domain is characterized as PPIase cyclophilin-type.
+At position 253 to 331, the domain is characterized as RRM.
+At position 214 to 429, the domain is characterized as START.
+At position 567 to 649, the domain is characterized as Carrier.
+At position 215 to 416, the domain is characterized as Peptidase M12B.
+At position 423 to 510, the domain is characterized as Disintegrin.
+At position 659 to 687, the domain is characterized as EGF-like.
+At position 909 to 1034, the domain is characterized as CBM6.
+At position 163 to 443, the domain is characterized as ABC transmembrane type-1 1.
+At position 508 to 732, the domain is characterized as ABC transporter 1.
+At position 806 to 1105, the domain is characterized as ABC transmembrane type-1 2.
+At position 1141 to 1375, the domain is characterized as ABC transporter 2.
+At position 291 to 535, the domain is characterized as Clu.
+At position 10 to 99, the domain is characterized as Acylphosphatase-like.
+At position 97 to 137, the domain is characterized as LRRCT.
+At position 567 to 810, the domain is characterized as MIF4G.
+At position 31 to 142, the domain is characterized as Ig-like V-type.
+At position 146 to 235, the domain is characterized as Ig-like C2-type 1.
+At position 644 to 707, the domain is characterized as SAM.
+At position 779 to 989, the domain is characterized as DDHD.
+At position 128 to 422, the domain is characterized as PPM-type phosphatase.
+At position 9 to 173, the domain is characterized as N-acetyltransferase.
+At position 5 to 145, the domain is characterized as MABP.
+At position 216 to 267, the domain is characterized as UMA.
+At position 8 to 85, the domain is characterized as GST N-terminal.
+At position 87 to 207, the domain is characterized as GST C-terminal.
+At position 50 to 184, the domain is characterized as Thioredoxin.
+At position 29 to 87, the domain is characterized as VWFC.
+At position 1218 to 1453, the domain is characterized as Fibrillar collagen NC1.
+At position 113 to 380, the domain is characterized as Protein kinase.
+At position 48 to 191, the domain is characterized as SCP.
+At position 15 to 142, the domain is characterized as RNase III.
+At position 169 to 240, the domain is characterized as DRBM.
+At position 1349 to 1604, the domain is characterized as Protein kinase.
+At position 118 to 221, the domain is characterized as PH.
+At position 301 to 362, the domain is characterized as SH3.
+At position 8 to 70, the domain is characterized as TRAM.
+At position 199 to 262, the domain is characterized as bZIP.
+At position 12 to 296, the domain is characterized as Lon N-terminal.
+At position 692 to 922, the domain is characterized as Lon proteolytic.
+At position 134 to 161, the domain is characterized as Oxidoreductase-like.
+At position 63 to 137, the domain is characterized as FAR1.
+At position 246 to 342, the domain is characterized as MULE.
+At position 56 to 271, the domain is characterized as Radical SAM core.
+At position 364 to 584, the domain is characterized as Protein kinase.
+At position 587 to 722, the domain is characterized as KEN.
+At position 61 to 97, the domain is characterized as VM.
+At position 16 to 143, the domain is characterized as VHS.
+At position 370 to 387, the domain is characterized as ITAM.
+At position 29 to 69, the domain is characterized as EGF-like 1; calcium-binding.
+At position 70 to 111, the domain is characterized as EGF-like 2; calcium-binding.
+At position 112 to 148, the domain is characterized as EGF-like 3; calcium-binding.
+At position 157 to 198, the domain is characterized as EGF-like 4.
+At position 199 to 237, the domain is characterized as EGF-like 5.
+At position 238 to 276, the domain is characterized as EGF-like 6.
+At position 277 to 317, the domain is characterized as EGF-like 7; calcium-binding.
+At position 318 to 356, the domain is characterized as EGF-like 8; calcium-binding.
+At position 357 to 398, the domain is characterized as EGF-like 9; calcium-binding.
+At position 804 to 916, the domain is characterized as CUB.
+At position 5 to 245, the domain is characterized as CN hydrolase.
+At position 940 to 1014, the domain is characterized as U-box.
+At position 640 to 715, the domain is characterized as BRCT.
+At position 4 to 378, the domain is characterized as Trm1 methyltransferase.
+At position 14 to 170, the domain is characterized as N-acetyltransferase.
+At position 8 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 196 to 324, the domain is characterized as Galectin 2.
+At position 109 to 298, the domain is characterized as Macro 1.
+At position 313 to 492, the domain is characterized as Macro 2.
+At position 635 to 853, the domain is characterized as PARP catalytic.
+At position 77 to 179, the domain is characterized as Glutaredoxin.
+At position 1 to 419, the domain is characterized as PIPK.
+At position 175 to 436, the domain is characterized as ABC transporter 1.
+At position 504 to 713, the domain is characterized as ABC transporter 2.
+At position 293 to 540, the domain is characterized as GT92.
+At position 64 to 240, the domain is characterized as FAD-binding PCMH-type.
+At position 464 to 581, the domain is characterized as Toprim.
+At position 44 to 171, the domain is characterized as PLAT.
+At position 174 to 862, the domain is characterized as Lipoxygenase.
+At position 238 to 269, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 286 to 315, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 577 to 606, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 610 to 639, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 150 to 404, the domain is characterized as ABC transporter 1.
+At position 859 to 1103, the domain is characterized as ABC transporter 2.
+At position 165 to 393, the domain is characterized as NR LBD.
+At position 1 to 369, the domain is characterized as Trm1 methyltransferase.
+At position 537 to 623, the domain is characterized as GED.
+At position 47 to 150, the domain is characterized as FHA.
+At position 199 to 472, the domain is characterized as Protein kinase.
+At position 11 to 128, the domain is characterized as MTTase N-terminal.
+At position 385 to 449, the domain is characterized as TRAM.
+At position 11 to 128, the domain is characterized as C-type lectin.
+At position 61 to 131, the domain is characterized as Ig-like V-type 1.
+At position 138 to 222, the domain is characterized as Ig-like C1-type.
+At position 235 to 328, the domain is characterized as Ig-like V-type 2.
+At position 37 to 432, the domain is characterized as Glutamine amidotransferase type-2.
+At position 497 to 573, the domain is characterized as Carrier 1.
+At position 1550 to 1625, the domain is characterized as Carrier 2.
+At position 1 to 107, the domain is characterized as Ras-associating.
+At position 197 to 271, the domain is characterized as RRM.
+At position 28 to 365, the domain is characterized as PPM-type phosphatase.
+At position 1 to 250, the domain is characterized as EAL.
+At position 117 to 321, the domain is characterized as TLC.
+At position 68 to 118, the domain is characterized as P-type.
+At position 30 to 123, the domain is characterized as LCCL.
+At position 167 to 352, the domain is characterized as VWFA 1.
+At position 369 to 539, the domain is characterized as VWFA 2.
+At position 199 to 451, the domain is characterized as Lon N-terminal.
+At position 891 to 1077, the domain is characterized as Lon proteolytic.
+At position 103 to 226, the domain is characterized as MPN.
+At position 50 to 102, the domain is characterized as bHLH.
+At position 4 to 122, the domain is characterized as PX.
+At position 59 to 91, the domain is characterized as ShKT 1.
+At position 107 to 143, the domain is characterized as ShKT 2.
+At position 149 to 183, the domain is characterized as ShKT 3.
+At position 115 to 354, the domain is characterized as ATP-grasp.
+At position 267 to 357, the domain is characterized as PpiC.
+At position 39 to 127, the domain is characterized as PPIase FKBP-type.
+At position 106 to 224, the domain is characterized as MRH.
+At position 36 to 155, the domain is characterized as SCP.
+At position 43 to 187, the domain is characterized as Nudix hydrolase.
+At position 74 to 348, the domain is characterized as PPM-type phosphatase.
+At position 250 to 423, the domain is characterized as tr-type G.
+At position 527 to 629, the domain is characterized as PDZ.
+At position 154 to 204, the domain is characterized as DHHC.
+At position 16 to 115, the domain is characterized as PilZ.
+At position 386 to 426, the domain is characterized as EGF-like 1.
+At position 430 to 667, the domain is characterized as Nidogen G2 beta-barrel.
+At position 668 to 709, the domain is characterized as EGF-like 2.
+At position 710 to 751, the domain is characterized as EGF-like 3; calcium-binding.
+At position 758 to 801, the domain is characterized as EGF-like 4.
+At position 802 to 840, the domain is characterized as EGF-like 5; calcium-binding.
+At position 846 to 919, the domain is characterized as Thyroglobulin type-1.
+At position 1208 to 1244, the domain is characterized as EGF-like 6.
+At position 342 to 578, the domain is characterized as PRORP.
+At position 229 to 299, the domain is characterized as HTH OST-type 2.
+At position 340 to 410, the domain is characterized as HTH OST-type 3.
+At position 496 to 554, the domain is characterized as Tudor 1.
+At position 686 to 743, the domain is characterized as Tudor 2.
+At position 142 to 194, the domain is characterized as HAMP.
+At position 202 to 414, the domain is characterized as Histidine kinase.
+At position 139 to 336, the domain is characterized as ATP-grasp.
+At position 337 to 608, the domain is characterized as Protein kinase.
+At position 118 to 150, the domain is characterized as EF-hand 4.
+At position 165 to 227, the domain is characterized as CBS 1.
+At position 260 to 324, the domain is characterized as CBS 2.
+At position 350 to 408, the domain is characterized as CBS 3.
+At position 432 to 487, the domain is characterized as CBS 4.
+At position 159 to 347, the domain is characterized as Helicase ATP-binding.
+At position 388 to 589, the domain is characterized as Helicase C-terminal.
+At position 646 to 961, the domain is characterized as SEC63.
+At position 8 to 82, the domain is characterized as S1-like.
+At position 9 to 54, the domain is characterized as SpoVT-AbrB 1.
+At position 163 to 214, the domain is characterized as LRRCT 1.
+At position 225 to 268, the domain is characterized as LRRNT.
+At position 350 to 402, the domain is characterized as LRRCT 2.
+At position 60 to 718, the domain is characterized as PFL.
+At position 725 to 846, the domain is characterized as Glycine radical.
+At position 123 to 300, the domain is characterized as Helicase ATP-binding.
+At position 333 to 476, the domain is characterized as Helicase C-terminal.
+At position 69 to 107, the domain is characterized as Chitin-binding type-1 2.
+At position 701 to 949, the domain is characterized as DDHD.
+At position 1735 to 1870, the domain is characterized as BEACH-type PH.
+At position 1907 to 2202, the domain is characterized as BEACH.
+At position 48 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 302, the domain is characterized as Ig-like C2-type 3.
+At position 330 to 383, the domain is characterized as Ig-like C2-type 4.
+At position 417 to 470, the domain is characterized as Ig-like C2-type 5.
+At position 148 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 241 to 326, the domain is characterized as Ig-like C2-type 2.
+At position 334 to 405, the domain is characterized as Ig-like C2-type 3.
+At position 8 to 80, the domain is characterized as Sm.
+At position 31 to 106, the domain is characterized as Inhibitor I9.
+At position 102 to 610, the domain is characterized as Peptidase S8.
+At position 446 to 505, the domain is characterized as SH3.
+At position 345 to 430, the domain is characterized as OCT.
+At position 33 to 241, the domain is characterized as AIG1-type G.
+At position 162 to 194, the domain is characterized as EF-hand 3.
+At position 230 to 403, the domain is characterized as PCI.
+At position 204 to 534, the domain is characterized as Kinesin motor.
+At position 155 to 205, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 11 to 94, the domain is characterized as HTH IS408-type.
+At position 140 to 335, the domain is characterized as Integrase catalytic.
+At position 154 to 193, the domain is characterized as Pentapeptide repeat 1.
+At position 199 to 238, the domain is characterized as Pentapeptide repeat 2.
+At position 434 to 562, the domain is characterized as Guanylate cyclase.
+At position 121 to 432, the domain is characterized as IF rod.
+At position 54 to 332, the domain is characterized as AB hydrolase-1.
+At position 1093 to 1358, the domain is characterized as Glutamine amidotransferase type-1.
+At position 249 to 494, the domain is characterized as ABC transporter 2.
+At position 16 to 257, the domain is characterized as NR LBD.
+At position 355 to 407, the domain is characterized as bHLH.
+At position 6 to 330, the domain is characterized as Asparaginase/glutaminase.
+At position 107 to 608, the domain is characterized as Peptidase S8.
+At position 190 to 225, the domain is characterized as EF-hand 1.
+At position 229 to 256, the domain is characterized as EF-hand 2.
+At position 140 to 231, the domain is characterized as PpiC.
+At position 73 to 313, the domain is characterized as AB hydrolase-1.
+At position 549 to 610, the domain is characterized as SAM.
+At position 651 to 726, the domain is characterized as Carrier.
+At position 140 to 249, the domain is characterized as C-type lectin.
+At position 21 to 56, the domain is characterized as CBM1.
+At position 81 to 396, the domain is characterized as GH10.
+At position 149 to 359, the domain is characterized as DOG1.
+At position 1 to 290, the domain is characterized as SPX.
+At position 550 to 744, the domain is characterized as EXS.
+At position 1 to 127, the domain is characterized as MGS-like.
+At position 18 to 246, the domain is characterized as ABC transporter.
+At position 179 to 223, the domain is characterized as EGF-like.
+At position 221 to 477, the domain is characterized as ZP.
+At position 12 to 309, the domain is characterized as tr-type G.
+At position 194 to 279, the domain is characterized as KH.
+At position 320 to 413, the domain is characterized as HD.
+At position 1 to 173, the domain is characterized as Velvet.
+At position 482 to 817, the domain is characterized as Protein kinase.
+At position 875 to 1005, the domain is characterized as Guanylate cyclase.
+At position 1 to 20, the domain is characterized as Chitin-binding type-1 1.
+At position 22 to 45, the domain is characterized as Chitin-binding type-1 2.
+At position 22 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 198, the domain is characterized as Ig-like C2-type 2.
+At position 213 to 305, the domain is characterized as Ig-like C2-type 3.
+At position 316 to 407, the domain is characterized as Ig-like C2-type 4.
+At position 408 to 513, the domain is characterized as Ig-like C2-type 5.
+At position 584 to 917, the domain is characterized as Protein kinase.
+At position 64 to 401, the domain is characterized as Kinesin motor.
+At position 95 to 166, the domain is characterized as PRC barrel.
+At position 187 to 368, the domain is characterized as Histidine kinase.
+At position 402 to 569, the domain is characterized as tr-type G.
+At position 4 to 141, the domain is characterized as SET.
+At position 72 to 179, the domain is characterized as MTTase N-terminal.
+At position 84 to 118, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 955 to 987, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 989 to 1019, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 189 to 381, the domain is characterized as GMPS ATP-PPase.
+At position 36 to 198, the domain is characterized as EngB-type G.
+At position 24 to 98, the domain is characterized as BTB.
+At position 224 to 523, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 138 to 208, the domain is characterized as BTB.
+At position 43 to 104, the domain is characterized as Sushi 1.
+At position 105 to 168, the domain is characterized as Sushi 2.
+At position 58 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 931 to 1071, the domain is characterized as MGS-like.
+At position 25 to 98, the domain is characterized as H15.
+At position 780 to 914, the domain is characterized as C1q.
+At position 44 to 188, the domain is characterized as Tyrosine-protein phosphatase.
+At position 45 to 74, the domain is characterized as HhH.
+At position 98 to 219, the domain is characterized as PX.
+At position 243 to 446, the domain is characterized as BAR.
+At position 241 to 362, the domain is characterized as C2 2.
+At position 405 to 536, the domain is characterized as C2 3.
+At position 952 to 1077, the domain is characterized as C2 4.
+At position 1124 to 1250, the domain is characterized as C2 5.
+At position 1470 to 1588, the domain is characterized as C2 6.
+At position 1711 to 1860, the domain is characterized as C2 7.
+At position 18 to 198, the domain is characterized as Guanylate kinase-like.
+At position 419 to 455, the domain is characterized as DFDF.
+At position 602 to 686, the domain is characterized as BRCT.
+At position 205 to 270, the domain is characterized as HTH OST-type 2.
+At position 366 to 434, the domain is characterized as HTH OST-type 3.
+At position 519 to 576, the domain is characterized as Tudor 1.
+At position 708 to 765, the domain is characterized as Tudor 2.
+At position 96 to 192, the domain is characterized as PH 1.
+At position 227 to 324, the domain is characterized as PH 2.
+At position 8 to 104, the domain is characterized as Rieske.
+At position 56 to 238, the domain is characterized as FAD-binding PCMH-type.
+At position 2 to 180, the domain is characterized as Guanylate kinase-like.
+At position 190 to 253, the domain is characterized as LRRCT.
+At position 312 to 399, the domain is characterized as Fibronectin type-III.
+At position 4 to 297, the domain is characterized as Protein kinase.
+At position 5 to 220, the domain is characterized as tr-type G.
+At position 106 to 260, the domain is characterized as NHR 1.
+At position 368 to 523, the domain is characterized as NHR 2.
+At position 75 to 326, the domain is characterized as AB hydrolase-1.
+At position 160 to 372, the domain is characterized as Radical SAM core.
+At position 111 to 161, the domain is characterized as DHHC.
+At position 230 to 289, the domain is characterized as OVATE.
+At position 253 to 521, the domain is characterized as Protein kinase.
+At position 522 to 593, the domain is characterized as AGC-kinase C-terminal.
+At position 16 to 52, the domain is characterized as S1 motif.
+At position 96 to 253, the domain is characterized as PPIase cyclophilin-type.
+At position 268 to 520, the domain is characterized as EAL.
+At position 240 to 284, the domain is characterized as GRAM 1.
+At position 289 to 385, the domain is characterized as PH.
+At position 765 to 870, the domain is characterized as GRAM 2.
+At position 184 to 305, the domain is characterized as C2 2.
+At position 345 to 467, the domain is characterized as C2 3.
+At position 292 to 494, the domain is characterized as Pentraxin (PTX).
+At position 297 to 729, the domain is characterized as Peptidase S8.
+At position 1031 to 1314, the domain is characterized as ABC transmembrane type-1.
+At position 1450 to 1687, the domain is characterized as ABC transporter.
+At position 17 to 50, the domain is characterized as bZIP.
+At position 195 to 464, the domain is characterized as NR LBD.
+At position 91 to 134, the domain is characterized as LysM.
+At position 206 to 261, the domain is characterized as GRAM.
+At position 678 to 839, the domain is characterized as TLDc.
+At position 491 to 610, the domain is characterized as Ricin B-type lectin.
+At position 10 to 55, the domain is characterized as G-patch.
+At position 46 to 142, the domain is characterized as RRM.
+At position 1 to 305, the domain is characterized as 5'-3' exonuclease.
+At position 306 to 501, the domain is characterized as 3'-5' exonuclease.
+At position 13 to 83, the domain is characterized as Sm.
+At position 212 to 404, the domain is characterized as ATP-grasp 1.
+At position 748 to 946, the domain is characterized as ATP-grasp 2.
+At position 1014 to 1160, the domain is characterized as MGS-like.
+At position 210 to 337, the domain is characterized as SET.
+At position 376 to 547, the domain is characterized as tr-type G.
+At position 131 to 180, the domain is characterized as bHLH.
+At position 125 to 391, the domain is characterized as Protein kinase.
+At position 21 to 166, the domain is characterized as N-acetyltransferase.
+At position 105 to 340, the domain is characterized as Radical SAM core.
+At position 89 to 257, the domain is characterized as GST C-terminal.
+At position 35 to 269, the domain is characterized as Cupin type-1 1.
+At position 32 to 152, the domain is characterized as C-type lectin.
+At position 182 to 349, the domain is characterized as JmjC.
+At position 115 to 186, the domain is characterized as PRC barrel.
+At position 143 to 330, the domain is characterized as Helicase ATP-binding.
+At position 355 to 505, the domain is characterized as Helicase C-terminal.
+At position 21 to 148, the domain is characterized as RNase III.
+At position 175 to 242, the domain is characterized as DRBM.
+At position 49 to 462, the domain is characterized as USP.
+At position 6 to 75, the domain is characterized as Histone-fold.
+At position 27 to 272, the domain is characterized as ABC transporter.
+At position 70 to 305, the domain is characterized as Radical SAM core.
+At position 213 to 375, the domain is characterized as TrmE-type G.
+At position 108 to 287, the domain is characterized as Helicase ATP-binding.
+At position 323 to 465, the domain is characterized as Helicase C-terminal.
+At position 68 to 164, the domain is characterized as Ig-like C2-type 1.
+At position 262 to 346, the domain is characterized as Ig-like C2-type 3.
+At position 351 to 446, the domain is characterized as Ig-like C2-type 4.
+At position 455 to 541, the domain is characterized as Ig-like C2-type 5.
+At position 563 to 657, the domain is characterized as Fibronectin type-III 1.
+At position 676 to 773, the domain is characterized as Fibronectin type-III 2.
+At position 778 to 874, the domain is characterized as Fibronectin type-III 3.
+At position 486 to 1092, the domain is characterized as cDENN FNIP1/2-type.
+At position 1102 to 1157, the domain is characterized as dDENN FNIP1/2-type.
+At position 459 to 522, the domain is characterized as bZIP.
+At position 20 to 88, the domain is characterized as HTH gntR-type.
+At position 74 to 168, the domain is characterized as CS.
+At position 169 to 229, the domain is characterized as SGS.
+At position 158 to 259, the domain is characterized as Fe2OG dioxygenase.
+At position 112 to 360, the domain is characterized as Lon N-terminal.
+At position 749 to 939, the domain is characterized as Lon proteolytic.
+At position 27 to 93, the domain is characterized as PQ-loop 1.
+At position 150 to 205, the domain is characterized as PQ-loop 2.
+At position 383 to 500, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 501 to 604, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 662 to 741, the domain is characterized as POLO box.
+At position 12 to 203, the domain is characterized as EngB-type G.
+At position 178 to 451, the domain is characterized as NR LBD.
+At position 90 to 331, the domain is characterized as Dynamin-type G.
+At position 6 to 62, the domain is characterized as F-box.
+At position 391 to 423, the domain is characterized as FBD.
+At position 108 to 261, the domain is characterized as PINIT.
+At position 252 to 309, the domain is characterized as PQ-loop.
+At position 8 to 70, the domain is characterized as TGS.
+At position 46 to 190, the domain is characterized as Thioredoxin.
+At position 24 to 242, the domain is characterized as Radical SAM core.
+At position 37 to 330, the domain is characterized as AB hydrolase-1.
+At position 38 to 147, the domain is characterized as Cadherin 1.
+At position 324 to 421, the domain is characterized as ERCC4.
+At position 163 to 334, the domain is characterized as OBG-type G.
+At position 12 to 178, the domain is characterized as 3'-5' exonuclease.
+At position 217 to 298, the domain is characterized as HRDC.
+At position 916 to 1047, the domain is characterized as MHD1.
+At position 7 to 189, the domain is characterized as YrdC-like.
+At position 25 to 228, the domain is characterized as Velvet.
+At position 162 to 248, the domain is characterized as Ras-associating.
+At position 292 to 401, the domain is characterized as PH.
+At position 339 to 377, the domain is characterized as CBM10.
+At position 7 to 88, the domain is characterized as Disintegrin.
+At position 126 to 305, the domain is characterized as Helicase ATP-binding.
+At position 337 to 484, the domain is characterized as Helicase C-terminal.
+At position 63 to 126, the domain is characterized as EamA 1.
+At position 169 to 298, the domain is characterized as EamA 2.
+At position 57 to 237, the domain is characterized as tr-type G.
+At position 1 to 72, the domain is characterized as Carrier.
+At position 447 to 619, the domain is characterized as tr-type G.
+At position 84 to 159, the domain is characterized as Ubiquitin-like.
+At position 86 to 304, the domain is characterized as Radical SAM core.
+At position 35 to 72, the domain is characterized as VM.
+At position 278 to 426, the domain is characterized as SIS 1.
+At position 4 to 77, the domain is characterized as 4Fe-4S Wbl-type.
+At position 53 to 235, the domain is characterized as IRG-type G.
+At position 53 to 389, the domain is characterized as YjeF C-terminal.
+At position 580 to 914, the domain is characterized as Protein kinase.
+At position 113 to 248, the domain is characterized as Fatty acid hydroxylase.
+At position 23 to 335, the domain is characterized as PNPLA.
+At position 35 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 99 to 141, the domain is characterized as CAP-Gly 1.
+At position 239 to 281, the domain is characterized as CAP-Gly 2.
+At position 23 to 293, the domain is characterized as GH26.
+At position 520 to 811, the domain is characterized as Protein kinase.
+At position 404 to 675, the domain is characterized as Protein kinase.
+At position 119 to 711, the domain is characterized as Lipoxygenase.
+At position 43 to 126, the domain is characterized as RRM 1.
+At position 428 to 506, the domain is characterized as RRM 3.
+At position 86 to 392, the domain is characterized as Peptidase A1.
+At position 68 to 306, the domain is characterized as Lon N-terminal.
+At position 305 to 413, the domain is characterized as CULT.
+At position 16 to 85, the domain is characterized as Chitin-binding type R&R.
+At position 12 to 162, the domain is characterized as NAC.
+At position 581 to 641, the domain is characterized as KH.
+At position 672 to 731, the domain is characterized as S1 motif.
+At position 406 to 574, the domain is characterized as Helicase ATP-binding.
+At position 757 to 912, the domain is characterized as Helicase C-terminal.
+At position 35 to 90, the domain is characterized as HTH cro/C1-type.
+At position 249 to 446, the domain is characterized as PCI.
+At position 616 to 711, the domain is characterized as S1 motif.
+At position 12 to 47, the domain is characterized as EF-hand 1; degenerate.
+At position 123 to 364, the domain is characterized as AB hydrolase-1.
+At position 130 to 194, the domain is characterized as COMM.
+At position 27 to 198, the domain is characterized as BPL/LPL catalytic.
+At position 22 to 76, the domain is characterized as SMP 1.
+At position 138 to 194, the domain is characterized as SMP 2.
+At position 203 to 261, the domain is characterized as SMP 3.
+At position 543 to 848, the domain is characterized as Protein kinase.
+At position 918 to 1048, the domain is characterized as Guanylate cyclase.
+At position 68 to 192, the domain is characterized as PH.
+At position 100 to 324, the domain is characterized as Radical SAM core.
+At position 97 to 235, the domain is characterized as Nudix hydrolase.
+At position 295 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 130 to 388, the domain is characterized as NR LBD.
+At position 287 to 379, the domain is characterized as SH2 2.
+At position 484 to 740, the domain is characterized as Protein kinase.
+At position 243 to 347, the domain is characterized as HD.
+At position 22 to 301, the domain is characterized as ABC transmembrane type-1.
+At position 343 to 566, the domain is characterized as ABC transporter.
+At position 67 to 150, the domain is characterized as UBX.
+At position 7 to 90, the domain is characterized as Core-binding (CB).
+At position 33 to 149, the domain is characterized as HSR.
+At position 293 to 374, the domain is characterized as SAND.
+At position 484 to 554, the domain is characterized as Bromo.
+At position 34 to 118, the domain is characterized as Ig-like.
+At position 107 to 136, the domain is characterized as IQ.
+At position 410 to 477, the domain is characterized as HMA.
+At position 383 to 553, the domain is characterized as tr-type G.
+At position 570 to 737, the domain is characterized as tr-type G.
+At position 8 to 82, the domain is characterized as KRAB.
+At position 240 to 406, the domain is characterized as Helicase ATP-binding.
+At position 490 to 709, the domain is characterized as Helicase C-terminal.
+At position 373 to 804, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1291 to 1610, the domain is characterized as PKS/mFAS DH.
+At position 1666 to 1740, the domain is characterized as Carrier.
+At position 149 to 235, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 353, the domain is characterized as Ig-like C2-type 2.
+At position 406 to 559, the domain is characterized as TIR.
+At position 5 to 233, the domain is characterized as ATP-grasp.
+At position 50 to 232, the domain is characterized as Rab-GAP TBC.
+At position 36 to 159, the domain is characterized as RRM 1.
+At position 192 to 271, the domain is characterized as RRM 2.
+At position 360 to 432, the domain is characterized as RRM 3.
+At position 8 to 292, the domain is characterized as Deacetylase sirtuin-type.
+At position 195 to 253, the domain is characterized as TRAM.
+At position 22 to 162, the domain is characterized as Rhodanese 1.
+At position 202 to 320, the domain is characterized as Rhodanese 2.
+At position 44 to 204, the domain is characterized as Tyrosine-protein phosphatase.
+At position 572 to 670, the domain is characterized as PilZ.
+At position 375 to 432, the domain is characterized as HTH myb-type.
+At position 5 to 134, the domain is characterized as MPN.
+At position 192 to 324, the domain is characterized as TIR.
+At position 3 to 185, the domain is characterized as YrdC-like.
+At position 252 to 446, the domain is characterized as GATase cobBQ-type.
+At position 2 to 49, the domain is characterized as RsgI N-terminal anti-sigma.
+At position 402 to 701, the domain is characterized as GH10.
+At position 2 to 68, the domain is characterized as BON 1.
+At position 78 to 146, the domain is characterized as BON 2.
+At position 231 to 957, the domain is characterized as USP.
+At position 206 to 367, the domain is characterized as CP-type G.
+At position 71 to 254, the domain is characterized as ABC transmembrane type-1 1.
+At position 327 to 517, the domain is characterized as ABC transmembrane type-1 2.
+At position 486 to 658, the domain is characterized as SSD.
+At position 12 to 126, the domain is characterized as Response regulatory.
+At position 152 to 381, the domain is characterized as Sigma-54 factor interaction.
+At position 395 to 522, the domain is characterized as PINc.
+At position 72 to 187, the domain is characterized as Response regulatory.
+At position 214 to 425, the domain is characterized as HD-GYP.
+At position 7 to 80, the domain is characterized as RRM.
+At position 586 to 930, the domain is characterized as PDEase.
+At position 19 to 108, the domain is characterized as Ig-like.
+At position 351 to 609, the domain is characterized as Protein kinase.
+At position 207 to 288, the domain is characterized as Peptidase A2.
+At position 927 to 970, the domain is characterized as UBA.
+At position 129 to 434, the domain is characterized as PPM-type phosphatase.
+At position 147 to 256, the domain is characterized as RRM.
+At position 37 to 323, the domain is characterized as Protein kinase.
+At position 272 to 629, the domain is characterized as TTL.
+At position 49 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 109 to 141, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 78 to 354, the domain is characterized as Protein kinase.
+At position 6 to 328, the domain is characterized as DhaK.
+At position 331 to 417, the domain is characterized as PPIase FKBP-type.
+At position 376 to 649, the domain is characterized as Protein kinase.
+At position 650 to 721, the domain is characterized as AGC-kinase C-terminal.
+At position 969 to 1057, the domain is characterized as PDZ.
+At position 740 to 795, the domain is characterized as Sushi.
+At position 796 to 839, the domain is characterized as EGF-like; calcium-binding.
+At position 6 to 101, the domain is characterized as Rieske.
+At position 22 to 196, the domain is characterized as FAD-binding PCMH-type.
+At position 33 to 317, the domain is characterized as Protein kinase.
+At position 94 to 123, the domain is characterized as EGF-like.
+At position 160 to 239, the domain is characterized as SPOR.
+At position 134 to 363, the domain is characterized as Radical SAM core.
+At position 366 to 425, the domain is characterized as TRAM.
+At position 384 to 564, the domain is characterized as Reticulon.
+At position 108 to 290, the domain is characterized as ATP-grasp.
+At position 13 to 141, the domain is characterized as EamA 1.
+At position 152 to 289, the domain is characterized as EamA 2.
+At position 15 to 260, the domain is characterized as Protein kinase.
+At position 93 to 218, the domain is characterized as GST C-terminal.
+At position 30 to 216, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 208, the domain is characterized as Phosphatase tensin-type.
+At position 214 to 352, the domain is characterized as C2 tensin-type.
+At position 827 to 1226, the domain is characterized as FH2.
+At position 15 to 47, the domain is characterized as LisH.
+At position 1229 to 1463, the domain is characterized as Fibrillar collagen NC1.
+At position 143 to 221, the domain is characterized as Carrier.
+At position 1011 to 1531, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 251 to 338, the domain is characterized as PKD.
+At position 261 to 315, the domain is characterized as TSP type-1 1.
+At position 354 to 407, the domain is characterized as TSP type-1 2.
+At position 409 to 462, the domain is characterized as TSP type-1 3.
+At position 467 to 520, the domain is characterized as TSP type-1 4.
+At position 522 to 575, the domain is characterized as TSP type-1 5.
+At position 881 to 938, the domain is characterized as GPS.
+At position 224 to 358, the domain is characterized as PADR1 zinc-binding.
+At position 539 to 635, the domain is characterized as WGR.
+At position 659 to 776, the domain is characterized as PARP alpha-helical.
+At position 785 to 1011, the domain is characterized as PARP catalytic.
+At position 28 to 85, the domain is characterized as bHLH.
+At position 97 to 130, the domain is characterized as Orange.
+At position 27 to 48, the domain is characterized as EF-hand 1.
+At position 632 to 797, the domain is characterized as SSD.
+At position 85 to 357, the domain is characterized as ABC transporter 1.
+At position 434 to 647, the domain is characterized as ABC transmembrane type-2 1.
+At position 749 to 1001, the domain is characterized as ABC transporter 2.
+At position 1074 to 1288, the domain is characterized as ABC transmembrane type-2 2.
+At position 29 to 108, the domain is characterized as BTB.
+At position 214 to 465, the domain is characterized as NPH3.
+At position 58 to 477, the domain is characterized as Kinesin motor.
+At position 7 to 115, the domain is characterized as HIT.
+At position 299 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 83, the domain is characterized as GIY-YIG.
+At position 587 to 682, the domain is characterized as Cadherin 6.
+At position 194 to 278, the domain is characterized as TonB C-terminal.
+At position 1 to 380, the domain is characterized as FH2.
+At position 42 to 82, the domain is characterized as Chaplin 1.
+At position 120 to 160, the domain is characterized as Chaplin 2.
+At position 12 to 231, the domain is characterized as Glutamine amidotransferase type-2.
+At position 6 to 243, the domain is characterized as ABC transporter.
+At position 19 to 324, the domain is characterized as Asparaginase/glutaminase.
+At position 1 to 74, the domain is characterized as sHSP.
+At position 380 to 441, the domain is characterized as SH3 3.
+At position 23 to 124, the domain is characterized as Ig-like V-type.
+At position 128 to 226, the domain is characterized as Ig-like C2-type 1.
+At position 231 to 313, the domain is characterized as Ig-like C2-type 2.
+At position 355 to 732, the domain is characterized as FH2.
+At position 59 to 130, the domain is characterized as POTRA 1.
+At position 131 to 209, the domain is characterized as POTRA 2.
+At position 212 to 298, the domain is characterized as POTRA 3.
+At position 301 to 383, the domain is characterized as POTRA 4.
+At position 386 to 459, the domain is characterized as POTRA 5.
+At position 376 to 443, the domain is characterized as TRAM.
+At position 97 to 769, the domain is characterized as Peptidase M13.
+At position 202 to 246, the domain is characterized as Integrase catalytic.
+At position 149 to 334, the domain is characterized as PID.
+At position 499 to 590, the domain is characterized as SH2.
+At position 129 to 246, the domain is characterized as PilZ.
+At position 471 to 676, the domain is characterized as Helicase ATP-binding.
+At position 943 to 1114, the domain is characterized as Helicase C-terminal.
+At position 650 to 796, the domain is characterized as MOSC.
+At position 918 to 1056, the domain is characterized as MGS-like.
+At position 73 to 133, the domain is characterized as LIM zinc-binding 1.
+At position 134 to 196, the domain is characterized as LIM zinc-binding 2.
+At position 1 to 94, the domain is characterized as Core-binding (CB).
+At position 115 to 292, the domain is characterized as Tyr recombinase.
+At position 37 to 123, the domain is characterized as PAN.
+At position 128 to 206, the domain is characterized as Kringle 1.
+At position 211 to 288, the domain is characterized as Kringle 2.
+At position 305 to 383, the domain is characterized as Kringle 3.
+At position 495 to 723, the domain is characterized as Peptidase S1.
+At position 183 to 218, the domain is characterized as EF-hand 1.
+At position 249 to 284, the domain is characterized as EF-hand 2.
+At position 23 to 94, the domain is characterized as H15.
+At position 17 to 67, the domain is characterized as F-box.
+At position 376 to 428, the domain is characterized as FBD.
+At position 355 to 407, the domain is characterized as TSP type-1.
+At position 45 to 323, the domain is characterized as Pyruvate carboxyltransferase.
+At position 110 to 242, the domain is characterized as Nudix hydrolase.
+At position 487 to 648, the domain is characterized as VPS9.
+At position 101 to 302, the domain is characterized as AIG1-type G.
+At position 12 to 129, the domain is characterized as Thioredoxin.
+At position 46 to 152, the domain is characterized as Cyclin N-terminal.
+At position 1 to 100, the domain is characterized as C2 1.
+At position 145 to 265, the domain is characterized as C2 2.
+At position 307 to 424, the domain is characterized as C2 3.
+At position 1055 to 1186, the domain is characterized as C2 4.
+At position 1225 to 1345, the domain is characterized as C2 5.
+At position 30 to 131, the domain is characterized as Chorein N-terminal.
+At position 1 to 195, the domain is characterized as ABC transporter.
+At position 641 to 809, the domain is characterized as DDE-1.
+At position 168 to 251, the domain is characterized as PNT.
+At position 6 to 164, the domain is characterized as DHFR.
+At position 45 to 170, the domain is characterized as CBM-cenC.
+At position 388 to 543, the domain is characterized as Exonuclease.
+At position 111 to 334, the domain is characterized as Radical SAM core.
+At position 68 to 210, the domain is characterized as GAF.
+At position 256 to 484, the domain is characterized as Sigma-54 factor interaction.
+At position 190 to 240, the domain is characterized as DHHC.
+At position 592 to 671, the domain is characterized as BRCT.
+At position 593 to 672, the domain is characterized as KIX.
+At position 881 to 953, the domain is characterized as Bromo.
+At position 1112 to 1492, the domain is characterized as CBP/p300-type HAT.
+At position 37 to 103, the domain is characterized as Histone-fold.
+At position 362 to 559, the domain is characterized as MIF4G.
+At position 654 to 770, the domain is characterized as MI.
+At position 8 to 155, the domain is characterized as UBC core.
+At position 249 to 417, the domain is characterized as GATase cobBQ-type.
+At position 108 to 170, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 249 to 487, the domain is characterized as PABS.
+At position 143 to 423, the domain is characterized as Protein kinase.
+At position 30 to 123, the domain is characterized as Ig-like.
+At position 1058 to 1121, the domain is characterized as Pre-SET.
+At position 1124 to 1241, the domain is characterized as SET.
+At position 322 to 454, the domain is characterized as ZU5 1.
+At position 455 to 596, the domain is characterized as ZU5 2.
+At position 788 to 873, the domain is characterized as Death.
+At position 309 to 439, the domain is characterized as Ricin B-type lectin 1.
+At position 443 to 566, the domain is characterized as Ricin B-type lectin 2.
+At position 32 to 136, the domain is characterized as Calponin-homology (CH) 1.
+At position 145 to 251, the domain is characterized as Calponin-homology (CH) 2.
+At position 747 to 782, the domain is characterized as EF-hand 1.
+At position 788 to 823, the domain is characterized as EF-hand 2.
+At position 6 to 277, the domain is characterized as Pyruvate carboxyltransferase.
+At position 22 to 115, the domain is characterized as Cystatin.
+At position 30 to 242, the domain is characterized as MIF4G.
+At position 6 to 121, the domain is characterized as VOC 1.
+At position 146 to 267, the domain is characterized as VOC 2.
+At position 416 to 535, the domain is characterized as SMC hinge.
+At position 127 to 304, the domain is characterized as Prephenate dehydratase.
+At position 320 to 411, the domain is characterized as ACT.
+At position 247 to 341, the domain is characterized as PDZ.
+At position 1413 to 1476, the domain is characterized as SAM.
+At position 574 to 648, the domain is characterized as RRM.
+At position 346 to 396, the domain is characterized as GPS.
+At position 119 to 170, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 242 to 438, the domain is characterized as Laminin G-like 1.
+At position 439 to 477, the domain is characterized as EGF-like 1.
+At position 481 to 664, the domain is characterized as Laminin G-like 2.
+At position 660 to 839, the domain is characterized as Laminin G-like 3.
+At position 841 to 879, the domain is characterized as EGF-like 2.
+At position 1087 to 1259, the domain is characterized as Laminin G-like 4.
+At position 1260 to 1297, the domain is characterized as EGF-like 3.
+At position 1316 to 1526, the domain is characterized as Laminin G-like 5.
+At position 1527 to 1565, the domain is characterized as EGF-like 4.
+At position 1569 to 1765, the domain is characterized as Laminin G-like 6.
+At position 127 to 192, the domain is characterized as HTH luxR-type.
+At position 198 to 299, the domain is characterized as tRNA-binding.
+At position 414 to 447, the domain is characterized as WW 3.
+At position 477 to 593, the domain is characterized as PH.
+At position 677 to 866, the domain is characterized as Rho-GAP.
+At position 53 to 172, the domain is characterized as RGS.
+At position 187 to 446, the domain is characterized as Protein kinase.
+At position 447 to 512, the domain is characterized as AGC-kinase C-terminal.
+At position 8 to 96, the domain is characterized as RH1.
+At position 282 to 401, the domain is characterized as RH2.
+At position 80 to 166, the domain is characterized as Cytochrome c.
+At position 346 to 621, the domain is characterized as Protein kinase.
+At position 987 to 1261, the domain is characterized as Protein kinase.
+At position 1264 to 1431, the domain is characterized as KEN.
+At position 139 to 439, the domain is characterized as Peptidase S8.
+At position 612 to 744, the domain is characterized as B12-binding.
+At position 38 to 153, the domain is characterized as Ig-like V-type.
+At position 259 to 357, the domain is characterized as Link 2.
+At position 1008 to 1044, the domain is characterized as EGF-like 1.
+At position 1046 to 1082, the domain is characterized as EGF-like 2; calcium-binding.
+At position 1084 to 1213, the domain is characterized as C-type lectin.
+At position 1213 to 1273, the domain is characterized as Sushi.
+At position 102 to 179, the domain is characterized as PRC barrel.
+At position 253 to 369, the domain is characterized as C2.
+At position 13 to 235, the domain is characterized as ABC transporter.
+At position 114 to 404, the domain is characterized as ABC transmembrane type-1.
+At position 439 to 675, the domain is characterized as ABC transporter.
+At position 26 to 111, the domain is characterized as UPAR/Ly6.
+At position 1 to 113, the domain is characterized as C2 1.
+At position 122 to 244, the domain is characterized as C2 2.
+At position 284 to 504, the domain is characterized as VWFA.
+At position 61 to 171, the domain is characterized as Thioredoxin.
+At position 204 to 376, the domain is characterized as PCI.
+At position 173 to 250, the domain is characterized as TFIIS N-terminal.
+At position 47 to 265, the domain is characterized as Ch-type lysozyme.
+At position 390 to 611, the domain is characterized as Histidine kinase.
+At position 629 to 742, the domain is characterized as Response regulatory.
+At position 355 to 399, the domain is characterized as LEM.
+At position 448 to 566, the domain is characterized as GIY-YIG.
+At position 67 to 353, the domain is characterized as Protein kinase.
+At position 8 to 280, the domain is characterized as YjeF C-terminal.
+At position 322 to 605, the domain is characterized as ABC transmembrane type-1 1.
+At position 637 to 861, the domain is characterized as ABC transporter 1.
+At position 979 to 1264, the domain is characterized as ABC transmembrane type-1 2.
+At position 1300 to 1534, the domain is characterized as ABC transporter 2.
+At position 80 to 191, the domain is characterized as DUF1279.
+At position 43 to 159, the domain is characterized as CUB 1.
+At position 211 to 250, the domain is characterized as LDL-receptor class A 2.
+At position 254 to 365, the domain is characterized as CUB 2.
+At position 415 to 453, the domain is characterized as LDL-receptor class A 3.
+At position 454 to 490, the domain is characterized as LDL-receptor class A 4.
+At position 573 to 846, the domain is characterized as Protein kinase.
+At position 16 to 261, the domain is characterized as ABC transporter.
+At position 311 to 521, the domain is characterized as ABC transmembrane type-2.
+At position 42 to 406, the domain is characterized as GH10.
+At position 32 to 152, the domain is characterized as FZ.
+At position 169 to 292, the domain is characterized as NTR.
+At position 256 to 494, the domain is characterized as START.
+At position 6 to 77, the domain is characterized as Ubiquitin-like.
+At position 136 to 296, the domain is characterized as FCP1 homology.
+At position 52 to 86, the domain is characterized as EF-hand 1.
+At position 276 to 304, the domain is characterized as MIT.
+At position 343 to 444, the domain is characterized as Protein kinase 1.
+At position 789 to 1046, the domain is characterized as Protein kinase 2.
+At position 58 to 165, the domain is characterized as Ig-like V-type.
+At position 76 to 186, the domain is characterized as Expansin-like EG45.
+At position 196 to 275, the domain is characterized as Expansin-like CBD.
+At position 374 to 496, the domain is characterized as GGDEF.
+At position 1084 to 1135, the domain is characterized as GRIP.
+At position 58 to 111, the domain is characterized as HAMP.
+At position 130 to 366, the domain is characterized as Methyl-accepting transducer.
+At position 1 to 233, the domain is characterized as RMT2.
+At position 111 to 170, the domain is characterized as SH3 2.
+At position 195 to 257, the domain is characterized as SH3 3.
+At position 285 to 380, the domain is characterized as SH2.
+At position 442 to 549, the domain is characterized as SH2.
+At position 1039 to 1202, the domain is characterized as PA14.
+At position 3 to 62, the domain is characterized as LIM zinc-binding 1.
+At position 63 to 120, the domain is characterized as LIM zinc-binding 2.
+At position 702 to 959, the domain is characterized as Protein kinase.
+At position 1 to 126, the domain is characterized as SAM-dependent MTase C5-type.
+At position 39 to 164, the domain is characterized as Glutamine amidotransferase type-1.
+At position 146 to 189, the domain is characterized as UBA 1.
+At position 242 to 285, the domain is characterized as STI1.
+At position 325 to 365, the domain is characterized as UBA 2.
+At position 17 to 51, the domain is characterized as LRRNT.
+At position 85 to 137, the domain is characterized as LRRCT.
+At position 94 to 172, the domain is characterized as S1 motif.
+At position 182 to 237, the domain is characterized as KH.
+At position 38 to 386, the domain is characterized as Protein kinase.
+At position 100 to 353, the domain is characterized as ABC transporter 1.
+At position 473 to 698, the domain is characterized as ABC transmembrane type-2 1.
+At position 783 to 1035, the domain is characterized as ABC transporter 2.
+At position 1121 to 1388, the domain is characterized as ABC transmembrane type-2 2.
+At position 134 to 377, the domain is characterized as Radical SAM core.
+At position 194 to 371, the domain is characterized as Hflx-type G.
+At position 737 to 1039, the domain is characterized as Autotransporter.
+At position 164 to 438, the domain is characterized as CP-type G.
+At position 97 to 159, the domain is characterized as S4 RNA-binding.
+At position 335 to 374, the domain is characterized as CBM10 1.
+At position 383 to 422, the domain is characterized as CBM10 2.
+At position 461 to 661, the domain is characterized as GH11.
+At position 9 to 267, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 180, the domain is characterized as DCUN1.
+At position 459 to 631, the domain is characterized as tr-type G.
+At position 1001 to 1071, the domain is characterized as Bromo.
+At position 159 to 262, the domain is characterized as Fibronectin type-III.
+At position 138 to 232, the domain is characterized as BRICHOS.
+At position 3 to 97, the domain is characterized as ATP-cone.
+At position 85 to 194, the domain is characterized as C-type lectin.
+At position 419 to 659, the domain is characterized as ABC transporter.
+At position 24 to 664, the domain is characterized as Vitellogenin.
+At position 1536 to 1714, the domain is characterized as VWFD.
+At position 97 to 771, the domain is characterized as Myosin motor.
+At position 428 to 465, the domain is characterized as EGF-like.
+At position 521 to 706, the domain is characterized as VWFA.
+At position 11 to 238, the domain is characterized as ATP-grasp.
+At position 476 to 601, the domain is characterized as DBINO.
+At position 718 to 890, the domain is characterized as Helicase ATP-binding.
+At position 1303 to 1467, the domain is characterized as Helicase C-terminal.
+At position 41 to 224, the domain is characterized as BPL/LPL catalytic.
+At position 20 to 343, the domain is characterized as F5/8 type A 1.
+At position 207 to 343, the domain is characterized as Plastocyanin-like 2.
+At position 393 to 724, the domain is characterized as F5/8 type A 2.
+At position 393 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 577 to 724, the domain is characterized as Plastocyanin-like 4.
+At position 1705 to 2032, the domain is characterized as F5/8 type A 3.
+At position 1705 to 1869, the domain is characterized as Plastocyanin-like 5.
+At position 1879 to 2032, the domain is characterized as Plastocyanin-like 6.
+At position 2032 to 2180, the domain is characterized as F5/8 type C 1.
+At position 2185 to 2337, the domain is characterized as F5/8 type C 2.
+At position 639 to 699, the domain is characterized as Tudor.
+At position 162 to 211, the domain is characterized as KH.
+At position 341 to 620, the domain is characterized as Protein kinase.
+At position 218 to 276, the domain is characterized as Collagen-like.
+At position 9 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 238 to 423, the domain is characterized as FAD-binding PCMH-type.
+At position 433 to 718, the domain is characterized as Protein kinase.
+At position 227 to 314, the domain is characterized as Ig-like C2-type.
+At position 197 to 244, the domain is characterized as F-box.
+At position 12 to 93, the domain is characterized as RRM 1.
+At position 100 to 180, the domain is characterized as RRM 2.
+At position 330 to 408, the domain is characterized as RRM 3.
+At position 174 to 400, the domain is characterized as NR LBD.
+At position 68 to 316, the domain is characterized as Protein kinase.
+At position 10 to 72, the domain is characterized as Ubiquitin-like.
+At position 11 to 149, the domain is characterized as DAC.
+At position 746 to 860, the domain is characterized as GAE.
+At position 669 to 950, the domain is characterized as Protein kinase.
+At position 91 to 309, the domain is characterized as Radical SAM core.
+At position 51 to 172, the domain is characterized as Thioredoxin.
+At position 212 to 300, the domain is characterized as Ig-like C2-type 3.
+At position 307 to 412, the domain is characterized as Ig-like C2-type 4.
+At position 415 to 500, the domain is characterized as Ig-like C2-type 5.
+At position 508 to 607, the domain is characterized as Fibronectin type-III 1.
+At position 609 to 704, the domain is characterized as Fibronectin type-III 2.
+At position 44 to 79, the domain is characterized as EF-hand 1.
+At position 8 to 370, the domain is characterized as Kinesin motor.
+At position 608 to 718, the domain is characterized as tRNA-binding.
+At position 12 to 130, the domain is characterized as DMAP1-binding.
+At position 5 to 106, the domain is characterized as BTB.
+At position 14 to 243, the domain is characterized as ABC transporter.
+At position 274 to 465, the domain is characterized as B30.2/SPRY.
+At position 36 to 175, the domain is characterized as CUB.
+At position 182 to 225, the domain is characterized as LDL-receptor class A.
+At position 81 to 274, the domain is characterized as MHYT.
+At position 375 to 507, the domain is characterized as GGDEF.
+At position 516 to 770, the domain is characterized as EAL.
+At position 273 to 358, the domain is characterized as DEP.
+At position 420 to 689, the domain is characterized as RGS.
+At position 149 to 230, the domain is characterized as PRC barrel.
+At position 4 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 157 to 212, the domain is characterized as AWS.
+At position 214 to 331, the domain is characterized as SET.
+At position 338 to 354, the domain is characterized as Post-SET.
+At position 603 to 634, the domain is characterized as WW.
+At position 280 to 586, the domain is characterized as UvrD-like helicase C-terminal.
+At position 9 to 206, the domain is characterized as MIF4G.
+At position 349 to 613, the domain is characterized as Protein kinase.
+At position 701 to 759, the domain is characterized as SH3.
+At position 56 to 138, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 229, the domain is characterized as Ig-like C2-type 2.
+At position 245 to 333, the domain is characterized as Ig-like C2-type 3.
+At position 338 to 428, the domain is characterized as Ig-like C2-type 4.
+At position 432 to 521, the domain is characterized as Ig-like C2-type 5.
+At position 525 to 615, the domain is characterized as Ig-like C2-type 6.
+At position 622 to 718, the domain is characterized as Fibronectin type-III 1.
+At position 723 to 819, the domain is characterized as Fibronectin type-III 2.
+At position 824 to 922, the domain is characterized as Fibronectin type-III 3.
+At position 926 to 1020, the domain is characterized as Fibronectin type-III 4.
+At position 1024 to 1123, the domain is characterized as Fibronectin type-III 5.
+At position 1128 to 1226, the domain is characterized as Fibronectin type-III 6.
+At position 1231 to 1328, the domain is characterized as Fibronectin type-III 7.
+At position 1332 to 1426, the domain is characterized as Fibronectin type-III 8.
+At position 1431 to 1528, the domain is characterized as Fibronectin type-III 9.
+At position 1533 to 1651, the domain is characterized as Fibronectin type-III 10.
+At position 1656 to 1752, the domain is characterized as Fibronectin type-III 11.
+At position 1756 to 1851, the domain is characterized as Fibronectin type-III 12.
+At position 1854 to 1955, the domain is characterized as Fibronectin type-III 13.
+At position 54 to 215, the domain is characterized as FAD-binding PCMH-type.
+At position 127 to 162, the domain is characterized as EF-hand.
+At position 32 to 77, the domain is characterized as KRAB.
+At position 317 to 383, the domain is characterized as PWWP.
+At position 24 to 82, the domain is characterized as Chromo 1.
+At position 154 to 212, the domain is characterized as Chromo 2.
+At position 140 to 367, the domain is characterized as Radical SAM core.
+At position 370 to 430, the domain is characterized as TRAM.
+At position 1 to 157, the domain is characterized as PTS EIIB type-4.
+At position 42 to 165, the domain is characterized as sHSP.
+At position 11 to 478, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 479 to 790, the domain is characterized as UvrD-like helicase C-terminal.
+At position 460 to 718, the domain is characterized as Protein kinase.
+At position 734 to 805, the domain is characterized as U-box.
+At position 148 to 236, the domain is characterized as Ig-like C2-type 2.
+At position 245 to 345, the domain is characterized as Ig-like C2-type 3.
+At position 465 to 753, the domain is characterized as Protein kinase.
+At position 436 to 532, the domain is characterized as Fibronectin type-III 2.
+At position 622 to 883, the domain is characterized as Protein kinase.
+At position 292 to 530, the domain is characterized as Glutamine amidotransferase type-1.
+At position 146 to 342, the domain is characterized as B30.2/SPRY.
+At position 13 to 81, the domain is characterized as HTH gntR-type.
+At position 27 to 161, the domain is characterized as Nudix hydrolase.
+At position 145 to 328, the domain is characterized as MIF4G.
+At position 427 to 543, the domain is characterized as MI.
+At position 78 to 164, the domain is characterized as CRIC.
+At position 196 to 285, the domain is characterized as PDZ.
+At position 403 to 502, the domain is characterized as PH.
+At position 3 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 69 to 283, the domain is characterized as Radical SAM core.
+At position 178 to 353, the domain is characterized as Exonuclease.
+At position 27 to 225, the domain is characterized as GH16.
+At position 59 to 95, the domain is characterized as LRRNT.
+At position 85 to 235, the domain is characterized as Flavodoxin-like.
+At position 291 to 540, the domain is characterized as FAD-binding FR-type.
+At position 59 to 134, the domain is characterized as Carrier.
+At position 140 to 208, the domain is characterized as DRBM 2.
+At position 272 to 340, the domain is characterized as DRBM 3.
+At position 344 to 431, the domain is characterized as Fibronectin type-III.
+At position 39 to 113, the domain is characterized as H15.
+At position 250 to 373, the domain is characterized as C2.
+At position 63 to 310, the domain is characterized as Protein kinase.
+At position 31 to 387, the domain is characterized as IF rod.
+At position 428 to 545, the domain is characterized as LTD.
+At position 97 to 250, the domain is characterized as Cytochrome c.
+At position 22 to 241, the domain is characterized as Glutamine amidotransferase type-2.
+At position 411 to 507, the domain is characterized as Zinc-hook.
+At position 23 to 156, the domain is characterized as 6-Cys 1.
+At position 159 to 298, the domain is characterized as 6-Cys 2.
+At position 194 to 545, the domain is characterized as Asparagine synthetase.
+At position 341 to 951, the domain is characterized as USP.
+At position 704 to 723, the domain is characterized as UIM 1.
+At position 806 to 825, the domain is characterized as UIM 2.
+At position 828 to 847, the domain is characterized as UIM 3.
+At position 259 to 456, the domain is characterized as GATase cobBQ-type.
+At position 208 to 383, the domain is characterized as EngA-type G 2.
+At position 4 to 70, the domain is characterized as Cytochrome b5 heme-binding.
+At position 22 to 148, the domain is characterized as PH.
+At position 821 to 993, the domain is characterized as Rho-GAP.
+At position 194 to 288, the domain is characterized as Ras-associating.
+At position 290 to 337, the domain is characterized as SARAH.
+At position 119 to 228, the domain is characterized as C-type lectin.
+At position 143 to 468, the domain is characterized as Tyrosine-protein phosphatase.
+At position 9 to 160, the domain is characterized as NAC.
+At position 576 to 656, the domain is characterized as Carrier.
+At position 94 to 169, the domain is characterized as RRM.
+At position 101 to 199, the domain is characterized as TAFH.
+At position 421 to 549, the domain is characterized as Guanylate cyclase.
+At position 36 to 80, the domain is characterized as Clip.
+At position 148 to 392, the domain is characterized as Peptidase S1.
+At position 356 to 413, the domain is characterized as COS.
+At position 416 to 511, the domain is characterized as Fibronectin type-III.
+At position 509 to 723, the domain is characterized as B30.2/SPRY.
+At position 384 to 765, the domain is characterized as GRAS.
+At position 39 to 142, the domain is characterized as Calponin-homology (CH).
+At position 18 to 212, the domain is characterized as RNase H type-2.
+At position 974 to 1046, the domain is characterized as Bromo.
+At position 524 to 642, the domain is characterized as SMC hinge.
+At position 424 to 441, the domain is characterized as WH2.
+At position 239 to 509, the domain is characterized as PI3K/PI4K catalytic.
+At position 92 to 350, the domain is characterized as Protein kinase.
+At position 393 to 428, the domain is characterized as EF-hand 1.
+At position 429 to 464, the domain is characterized as EF-hand 2.
+At position 501 to 534, the domain is characterized as EF-hand 4.
+At position 477 to 913, the domain is characterized as Hexokinase 2.
+At position 101 to 364, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 692 to 727, the domain is characterized as EF-hand 1.
+At position 756 to 791, the domain is characterized as EF-hand 2.
+At position 5 to 148, the domain is characterized as PTS EIIA type-2.
+At position 438 to 597, the domain is characterized as Helicase C-terminal.
+At position 254 to 555, the domain is characterized as Letm1 RBD.
+At position 683 to 718, the domain is characterized as EF-hand.
+At position 276 to 311, the domain is characterized as EF-hand.
+At position 438 to 595, the domain is characterized as Ferric oxidoreductase.
+At position 634 to 754, the domain is characterized as FAD-binding FR-type.
+At position 331 to 463, the domain is characterized as MATH.
+At position 75 to 435, the domain is characterized as SAM-dependent MTase C5-type.
+At position 87 to 171, the domain is characterized as Saposin B-type.
+At position 168 to 329, the domain is characterized as Helicase ATP-binding.
+At position 350 to 504, the domain is characterized as Helicase C-terminal.
+At position 29 to 158, the domain is characterized as VHS.
+At position 201 to 289, the domain is characterized as GAT.
+At position 54 to 113, the domain is characterized as SH3.
+At position 4 to 40, the domain is characterized as Peptidase S8.
+At position 4 to 120, the domain is characterized as Response regulatory 1.
+At position 155 to 269, the domain is characterized as Response regulatory 2.
+At position 319 to 454, the domain is characterized as GGDEF.
+At position 11 to 125, the domain is characterized as VPS28 N-terminal.
+At position 148 to 242, the domain is characterized as VPS28 C-terminal.
+At position 24 to 86, the domain is characterized as HTH iclR-type.
+At position 101 to 272, the domain is characterized as IclR-ED.
+At position 31 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 567 to 793, the domain is characterized as MIF4G.
+At position 1044 to 1166, the domain is characterized as MI.
+At position 1231 to 1401, the domain is characterized as W2.
+At position 29 to 137, the domain is characterized as Histone-fold.
+At position 168 to 219, the domain is characterized as F-box.
+At position 17 to 103, the domain is characterized as GS beta-grasp.
+At position 110 to 445, the domain is characterized as GS catalytic.
+At position 28 to 167, the domain is characterized as Ephrin RBD.
+At position 113 to 204, the domain is characterized as Ig-like C1-type.
+At position 202 to 343, the domain is characterized as AXH.
+At position 28 to 122, the domain is characterized as UPAR/Ly6.
+At position 166 to 428, the domain is characterized as Protein kinase.
+At position 2 to 219, the domain is characterized as Glutamine amidotransferase type-1.
+At position 98 to 203, the domain is characterized as PilZ.
+At position 212 to 258, the domain is characterized as F-box.
+At position 352 to 437, the domain is characterized as OCT.
+At position 90 to 253, the domain is characterized as EngA-type G 1.
+At position 263 to 436, the domain is characterized as EngA-type G 2.
+At position 437 to 519, the domain is characterized as KH-like.
+At position 24 to 436, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 905 to 1191, the domain is characterized as PKS/mFAS DH.
+At position 2025 to 2101, the domain is characterized as Carrier.
+At position 128 to 370, the domain is characterized as SMP-LTD.
+At position 23 to 75, the domain is characterized as HTH myb-type 1.
+At position 76 to 130, the domain is characterized as HTH myb-type 2.
+At position 622 to 817, the domain is characterized as DH.
+At position 483 to 794, the domain is characterized as CNH.
+At position 685 to 772, the domain is characterized as BRCT.
+At position 1 to 327, the domain is characterized as Hcy-binding.
+At position 356 to 532, the domain is characterized as SEC7.
+At position 569 to 681, the domain is characterized as PH.
+At position 29 to 62, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 215 to 259, the domain is characterized as TSP type-1.
+At position 286 to 449, the domain is characterized as AMOP.
+At position 73 to 234, the domain is characterized as Thioredoxin.
+At position 609 to 668, the domain is characterized as KH.
+At position 680 to 749, the domain is characterized as S1 motif.
+At position 42 to 267, the domain is characterized as Radical SAM core.
+At position 235 to 264, the domain is characterized as GS.
+At position 265 to 606, the domain is characterized as Protein kinase.
+At position 36 to 75, the domain is characterized as VM.
+At position 69 to 128, the domain is characterized as Tudor.
+At position 21 to 131, the domain is characterized as MTTase N-terminal.
+At position 150 to 387, the domain is characterized as Radical SAM core.
+At position 390 to 455, the domain is characterized as TRAM.
+At position 52 to 262, the domain is characterized as Helicase ATP-binding.
+At position 295 to 452, the domain is characterized as Helicase C-terminal.
+At position 19 to 147, the domain is characterized as SCP.
+At position 183 to 216, the domain is characterized as ShKT.
+At position 30 to 234, the domain is characterized as Brix.
+At position 26 to 156, the domain is characterized as B12-binding.
+At position 339 to 545, the domain is characterized as MCM.
+At position 1 to 75, the domain is characterized as KRAB.
+At position 63 to 129, the domain is characterized as TGS.
+At position 261 to 433, the domain is characterized as Helicase ATP-binding.
+At position 478 to 632, the domain is characterized as Helicase C-terminal.
+At position 207 to 305, the domain is characterized as HTH araC/xylS-type.
+At position 111 to 203, the domain is characterized as PUA.
+At position 136 to 210, the domain is characterized as PRC barrel.
+At position 19 to 287, the domain is characterized as ZP.
+At position 1 to 185, the domain is characterized as CNNM transmembrane.
+At position 204 to 267, the domain is characterized as CBS 1.
+At position 272 to 329, the domain is characterized as CBS 2.
+At position 1 to 41, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 47 to 87, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 88 to 130, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 72 to 108, the domain is characterized as LDL-receptor class A.
+At position 109 to 205, the domain is characterized as SRCR.
+At position 217 to 449, the domain is characterized as Peptidase S1.
+At position 26 to 106, the domain is characterized as GIY-YIG.
+At position 216 to 251, the domain is characterized as UVR.
+At position 681 to 956, the domain is characterized as Protein kinase.
+At position 680 to 745, the domain is characterized as Chromo 1.
+At position 760 to 826, the domain is characterized as Chromo 2.
+At position 859 to 1033, the domain is characterized as Helicase ATP-binding.
+At position 1174 to 1330, the domain is characterized as Helicase C-terminal.
+At position 615 to 693, the domain is characterized as BRCT.
+At position 50 to 106, the domain is characterized as Ig-like C2-type 1.
+At position 131 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 26 to 142, the domain is characterized as Cadherin 1.
+At position 143 to 252, the domain is characterized as Cadherin 2.
+At position 253 to 358, the domain is characterized as Cadherin 3.
+At position 365 to 469, the domain is characterized as Cadherin 4.
+At position 470 to 572, the domain is characterized as Cadherin 5.
+At position 573 to 675, the domain is characterized as Cadherin 6.
+At position 679 to 784, the domain is characterized as Cadherin 7.
+At position 235 to 349, the domain is characterized as SEA 1.
+At position 900 to 1013, the domain is characterized as SEA 2.
+At position 1013 to 1054, the domain is characterized as EGF-like 1.
+At position 1055 to 1096, the domain is characterized as EGF-like 2.
+At position 117 to 221, the domain is characterized as Rieske.
+At position 408 to 485, the domain is characterized as UBX.
+At position 67 to 127, the domain is characterized as MADS-box.
+At position 30 to 217, the domain is characterized as BPL/LPL catalytic.
+At position 8 to 447, the domain is characterized as Hexokinase.
+At position 496 to 584, the domain is characterized as PDZ.
+At position 594 to 670, the domain is characterized as BRCT.
+At position 34 to 156, the domain is characterized as C-type lectin.
+At position 44 to 296, the domain is characterized as Protein kinase.
+At position 404 to 482, the domain is characterized as POLO box 1.
+At position 504 to 586, the domain is characterized as POLO box 2.
+At position 3 to 108, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 225 to 377, the domain is characterized as RNase NYN.
+At position 22 to 69, the domain is characterized as F-box.
+At position 97 to 188, the domain is characterized as HTH La-type RNA-binding.
+At position 193 to 283, the domain is characterized as RRM.
+At position 421 to 578, the domain is characterized as Exonuclease.
+At position 85 to 274, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 189 to 310, the domain is characterized as C2.
+At position 371 to 629, the domain is characterized as Protein kinase.
+At position 630 to 700, the domain is characterized as AGC-kinase C-terminal.
+At position 137 to 260, the domain is characterized as Nudix hydrolase.
+At position 24 to 161, the domain is characterized as C1q 1.
+At position 170 to 315, the domain is characterized as C1q 2.
+At position 89 to 209, the domain is characterized as GST C-terminal.
+At position 74 to 175, the domain is characterized as Thioredoxin.
+At position 636 to 827, the domain is characterized as FtsK.
+At position 204 to 499, the domain is characterized as Deacetylase sirtuin-type.
+At position 9 to 220, the domain is characterized as Radical SAM core.
+At position 35 to 157, the domain is characterized as Calponin-homology (CH).
+At position 198 to 271, the domain is characterized as GAR.
+At position 346 to 507, the domain is characterized as Helicase C-terminal.
+At position 226 to 343, the domain is characterized as xRRM.
+At position 291 to 430, the domain is characterized as SIS 1.
+At position 463 to 604, the domain is characterized as SIS 2.
+At position 6 to 118, the domain is characterized as PCI.
+At position 24 to 169, the domain is characterized as FAS1.
+At position 146 to 312, the domain is characterized as JmjC.
+At position 1 to 235, the domain is characterized as Radical SAM core.
+At position 525 to 756, the domain is characterized as ABC transporter.
+At position 1 to 76, the domain is characterized as GIY-YIG.
+At position 6 to 124, the domain is characterized as C2.
+At position 14 to 72, the domain is characterized as TRAM.
+At position 291 to 425, the domain is characterized as DAGKc.
+At position 32 to 150, the domain is characterized as Ig-like V-type.
+At position 80 to 297, the domain is characterized as MIF4G.
+At position 367 to 640, the domain is characterized as Protein kinase.
+At position 641 to 712, the domain is characterized as AGC-kinase C-terminal.
+At position 950 to 1038, the domain is characterized as PDZ.
+At position 631 to 700, the domain is characterized as S1 motif.
+At position 92 to 222, the domain is characterized as MPN.
+At position 47 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 239 to 324, the domain is characterized as Ig-like C2-type 3.
+At position 332 to 395, the domain is characterized as Ig-like C2-type 4.
+At position 403 to 481, the domain is characterized as Ig-like C2-type 5.
+At position 486 to 561, the domain is characterized as Ig-like C2-type 6.
+At position 566 to 645, the domain is characterized as Ig-like C2-type 7.
+At position 659 to 734, the domain is characterized as Ig-like C2-type 8.
+At position 738 to 819, the domain is characterized as Ig-like C2-type 9.
+At position 107 to 337, the domain is characterized as Radical SAM core.
+At position 251 to 389, the domain is characterized as Flavodoxin-like.
+At position 413 to 489, the domain is characterized as B5.
+At position 727 to 820, the domain is characterized as FDX-ACB.
+At position 69 to 154, the domain is characterized as RRM 1.
+At position 17 to 70, the domain is characterized as F-box.
+At position 370 to 421, the domain is characterized as FBD.
+At position 46 to 217, the domain is characterized as MENTAL.
+At position 230 to 443, the domain is characterized as START.
+At position 14 to 86, the domain is characterized as Sm.
+At position 60 to 219, the domain is characterized as FCP1 homology.
+At position 968 to 1043, the domain is characterized as Carrier.
+At position 369 to 801, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1666 to 1743, the domain is characterized as Carrier 1.
+At position 1801 to 1878, the domain is characterized as Carrier 2.
+At position 109 to 400, the domain is characterized as Cbl-PTB.
+At position 6 to 61, the domain is characterized as HTH deoR-type.
+At position 124 to 217, the domain is characterized as PB1.
+At position 338 to 533, the domain is characterized as Protein kinase.
+At position 226 to 322, the domain is characterized as BEN.
+At position 565 to 645, the domain is characterized as BTB 1.
+At position 769 to 837, the domain is characterized as BTB 2.
+At position 1235 to 1399, the domain is characterized as PNPLA.
+At position 22 to 200, the domain is characterized as Reticulon.
+At position 322 to 675, the domain is characterized as PUM-HD.
+At position 45 to 434, the domain is characterized as Helicase ATP-binding.
+At position 311 to 439, the domain is characterized as C2 B9-type.
+At position 103 to 264, the domain is characterized as Integrase catalytic.
+At position 73 to 148, the domain is characterized as Lipoyl-binding.
+At position 160 to 229, the domain is characterized as S4 RNA-binding.
+At position 403 to 462, the domain is characterized as MIR 2.
+At position 472 to 528, the domain is characterized as MIR 3.
+At position 502 to 714, the domain is characterized as NEL.
+At position 58 to 368, the domain is characterized as AB hydrolase-1.
+At position 22 to 280, the domain is characterized as Protein kinase.
+At position 323 to 358, the domain is characterized as EF-hand 1.
+At position 359 to 394, the domain is characterized as EF-hand 2.
+At position 395 to 430, the domain is characterized as EF-hand 3.
+At position 434 to 464, the domain is characterized as EF-hand 4.
+At position 72 to 144, the domain is characterized as S1 motif.
+At position 152 to 211, the domain is characterized as KH.
+At position 1 to 149, the domain is characterized as UBC core.
+At position 25 to 171, the domain is characterized as Jacalin-type lectin.
+At position 1 to 64, the domain is characterized as S5 DRBM.
+At position 80 to 169, the domain is characterized as Ig-like C2-type 1.
+At position 182 to 260, the domain is characterized as Ig-like C2-type 2.
+At position 2 to 252, the domain is characterized as tr-type G.
+At position 6 to 69, the domain is characterized as S5 DRBM.
+At position 596 to 779, the domain is characterized as Helicase ATP-binding.
+At position 904 to 1069, the domain is characterized as Helicase C-terminal.
+At position 273 to 471, the domain is characterized as Ku.
+At position 585 to 619, the domain is characterized as SAP.
+At position 256 to 305, the domain is characterized as bHLH.
+At position 15 to 118, the domain is characterized as PH.
+At position 193 to 450, the domain is characterized as Protein kinase.
+At position 451 to 528, the domain is characterized as AGC-kinase C-terminal.
+At position 11 to 86, the domain is characterized as Sm.
+At position 423 to 480, the domain is characterized as F-box.
+At position 23 to 313, the domain is characterized as GH10.
+At position 157 to 286, the domain is characterized as Guanylate cyclase.
+At position 239 to 266, the domain is characterized as KOW 1.
+At position 501 to 528, the domain is characterized as KOW 2.
+At position 607 to 634, the domain is characterized as KOW 3.
+At position 232 to 297, the domain is characterized as SEP.
+At position 344 to 421, the domain is characterized as UBX.
+At position 23 to 102, the domain is characterized as RRM 1.
+At position 179 to 253, the domain is characterized as RRM 2.
+At position 1 to 219, the domain is characterized as ABC transporter.
+At position 27 to 152, the domain is characterized as Death.
+At position 161 to 213, the domain is characterized as bHLH.
+At position 34 to 147, the domain is characterized as EH 1.
+At position 282 to 373, the domain is characterized as EH 2.
+At position 315 to 350, the domain is characterized as EF-hand.
+At position 96 to 159, the domain is characterized as S5 DRBM.
+At position 16 to 267, the domain is characterized as Protein kinase.
+At position 141 to 453, the domain is characterized as Peptidase S8.
+At position 462 to 596, the domain is characterized as P/Homo B.
+At position 10 to 160, the domain is characterized as UBC core.
+At position 12 to 142, the domain is characterized as EamA 1.
+At position 210 to 316, the domain is characterized as EamA 2.
+At position 207 to 517, the domain is characterized as Protein kinase.
+At position 518 to 586, the domain is characterized as AGC-kinase C-terminal.
+At position 43 to 226, the domain is characterized as tr-type G.
+At position 225 to 489, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 3 to 209, the domain is characterized as Lon N-terminal.
+At position 605 to 790, the domain is characterized as Lon proteolytic.
+At position 546 to 700, the domain is characterized as STAS.
+At position 485 to 540, the domain is characterized as Kazal-like.
+At position 16 to 129, the domain is characterized as Response regulatory.
+At position 365 to 781, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1229 to 1536, the domain is characterized as PKS/mFAS DH.
+At position 1581 to 1655, the domain is characterized as Carrier.
+At position 46 to 134, the domain is characterized as Ig-like 1.
+At position 141 to 235, the domain is characterized as Ig-like 2.
+At position 267 to 356, the domain is characterized as Ig-like 3.
+At position 361 to 448, the domain is characterized as Ig-like 4.
+At position 454 to 541, the domain is characterized as Ig-like 5.
+At position 545 to 632, the domain is characterized as Ig-like 6.
+At position 1064 to 1156, the domain is characterized as Fibronectin type-III 5.
+At position 135 to 358, the domain is characterized as DAGKc.
+At position 481 to 672, the domain is characterized as VWFA.
+At position 817 to 852, the domain is characterized as EF-hand 1.
+At position 853 to 888, the domain is characterized as EF-hand 2.
+At position 1030 to 1210, the domain is characterized as Ferric oxidoreductase.
+At position 1211 to 1318, the domain is characterized as FAD-binding FR-type.
+At position 146 to 314, the domain is characterized as 3'-5' exonuclease.
+At position 44 to 166, the domain is characterized as CUB.
+At position 166 to 225, the domain is characterized as Sushi.
+At position 240 to 479, the domain is characterized as Peptidase S1.
+At position 83 to 145, the domain is characterized as bHLH.
+At position 4 to 75, the domain is characterized as J.
+At position 90 to 158, the domain is characterized as DPH-type MB.
+At position 1196 to 1258, the domain is characterized as SAM.
+At position 5 to 85, the domain is characterized as RRM.
+At position 173 to 437, the domain is characterized as Protein kinase.
+At position 1004 to 1186, the domain is characterized as Rho-GAP.
+At position 29 to 58, the domain is characterized as EGF-like 1; truncated.
+At position 59 to 104, the domain is characterized as EGF-like 2.
+At position 104 to 148, the domain is characterized as EGF-like 3.
+At position 151 to 191, the domain is characterized as EGF-like 4.
+At position 44 to 101, the domain is characterized as Tudor.
+At position 197 to 375, the domain is characterized as Helicase ATP-binding.
+At position 386 to 547, the domain is characterized as Helicase C-terminal.
+At position 101 to 148, the domain is characterized as Fibronectin type-II.
+At position 158 to 196, the domain is characterized as EGF-like 1.
+At position 198 to 238, the domain is characterized as Fibronectin type-I.
+At position 239 to 277, the domain is characterized as EGF-like 2.
+At position 283 to 365, the domain is characterized as Kringle.
+At position 407 to 645, the domain is characterized as Peptidase S1.
+At position 36 to 136, the domain is characterized as Inhibitor I9.
+At position 145 to 684, the domain is characterized as Peptidase S8.
+At position 408 to 503, the domain is characterized as PA.
+At position 482 to 793, the domain is characterized as CNH.
+At position 256 to 425, the domain is characterized as DUF724.
+At position 120 to 197, the domain is characterized as Sm.
+At position 9 to 254, the domain is characterized as PPM-type phosphatase.
+At position 1023 to 1310, the domain is characterized as CNH.
+At position 514 to 604, the domain is characterized as Fibronectin type-III 3.
+At position 609 to 706, the domain is characterized as Fibronectin type-III 4.
+At position 711 to 819, the domain is characterized as Fibronectin type-III 5.
+At position 820 to 914, the domain is characterized as Fibronectin type-III 6.
+At position 918 to 1010, the domain is characterized as Fibronectin type-III 7.
+At position 1014 to 1098, the domain is characterized as Fibronectin type-III 8.
+At position 1 to 141, the domain is characterized as CheB-type methylesterase.
+At position 168 to 440, the domain is characterized as CheR-type methyltransferase.
+At position 89 to 185, the domain is characterized as Rieske.
+At position 166 to 386, the domain is characterized as Radical SAM core.
+At position 3 to 359, the domain is characterized as YjeF C-terminal.
+At position 372 to 560, the domain is characterized as DH.
+At position 589 to 688, the domain is characterized as PH 1.
+At position 820 to 920, the domain is characterized as PH 2.
+At position 12 to 25, the domain is characterized as CRIB.
+At position 408 to 659, the domain is characterized as Protein kinase.
+At position 26 to 230, the domain is characterized as DarT.
+At position 450 to 619, the domain is characterized as tr-type G.
+At position 628 to 789, the domain is characterized as MOSC.
+At position 64 to 133, the domain is characterized as S1 motif.
+At position 141 to 199, the domain is characterized as KH.
+At position 51 to 209, the domain is characterized as SIS.
+At position 3 to 90, the domain is characterized as HPr.
+At position 76 to 226, the domain is characterized as HD.
+At position 65 to 128, the domain is characterized as bZIP.
+At position 293 to 372, the domain is characterized as Ubiquitin-like.
+At position 463 to 522, the domain is characterized as HTH myb-type.
+At position 608 to 710, the domain is characterized as tRNA-binding.
+At position 70 to 315, the domain is characterized as ABC transporter 1.
+At position 344 to 566, the domain is characterized as ABC transporter 2.
+At position 481 to 728, the domain is characterized as ABC transporter.
+At position 11 to 182, the domain is characterized as BUB1 N-terminal.
+At position 787 to 1085, the domain is characterized as Protein kinase.
+At position 35 to 121, the domain is characterized as BRCT.
+At position 275 to 505, the domain is characterized as UmuC.
+At position 178 to 518, the domain is characterized as PUM-HD.
+At position 419 to 588, the domain is characterized as tr-type G.
+At position 174 to 185, the domain is characterized as EGF-like 1; incomplete.
+At position 186 to 216, the domain is characterized as EGF-like 2.
+At position 217 to 247, the domain is characterized as EGF-like 3.
+At position 248 to 279, the domain is characterized as EGF-like 4.
+At position 280 to 310, the domain is characterized as EGF-like 5.
+At position 311 to 341, the domain is characterized as EGF-like 6.
+At position 342 to 372, the domain is characterized as EGF-like 7.
+At position 373 to 403, the domain is characterized as EGF-like 8.
+At position 404 to 434, the domain is characterized as EGF-like 9.
+At position 435 to 465, the domain is characterized as EGF-like 10.
+At position 466 to 496, the domain is characterized as EGF-like 11.
+At position 497 to 527, the domain is characterized as EGF-like 12.
+At position 528 to 558, the domain is characterized as EGF-like 13.
+At position 559 to 589, the domain is characterized as EGF-like 14.
+At position 895 to 988, the domain is characterized as Fibronectin type-III 4.
+At position 989 to 1077, the domain is characterized as Fibronectin type-III 5.
+At position 1078 to 1165, the domain is characterized as Fibronectin type-III 6.
+At position 1167 to 1259, the domain is characterized as Fibronectin type-III 7.
+At position 1260 to 1348, the domain is characterized as Fibronectin type-III 8.
+At position 1349 to 1440, the domain is characterized as Fibronectin type-III 9.
+At position 1442 to 1530, the domain is characterized as Fibronectin type-III 10.
+At position 1531 to 1620, the domain is characterized as Fibronectin type-III 11.
+At position 1621 to 1710, the domain is characterized as Fibronectin type-III 12.
+At position 1711 to 1797, the domain is characterized as Fibronectin type-III 13.
+At position 1798 to 1886, the domain is characterized as Fibronectin type-III 14.
+At position 1884 to 2099, the domain is characterized as Fibrinogen C-terminal.
+At position 106 to 161, the domain is characterized as TSP type-1 1.
+At position 163 to 218, the domain is characterized as TSP type-1 2.
+At position 256 to 362, the domain is characterized as SCP.
+At position 53 to 370, the domain is characterized as AB hydrolase-1.
+At position 339 to 439, the domain is characterized as Rhodanese.
+At position 690 to 885, the domain is characterized as DH.
+At position 901 to 1007, the domain is characterized as PH.
+At position 1513 to 1657, the domain is characterized as VPS9.
+At position 226 to 388, the domain is characterized as TrmE-type G.
+At position 717 to 965, the domain is characterized as I/LWEQ.
+At position 85 to 439, the domain is characterized as PPM-type phosphatase.
+At position 4 to 167, the domain is characterized as Thioredoxin.
+At position 10 to 161, the domain is characterized as Tyrosine-protein phosphatase.
+At position 391 to 427, the domain is characterized as CBM10 1.
+At position 436 to 473, the domain is characterized as CBM10 2.
+At position 43 to 111, the domain is characterized as BTB.
+At position 219 to 484, the domain is characterized as NPH3.
+At position 36 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 31 to 305, the domain is characterized as Protein kinase.
+At position 366 to 438, the domain is characterized as SAM.
+At position 220 to 310, the domain is characterized as PA.
+At position 498 to 739, the domain is characterized as Fibrinogen C-terminal.
+At position 39 to 166, the domain is characterized as Calponin-homology (CH).
+At position 207 to 279, the domain is characterized as GAR.
+At position 39 to 105, the domain is characterized as BTB.
+At position 466 to 635, the domain is characterized as tr-type G.
+At position 37 to 140, the domain is characterized as SCP.
+At position 14 to 235, the domain is characterized as ABC transporter.
+At position 11 to 157, the domain is characterized as Toprim.
+At position 131 to 360, the domain is characterized as Histidine kinase.
+At position 77 to 362, the domain is characterized as ABC transmembrane type-1.
+At position 396 to 633, the domain is characterized as ABC transporter.
+At position 474 to 609, the domain is characterized as Ricin B-type lectin.
+At position 32 to 132, the domain is characterized as Ig-like C2-type 1.
+At position 551 to 753, the domain is characterized as Helicase ATP-binding.
+At position 1047 to 1227, the domain is characterized as Helicase C-terminal.
+At position 30 to 130, the domain is characterized as Fibronectin type-III 1.
+At position 133 to 221, the domain is characterized as Fibronectin type-III 2.
+At position 236 to 334, the domain is characterized as Fibronectin type-III 3.
+At position 197 to 232, the domain is characterized as EF-hand 3.
+At position 278 to 313, the domain is characterized as EF-hand 5.
+At position 314 to 349, the domain is characterized as EF-hand 6.
+At position 176 to 484, the domain is characterized as USP.
+At position 131 to 218, the domain is characterized as PB1.
+At position 258 to 397, the domain is characterized as PADR1 zinc-binding.
+At position 464 to 563, the domain is characterized as WGR.
+At position 586 to 704, the domain is characterized as PARP alpha-helical.
+At position 717 to 945, the domain is characterized as PARP catalytic.
+At position 174 to 203, the domain is characterized as GS.
+At position 204 to 494, the domain is characterized as Protein kinase.
+At position 343 to 385, the domain is characterized as LRRCT.
+At position 15 to 197, the domain is characterized as KIND.
+At position 342 to 642, the domain is characterized as FERM.
+At position 775 to 861, the domain is characterized as PDZ 1.
+At position 950 to 1035, the domain is characterized as PDZ 2.
+At position 1079 to 1167, the domain is characterized as PDZ 3.
+At position 208 to 400, the domain is characterized as Peptidase M12B.
+At position 406 to 493, the domain is characterized as Disintegrin.
+At position 631 to 664, the domain is characterized as EGF-like.
+At position 6 to 199, the domain is characterized as ABC transmembrane type-1.
+At position 93 to 455, the domain is characterized as GBD/FH3.
+At position 540 to 610, the domain is characterized as FH1.
+At position 615 to 1013, the domain is characterized as FH2.
+At position 1036 to 1066, the domain is characterized as DAD.
+At position 63 to 111, the domain is characterized as Kazal-like 2.
+At position 100 to 160, the domain is characterized as S4 RNA-binding.
+At position 27 to 111, the domain is characterized as Inhibitor I9.
+At position 116 to 618, the domain is characterized as Peptidase S8.
+At position 388 to 470, the domain is characterized as PA.
+At position 1 to 128, the domain is characterized as Toprim.
+At position 196 to 467, the domain is characterized as ABC transporter 1.
+At position 545 to 758, the domain is characterized as ABC transmembrane type-2 1.
+At position 908 to 1160, the domain is characterized as ABC transporter 2.
+At position 1233 to 1447, the domain is characterized as ABC transmembrane type-2 2.
+At position 176 to 365, the domain is characterized as Helicase ATP-binding.
+At position 376 to 536, the domain is characterized as Helicase C-terminal.
+At position 92 to 182, the domain is characterized as CTCK.
+At position 38 to 115, the domain is characterized as U-box.
+At position 274 to 428, the domain is characterized as PPIase cyclophilin-type.
+At position 492 to 661, the domain is characterized as tr-type G.
+At position 95 to 170, the domain is characterized as S4 RNA-binding.
+At position 252 to 428, the domain is characterized as GATase cobBQ-type.
+At position 97 to 284, the domain is characterized as PXA.
+At position 373 to 496, the domain is characterized as RGS.
+At position 570 to 691, the domain is characterized as PX.
+At position 658 to 694, the domain is characterized as Anaphylatoxin-like.
+At position 1479 to 1616, the domain is characterized as NTR.
+At position 197 to 394, the domain is characterized as Peptidase M12B.
+At position 402 to 486, the domain is characterized as Disintegrin.
+At position 379 to 486, the domain is characterized as PAZ.
+At position 660 to 966, the domain is characterized as Piwi.
+At position 225 to 353, the domain is characterized as Galectin 2.
+At position 315 to 487, the domain is characterized as TR mART core.
+At position 462 to 625, the domain is characterized as Helicase ATP-binding.
+At position 753 to 907, the domain is characterized as Helicase C-terminal.
+At position 25 to 118, the domain is characterized as UPAR/Ly6 1.
+At position 118 to 213, the domain is characterized as UPAR/Ly6 2.
+At position 214 to 299, the domain is characterized as UPAR/Ly6 3.
+At position 354 to 631, the domain is characterized as Protein kinase.
+At position 260 to 400, the domain is characterized as GST C-terminal.
+At position 463 to 801, the domain is characterized as BEACH.
+At position 1064 to 1400, the domain is characterized as Protein kinase.
+At position 573 to 672, the domain is characterized as tRNA-binding.
+At position 826 to 859, the domain is characterized as WW 1.
+At position 1016 to 1049, the domain is characterized as WW 2.
+At position 1269 to 1604, the domain is characterized as HECT.
+At position 3 to 131, the domain is characterized as ADF-H.
+At position 422 to 481, the domain is characterized as SH3.
+At position 917 to 1192, the domain is characterized as Protein kinase.
+At position 4 to 366, the domain is characterized as SAM-dependent MTase C5-type.
+At position 426 to 487, the domain is characterized as PDZ.
+At position 389 to 455, the domain is characterized as TRAM.
+At position 371 to 405, the domain is characterized as SAP.
+At position 165 to 269, the domain is characterized as MaoC-like.
+At position 28 to 258, the domain is characterized as Peptidase S1.
+At position 1125 to 1446, the domain is characterized as DOT1.
+At position 98 to 402, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 130 to 158, the domain is characterized as IQ 1.
+At position 159 to 181, the domain is characterized as IQ 2.
+At position 42 to 653, the domain is characterized as Vitellogenin.
+At position 2353 to 2516, the domain is characterized as VWFD.
+At position 204 to 289, the domain is characterized as KH.
+At position 612 to 692, the domain is characterized as BRCT.
+At position 772 to 922, the domain is characterized as TIR.
+At position 279 to 359, the domain is characterized as KRAB 2.
+At position 112 to 311, the domain is characterized as MAGE.
+At position 1532 to 1766, the domain is characterized as Rap-GAP.
+At position 65 to 325, the domain is characterized as PPM-type phosphatase.
+At position 207 to 251, the domain is characterized as CHCH.
+At position 33 to 190, the domain is characterized as Helicase ATP-binding.
+At position 969 to 1086, the domain is characterized as SET.
+At position 1095 to 1111, the domain is characterized as Post-SET.
+At position 275 to 373, the domain is characterized as PH.
+At position 447 to 572, the domain is characterized as Arf-GAP.
+At position 4 to 122, the domain is characterized as RabBD.
+At position 356 to 478, the domain is characterized as C2 1.
+At position 507 to 633, the domain is characterized as C2 2.
+At position 45 to 86, the domain is characterized as Chitin-binding type-1 1.
+At position 87 to 127, the domain is characterized as Chitin-binding type-1 2.
+At position 128 to 168, the domain is characterized as Chitin-binding type-1 3.
+At position 484 to 632, the domain is characterized as N-acetyltransferase.
+At position 721 to 791, the domain is characterized as Bromo.
+At position 5 to 60, the domain is characterized as F-box.
+At position 348 to 405, the domain is characterized as FBD.
+At position 63 to 174, the domain is characterized as HD.
+At position 31 to 79, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 35 to 770, the domain is characterized as PFL.
+At position 778 to 897, the domain is characterized as Glycine radical.
+At position 366 to 480, the domain is characterized as Rhodanese.
+At position 49 to 149, the domain is characterized as GAF.
+At position 24 to 311, the domain is characterized as Dynamin-type G.
+At position 592 to 678, the domain is characterized as GED.
+At position 6 to 474, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 512 to 811, the domain is characterized as UvrD-like helicase C-terminal.
+At position 101 to 137, the domain is characterized as DHHC.
+At position 228 to 355, the domain is characterized as PpiC.
+At position 187 to 246, the domain is characterized as SH3 1.
+At position 249 to 312, the domain is characterized as SH3 2.
+At position 458 to 519, the domain is characterized as SH3 3.
+At position 819 to 878, the domain is characterized as SH3 4.
+At position 53 to 280, the domain is characterized as Peptidase S1.
+At position 264 to 380, the domain is characterized as PH.
+At position 134 to 345, the domain is characterized as ATP-grasp.
+At position 527 to 687, the domain is characterized as STAS.
+At position 26 to 85, the domain is characterized as Kazal-like.
+At position 40 to 158, the domain is characterized as Ig-like V-type.
+At position 168 to 251, the domain is characterized as Ig-like C2-type.
+At position 18 to 342, the domain is characterized as Kinesin motor.
+At position 357 to 448, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 563 to 722, the domain is characterized as Helicase C-terminal.
+At position 15 to 179, the domain is characterized as FAD-binding PCMH-type.
+At position 613 to 666, the domain is characterized as BRCT.
+At position 52 to 301, the domain is characterized as GP-PDE.
+At position 63 to 233, the domain is characterized as Helicase ATP-binding.
+At position 244 to 405, the domain is characterized as Helicase C-terminal.
+At position 388 to 451, the domain is characterized as Thioredoxin.
+At position 243 to 383, the domain is characterized as MPN.
+At position 14 to 89, the domain is characterized as Ubiquitin-like.
+At position 288 to 399, the domain is characterized as SCP2.
+At position 55 to 366, the domain is characterized as AB hydrolase-1.
+At position 43 to 238, the domain is characterized as Cupin type-1 1.
+At position 298 to 447, the domain is characterized as Cupin type-1 2.
+At position 93 to 190, the domain is characterized as Toprim.
+At position 519 to 702, the domain is characterized as Flavodoxin-like.
+At position 755 to 1001, the domain is characterized as FAD-binding FR-type.
+At position 24 to 211, the domain is characterized as RNase H type-2.
+At position 7 to 122, the domain is characterized as Response regulatory.
+At position 157 to 261, the domain is characterized as HTH LytTR-type.
+At position 26 to 98, the domain is characterized as SH3.
+At position 782 to 914, the domain is characterized as N-terminal Ras-GEF.
+At position 952 to 1199, the domain is characterized as Ras-GEF.
+At position 85 to 232, the domain is characterized as FAS1.
+At position 65 to 760, the domain is characterized as Myosin motor.
+At position 763 to 792, the domain is characterized as IQ 2.
+At position 832 to 861, the domain is characterized as IQ 5.
+At position 855 to 884, the domain is characterized as IQ 6.
+At position 989 to 1189, the domain is characterized as MyTH4 1.
+At position 1194 to 1503, the domain is characterized as FERM 1.
+At position 1498 to 1564, the domain is characterized as SH3.
+At position 1641 to 1790, the domain is characterized as MyTH4 2.
+At position 1790 to 1896, the domain is characterized as MyTH4 3.
+At position 1796 to 2099, the domain is characterized as FERM 2.
+At position 9 to 227, the domain is characterized as ABC transporter.
+At position 46 to 312, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 319 to 569, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 33 to 124, the domain is characterized as Fibronectin type-III.
+At position 123 to 214, the domain is characterized as Rieske.
+At position 19 to 156, the domain is characterized as Thioredoxin.
+At position 27 to 299, the domain is characterized as GH18.
+At position 124 to 185, the domain is characterized as CX.
+At position 461 to 582, the domain is characterized as RCK N-terminal.
+At position 12 to 288, the domain is characterized as tr-type G.
+At position 318 to 544, the domain is characterized as TLDc.
+At position 161 to 257, the domain is characterized as PPIase FKBP-type.
+At position 101 to 273, the domain is characterized as Helicase ATP-binding.
+At position 341 to 495, the domain is characterized as Helicase C-terminal.
+At position 181 to 243, the domain is characterized as t-SNARE coiled-coil homology.
+At position 22 to 144, the domain is characterized as MsrB.
+At position 92 to 260, the domain is characterized as FAD-binding PCMH-type.
+At position 517 to 592, the domain is characterized as Cytochrome b5 heme-binding.
+At position 634 to 746, the domain is characterized as FAD-binding FR-type.
+At position 4 to 159, the domain is characterized as Flavodoxin-like.
+At position 25 to 108, the domain is characterized as UPAR/Ly6.
+At position 346 to 423, the domain is characterized as OCT.
+At position 75 to 152, the domain is characterized as RRM 1.
+At position 167 to 248, the domain is characterized as RRM 2.
+At position 572 to 634, the domain is characterized as FIP-RBD.
+At position 52 to 138, the domain is characterized as FAR1.
+At position 219 to 315, the domain is characterized as MULE.
+At position 37 to 129, the domain is characterized as HTH arsR-type.
+At position 34 to 584, the domain is characterized as PLA2c.
+At position 63 to 296, the domain is characterized as GB1/RHD3-type G.
+At position 60 to 105, the domain is characterized as WAP.
+At position 49 to 344, the domain is characterized as USP.
+At position 331 to 360, the domain is characterized as LRRCT.
+At position 190 to 256, the domain is characterized as SCA7.
+At position 14 to 266, the domain is characterized as Protein kinase.
+At position 287 to 327, the domain is characterized as UBA.
+At position 456 to 504, the domain is characterized as KA1.
+At position 1 to 314, the domain is characterized as Protein kinase.
+At position 133 to 330, the domain is characterized as HD-GYP.
+At position 8 to 121, the domain is characterized as C-type lectin.
+At position 28 to 216, the domain is characterized as RNase H type-2.
+At position 627 to 928, the domain is characterized as Autotransporter.
+At position 91 to 289, the domain is characterized as MAGE.
+At position 243 to 364, the domain is characterized as C2 1.
+At position 417 to 535, the domain is characterized as C2 2.
+At position 262 to 404, the domain is characterized as Flavodoxin-like.
+At position 195 to 366, the domain is characterized as EngA-type G 2.
+At position 220 to 457, the domain is characterized as CN hydrolase.
+At position 22 to 328, the domain is characterized as Protein kinase.
+At position 101 to 310, the domain is characterized as NR LBD.
+At position 130 to 191, the domain is characterized as SH3.
+At position 24 to 120, the domain is characterized as PPIase FKBP-type.
+At position 428 to 579, the domain is characterized as Tyrosine-protein phosphatase.
+At position 20 to 300, the domain is characterized as Protein kinase.
+At position 203 to 304, the domain is characterized as Fe2OG dioxygenase.
+At position 28 to 57, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 58 to 89, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 132 to 161, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 11 to 84, the domain is characterized as RRM.
+At position 26 to 268, the domain is characterized as AB hydrolase-1.
+At position 577 to 672, the domain is characterized as Cadherin 6.
+At position 423 to 583, the domain is characterized as PA14.
+At position 247 to 323, the domain is characterized as Histone-fold.
+At position 30 to 87, the domain is characterized as FHA.
+At position 84 to 271, the domain is characterized as RNase H type-2.
+At position 27 to 144, the domain is characterized as MTTase N-terminal.
+At position 167 to 400, the domain is characterized as Radical SAM core.
+At position 403 to 466, the domain is characterized as TRAM.
+At position 544 to 612, the domain is characterized as HP.
+At position 37 to 306, the domain is characterized as Dynamin-type G.
+At position 532 to 624, the domain is characterized as GED.
+At position 289 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 55 to 169, the domain is characterized as MRH 1.
+At position 178 to 326, the domain is characterized as MRH 2.
+At position 332 to 477, the domain is characterized as MRH 3.
+At position 482 to 628, the domain is characterized as MRH 4.
+At position 634 to 770, the domain is characterized as MRH 5.
+At position 773 to 932, the domain is characterized as MRH 6.
+At position 940 to 1088, the domain is characterized as MRH 7.
+At position 1091 to 1228, the domain is characterized as MRH 8.
+At position 1234 to 1372, the domain is characterized as MRH 9.
+At position 1376 to 1517, the domain is characterized as MRH 10.
+At position 1523 to 1657, the domain is characterized as MRH 11.
+At position 1659 to 1806, the domain is characterized as MRH 12.
+At position 1811 to 1998, the domain is characterized as MRH 13.
+At position 1907 to 1953, the domain is characterized as Fibronectin type-II.
+At position 2001 to 2136, the domain is characterized as MRH 14.
+At position 2144 to 2289, the domain is characterized as MRH 15.
+At position 4 to 294, the domain is characterized as Protein kinase.
+At position 302 to 442, the domain is characterized as RanBD1.
+At position 611 to 709, the domain is characterized as GTD-binding.
+At position 32 to 178, the domain is characterized as sHSP.
+At position 539 to 706, the domain is characterized as tr-type G.
+At position 3 to 163, the domain is characterized as TIR 1.
+At position 192 to 411, the domain is characterized as NB-ARC.
+At position 1399 to 1559, the domain is characterized as TIR 2.
+At position 134 to 226, the domain is characterized as WSC 1.
+At position 237 to 331, the domain is characterized as WSC 2.
+At position 76 to 122, the domain is characterized as F-box.
+At position 1 to 55, the domain is characterized as CSD.
+At position 184 to 451, the domain is characterized as SF4 helicase; first part.
+At position 502 to 651, the domain is characterized as DOD-type homing endonuclease.
+At position 614 to 878, the domain is characterized as SF4 helicase; second part.
+At position 675 to 863, the domain is characterized as ATP-grasp 2.
+At position 925 to 1027, the domain is characterized as MGS-like.
+At position 618 to 720, the domain is characterized as Fibronectin type-III 1.
+At position 1403 to 1503, the domain is characterized as Fibronectin type-III 2.
+At position 1507 to 1628, the domain is characterized as Fibronectin type-III 3.
+At position 1629 to 1732, the domain is characterized as Fibronectin type-III 4.
+At position 1738 to 1843, the domain is characterized as Fibronectin type-III 5.
+At position 1928 to 2199, the domain is characterized as Protein kinase.
+At position 36 to 152, the domain is characterized as sHSP.
+At position 601 to 678, the domain is characterized as BRCT.
+At position 29 to 137, the domain is characterized as Ig-like C2-type 1.
+At position 431 to 525, the domain is characterized as Fibronectin type-III 1.
+At position 527 to 623, the domain is characterized as Fibronectin type-III 2.
+At position 632 to 741, the domain is characterized as Fibronectin type-III 3.
+At position 752 to 845, the domain is characterized as Fibronectin type-III 4.
+At position 850 to 945, the domain is characterized as Fibronectin type-III 5.
+At position 202 to 247, the domain is characterized as TSP type-1.
+At position 261 to 335, the domain is characterized as CTCK.
+At position 59 to 168, the domain is characterized as PX; atypical.
+At position 186 to 248, the domain is characterized as SH3.
+At position 315 to 510, the domain is characterized as Rho-GAP.
+At position 73 to 235, the domain is characterized as Laminin G-like.
+At position 554 to 608, the domain is characterized as Collagen-like 1.
+At position 818 to 873, the domain is characterized as Collagen-like 2.
+At position 845 to 902, the domain is characterized as Collagen-like 3.
+At position 986 to 1043, the domain is characterized as Collagen-like 4.
+At position 1269 to 1326, the domain is characterized as Collagen-like 5.
+At position 1446 to 1503, the domain is characterized as Collagen-like 6.
+At position 1497 to 1549, the domain is characterized as Collagen-like 7.
+At position 1589 to 1783, the domain is characterized as Fibrillar collagen NC1.
+At position 25 to 277, the domain is characterized as AB hydrolase-1.
+At position 203 to 367, the domain is characterized as PINIT.
+At position 10 to 76, the domain is characterized as PQ-loop 1.
+At position 211 to 274, the domain is characterized as PQ-loop 2.
+At position 75 to 187, the domain is characterized as TBDR plug.
+At position 192 to 747, the domain is characterized as TBDR beta-barrel.
+At position 23 to 214, the domain is characterized as ABC transmembrane type-1.
+At position 4 to 74, the domain is characterized as SH3 1.
+At position 75 to 134, the domain is characterized as SH3 2.
+At position 396 to 458, the domain is characterized as SH3 3.
+At position 57 to 132, the domain is characterized as J.
+At position 10 to 81, the domain is characterized as S1 motif.
+At position 53 to 234, the domain is characterized as Helicase ATP-binding.
+At position 245 to 467, the domain is characterized as Helicase C-terminal.
+At position 227 to 388, the domain is characterized as TrmE-type G.
+At position 35 to 260, the domain is characterized as Alpha-carbonic anhydrase.
+At position 79 to 379, the domain is characterized as AB hydrolase-1.
+At position 710 to 998, the domain is characterized as ABC transmembrane type-1 2.
+At position 1033 to 1271, the domain is characterized as ABC transporter 2.
+At position 4 to 267, the domain is characterized as Protein kinase.
+At position 294 to 317, the domain is characterized as IQ 1.
+At position 318 to 338, the domain is characterized as IQ 2.
+At position 387 to 416, the domain is characterized as IQ 3.
+At position 417 to 437, the domain is characterized as IQ 4.
+At position 49 to 212, the domain is characterized as Thioredoxin.
+At position 6 to 445, the domain is characterized as Hexokinase.
+At position 9 to 75, the domain is characterized as Sm.
+At position 497 to 514, the domain is characterized as WH2.
+At position 27 to 240, the domain is characterized as Cytochrome b561.
+At position 3 to 184, the domain is characterized as Glutamine amidotransferase type-1.
+At position 133 to 246, the domain is characterized as PilZ.
+At position 54 to 278, the domain is characterized as L-type lectin-like.
+At position 19 to 135, the domain is characterized as MTTase N-terminal.
+At position 200 to 430, the domain is characterized as Radical SAM core.
+At position 433 to 504, the domain is characterized as TRAM.
+At position 5 to 119, the domain is characterized as MaoC-like.
+At position 10 to 176, the domain is characterized as MH1.
+At position 274 to 467, the domain is characterized as MH2.
+At position 210 to 326, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 24 to 58, the domain is characterized as SAP.
+At position 95 to 304, the domain is characterized as ABC transmembrane type-1.
+At position 4 to 208, the domain is characterized as ABC transporter.
+At position 587 to 667, the domain is characterized as BRCT.
+At position 9 to 156, the domain is characterized as N-acetyltransferase.
+At position 284 to 344, the domain is characterized as LIM zinc-binding.
+At position 59 to 164, the domain is characterized as FAD-binding FR-type.
+At position 52 to 137, the domain is characterized as Ubiquitin-like.
+At position 7 to 104, the domain is characterized as ASCH.
+At position 430 to 545, the domain is characterized as Toprim.
+At position 129 to 210, the domain is characterized as MtN3/slv 2.
+At position 102 to 493, the domain is characterized as Kinesin motor.
+At position 379 to 427, the domain is characterized as SOCS box.
+At position 228 to 263, the domain is characterized as EF-hand 2.
+At position 264 to 299, the domain is characterized as EF-hand 3.
+At position 369 to 585, the domain is characterized as DUSP.
+At position 734 to 1567, the domain is characterized as USP.
+At position 1518 to 1617, the domain is characterized as MaoC-like.
+At position 282 to 457, the domain is characterized as Helicase ATP-binding.
+At position 485 to 630, the domain is characterized as Helicase C-terminal.
+At position 184 to 344, the domain is characterized as GAF.
+At position 387 to 521, the domain is characterized as Histidine kinase.
+At position 645 to 774, the domain is characterized as Response regulatory.
+At position 938 to 1076, the domain is characterized as MGS-like.
+At position 272 to 368, the domain is characterized as SH2.
+At position 393 to 646, the domain is characterized as Protein kinase.
+At position 47 to 110, the domain is characterized as BTB.
+At position 265 to 368, the domain is characterized as HTH La-type RNA-binding.
+At position 42 to 356, the domain is characterized as PPM-type phosphatase.
+At position 384 to 762, the domain is characterized as PDEase.
+At position 6 to 131, the domain is characterized as RNase III.
+At position 156 to 225, the domain is characterized as DRBM.
+At position 2 to 42, the domain is characterized as Helicase C-terminal.
+At position 130 to 181, the domain is characterized as bHLH.
+At position 40 to 365, the domain is characterized as RHD.
+At position 801 to 888, the domain is characterized as Death.
+At position 67 to 128, the domain is characterized as KH.
+At position 273 to 448, the domain is characterized as Helicase ATP-binding.
+At position 460 to 621, the domain is characterized as Helicase C-terminal.
+At position 91 to 164, the domain is characterized as PRC barrel.
+At position 76 to 183, the domain is characterized as SprT-like.
+At position 89 to 145, the domain is characterized as HTH myb-type.
+At position 100 to 137, the domain is characterized as LRRNT.
+At position 100 to 168, the domain is characterized as MIB/HERC2 1.
+At position 237 to 315, the domain is characterized as MIB/HERC2 2.
+At position 7 to 197, the domain is characterized as AMMECR1.
+At position 129 to 235, the domain is characterized as HTH APSES-type.
+At position 24 to 172, the domain is characterized as UEV.
+At position 386 to 454, the domain is characterized as SB.
+At position 54 to 385, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 387 to 720, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 8 to 119, the domain is characterized as HIT.
+At position 50 to 597, the domain is characterized as PLA2c.
+At position 501 to 806, the domain is characterized as CNH.
+At position 242 to 418, the domain is characterized as TR mART core.
+At position 24 to 74, the domain is characterized as PSI.
+At position 126 to 329, the domain is characterized as VWFA.
+At position 111 to 206, the domain is characterized as Fibronectin type-III 1.
+At position 207 to 295, the domain is characterized as Fibronectin type-III 2.
+At position 567 to 667, the domain is characterized as Fibronectin type-III 3.
+At position 943 to 1038, the domain is characterized as Fibronectin type-III 4.
+At position 1039 to 1146, the domain is characterized as Fibronectin type-III 5.
+At position 1442 to 1549, the domain is characterized as Fibronectin type-III 6.
+At position 1550 to 1649, the domain is characterized as Fibronectin type-III 7.
+At position 1651 to 1744, the domain is characterized as Fibronectin type-III 8.
+At position 1745 to 1846, the domain is characterized as Fibronectin type-III 9.
+At position 1938 to 2216, the domain is characterized as Protein kinase.
+At position 15 to 121, the domain is characterized as PRD.
+At position 576 to 627, the domain is characterized as LRRCT.
+At position 118 to 283, the domain is characterized as 3'-5' exonuclease.
+At position 334 to 414, the domain is characterized as HRDC.
+At position 137 to 221, the domain is characterized as Ig-like C2-type 1.
+At position 223 to 319, the domain is characterized as Ig-like C2-type 2.
+At position 592 to 770, the domain is characterized as Helicase ATP-binding.
+At position 797 to 945, the domain is characterized as Helicase C-terminal.
+At position 152 to 223, the domain is characterized as PA.
+At position 3 to 190, the domain is characterized as RNase H type-2.
+At position 1 to 83, the domain is characterized as Ubiquitin-like.
+At position 408 to 446, the domain is characterized as UBA.
+At position 133 to 239, the domain is characterized as BACK.
+At position 498 to 621, the domain is characterized as C2.
+At position 266 to 343, the domain is characterized as PUA.
+At position 64 to 200, the domain is characterized as RanBD1.
+At position 518 to 643, the domain is characterized as DBINO.
+At position 758 to 930, the domain is characterized as Helicase ATP-binding.
+At position 1323 to 1479, the domain is characterized as Helicase C-terminal.
+At position 382 to 433, the domain is characterized as Tudor-knot.
+At position 538 to 813, the domain is characterized as MYST-type HAT.
+At position 445 to 480, the domain is characterized as Anaphylatoxin-like 1.
+At position 488 to 519, the domain is characterized as Anaphylatoxin-like 2.
+At position 521 to 553, the domain is characterized as Anaphylatoxin-like 3.
+At position 604 to 645, the domain is characterized as EGF-like 1; calcium-binding.
+At position 679 to 718, the domain is characterized as EGF-like 2.
+At position 719 to 763, the domain is characterized as EGF-like 3; calcium-binding.
+At position 764 to 809, the domain is characterized as EGF-like 4; calcium-binding.
+At position 810 to 857, the domain is characterized as EGF-like 5; calcium-binding.
+At position 858 to 900, the domain is characterized as EGF-like 6; calcium-binding.
+At position 901 to 942, the domain is characterized as EGF-like 7; calcium-binding.
+At position 943 to 981, the domain is characterized as EGF-like 8; calcium-binding.
+At position 982 to 1024, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1025 to 1069, the domain is characterized as EGF-like 10; calcium-binding.
+At position 159 to 358, the domain is characterized as NodB homology.
+At position 6 to 129, the domain is characterized as VOC.
+At position 95 to 272, the domain is characterized as PXA.
+At position 533 to 663, the domain is characterized as PX.
+At position 690 to 967, the domain is characterized as Protein kinase.
+At position 52 to 229, the domain is characterized as BPL/LPL catalytic.
+At position 18 to 210, the domain is characterized as DPCK.
+At position 2 to 369, the domain is characterized as Protein kinase.
+At position 290 to 460, the domain is characterized as CYTH.
+At position 15 to 220, the domain is characterized as ABC transmembrane type-1.
+At position 11 to 93, the domain is characterized as Toprim.
+At position 24 to 224, the domain is characterized as GH16.
+At position 144 to 217, the domain is characterized as HTH crp-type.
+At position 198 to 296, the domain is characterized as Ig-like.
+At position 130 to 324, the domain is characterized as ATP-grasp.
+At position 6 to 100, the domain is characterized as ASCH.
+At position 280 to 361, the domain is characterized as PUA.
+At position 113 to 163, the domain is characterized as DHHC.
+At position 32 to 159, the domain is characterized as Ig-like V-type 1.
+At position 167 to 294, the domain is characterized as Ig-like V-type 2.
+At position 9 to 210, the domain is characterized as DhaL.
+At position 218 to 266, the domain is characterized as F-box.
+At position 36 to 172, the domain is characterized as C-type lectin.
+At position 2 to 144, the domain is characterized as Era-type G.
+At position 282 to 360, the domain is characterized as RRM.
+At position 125 to 276, the domain is characterized as PA14.
+At position 4 to 91, the domain is characterized as GST N-terminal.
+At position 93 to 211, the domain is characterized as GST C-terminal.
+At position 31 to 282, the domain is characterized as Protein kinase.
+At position 438 to 623, the domain is characterized as N-acetyltransferase.
+At position 6 to 151, the domain is characterized as N-acetyltransferase 1.
+At position 153 to 301, the domain is characterized as N-acetyltransferase 2.
+At position 28 to 356, the domain is characterized as Alpha-carbonic anhydrase.
+At position 190 to 374, the domain is characterized as Helicase ATP-binding.
+At position 401 to 552, the domain is characterized as Helicase C-terminal.
+At position 141 to 216, the domain is characterized as Rho RNA-BD.
+At position 18 to 96, the domain is characterized as S1-like.
+At position 29 to 213, the domain is characterized as GH11.
+At position 259 to 559, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 6 to 378, the domain is characterized as Trm1 methyltransferase.
+At position 84 to 267, the domain is characterized as ATP-grasp.
+At position 1 to 145, the domain is characterized as SPX.
+At position 334 to 596, the domain is characterized as Protein kinase.
+At position 63 to 349, the domain is characterized as ABC transmembrane type-1 1.
+At position 384 to 620, the domain is characterized as ABC transporter 1.
+At position 720 to 1007, the domain is characterized as ABC transmembrane type-1 2.
+At position 1042 to 1279, the domain is characterized as ABC transporter 2.
+At position 141 to 350, the domain is characterized as ATP-grasp.
+At position 280 to 505, the domain is characterized as TLDc.
+At position 259 to 460, the domain is characterized as Peptidase M12B.
+At position 461 to 551, the domain is characterized as Disintegrin.
+At position 552 to 607, the domain is characterized as TSP type-1 1.
+At position 847 to 907, the domain is characterized as TSP type-1 2.
+At position 908 to 967, the domain is characterized as TSP type-1 3.
+At position 968 to 1022, the domain is characterized as TSP type-1 4.
+At position 1059 to 1097, the domain is characterized as PLAC.
+At position 405 to 455, the domain is characterized as DHHC.
+At position 51 to 163, the domain is characterized as Plastocyanin-like 1.
+At position 243 to 374, the domain is characterized as Plastocyanin-like 2.
+At position 421 to 548, the domain is characterized as Plastocyanin-like 3.
+At position 145 to 683, the domain is characterized as USP.
+At position 685 to 778, the domain is characterized as DUSP 1.
+At position 787 to 890, the domain is characterized as DUSP 2.
+At position 3 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 72 to 424, the domain is characterized as IF rod.
+At position 452 to 543, the domain is characterized as Cache.
+At position 2 to 131, the domain is characterized as DAGKc.
+At position 53 to 88, the domain is characterized as QLQ.
+At position 114 to 158, the domain is characterized as WRC.
+At position 26 to 258, the domain is characterized as PABS.
+At position 440 to 583, the domain is characterized as Thioredoxin.
+At position 49 to 240, the domain is characterized as DH.
+At position 271 to 392, the domain is characterized as PH.
+At position 421 to 496, the domain is characterized as DEP 1.
+At position 523 to 597, the domain is characterized as DEP 2.
+At position 625 to 703, the domain is characterized as PDZ.
+At position 28 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 131 to 219, the domain is characterized as Fibronectin type-III 2.
+At position 234 to 332, the domain is characterized as Fibronectin type-III 3.
+At position 18 to 81, the domain is characterized as TRAM.
+At position 13 to 137, the domain is characterized as ApaG.
+At position 135 to 229, the domain is characterized as Rhodanese.
+At position 171 to 256, the domain is characterized as Expansin-like CBD.
+At position 24 to 124, the domain is characterized as AB hydrolase-1.
+At position 64 to 345, the domain is characterized as Protein kinase.
+At position 67 to 105, the domain is characterized as EGF-like 1.
+At position 132 to 329, the domain is characterized as Laminin G-like 1.
+At position 336 to 528, the domain is characterized as Laminin G-like 2.
+At position 532 to 569, the domain is characterized as EGF-like 2.
+At position 574 to 747, the domain is characterized as Laminin G-like 3.
+At position 761 to 936, the domain is characterized as Laminin G-like 4.
+At position 939 to 976, the domain is characterized as EGF-like 3.
+At position 982 to 1180, the domain is characterized as Laminin G-like 5.
+At position 159 to 354, the domain is characterized as Peptidase M12A.
+At position 397 to 516, the domain is characterized as CUB.
+At position 532 to 564, the domain is characterized as ShKT.
+At position 275 to 528, the domain is characterized as Protein kinase.
+At position 23 to 100, the domain is characterized as UPAR/Ly6.
+At position 628 to 691, the domain is characterized as S1 motif.
+At position 82 to 258, the domain is characterized as FAD-binding PCMH-type.
+At position 900 to 965, the domain is characterized as HP.
+At position 13 to 196, the domain is characterized as RNase H type-2.
+At position 130 to 567, the domain is characterized as Urease.
+At position 901 to 1117, the domain is characterized as Histidine kinase.
+At position 456 to 525, the domain is characterized as PAH 3.
+At position 149 to 222, the domain is characterized as Ubiquitin-like.
+At position 30 to 248, the domain is characterized as tr-type G.
+At position 58 to 154, the domain is characterized as Ig-like C2-type 1.
+At position 160 to 246, the domain is characterized as Ig-like C2-type 2.
+At position 256 to 341, the domain is characterized as Ig-like C2-type 3.
+At position 14 to 79, the domain is characterized as Ubiquitin-like.
+At position 357 to 424, the domain is characterized as S4 RNA-binding.
+At position 362 to 447, the domain is characterized as Death.
+At position 337 to 388, the domain is characterized as FBD.
+At position 24 to 87, the domain is characterized as LCN-type CS-alpha/beta.
+At position 259 to 639, the domain is characterized as GRAS.
+At position 308 to 366, the domain is characterized as SH3.
+At position 10 to 54, the domain is characterized as CHCH.
+At position 15 to 198, the domain is characterized as HORMA.
+At position 124 to 160, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 26 to 104, the domain is characterized as Ubiquitin-like.
+At position 195 to 394, the domain is characterized as MAGE.
+At position 145 to 458, the domain is characterized as IF rod.
+At position 36 to 263, the domain is characterized as Radical SAM core.
+At position 52 to 287, the domain is characterized as Radical SAM core.
+At position 31 to 126, the domain is characterized as Phytocyanin.
+At position 247 to 440, the domain is characterized as GATase cobBQ-type.
+At position 1 to 170, the domain is characterized as 3'-5' exonuclease.
+At position 98 to 261, the domain is characterized as CP-type G.
+At position 25 to 209, the domain is characterized as RNase H type-2.
+At position 148 to 300, the domain is characterized as DDE Tnp4.
+At position 342 to 586, the domain is characterized as Clu.
+At position 147 to 242, the domain is characterized as Ig-like C2-type.
+At position 1 to 159, the domain is characterized as Ferritin-like diiron.
+At position 166 to 204, the domain is characterized as Rubredoxin-like.
+At position 449 to 602, the domain is characterized as Helicase C-terminal.
+At position 646 to 681, the domain is characterized as UVR.
+At position 20 to 94, the domain is characterized as H15.
+At position 1 to 156, the domain is characterized as DHFR.
+At position 10 to 144, the domain is characterized as EamA 1.
+At position 156 to 284, the domain is characterized as EamA 2.
+At position 75 to 166, the domain is characterized as PDZ.
+At position 32 to 147, the domain is characterized as Ig-like V-type.
+At position 153 to 247, the domain is characterized as Ig-like C2-type 1.
+At position 252 to 337, the domain is characterized as Ig-like C2-type 2.
+At position 87 to 147, the domain is characterized as S4 RNA-binding.
+At position 453 to 628, the domain is characterized as C2 PI3K-type.
+At position 643 to 819, the domain is characterized as PIK helical.
+At position 888 to 1166, the domain is characterized as PI3K/PI4K catalytic.
+At position 1199 to 1311, the domain is characterized as PX.
+At position 1328 to 1445, the domain is characterized as C2.
+At position 682 to 763, the domain is characterized as ACT 1.
+At position 21 to 108, the domain is characterized as Acylphosphatase-like.
+At position 332 to 361, the domain is characterized as LRRCT.
+At position 108 to 195, the domain is characterized as PDZ.
+At position 107 to 163, the domain is characterized as J.
+At position 1 to 200, the domain is characterized as RNase H type-2.
+At position 16 to 61, the domain is characterized as F-box.
+At position 13 to 195, the domain is characterized as tr-type G.
+At position 1325 to 1844, the domain is characterized as FAT.
+At position 1939 to 2250, the domain is characterized as PI3K/PI4K catalytic.
+At position 2250 to 2282, the domain is characterized as FATC.
+At position 185 to 243, the domain is characterized as Pre-SET.
+At position 246 to 369, the domain is characterized as SET.
+At position 390 to 406, the domain is characterized as Post-SET.
+At position 325 to 370, the domain is characterized as UBA.
+At position 32 to 209, the domain is characterized as FAD-binding PCMH-type.
+At position 10 to 43, the domain is characterized as WW 1.
+At position 697 to 820, the domain is characterized as C2.
+At position 58 to 172, the domain is characterized as Thioredoxin.
+At position 136 to 243, the domain is characterized as Fibronectin type-III 1.
+At position 343 to 439, the domain is characterized as Fibronectin type-III 2.
+At position 32 to 101, the domain is characterized as S1 motif 1.
+At position 119 to 183, the domain is characterized as S1 motif 2.
+At position 197 to 265, the domain is characterized as S1 motif 3.
+At position 106 to 181, the domain is characterized as Bromo.
+At position 250 to 331, the domain is characterized as NET.
+At position 886 to 1158, the domain is characterized as PKS/mFAS DH.
+At position 1659 to 1736, the domain is characterized as Carrier.
+At position 187 to 361, the domain is characterized as tr-type G.
+At position 495 to 554, the domain is characterized as SH3.
+At position 23 to 96, the domain is characterized as BTB.
+At position 698 to 846, the domain is characterized as uDENN.
+At position 868 to 1001, the domain is characterized as cDENN.
+At position 1003 to 1096, the domain is characterized as dDENN.
+At position 151 to 407, the domain is characterized as ABC transporter 1.
+At position 846 to 1090, the domain is characterized as ABC transporter 2.
+At position 30 to 145, the domain is characterized as Response regulatory.
+At position 121 to 276, the domain is characterized as GST C-terminal.
+At position 10 to 231, the domain is characterized as YjeF N-terminal.
+At position 277 to 568, the domain is characterized as YjeF C-terminal.
+At position 2 to 132, the domain is characterized as Pru.
+At position 340 to 654, the domain is characterized as Peptidase S8.
+At position 662 to 791, the domain is characterized as P/Homo B.
+At position 63 to 137, the domain is characterized as RRM.
+At position 1 to 254, the domain is characterized as Macro.
+At position 357 to 397, the domain is characterized as UBA.
+At position 15 to 84, the domain is characterized as J.
+At position 488 to 604, the domain is characterized as HD.
+At position 728 to 809, the domain is characterized as ACT 1.
+At position 839 to 918, the domain is characterized as ACT 2.
+At position 47 to 369, the domain is characterized as AB hydrolase-1.
+At position 448 to 505, the domain is characterized as Kazal-like.
+At position 19 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 115 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 306, the domain is characterized as Ig-like C2-type 3.
+At position 314 to 402, the domain is characterized as Ig-like C2-type 4.
+At position 408 to 501, the domain is characterized as Ig-like C2-type 5.
+At position 506 to 586, the domain is characterized as Ig-like C2-type 6.
+At position 690 to 784, the domain is characterized as Ig-like C2-type 8.
+At position 788 to 885, the domain is characterized as Ig-like C2-type 9.
+At position 887 to 984, the domain is characterized as Fibronectin type-III 1.
+At position 989 to 1088, the domain is characterized as Fibronectin type-III 2.
+At position 1093 to 1189, the domain is characterized as Fibronectin type-III 3.
+At position 1193 to 1288, the domain is characterized as Fibronectin type-III 4.
+At position 1278 to 1377, the domain is characterized as Ig-like C2-type 10.
+At position 1383 to 1477, the domain is characterized as Fibronectin type-III 5.
+At position 1478 to 1578, the domain is characterized as Fibronectin type-III 6.
+At position 116 to 292, the domain is characterized as Helicase ATP-binding.
+At position 307 to 472, the domain is characterized as Helicase C-terminal.
+At position 59 to 272, the domain is characterized as HD.
+At position 70 to 117, the domain is characterized as F-box.
+At position 124 to 404, the domain is characterized as Peptidase S1.
+At position 28 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 429 to 517, the domain is characterized as Ig-like C2-type 3.
+At position 521 to 613, the domain is characterized as Ig-like C2-type 4.
+At position 637 to 725, the domain is characterized as Ig-like C2-type 5.
+At position 735 to 830, the domain is characterized as Ig-like C2-type 6.
+At position 1084 to 1172, the domain is characterized as Ig-like C2-type 7.
+At position 1225 to 1313, the domain is characterized as Ig-like C2-type 8.
+At position 1321 to 1414, the domain is characterized as Fibronectin type-III.
+At position 1453 to 1708, the domain is characterized as Protein kinase.
+At position 1794 to 1885, the domain is characterized as Ig-like C2-type 9.
+At position 123 to 213, the domain is characterized as Ig-like C1-type.
+At position 47 to 109, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 245 to 371, the domain is characterized as RCK N-terminal.
+At position 205 to 419, the domain is characterized as NR LBD.
+At position 277 to 327, the domain is characterized as Myb-like.
+At position 1 to 223, the domain is characterized as ABC transporter.
+At position 110 to 322, the domain is characterized as SMP-LTD.
+At position 296 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 92 to 282, the domain is characterized as Protein kinase.
+At position 7 to 178, the domain is characterized as Josephin.
+At position 219 to 239, the domain is characterized as UIM 1.
+At position 247 to 264, the domain is characterized as UIM 2.
+At position 431 to 584, the domain is characterized as F5/8 type C 2.
+At position 646 to 812, the domain is characterized as MAM.
+At position 59 to 167, the domain is characterized as THUMP.
+At position 234 to 293, the domain is characterized as SH3.
+At position 57 to 326, the domain is characterized as Protein kinase.
+At position 91 to 226, the domain is characterized as GST C-terminal.
+At position 104 to 416, the domain is characterized as IF rod.
+At position 84 to 201, the domain is characterized as PX.
+At position 15 to 99, the domain is characterized as WWE.
+At position 116 to 331, the domain is characterized as PARP catalytic.
+At position 114 to 292, the domain is characterized as NodB homology.
+At position 204 to 269, the domain is characterized as KH 1.
+At position 285 to 352, the domain is characterized as KH 2.
+At position 417 to 482, the domain is characterized as KH 3.
+At position 499 to 565, the domain is characterized as KH 4.
+At position 1 to 139, the domain is characterized as HTH rrf2-type.
+At position 41 to 234, the domain is characterized as Helicase ATP-binding.
+At position 250 to 400, the domain is characterized as Helicase C-terminal.
+At position 17 to 324, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 97 to 360, the domain is characterized as Peptidase S8.
+At position 173 to 290, the domain is characterized as SET.
+At position 32 to 149, the domain is characterized as Fibronectin type-III.
+At position 81 to 202, the domain is characterized as GST C-terminal.
+At position 210 to 465, the domain is characterized as Protein kinase.
+At position 8 to 83, the domain is characterized as Carrier.
+At position 1 to 16, the domain is characterized as C1q.
+At position 4 to 304, the domain is characterized as SAM-dependent MTase C5-type.
+At position 75 to 148, the domain is characterized as Inhibitor I9.
+At position 94 to 402, the domain is characterized as IF rod.
+At position 36 to 258, the domain is characterized as Cache.
+At position 113 to 424, the domain is characterized as IF rod.
+At position 242 to 457, the domain is characterized as VWFA.
+At position 467 to 546, the domain is characterized as Cache 1.
+At position 786 to 867, the domain is characterized as Cache 2.
+At position 97 to 182, the domain is characterized as CTCK.
+At position 2 to 148, the domain is characterized as Clp R.
+At position 197 to 369, the domain is characterized as EngA-type G 2.
+At position 24 to 243, the domain is characterized as AB hydrolase-1.
+At position 592 to 865, the domain is characterized as Protein kinase.
+At position 149 to 338, the domain is characterized as CheB-type methylesterase.
+At position 45 to 303, the domain is characterized as Protein kinase.
+At position 162 to 224, the domain is characterized as t-SNARE coiled-coil homology.
+At position 103 to 200, the domain is characterized as BRICHOS.
+At position 26 to 505, the domain is characterized as PPM-type phosphatase.
+At position 167 to 425, the domain is characterized as MHD.
+At position 1 to 296, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 276 to 582, the domain is characterized as UvrD-like helicase C-terminal.
+At position 406 to 590, the domain is characterized as Helicase ATP-binding.
+At position 624 to 778, the domain is characterized as Helicase C-terminal.
+At position 232 to 293, the domain is characterized as BTB.
+At position 413 to 538, the domain is characterized as CBM6 1.
+At position 740 to 863, the domain is characterized as CBM6 2.
+At position 141 to 367, the domain is characterized as Sigma-54 factor interaction.
+At position 1 to 273, the domain is characterized as CheR-type methyltransferase.
+At position 26 to 274, the domain is characterized as ABC transporter.
+At position 1002 to 1282, the domain is characterized as Protein kinase.
+At position 123 to 154, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 156 to 185, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 3 to 28, the domain is characterized as LCN-type CS-alpha/beta.
+At position 558 to 612, the domain is characterized as FHA.
+At position 370 to 414, the domain is characterized as FBD.
+At position 128 to 310, the domain is characterized as Guanylate kinase-like.
+At position 295 to 372, the domain is characterized as RRM.
+At position 1 to 111, the domain is characterized as Ig-like.
+At position 677 to 723, the domain is characterized as G-patch.
+At position 413 to 491, the domain is characterized as POLO box 1.
+At position 509 to 595, the domain is characterized as POLO box 2.
+At position 1 to 257, the domain is characterized as CheR-type methyltransferase.
+At position 42 to 271, the domain is characterized as Cupin type-1 1.
+At position 332 to 481, the domain is characterized as Cupin type-1 2.
+At position 13 to 169, the domain is characterized as N-acetyltransferase.
+At position 299 to 509, the domain is characterized as ABC transmembrane type-2.
+At position 560 to 620, the domain is characterized as KH.
+At position 651 to 710, the domain is characterized as S1 motif.
+At position 102 to 246, the domain is characterized as VPS9.
+At position 156 to 215, the domain is characterized as CBS 2.
+At position 211 to 273, the domain is characterized as BTB 1.
+At position 351 to 420, the domain is characterized as BTB 2.
+At position 466 to 537, the domain is characterized as BACK.
+At position 3 to 94, the domain is characterized as CARD.
+At position 679 to 791, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 862 to 940, the domain is characterized as POLO box.
+At position 355 to 553, the domain is characterized as B30.2/SPRY.
+At position 64 to 277, the domain is characterized as Radical SAM core.
+At position 100 to 195, the domain is characterized as FAD-binding FR-type.
+At position 96 to 213, the domain is characterized as Ferric oxidoreductase.
+At position 240 to 366, the domain is characterized as FAD-binding FR-type.
+At position 131 to 204, the domain is characterized as HTH crp-type.
+At position 37 to 115, the domain is characterized as Cystatin.
+At position 23 to 216, the domain is characterized as RNase H type-2.
+At position 12 to 294, the domain is characterized as Protein kinase.
+At position 59 to 278, the domain is characterized as Laminin G-like.
+At position 54 to 215, the domain is characterized as TLDc.
+At position 270 to 373, the domain is characterized as Cystatin kininogen-type 3.
+At position 53 to 86, the domain is characterized as WW 1.
+At position 100 to 133, the domain is characterized as WW 2.
+At position 690 to 810, the domain is characterized as C2.
+At position 1 to 58, the domain is characterized as TRAM.
+At position 192 to 332, the domain is characterized as DOD-type homing endonuclease.
+At position 30 to 270, the domain is characterized as ABC transporter.
+At position 100 to 280, the domain is characterized as PCI.
+At position 6 to 179, the domain is characterized as PCI.
+At position 53 to 152, the domain is characterized as SWIRM.
+At position 27 to 192, the domain is characterized as Helicase ATP-binding.
+At position 31 to 223, the domain is characterized as TR mART core.
+At position 54 to 87, the domain is characterized as WW 2.
+At position 164 to 282, the domain is characterized as PH.
+At position 305 to 488, the domain is characterized as Helicase ATP-binding.
+At position 513 to 661, the domain is characterized as Helicase C-terminal.
+At position 26 to 253, the domain is characterized as Methyl-accepting transducer.
+At position 321 to 701, the domain is characterized as PIPK.
+At position 1693 to 1722, the domain is characterized as IQ.
+At position 1 to 460, the domain is characterized as SPX.
+At position 717 to 927, the domain is characterized as EXS.
+At position 262 to 322, the domain is characterized as HTH myb-type.
+At position 5 to 94, the domain is characterized as GLUE N-terminal.
+At position 170 to 203, the domain is characterized as GLUE C-terminal.
+At position 280 to 385, the domain is characterized as Toprim.
+At position 430 to 698, the domain is characterized as SF4 helicase.
+At position 66 to 283, the domain is characterized as Radical SAM core.
+At position 42 to 340, the domain is characterized as GH10.
+At position 361 to 477, the domain is characterized as Ricin B-type lectin.
+At position 60 to 132, the domain is characterized as Bromo 1.
+At position 378 to 450, the domain is characterized as Bromo 2.
+At position 633 to 730, the domain is characterized as NET.
+At position 89 to 248, the domain is characterized as CP-type G.
+At position 490 to 663, the domain is characterized as Helicase C-terminal.
+At position 80 to 266, the domain is characterized as VWFD 1.
+At position 319 to 494, the domain is characterized as VWFD 2.
+At position 153 to 356, the domain is characterized as ABC transmembrane type-1.
+At position 174 to 435, the domain is characterized as Peptidase M66.
+At position 1 to 71, the domain is characterized as Core-binding (CB).
+At position 90 to 242, the domain is characterized as Tyr recombinase.
+At position 218 to 278, the domain is characterized as KH.
+At position 354 to 464, the domain is characterized as HD.
+At position 467 to 589, the domain is characterized as HD.
+At position 711 to 786, the domain is characterized as ACT 1.
+At position 822 to 892, the domain is characterized as ACT 2.
+At position 653 to 726, the domain is characterized as RRM.
+At position 409 to 474, the domain is characterized as Dockerin.
+At position 182 to 413, the domain is characterized as Radical SAM core.
+At position 415 to 480, the domain is characterized as TRAM.
+At position 449 to 618, the domain is characterized as tr-type G.
+At position 3 to 124, the domain is characterized as N-acetyltransferase.
+At position 231 to 566, the domain is characterized as Peptidase S8.
+At position 1 to 102, the domain is characterized as ABC transmembrane type-1.
+At position 6 to 96, the domain is characterized as ASCH.
+At position 16 to 91, the domain is characterized as HTH asnC-type.
+At position 381 to 813, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1297 to 1604, the domain is characterized as PKS/mFAS DH.
+At position 1653 to 1730, the domain is characterized as Carrier 1.
+At position 1779 to 1856, the domain is characterized as Carrier 2.
+At position 178 to 364, the domain is characterized as CheB-type methylesterase.
+At position 100 to 366, the domain is characterized as Protein kinase.
+At position 35 to 63, the domain is characterized as LRRNT.
+At position 314 to 365, the domain is characterized as LRRCT.
+At position 13 to 204, the domain is characterized as Lon N-terminal.
+At position 43 to 92, the domain is characterized as bHLH.
+At position 16 to 95, the domain is characterized as RRM 1.
+At position 213 to 287, the domain is characterized as RRM 2.
+At position 200 to 265, the domain is characterized as HTH luxR-type.
+At position 627 to 661, the domain is characterized as EGF-like 1.
+At position 782 to 816, the domain is characterized as EGF-like 2.
+At position 818 to 852, the domain is characterized as EGF-like 3.
+At position 896 to 933, the domain is characterized as EGF-like 4.
+At position 975 to 1008, the domain is characterized as EGF-like 5.
+At position 1043 to 1077, the domain is characterized as EGF-like 6.
+At position 1161 to 1194, the domain is characterized as EGF-like 7.
+At position 430 to 583, the domain is characterized as Helicase C-terminal.
+At position 278 to 391, the domain is characterized as PAZ.
+At position 555 to 847, the domain is characterized as Piwi.
+At position 41 to 250, the domain is characterized as MARVEL.
+At position 386 to 493, the domain is characterized as OCEL.
+At position 168 to 344, the domain is characterized as Helicase ATP-binding.
+At position 355 to 518, the domain is characterized as Helicase C-terminal.
+At position 147 to 239, the domain is characterized as BACK.
+At position 381 to 594, the domain is characterized as Rho-GAP.
+At position 256 to 316, the domain is characterized as LIM zinc-binding 1.
+At position 318 to 375, the domain is characterized as LIM zinc-binding 2.
+At position 376 to 435, the domain is characterized as LIM zinc-binding 3.
+At position 17 to 152, the domain is characterized as HTH marR-type.
+At position 1 to 208, the domain is characterized as CYTH.
+At position 28 to 149, the domain is characterized as FZ.
+At position 1 to 322, the domain is characterized as SPX.
+At position 581 to 775, the domain is characterized as EXS.
+At position 116 to 305, the domain is characterized as ATP-grasp.
+At position 2 to 58, the domain is characterized as HTH lacI-type.
+At position 125 to 416, the domain is characterized as Peptidase S8.
+At position 145 to 232, the domain is characterized as TonB C-terminal.
+At position 109 to 297, the domain is characterized as N-acetyltransferase.
+At position 143 to 342, the domain is characterized as Peptidase M12A.
+At position 344 to 456, the domain is characterized as CUB 1.
+At position 457 to 569, the domain is characterized as CUB 2.
+At position 569 to 610, the domain is characterized as EGF-like 1; calcium-binding.
+At position 613 to 725, the domain is characterized as CUB 3.
+At position 725 to 765, the domain is characterized as EGF-like 2; calcium-binding.
+At position 769 to 881, the domain is characterized as CUB 4.
+At position 882 to 998, the domain is characterized as CUB 5.
+At position 437 to 567, the domain is characterized as Guanylate cyclase.
+At position 408 to 605, the domain is characterized as FtsK.
+At position 98 to 169, the domain is characterized as SUI1.
+At position 89 to 159, the domain is characterized as DPH-type MB.
+At position 262 to 392, the domain is characterized as MPN.
+At position 21 to 136, the domain is characterized as WH1.
+At position 22 to 120, the domain is characterized as HTH araC/xylS-type.
+At position 214 to 484, the domain is characterized as SF4 helicase; first part.
+At position 534 to 683, the domain is characterized as DOD-type homing endonuclease.
+At position 646 to 915, the domain is characterized as SF4 helicase; second part.
+At position 307 to 466, the domain is characterized as ELMO.
+At position 72 to 114, the domain is characterized as CHCH.
+At position 6 to 425, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 951 to 1260, the domain is characterized as PKS/mFAS DH.
+At position 2444 to 2521, the domain is characterized as Carrier.
+At position 52 to 105, the domain is characterized as J.
+At position 180 to 354, the domain is characterized as PCI.
+At position 219 to 412, the domain is characterized as Helicase ATP-binding.
+At position 51 to 112, the domain is characterized as CBS 1.
+At position 214 to 271, the domain is characterized as CBS 3.
+At position 297 to 362, the domain is characterized as CBS 4.
+At position 514 to 692, the domain is characterized as Helicase ATP-binding.
+At position 703 to 867, the domain is characterized as Helicase C-terminal.
+At position 358 to 462, the domain is characterized as Fibronectin type-III 1.
+At position 468 to 560, the domain is characterized as Fibronectin type-III 2.
+At position 838 to 938, the domain is characterized as Fibronectin type-III 3.
+At position 1227 to 1317, the domain is characterized as Fibronectin type-III 4.
+At position 1324 to 1430, the domain is characterized as Fibronectin type-III 5.
+At position 1711 to 1814, the domain is characterized as Fibronectin type-III 6.
+At position 1821 to 1920, the domain is characterized as Fibronectin type-III 7.
+At position 1922 to 2010, the domain is characterized as Fibronectin type-III 8.
+At position 2014 to 2132, the domain is characterized as Fibronectin type-III 9.
+At position 2224 to 2495, the domain is characterized as Protein kinase.
+At position 1 to 100, the domain is characterized as B30.2/SPRY.
+At position 368 to 398, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 79 to 269, the domain is characterized as RNase H type-2.
+At position 39 to 388, the domain is characterized as IF rod.
+At position 420 to 538, the domain is characterized as LTD.
+At position 69 to 130, the domain is characterized as HMA 2.
+At position 226 to 289, the domain is characterized as HMA 3.
+At position 5 to 127, the domain is characterized as TIR.
+At position 208 to 349, the domain is characterized as Helicase ATP-binding.
+At position 359 to 523, the domain is characterized as Helicase C-terminal.
+At position 343 to 504, the domain is characterized as Helicase ATP-binding.
+At position 558 to 713, the domain is characterized as Helicase C-terminal.
+At position 78 to 171, the domain is characterized as Toprim.
+At position 30 to 115, the domain is characterized as Fibronectin type-III 1.
+At position 339 to 435, the domain is characterized as Fibronectin type-III 2.
+At position 445 to 541, the domain is characterized as Fibronectin type-III 3.
+At position 542 to 638, the domain is characterized as Fibronectin type-III 4.
+At position 641 to 734, the domain is characterized as Fibronectin type-III 5.
+At position 735 to 827, the domain is characterized as Fibronectin type-III 6.
+At position 948 to 1205, the domain is characterized as Tyrosine-protein phosphatase.
+At position 13 to 74, the domain is characterized as CBS 1.
+At position 74 to 133, the domain is characterized as CBS 2.
+At position 139 to 195, the domain is characterized as CBS 3.
+At position 217 to 274, the domain is characterized as CBS 4.
+At position 495 to 576, the domain is characterized as PB1.
+At position 183 to 496, the domain is characterized as IF rod.
+At position 307 to 556, the domain is characterized as NR LBD.
+At position 44 to 131, the domain is characterized as Phosphagen kinase N-terminal.
+At position 3 to 67, the domain is characterized as LCN-type CS-alpha/beta.
+At position 104 to 180, the domain is characterized as Biotinyl-binding.
+At position 30 to 168, the domain is characterized as Nudix hydrolase.
+At position 546 to 621, the domain is characterized as Cytochrome b5 heme-binding.
+At position 648 to 759, the domain is characterized as FAD-binding FR-type.
+At position 11 to 445, the domain is characterized as Helicase ATP-binding.
+At position 35 to 113, the domain is characterized as GIY-YIG.
+At position 223 to 258, the domain is characterized as UVR.
+At position 300 to 553, the domain is characterized as Glutamine amidotransferase type-1.
+At position 427 to 587, the domain is characterized as N-acetyltransferase.
+At position 97 to 166, the domain is characterized as POTRA.
+At position 506 to 579, the domain is characterized as BTB.
+At position 301 to 538, the domain is characterized as Glutamine amidotransferase type-1.
+At position 469 to 608, the domain is characterized as Thioredoxin.
+At position 47 to 372, the domain is characterized as RHD.
+At position 804 to 891, the domain is characterized as Death.
+At position 3 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 104 to 204, the domain is characterized as FAD-binding FR-type.
+At position 378 to 461, the domain is characterized as TRAM.
+At position 520 to 595, the domain is characterized as Cytochrome b5 heme-binding.
+At position 264 to 443, the domain is characterized as RHD.
+At position 93 to 144, the domain is characterized as HTH myb-type 1.
+At position 145 to 199, the domain is characterized as HTH myb-type 2.
+At position 5 to 113, the domain is characterized as VOC.
+At position 163 to 447, the domain is characterized as Protein kinase.
+At position 52 to 194, the domain is characterized as SCP.
+At position 2 to 257, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 139 to 292, the domain is characterized as Nudix hydrolase.
+At position 135 to 189, the domain is characterized as HTH cro/C1-type.
+At position 12 to 696, the domain is characterized as Myosin motor.
+At position 699 to 728, the domain is characterized as IQ 1.
+At position 722 to 751, the domain is characterized as IQ 2.
+At position 850 to 1024, the domain is characterized as TH1.
+At position 35 to 195, the domain is characterized as SIS.
+At position 11 to 341, the domain is characterized as DhaK.
+At position 381 to 585, the domain is characterized as DhaL.
+At position 16 to 90, the domain is characterized as AFP-like.
+At position 20 to 199, the domain is characterized as Guanylate kinase-like.
+At position 225 to 264, the domain is characterized as PAS.
+At position 347 to 542, the domain is characterized as Histidine kinase.
+At position 841 to 1099, the domain is characterized as Protein kinase.
+At position 2 to 254, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 260 to 506, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 212 to 254, the domain is characterized as EGF-like 1.
+At position 256 to 301, the domain is characterized as EGF-like 2.
+At position 303 to 343, the domain is characterized as EGF-like 3.
+At position 370 to 424, the domain is characterized as Ig-like C2-type 2.
+At position 444 to 543, the domain is characterized as Fibronectin type-III 1.
+At position 546 to 640, the domain is characterized as Fibronectin type-III 2.
+At position 644 to 737, the domain is characterized as Fibronectin type-III 3.
+At position 837 to 1116, the domain is characterized as Protein kinase.
+At position 16 to 80, the domain is characterized as BTB 1.
+At position 165 to 280, the domain is characterized as MATH 1.
+At position 455 to 552, the domain is characterized as MATH 2.
+At position 576 to 644, the domain is characterized as BTB 2.
+At position 220 to 440, the domain is characterized as Letm1 RBD.
+At position 652 to 733, the domain is characterized as S1 motif.
+At position 161 to 344, the domain is characterized as MIF4G.
+At position 453 to 569, the domain is characterized as MI.
+At position 22 to 258, the domain is characterized as CN hydrolase.
+At position 400 to 843, the domain is characterized as Urease.
+At position 121 to 246, the domain is characterized as Fe2OG dioxygenase.
+At position 259 to 299, the domain is characterized as ShKT.
+At position 21 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 198 to 305, the domain is characterized as Ig-like C2-type 3.
+At position 310 to 395, the domain is characterized as Ig-like C2-type 4.
+At position 410 to 504, the domain is characterized as Fibronectin type-III 1.
+At position 510 to 600, the domain is characterized as Fibronectin type-III 2.
+At position 605 to 700, the domain is characterized as Fibronectin type-III 3.
+At position 710 to 800, the domain is characterized as Fibronectin type-III 4.
+At position 825 to 924, the domain is characterized as Fibronectin type-III 5.
+At position 926 to 1023, the domain is characterized as Fibronectin type-III 6.
+At position 72 to 270, the domain is characterized as Helicase ATP-binding.
+At position 258 to 438, the domain is characterized as Helicase C-terminal.
+At position 3 to 80, the domain is characterized as SH3.
+At position 112 to 300, the domain is characterized as Rho-GAP.
+At position 332 to 427, the domain is characterized as SH2 1.
+At position 622 to 716, the domain is characterized as SH2 2.
+At position 170 to 411, the domain is characterized as NR LBD.
+At position 137 to 383, the domain is characterized as Radical SAM core.
+At position 148 to 207, the domain is characterized as SH3.
+At position 248 to 342, the domain is characterized as PDZ.
+At position 1411 to 1474, the domain is characterized as SAM.
+At position 32 to 210, the domain is characterized as Guanylate kinase-like.
+At position 1 to 368, the domain is characterized as Protein kinase.
+At position 422 to 589, the domain is characterized as tr-type G.
+At position 108 to 181, the domain is characterized as Lipoyl-binding 2.
+At position 258 to 295, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 609 to 713, the domain is characterized as tRNA-binding.
+At position 106 to 134, the domain is characterized as IQ 1.
+At position 135 to 157, the domain is characterized as IQ 2.
+At position 647 to 711, the domain is characterized as SAM 1.
+At position 719 to 782, the domain is characterized as SAM 2.
+At position 804 to 876, the domain is characterized as SAM 3.
+At position 457 to 666, the domain is characterized as MCM.
+At position 30 to 98, the domain is characterized as MOSC.
+At position 148 to 210, the domain is characterized as t-SNARE coiled-coil homology.
+At position 133 to 227, the domain is characterized as BRICHOS.
+At position 356 to 467, the domain is characterized as PLAT.
+At position 409 to 503, the domain is characterized as B5.
+At position 724 to 820, the domain is characterized as FDX-ACB.
+At position 95 to 138, the domain is characterized as LysM.
+At position 209 to 267, the domain is characterized as GRAM.
+At position 709 to 870, the domain is characterized as TLDc.
+At position 812 to 1003, the domain is characterized as TH1.
+At position 210 to 470, the domain is characterized as NR LBD.
+At position 52 to 234, the domain is characterized as IRG-type G.
+At position 14 to 115, the domain is characterized as SH2.
+At position 116 to 176, the domain is characterized as SH3 1.
+At position 214 to 277, the domain is characterized as SH3 2.
+At position 650 to 817, the domain is characterized as MOSC.
+At position 79 to 220, the domain is characterized as C-type lectin.
+At position 205 to 368, the domain is characterized as Ig-like C2-type 2.
+At position 40 to 86, the domain is characterized as F-box.
+At position 24 to 121, the domain is characterized as BRCT.
+At position 32 to 82, the domain is characterized as 3'-5' exonuclease.
+At position 42 to 253, the domain is characterized as Helicase ATP-binding.
+At position 292 to 446, the domain is characterized as Helicase C-terminal.
+At position 46 to 154, the domain is characterized as CS.
+At position 438 to 681, the domain is characterized as Peptidase S1.
+At position 177 to 374, the domain is characterized as Peptidase M12B.
+At position 383 to 472, the domain is characterized as Disintegrin.
+At position 86 to 156, the domain is characterized as PDZ 1.
+At position 210 to 279, the domain is characterized as PDZ 2.
+At position 858 to 930, the domain is characterized as PDZ 3.
+At position 3 to 110, the domain is characterized as HIT.
+At position 359 to 476, the domain is characterized as BRCT.
+At position 517 to 571, the domain is characterized as 3'-5' exonuclease.
+At position 579 to 792, the domain is characterized as SEC7.
+At position 27 to 152, the domain is characterized as Thioredoxin 1.
+At position 367 to 496, the domain is characterized as Thioredoxin 2.
+At position 396 to 563, the domain is characterized as tr-type G.
+At position 12 to 122, the domain is characterized as PX.
+At position 1644 to 1716, the domain is characterized as PAH 1.
+At position 1726 to 1797, the domain is characterized as PAH 2.
+At position 2163 to 2216, the domain is characterized as Myb-like.
+At position 365 to 387, the domain is characterized as WH2.
+At position 57 to 172, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 196 to 303, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 270 to 319, the domain is characterized as bHLH.
+At position 176 to 260, the domain is characterized as BRCT 1.
+At position 110 to 406, the domain is characterized as Piwi.
+At position 153 to 203, the domain is characterized as bHLH.
+At position 24 to 160, the domain is characterized as EamA 1.
+At position 200 to 326, the domain is characterized as EamA 2.
+At position 17 to 92, the domain is characterized as GIY-YIG.
+At position 47 to 515, the domain is characterized as Sema.
+At position 517 to 568, the domain is characterized as PSI.
+At position 585 to 640, the domain is characterized as Ig-like C2-type.
+At position 80 to 182, the domain is characterized as PA.
+At position 2 to 73, the domain is characterized as KRAB.
+At position 7 to 244, the domain is characterized as GP-PDE.
+At position 86 to 168, the domain is characterized as Ig-like C2-type 1.
+At position 173 to 259, the domain is characterized as Ig-like C2-type 2.
+At position 275 to 363, the domain is characterized as Ig-like C2-type 3.
+At position 368 to 458, the domain is characterized as Ig-like C2-type 4.
+At position 462 to 551, the domain is characterized as Ig-like C2-type 5.
+At position 556 to 645, the domain is characterized as Ig-like C2-type 6.
+At position 652 to 748, the domain is characterized as Fibronectin type-III 1.
+At position 753 to 849, the domain is characterized as Fibronectin type-III 2.
+At position 854 to 952, the domain is characterized as Fibronectin type-III 3.
+At position 956 to 1050, the domain is characterized as Fibronectin type-III 4.
+At position 1054 to 1153, the domain is characterized as Fibronectin type-III 5.
+At position 1158 to 1256, the domain is characterized as Fibronectin type-III 6.
+At position 1261 to 1358, the domain is characterized as Fibronectin type-III 7.
+At position 1362 to 1456, the domain is characterized as Fibronectin type-III 8.
+At position 1461 to 1558, the domain is characterized as Fibronectin type-III 9.
+At position 1563 to 1681, the domain is characterized as Fibronectin type-III 10.
+At position 1686 to 1782, the domain is characterized as Fibronectin type-III 11.
+At position 1786 to 1881, the domain is characterized as Fibronectin type-III 12.
+At position 1884 to 1982, the domain is characterized as Fibronectin type-III 13.
+At position 216 to 275, the domain is characterized as SH3.
+At position 95 to 262, the domain is characterized as Helicase ATP-binding.
+At position 431 to 631, the domain is characterized as Helicase C-terminal.
+At position 23 to 329, the domain is characterized as Transferrin-like 1.
+At position 340 to 666, the domain is characterized as Transferrin-like 2.
+At position 100 to 135, the domain is characterized as EF-hand 1.
+At position 141 to 169, the domain is characterized as EF-hand 2.
+At position 170 to 202, the domain is characterized as EF-hand 3.
+At position 203 to 239, the domain is characterized as EF-hand 4.
+At position 240 to 269, the domain is characterized as EF-hand 5.
+At position 38 to 94, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 1367 to 1655, the domain is characterized as Autotransporter.
+At position 117 to 278, the domain is characterized as PA14.
+At position 217 to 363, the domain is characterized as TrmE-type G.
+At position 164 to 367, the domain is characterized as SMP-LTD.
+At position 358 to 481, the domain is characterized as C2 1.
+At position 504 to 628, the domain is characterized as C2 2.
+At position 632 to 749, the domain is characterized as C2 3.
+At position 962 to 1086, the domain is characterized as C2 4.
+At position 1230 to 1330, the domain is characterized as SH2.
+At position 430 to 617, the domain is characterized as Thioredoxin.
+At position 10 to 112, the domain is characterized as MTTase N-terminal.
+At position 221 to 256, the domain is characterized as UVR.
+At position 106 to 459, the domain is characterized as PTS EIIC type-1.
+At position 1 to 167, the domain is characterized as PCI.
+At position 101 to 241, the domain is characterized as GST C-terminal.
+At position 4 to 137, the domain is characterized as Toprim.
+At position 368 to 402, the domain is characterized as SAP.
+At position 76 to 129, the domain is characterized as bHLH.
+At position 165 to 215, the domain is characterized as PAS.
+At position 523 to 563, the domain is characterized as EGF-like 1.
+At position 664 to 708, the domain is characterized as EGF-like 2.
+At position 712 to 764, the domain is characterized as EGF-like 3.
+At position 1079 to 1201, the domain is characterized as Fibronectin type-III.
+At position 476 to 592, the domain is characterized as HD.
+At position 730 to 815, the domain is characterized as ACT 1.
+At position 838 to 913, the domain is characterized as ACT 2.
+At position 285 to 363, the domain is characterized as B5.
+At position 1 to 133, the domain is characterized as PIK helical.
+At position 770 to 1049, the domain is characterized as PI3K/PI4K catalytic.
+At position 272 to 476, the domain is characterized as B30.2/SPRY.
+At position 316 to 402, the domain is characterized as RRM.
+At position 511 to 872, the domain is characterized as PUM-HD.
+At position 21 to 157, the domain is characterized as N-acetyltransferase.
+At position 54 to 165, the domain is characterized as Thioredoxin.
+At position 116 to 153, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 649 to 736, the domain is characterized as Ras-associating.
+At position 158 to 318, the domain is characterized as SUN.
+At position 21 to 70, the domain is characterized as F-box.
+At position 60 to 161, the domain is characterized as Glutaredoxin.
+At position 136 to 367, the domain is characterized as Bin3-type SAM.
+At position 24 to 60, the domain is characterized as LRRNT.
+At position 189 to 241, the domain is characterized as LRRCT.
+At position 243 to 329, the domain is characterized as Ig-like C2-type 1.
+At position 339 to 425, the domain is characterized as Ig-like C2-type 2.
+At position 430 to 517, the domain is characterized as Ig-like C2-type 3.
+At position 518 to 607, the domain is characterized as Ig-like C2-type 4.
+At position 1409 to 1467, the domain is characterized as VWFC.
+At position 151 to 439, the domain is characterized as GT92.
+At position 72 to 218, the domain is characterized as HD.
+At position 93 to 170, the domain is characterized as Winged helix Storkhead-box1.
+At position 557 to 650, the domain is characterized as Big-1 1.
+At position 657 to 748, the domain is characterized as Big-1 2.
+At position 781 to 831, the domain is characterized as BIG2.
+At position 21 to 178, the domain is characterized as Ephrin RBD.
+At position 146 to 173, the domain is characterized as ITAM.
+At position 178 to 408, the domain is characterized as SMP-LTD.
+At position 253 to 451, the domain is characterized as Helicase ATP-binding.
+At position 508 to 665, the domain is characterized as Helicase C-terminal.
+At position 104 to 186, the domain is characterized as Ig-like C2-type 1.
+At position 191 to 277, the domain is characterized as Ig-like C2-type 2.
+At position 293 to 378, the domain is characterized as Ig-like C2-type 3.
+At position 386 to 476, the domain is characterized as Ig-like C2-type 4.
+At position 574 to 663, the domain is characterized as Ig-like C2-type 6.
+At position 670 to 766, the domain is characterized as Fibronectin type-III 1.
+At position 771 to 867, the domain is characterized as Fibronectin type-III 2.
+At position 872 to 970, the domain is characterized as Fibronectin type-III 3.
+At position 974 to 1068, the domain is characterized as Fibronectin type-III 4.
+At position 1072 to 1171, the domain is characterized as Fibronectin type-III 5.
+At position 1176 to 1274, the domain is characterized as Fibronectin type-III 6.
+At position 1279 to 1376, the domain is characterized as Fibronectin type-III 7.
+At position 1380 to 1474, the domain is characterized as Fibronectin type-III 8.
+At position 1479 to 1576, the domain is characterized as Fibronectin type-III 9.
+At position 1581 to 1699, the domain is characterized as Fibronectin type-III 10.
+At position 1704 to 1800, the domain is characterized as Fibronectin type-III 11.
+At position 1804 to 1899, the domain is characterized as Fibronectin type-III 12.
+At position 1902 to 2000, the domain is characterized as Fibronectin type-III 13.
+At position 22 to 127, the domain is characterized as Calponin-homology (CH) 1.
+At position 136 to 242, the domain is characterized as Calponin-homology (CH) 2.
+At position 729 to 764, the domain is characterized as EF-hand 1.
+At position 765 to 800, the domain is characterized as EF-hand 2.
+At position 742 to 1010, the domain is characterized as Autotransporter.
+At position 176 to 236, the domain is characterized as CTLH.
+At position 17 to 291, the domain is characterized as Protein kinase.
+At position 40 to 239, the domain is characterized as MAGE.
+At position 170 to 256, the domain is characterized as PPIase FKBP-type.
+At position 1264 to 1497, the domain is characterized as Fibrillar collagen NC1.
+At position 138 to 200, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 5 to 348, the domain is characterized as PUM-HD.
+At position 573 to 673, the domain is characterized as tRNA-binding.
+At position 20 to 282, the domain is characterized as Alpha-carbonic anhydrase.
+At position 291 to 458, the domain is characterized as Helicase ATP-binding.
+At position 627 to 788, the domain is characterized as Helicase C-terminal.
+At position 1 to 98, the domain is characterized as HD.
+At position 547 to 700, the domain is characterized as GGDEF.
+At position 209 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 373 to 511, the domain is characterized as RGS.
+At position 559 to 680, the domain is characterized as PX.
+At position 28 to 91, the domain is characterized as HMA.
+At position 78 to 168, the domain is characterized as Fibronectin type-III.
+At position 166 to 262, the domain is characterized as BRCT.
+At position 95 to 225, the domain is characterized as MATH.
+At position 265 to 338, the domain is characterized as BTB.
+At position 256 to 640, the domain is characterized as GRAS.
+At position 140 to 180, the domain is characterized as UBA.
+At position 603 to 668, the domain is characterized as J.
+At position 489 to 662, the domain is characterized as Helicase ATP-binding.
+At position 683 to 850, the domain is characterized as Helicase C-terminal.
+At position 1553 to 1588, the domain is characterized as EF-hand.
+At position 135 to 185, the domain is characterized as UBA 1.
+At position 320 to 360, the domain is characterized as UBA 2.
+At position 383 to 467, the domain is characterized as SWIB/MDM2.
+At position 491 to 564, the domain is characterized as SUI1.
+At position 21 to 143, the domain is characterized as Ig-like V-type.
+At position 92 to 126, the domain is characterized as SAP.
+At position 26 to 58, the domain is characterized as LisH.
+At position 64 to 121, the domain is characterized as CTLH.
+At position 19 to 96, the domain is characterized as GIY-YIG.
+At position 5 to 56, the domain is characterized as HTH psq-type.
+At position 703 to 787, the domain is characterized as BRCT.
+At position 431 to 484, the domain is characterized as FHA.
+At position 616 to 662, the domain is characterized as G-patch.
+At position 76 to 175, the domain is characterized as HD.
+At position 421 to 482, the domain is characterized as TGS.
+At position 685 to 759, the domain is characterized as ACT.
+At position 54 to 124, the domain is characterized as POTRA.
+At position 1 to 198, the domain is characterized as RNase H type-2.
+At position 48 to 134, the domain is characterized as Cystatin.
+At position 34 to 86, the domain is characterized as Kazal-like.
+At position 87 to 153, the domain is characterized as Thyroglobulin type-1 1.
+At position 213 to 281, the domain is characterized as Thyroglobulin type-1 2.
+At position 73 to 247, the domain is characterized as CRAL-TRIO.
+At position 271 to 380, the domain is characterized as GOLD.
+At position 13 to 199, the domain is characterized as RNase H type-2.
+At position 194 to 259, the domain is characterized as KH 1.
+At position 275 to 342, the domain is characterized as KH 2.
+At position 408 to 473, the domain is characterized as KH 3.
+At position 490 to 556, the domain is characterized as KH 4.
+At position 174 to 260, the domain is characterized as PPIase FKBP-type.
+At position 524 to 743, the domain is characterized as FtsK.
+At position 160 to 413, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 348, the domain is characterized as SPX.
+At position 607 to 807, the domain is characterized as EXS.
+At position 71 to 423, the domain is characterized as IF rod.
+At position 289 to 434, the domain is characterized as Helicase C-terminal.
+At position 353 to 514, the domain is characterized as Helicase C-terminal.
+At position 542 to 669, the domain is characterized as RLR CTR.
+At position 27 to 63, the domain is characterized as LRRNT.
+At position 192 to 244, the domain is characterized as LRRCT.
+At position 342 to 428, the domain is characterized as Ig-like C2-type 2.
+At position 433 to 520, the domain is characterized as Ig-like C2-type 3.
+At position 521 to 610, the domain is characterized as Ig-like C2-type 4.
+At position 1413 to 1471, the domain is characterized as VWFC.
+At position 218 to 282, the domain is characterized as S5 DRBM.
+At position 153 to 407, the domain is characterized as Protein kinase.
+At position 408 to 479, the domain is characterized as AGC-kinase C-terminal.
+At position 20 to 352, the domain is characterized as PTS EIIC type-2.
+At position 426 to 518, the domain is characterized as PTS EIIB type-2.
+At position 927 to 1018, the domain is characterized as Fibronectin type-III 1.
+At position 1159 to 1255, the domain is characterized as Fibronectin type-III 2.
+At position 1250 to 1357, the domain is characterized as CBM20.
+At position 375 to 453, the domain is characterized as RRM 3.
+At position 84 to 387, the domain is characterized as Peptidase A1.
+At position 241 to 610, the domain is characterized as GH18.
+At position 11 to 37, the domain is characterized as Ig-like C1-type.
+At position 17 to 95, the domain is characterized as Carrier 1.
+At position 116 to 541, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1232 to 1309, the domain is characterized as Carrier 2.
+At position 31 to 96, the domain is characterized as VWFC 1.
+At position 109 to 175, the domain is characterized as VWFC 2.
+At position 250 to 315, the domain is characterized as VWFC 3.
+At position 38 to 120, the domain is characterized as SCAN box.
+At position 189 to 371, the domain is characterized as FAD-binding PCMH-type.
+At position 124 to 364, the domain is characterized as TLC.
+At position 24 to 318, the domain is characterized as FAE.
+At position 502 to 665, the domain is characterized as Helicase ATP-binding.
+At position 687 to 862, the domain is characterized as Helicase C-terminal.
+At position 221 to 414, the domain is characterized as Helicase ATP-binding.
+At position 425 to 586, the domain is characterized as Helicase C-terminal.
+At position 659 to 938, the domain is characterized as Autotransporter.
+At position 117 to 187, the domain is characterized as BTB.
+At position 19 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 163 to 411, the domain is characterized as ABC transporter 1.
+At position 846 to 1089, the domain is characterized as ABC transporter 2.
+At position 84 to 332, the domain is characterized as ABC transporter.
+At position 975 to 1050, the domain is characterized as Carrier.
+At position 95 to 368, the domain is characterized as Calpain catalytic.
+At position 464 to 633, the domain is characterized as tr-type G.
+At position 18 to 66, the domain is characterized as F-box.
+At position 156 to 426, the domain is characterized as SF4 helicase; first part.
+At position 308 to 566, the domain is characterized as SF4 helicase; second part.
+At position 24 to 212, the domain is characterized as RNase H type-2.
+At position 4 to 161, the domain is characterized as 3'-5' exonuclease.
+At position 338 to 402, the domain is characterized as S4 RNA-binding.
+At position 30 to 155, the domain is characterized as Thioredoxin.
+At position 400 to 509, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 317 to 454, the domain is characterized as C-CAP/cofactor C-like.
+At position 156 to 209, the domain is characterized as Myb-like 1.
+At position 244 to 298, the domain is characterized as Myb-like 2.
+At position 137 to 289, the domain is characterized as N-acetyltransferase.
+At position 253 to 285, the domain is characterized as WW.
+At position 370 to 509, the domain is characterized as PID 1.
+At position 542 to 699, the domain is characterized as PID 2.
+At position 583 to 704, the domain is characterized as PTB.
+At position 3 to 121, the domain is characterized as CMP/dCMP-type deaminase.
+At position 348 to 445, the domain is characterized as ERCC4.
+At position 34 to 206, the domain is characterized as Helicase ATP-binding.
+At position 234 to 384, the domain is characterized as Helicase C-terminal.
+At position 227 to 355, the domain is characterized as Galectin 2.
+At position 28 to 145, the domain is characterized as DOMON.
+At position 489 to 658, the domain is characterized as tr-type G.
+At position 492 to 592, the domain is characterized as PH.
+At position 1131 to 1378, the domain is characterized as PPM-type phosphatase.
+At position 142 to 235, the domain is characterized as PpiC.
+At position 149 to 209, the domain is characterized as KH.
+At position 276 to 369, the domain is characterized as HD.
+At position 232 to 252, the domain is characterized as ELK.
+At position 69 to 212, the domain is characterized as SCP.
+At position 417 to 473, the domain is characterized as HAMP.
+At position 513 to 734, the domain is characterized as Histidine kinase.
+At position 751 to 869, the domain is characterized as Response regulatory.
+At position 894 to 987, the domain is characterized as HPt.
+At position 245 to 459, the domain is characterized as Histidine kinase.
+At position 5 to 150, the domain is characterized as N-acetyltransferase.
+At position 405 to 552, the domain is characterized as PA14.
+At position 43 to 139, the domain is characterized as Expansin-like EG45.
+At position 210 to 409, the domain is characterized as Peptidase M12B.
+At position 417 to 503, the domain is characterized as Disintegrin.
+At position 649 to 681, the domain is characterized as EGF-like.
+At position 296 to 381, the domain is characterized as PDZ 1.
+At position 882 to 963, the domain is characterized as PDZ 2.
+At position 108 to 283, the domain is characterized as Prephenate dehydratase.
+At position 297 to 388, the domain is characterized as ACT.
+At position 42 to 76, the domain is characterized as SAP.
+At position 44 to 215, the domain is characterized as VWFA.
+At position 255 to 289, the domain is characterized as ShKT.
+At position 295 to 380, the domain is characterized as Ig-like C2-type.
+At position 485 to 543, the domain is characterized as Collagen-like.
+At position 318 to 468, the domain is characterized as PI-PLC X-box.
+At position 590 to 706, the domain is characterized as PI-PLC Y-box.
+At position 707 to 835, the domain is characterized as C2.
+At position 415 to 626, the domain is characterized as BURP.
+At position 44 to 74, the domain is characterized as EF-hand 2.
+At position 114 to 146, the domain is characterized as EF-hand 4.
+At position 133 to 227, the domain is characterized as Rhodanese.
+At position 34 to 281, the domain is characterized as PPM-type phosphatase.
+At position 398 to 557, the domain is characterized as N-acetyltransferase.
+At position 40 to 317, the domain is characterized as Protein kinase.
+At position 397 to 564, the domain is characterized as Phosphatase tensin-type.
+At position 570 to 708, the domain is characterized as C2 tensin-type.
+At position 1241 to 1305, the domain is characterized as J.
+At position 83 to 339, the domain is characterized as Protein kinase.
+At position 366 to 516, the domain is characterized as NTF2.
+At position 310 to 579, the domain is characterized as ABC transporter 1.
+At position 599 to 931, the domain is characterized as ABC transporter 2.
+At position 73 to 312, the domain is characterized as AB hydrolase-1.
+At position 593 to 876, the domain is characterized as Protein kinase.
+At position 160 to 473, the domain is characterized as IF rod.
+At position 112 to 171, the domain is characterized as CBS 1.
+At position 175 to 233, the domain is characterized as CBS 2.
+At position 11 to 128, the domain is characterized as PX.
+At position 353 to 487, the domain is characterized as PLAT.
+At position 1 to 119, the domain is characterized as CMP/dCMP-type deaminase.
+At position 16 to 170, the domain is characterized as TIR.
+At position 191 to 401, the domain is characterized as NB-ARC.
+At position 249 to 438, the domain is characterized as GATase cobBQ-type.
+At position 27 to 101, the domain is characterized as S1-like.
+At position 42 to 260, the domain is characterized as Radical SAM core.
+At position 8 to 102, the domain is characterized as Stress-response A/B barrel.
+At position 278 to 430, the domain is characterized as GAF 1.
+At position 462 to 643, the domain is characterized as GAF 2.
+At position 673 to 996, the domain is characterized as PDEase.
+At position 425 to 475, the domain is characterized as DHHC.
+At position 48 to 736, the domain is characterized as Myosin motor.
+At position 740 to 760, the domain is characterized as IQ 1.
+At position 761 to 786, the domain is characterized as IQ 2.
+At position 794 to 984, the domain is characterized as TH1.
+At position 1129 to 1189, the domain is characterized as SH3.
+At position 221 to 388, the domain is characterized as TrmE-type G.
+At position 1301 to 1366, the domain is characterized as J.
+At position 31 to 98, the domain is characterized as ACT 1.
+At position 259 to 333, the domain is characterized as ACT 2.
+At position 187 to 353, the domain is characterized as DDE Tnp4.
+At position 96 to 351, the domain is characterized as ABC transporter 1.
+At position 794 to 1037, the domain is characterized as ABC transporter 2.
+At position 771 to 928, the domain is characterized as HNH Cas9-type.
+At position 566 to 706, the domain is characterized as N-acetyltransferase.
+At position 69 to 229, the domain is characterized as CP-type G.
+At position 9 to 233, the domain is characterized as Radical SAM core.
+At position 45 to 146, the domain is characterized as SRCR 1.
+At position 170 to 283, the domain is characterized as SRCR 2.
+At position 308 to 408, the domain is characterized as SRCR 3.
+At position 418 to 526, the domain is characterized as SRCR 4.
+At position 130 to 216, the domain is characterized as PA.
+At position 398 to 589, the domain is characterized as PNPLA.
+At position 97 to 290, the domain is characterized as Peptidase M12A.
+At position 285 to 325, the domain is characterized as EGF-like.
+At position 336 to 449, the domain is characterized as CUB.
+At position 474 to 523, the domain is characterized as TSP type-1.
+At position 5 to 162, the domain is characterized as NAC.
+At position 30 to 91, the domain is characterized as FHA.
+At position 819 to 854, the domain is characterized as EF-hand 1.
+At position 855 to 890, the domain is characterized as EF-hand 2.
+At position 899 to 934, the domain is characterized as EF-hand 3.
+At position 1053 to 1235, the domain is characterized as Ferric oxidoreductase.
+At position 1236 to 1342, the domain is characterized as FAD-binding FR-type.
+At position 93 to 145, the domain is characterized as GST C-terminal.
+At position 1251 to 1317, the domain is characterized as HMA.
+At position 80 to 158, the domain is characterized as RRM 1.
+At position 168 to 245, the domain is characterized as RRM 2.
+At position 261 to 338, the domain is characterized as RRM 3.
+At position 364 to 441, the domain is characterized as RRM 4.
+At position 104 to 177, the domain is characterized as H15.
+At position 533 to 807, the domain is characterized as MYST-type HAT.
+At position 37 to 263, the domain is characterized as BURP.
+At position 15 to 138, the domain is characterized as EamA 1.
+At position 158 to 282, the domain is characterized as EamA 2.
+At position 844 to 1032, the domain is characterized as Reticulon.
+At position 328 to 637, the domain is characterized as NACHT.
+At position 1079 to 1364, the domain is characterized as FIIND.
+At position 1374 to 1463, the domain is characterized as CARD.
+At position 119 to 234, the domain is characterized as DOMON.
+At position 600 to 679, the domain is characterized as BRCT.
+At position 194 to 293, the domain is characterized as Fe2OG dioxygenase.
+At position 55 to 88, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 94 to 324, the domain is characterized as Radical SAM core.
+At position 186 to 326, the domain is characterized as FAS1 2.
+At position 311 to 357, the domain is characterized as G-patch.
+At position 15 to 148, the domain is characterized as Nudix hydrolase.
+At position 8 to 226, the domain is characterized as ABC transporter.
+At position 628 to 695, the domain is characterized as S1 motif.
+At position 185 to 237, the domain is characterized as bHLH.
+At position 22 to 142, the domain is characterized as C2.
+At position 45 to 137, the domain is characterized as DEP.
+At position 267 to 350, the domain is characterized as Toprim.
+At position 24 to 98, the domain is characterized as LCN-type CS-alpha/beta.
+At position 214 to 242, the domain is characterized as IQ 1.
+At position 243 to 265, the domain is characterized as IQ 2.
+At position 352 to 411, the domain is characterized as OVATE.
+At position 118 to 153, the domain is characterized as EF-hand 3.
+At position 162 to 197, the domain is characterized as EF-hand 4.
+At position 21 to 88, the domain is characterized as RRM 1.
+At position 170 to 256, the domain is characterized as RRM 2.
+At position 215 to 374, the domain is characterized as Tyrosine-protein phosphatase.
+At position 107 to 398, the domain is characterized as Protein kinase.
+At position 1490 to 2067, the domain is characterized as FAT.
+At position 2192 to 2512, the domain is characterized as PI3K/PI4K catalytic.
+At position 2499 to 2531, the domain is characterized as FATC.
+At position 13 to 185, the domain is characterized as FAD-binding PCMH-type.
+At position 34 to 138, the domain is characterized as Calponin-homology (CH) 1.
+At position 147 to 253, the domain is characterized as Calponin-homology (CH) 2.
+At position 778 to 813, the domain is characterized as EF-hand 1.
+At position 819 to 854, the domain is characterized as EF-hand 2.
+At position 86 to 359, the domain is characterized as Protein kinase.
+At position 377 to 475, the domain is characterized as RanBD1.
+At position 59 to 131, the domain is characterized as Histone-fold.
+At position 353 to 521, the domain is characterized as Helicase C-terminal.
+At position 496 to 665, the domain is characterized as tr-type G.
+At position 700 to 734, the domain is characterized as Anaphylatoxin-like.
+At position 1588 to 1735, the domain is characterized as NTR.
+At position 117 to 424, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 9 to 64, the domain is characterized as SANT.
+At position 169 to 442, the domain is characterized as ABC transporter 1.
+At position 520 to 733, the domain is characterized as ABC transmembrane type-2 1.
+At position 858 to 1110, the domain is characterized as ABC transporter 2.
+At position 1183 to 1397, the domain is characterized as ABC transmembrane type-2 2.
+At position 134 to 162, the domain is characterized as KOW.
+At position 62 to 97, the domain is characterized as EF-hand 1.
+At position 1 to 186, the domain is characterized as GMPS ATP-PPase.
+At position 213 to 399, the domain is characterized as Glutamine amidotransferase type-1.
+At position 129 to 566, the domain is characterized as Urease.
+At position 462 to 882, the domain is characterized as FH2.
+At position 125 to 209, the domain is characterized as PDZ.
+At position 5 to 34, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 50 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 84 to 113, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 31 to 132, the domain is characterized as Ig-like V-type.
+At position 110 to 321, the domain is characterized as Radical SAM core.
+At position 5 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 106 to 211, the domain is characterized as FAD-binding FR-type.
+At position 5 to 132, the domain is characterized as CMP/dCMP-type deaminase.
+At position 594 to 656, the domain is characterized as R3H.
+At position 720 to 767, the domain is characterized as G-patch.
+At position 13 to 88, the domain is characterized as U-box.
+At position 278 to 360, the domain is characterized as PDZ 2.
+At position 829 to 912, the domain is characterized as PDZ 3.
+At position 97 to 167, the domain is characterized as J.
+At position 137 to 248, the domain is characterized as Thioredoxin.
+At position 283 to 395, the domain is characterized as PRD 2.
+At position 7 to 290, the domain is characterized as Protein kinase.
+At position 301 to 335, the domain is characterized as KOW.
+At position 490 to 512, the domain is characterized as GoLoco 1.
+At position 543 to 565, the domain is characterized as GoLoco 2.
+At position 205 to 304, the domain is characterized as Toprim.
+At position 8 to 83, the domain is characterized as RRM.
+At position 175 to 452, the domain is characterized as MYST-type HAT.
+At position 26 to 336, the domain is characterized as Dynamin-type G.
+At position 618 to 704, the domain is characterized as GED.
+At position 2 to 203, the domain is characterized as CNNM transmembrane.
+At position 222 to 281, the domain is characterized as CBS 1.
+At position 897 to 953, the domain is characterized as HTH myb-type.
+At position 959 to 1010, the domain is characterized as Myb-like 1.
+At position 1268 to 1316, the domain is characterized as Myb-like 2.
+At position 32 to 85, the domain is characterized as Myosin N-terminal SH3-like.
+At position 89 to 787, the domain is characterized as Myosin motor.
+At position 790 to 819, the domain is characterized as IQ.
+At position 197 to 481, the domain is characterized as Dilute.
+At position 1 to 334, the domain is characterized as Trm1 methyltransferase.
+At position 46 to 180, the domain is characterized as MATH.
+At position 216 to 282, the domain is characterized as BTB.
+At position 680 to 920, the domain is characterized as VLIG-type G.
+At position 607 to 694, the domain is characterized as BRCT.
+At position 606 to 780, the domain is characterized as PCI.
+At position 60 to 167, the domain is characterized as PH.
+At position 213 to 412, the domain is characterized as Rho-GAP.
+At position 628 to 708, the domain is characterized as BRCT.
+At position 58 to 728, the domain is characterized as Myosin motor.
+At position 731 to 753, the domain is characterized as IQ 1.
+At position 754 to 783, the domain is characterized as IQ 2.
+At position 800 to 822, the domain is characterized as IQ 3.
+At position 823 to 852, the domain is characterized as IQ 4.
+At position 1003 to 1239, the domain is characterized as MyTH4 1.
+At position 1244 to 1554, the domain is characterized as FERM 1.
+At position 1552 to 1621, the domain is characterized as SH3.
+At position 1697 to 1845, the domain is characterized as MyTH4 2.
+At position 1851 to 2154, the domain is characterized as FERM 2.
+At position 404 to 436, the domain is characterized as EF-hand 2.
+At position 265 to 472, the domain is characterized as TRUD.
+At position 324 to 412, the domain is characterized as PPIase FKBP-type.
+At position 4 to 279, the domain is characterized as tr-type G.
+At position 97 to 201, the domain is characterized as C-type lectin.
+At position 20 to 81, the domain is characterized as PUB.
+At position 439 to 644, the domain is characterized as PAW.
+At position 14 to 200, the domain is characterized as RNase H type-2.
+At position 20 to 152, the domain is characterized as HTH marR-type.
+At position 38 to 129, the domain is characterized as ARID.
+At position 201 to 297, the domain is characterized as CRM 1.
+At position 319 to 415, the domain is characterized as CRM 2.
+At position 25 to 271, the domain is characterized as Pterin-binding.
+At position 537 to 614, the domain is characterized as PABC.
+At position 20 to 164, the domain is characterized as MPN.
+At position 40 to 103, the domain is characterized as KH; atypical.
+At position 1172 to 1282, the domain is characterized as SH2.
+At position 1310 to 1444, the domain is characterized as PTB.
+At position 201 to 457, the domain is characterized as NR LBD.
+At position 370 to 686, the domain is characterized as Protein kinase.
+At position 687 to 771, the domain is characterized as AGC-kinase C-terminal.
+At position 70 to 290, the domain is characterized as Radical SAM core.
+At position 20 to 106, the domain is characterized as GIY-YIG.
+At position 42 to 169, the domain is characterized as SCP.
+At position 578 to 764, the domain is characterized as Reticulon.
+At position 80 to 202, the domain is characterized as EamA 1.
+At position 233 to 357, the domain is characterized as EamA 2.
+At position 109 to 281, the domain is characterized as Helicase ATP-binding.
+At position 349 to 538, the domain is characterized as Helicase C-terminal.
+At position 223 to 411, the domain is characterized as Helicase ATP-binding.
+At position 37 to 263, the domain is characterized as Radical SAM core.
+At position 752 to 940, the domain is characterized as Reticulon.
+At position 25 to 314, the domain is characterized as GP-PDE.
+At position 225 to 324, the domain is characterized as FAD-binding FR-type.
+At position 113 to 395, the domain is characterized as Protein kinase.
+At position 3 to 117, the domain is characterized as MTTase N-terminal.
+At position 17 to 83, the domain is characterized as HTH gntR-type.
+At position 65 to 183, the domain is characterized as NlpC/P60.
+At position 154 to 382, the domain is characterized as Helicase ATP-binding.
+At position 394 to 556, the domain is characterized as Helicase C-terminal.
+At position 111 to 196, the domain is characterized as BMC.
+At position 143 to 216, the domain is characterized as HTH crp-type.
+At position 52 to 228, the domain is characterized as VWFA 1; binding site for platelet glycoprotein Ib.
+At position 273 to 430, the domain is characterized as VWFA 2.
+At position 3 to 126, the domain is characterized as MSP.
+At position 969 to 1167, the domain is characterized as Roc.
+At position 1694 to 1992, the domain is characterized as Protein kinase.
+At position 114 to 335, the domain is characterized as Radical SAM core.
+At position 53 to 273, the domain is characterized as Ch-type lysozyme.
+At position 8 to 344, the domain is characterized as DhaK.
+At position 384 to 587, the domain is characterized as DhaL.
+At position 218 to 361, the domain is characterized as FCP1 homology.
+At position 45 to 496, the domain is characterized as Hexokinase.
+At position 139 to 184, the domain is characterized as LRRCT.
+At position 1 to 95, the domain is characterized as YcgL.
+At position 54 to 348, the domain is characterized as PPM-type phosphatase.
+At position 24 to 112, the domain is characterized as RH1.
+At position 456 to 542, the domain is characterized as RH2.
+At position 29 to 131, the domain is characterized as EthD.
+At position 312 to 414, the domain is characterized as 3'-5' exonuclease.
+At position 22 to 73, the domain is characterized as Tudor-knot.
+At position 152 to 423, the domain is characterized as MYST-type HAT.
+At position 16 to 260, the domain is characterized as Protein kinase.
+At position 172 to 297, the domain is characterized as BAH.
+At position 335 to 868, the domain is characterized as SAM-dependent MTase C5-type.
+At position 437 to 500, the domain is characterized as Chromo.
+At position 104 to 295, the domain is characterized as Rho-GAP.
+At position 27 to 136, the domain is characterized as KRAB.
+At position 477 to 647, the domain is characterized as Helicase C-terminal.
+At position 87 to 215, the domain is characterized as VIT.
+At position 339 to 507, the domain is characterized as VWFA.
+At position 679 to 741, the domain is characterized as t-SNARE coiled-coil homology.
+At position 9 to 70, the domain is characterized as PWWP.
+At position 1059 to 1247, the domain is characterized as DH.
+At position 130 to 253, the domain is characterized as C2 2.
+At position 294 to 513, the domain is characterized as VWFA.
+At position 427 to 534, the domain is characterized as Rhodanese.
+At position 722 to 800, the domain is characterized as RRM 1.
+At position 819 to 896, the domain is characterized as RRM 2.
+At position 227 to 292, the domain is characterized as KH.
+At position 30 to 113, the domain is characterized as PB1.
+At position 264 to 532, the domain is characterized as Protein kinase.
+At position 533 to 604, the domain is characterized as AGC-kinase C-terminal.
+At position 207 to 526, the domain is characterized as NACHT.
+At position 840 to 1092, the domain is characterized as ABC transporter 2.
+At position 1165 to 1379, the domain is characterized as ABC transmembrane type-2 2.
+At position 199 to 354, the domain is characterized as C1q.
+At position 84 to 172, the domain is characterized as RRM.
+At position 1577 to 1694, the domain is characterized as SET.
+At position 1700 to 1716, the domain is characterized as Post-SET.
+At position 131 to 236, the domain is characterized as Fibronectin type-III 1.
+At position 240 to 330, the domain is characterized as Fibronectin type-III 2.
+At position 431 to 524, the domain is characterized as Fibronectin type-III 4.
+At position 527 to 624, the domain is characterized as Fibronectin type-III 5.
+At position 380 to 444, the domain is characterized as TRAM.
+At position 41 to 116, the domain is characterized as Inhibitor I9.
+At position 124 to 610, the domain is characterized as Peptidase S8.
+At position 175 to 292, the domain is characterized as SCP.
+At position 369 to 784, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1617 to 1691, the domain is characterized as Carrier 1.
+At position 1736 to 1812, the domain is characterized as Carrier 2.
+At position 401 to 482, the domain is characterized as B5.
+At position 718 to 811, the domain is characterized as FDX-ACB.
+At position 28 to 129, the domain is characterized as Phytocyanin.
+At position 131 to 457, the domain is characterized as G-alpha.
+At position 302 to 535, the domain is characterized as Glutamine amidotransferase type-1.
+At position 13 to 98, the domain is characterized as GS beta-grasp.
+At position 105 to 439, the domain is characterized as GS catalytic.
+At position 75 to 184, the domain is characterized as NB-ARC 1.
+At position 207 to 281, the domain is characterized as NB-ARC 2.
+At position 32 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 160 to 271, the domain is characterized as TBDR plug.
+At position 276 to 826, the domain is characterized as TBDR beta-barrel.
+At position 25 to 97, the domain is characterized as Importin N-terminal.
+At position 392 to 786, the domain is characterized as PDEase.
+At position 3 to 170, the domain is characterized as Miro 1.
+At position 308 to 343, the domain is characterized as EF-hand 2.
+At position 420 to 625, the domain is characterized as Miro 2.
+At position 270 to 361, the domain is characterized as PDZ 1.
+At position 367 to 458, the domain is characterized as PDZ 2.
+At position 1061 to 1497, the domain is characterized as CBP/p300-type HAT.
+At position 26 to 384, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 177 to 365, the domain is characterized as Helicase ATP-binding.
+At position 392 to 536, the domain is characterized as Helicase C-terminal.
+At position 34 to 92, the domain is characterized as VWFC.
+At position 1225 to 1460, the domain is characterized as Fibrillar collagen NC1.
+At position 1 to 49, the domain is characterized as C-type lysozyme.
+At position 318 to 835, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 844 to 910, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 57 to 183, the domain is characterized as BAH.
+At position 1 to 295, the domain is characterized as Protein kinase.
+At position 1730 to 1781, the domain is characterized as PAC.
+At position 1792 to 2018, the domain is characterized as Histidine kinase.
+At position 2211 to 2333, the domain is characterized as Response regulatory.
+At position 141 to 283, the domain is characterized as RNase III 1.
+At position 415 to 515, the domain is characterized as RNase III 2.
+At position 1 to 30, the domain is characterized as HTH myb-type.
+At position 36 to 142, the domain is characterized as Ig-like V-type.
+At position 146 to 233, the domain is characterized as Ig-like C2-type.
+At position 32 to 83, the domain is characterized as HTH myb-type 1.
+At position 84 to 139, the domain is characterized as HTH myb-type 2.
+At position 140 to 190, the domain is characterized as HTH myb-type 3.
+At position 22 to 184, the domain is characterized as MAM.
+At position 186 to 277, the domain is characterized as Ig-like C2-type.
+At position 382 to 480, the domain is characterized as Fibronectin type-III 2.
+At position 481 to 587, the domain is characterized as Fibronectin type-III 3.
+At position 589 to 671, the domain is characterized as Fibronectin type-III 4.
+At position 900 to 1154, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1186 to 1448, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 6 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 10 to 145, the domain is characterized as Response regulatory.
+At position 403 to 663, the domain is characterized as Protein kinase.
+At position 665 to 736, the domain is characterized as AGC-kinase C-terminal.
+At position 957 to 1051, the domain is characterized as Fibronectin type-III.
+At position 184 to 282, the domain is characterized as HTH araC/xylS-type.
+At position 25 to 325, the domain is characterized as Protein kinase.
+At position 16 to 122, the domain is characterized as Calponin-homology (CH).
+At position 388 to 417, the domain is characterized as IQ 1.
+At position 432 to 461, the domain is characterized as IQ 2.
+At position 460 to 638, the domain is characterized as DH.
+At position 940 to 1038, the domain is characterized as PH 1.
+At position 1271 to 1389, the domain is characterized as Arf-GAP.
+At position 1532 to 1631, the domain is characterized as PH 2.
+At position 25 to 125, the domain is characterized as Phytocyanin.
+At position 92 to 219, the domain is characterized as JmjC.
+At position 24 to 142, the domain is characterized as C2 1.
+At position 180 to 298, the domain is characterized as C2 2.
+At position 341 to 463, the domain is characterized as C2 3.
+At position 40 to 131, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 391 to 444, the domain is characterized as FHA.
+At position 457 to 963, the domain is characterized as GBD/FH3.
+At position 1072 to 1098, the domain is characterized as FH1.
+At position 1106 to 1495, the domain is characterized as FH2.
+At position 1563 to 1593, the domain is characterized as DAD.
+At position 272 to 299, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 71 to 279, the domain is characterized as ABC transmembrane type-1.
+At position 127 to 198, the domain is characterized as HARP 1.
+At position 231 to 302, the domain is characterized as HARP 2.
+At position 348 to 504, the domain is characterized as Helicase ATP-binding.
+At position 620 to 773, the domain is characterized as Helicase C-terminal.
+At position 389 to 478, the domain is characterized as Disintegrin.
+At position 617 to 650, the domain is characterized as EGF-like.
+At position 67 to 122, the domain is characterized as F-box.
+At position 680 to 776, the domain is characterized as IPT/TIG.
+At position 159 to 308, the domain is characterized as GAF.
+At position 351 to 589, the domain is characterized as Histidine kinase.
+At position 93 to 170, the domain is characterized as PRC barrel.
+At position 433 to 595, the domain is characterized as Helicase C-terminal.
+At position 123 to 296, the domain is characterized as Helicase ATP-binding.
+At position 325 to 474, the domain is characterized as Helicase C-terminal.
+At position 345 to 671, the domain is characterized as Kinesin motor.
+At position 1 to 134, the domain is characterized as Toprim.
+At position 31 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 431 to 523, the domain is characterized as CARD.
+At position 230 to 428, the domain is characterized as DH.
+At position 213 to 268, the domain is characterized as GRAM.
+At position 705 to 866, the domain is characterized as TLDc.
+At position 69 to 219, the domain is characterized as N-acetyltransferase.
+At position 1 to 120, the domain is characterized as C-type lectin.
+At position 1 to 64, the domain is characterized as PFL.
+At position 71 to 195, the domain is characterized as Glycine radical.
+At position 154 to 205, the domain is characterized as HTH bat-type.
+At position 32 to 66, the domain is characterized as Chitin-binding type-1.
+At position 11 to 70, the domain is characterized as Sm.
+At position 926 to 1202, the domain is characterized as PKS/mFAS DH.
+At position 1698 to 1772, the domain is characterized as Carrier.
+At position 542 to 635, the domain is characterized as PB1.
+At position 99 to 239, the domain is characterized as GST C-terminal.
+At position 421 to 610, the domain is characterized as VWFA.
+At position 319 to 597, the domain is characterized as ABC transporter 1.
+At position 617 to 944, the domain is characterized as ABC transporter 2.
+At position 216 to 402, the domain is characterized as PCI.
+At position 91 to 366, the domain is characterized as Protein kinase.
+At position 132 to 460, the domain is characterized as Kinesin motor.
+At position 203 to 372, the domain is characterized as tr-type G.
+At position 903 to 1015, the domain is characterized as VRR-NUC.
+At position 137 to 369, the domain is characterized as Histidine kinase.
+At position 30 to 342, the domain is characterized as Protein kinase.
+At position 46 to 131, the domain is characterized as Fibronectin type-III 1.
+At position 332 to 434, the domain is characterized as Fibronectin type-III 2.
+At position 435 to 534, the domain is characterized as Fibronectin type-III 3.
+At position 538 to 629, the domain is characterized as Fibronectin type-III 4.
+At position 627 to 719, the domain is characterized as Fibronectin type-III 5.
+At position 724 to 833, the domain is characterized as Fibronectin type-III 6.
+At position 100 to 294, the domain is characterized as ATP-grasp.
+At position 443 to 490, the domain is characterized as SARAH.
+At position 120 to 367, the domain is characterized as ABC transporter 1.
+At position 803 to 1045, the domain is characterized as ABC transporter 2.
+At position 319 to 358, the domain is characterized as STI1.
+At position 42 to 148, the domain is characterized as Expansin-like EG45.
+At position 162 to 244, the domain is characterized as Expansin-like CBD.
+At position 5 to 195, the domain is characterized as RNase H type-2.
+At position 41 to 413, the domain is characterized as GRAS.
+At position 29 to 74, the domain is characterized as F-box.
+At position 149 to 229, the domain is characterized as PDZ 2.
+At position 333 to 428, the domain is characterized as Fibronectin type-III 2.
+At position 444 to 528, the domain is characterized as Ig-like C2-type 2.
+At position 189 to 502, the domain is characterized as Protein kinase.
+At position 236 to 322, the domain is characterized as Ig-like C2-type 1.
+At position 365 to 453, the domain is characterized as Ig-like C2-type 2.
+At position 458 to 545, the domain is characterized as Ig-like C2-type 3.
+At position 553 to 643, the domain is characterized as Ig-like C2-type 4.
+At position 1463 to 1524, the domain is characterized as VWFC.
+At position 2 to 72, the domain is characterized as Sm.
+At position 80 to 174, the domain is characterized as AD.
+At position 5 to 152, the domain is characterized as PTS EIIA type-2.
+At position 235 to 446, the domain is characterized as Helicase ATP-binding.
+At position 486 to 654, the domain is characterized as Helicase C-terminal.
+At position 137 to 174, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 9 to 73, the domain is characterized as KH 1.
+At position 113 to 178, the domain is characterized as KH 2.
+At position 205 to 270, the domain is characterized as KH 3.
+At position 161 to 336, the domain is characterized as Helicase ATP-binding.
+At position 364 to 511, the domain is characterized as Helicase C-terminal.
+At position 371 to 537, the domain is characterized as Helicase C-terminal.
+At position 564 to 658, the domain is characterized as Dicer dsRNA-binding fold.
+At position 919 to 1059, the domain is characterized as RNase III 1.
+At position 1098 to 1281, the domain is characterized as RNase III 2.
+At position 158 to 202, the domain is characterized as EGF-like.
+At position 200 to 456, the domain is characterized as ZP.
+At position 196 to 825, the domain is characterized as USP.
+At position 45 to 292, the domain is characterized as Radical SAM core.
+At position 64 to 112, the domain is characterized as GIY-YIG.
+At position 272 to 360, the domain is characterized as CS.
+At position 49 to 105, the domain is characterized as FHA.
+At position 9 to 319, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 308, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 288 to 620, the domain is characterized as UvrD-like helicase C-terminal.
+At position 13 to 233, the domain is characterized as ABC transporter.
+At position 85 to 314, the domain is characterized as OBG-type G.
+At position 314 to 389, the domain is characterized as TGS.
+At position 317 to 444, the domain is characterized as Guanylate cyclase 1.
+At position 1110 to 1255, the domain is characterized as Guanylate cyclase 2.
+At position 1 to 235, the domain is characterized as ABC transporter.
+At position 155 to 185, the domain is characterized as EF-hand 4.
+At position 211 to 310, the domain is characterized as Fe2OG dioxygenase.
+At position 159 to 203, the domain is characterized as DSL.
+At position 204 to 237, the domain is characterized as EGF-like 1.
+At position 241 to 268, the domain is characterized as EGF-like 2.
+At position 270 to 308, the domain is characterized as EGF-like 3.
+At position 310 to 346, the domain is characterized as EGF-like 4; calcium-binding.
+At position 348 to 385, the domain is characterized as EGF-like 5.
+At position 387 to 423, the domain is characterized as EGF-like 6.
+At position 425 to 461, the domain is characterized as EGF-like 7; calcium-binding.
+At position 463 to 499, the domain is characterized as EGF-like 8.
+At position 89 to 121, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 17 to 92, the domain is characterized as Ubiquitin-like.
+At position 23 to 125, the domain is characterized as Phytocyanin.
+At position 165 to 352, the domain is characterized as CheB-type methylesterase.
+At position 32 to 200, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 113, the domain is characterized as VWFD.
+At position 616 to 708, the domain is characterized as CTCK.
+At position 1295 to 1370, the domain is characterized as Death.
+At position 290 to 660, the domain is characterized as GRAS.
+At position 51 to 232, the domain is characterized as tr-type G.
+At position 246 to 449, the domain is characterized as Helicase ATP-binding.
+At position 494 to 643, the domain is characterized as Helicase C-terminal.
+At position 601 to 684, the domain is characterized as BRCT.
+At position 160 to 235, the domain is characterized as PPIase FKBP-type.
+At position 2 to 60, the domain is characterized as TGS.
+At position 61 to 264, the domain is characterized as MIF4G 1.
+At position 469 to 655, the domain is characterized as MIF4G 2.
+At position 672 to 871, the domain is characterized as MIF4G 3.
+At position 171 to 359, the domain is characterized as Glutamine amidotransferase type-1.
+At position 258 to 296, the domain is characterized as LRRCT.
+At position 68 to 244, the domain is characterized as FAD-binding PCMH-type.
+At position 567 to 668, the domain is characterized as tRNA-binding.
+At position 35 to 129, the domain is characterized as GS beta-grasp.
+At position 136 to 472, the domain is characterized as GS catalytic.
+At position 42 to 143, the domain is characterized as Rhodanese.
+At position 47 to 153, the domain is characterized as sHSP.
+At position 65 to 215, the domain is characterized as Cupin type-1.
+At position 174 to 515, the domain is characterized as PUM-HD.
+At position 266 to 515, the domain is characterized as EAL.
+At position 137 to 365, the domain is characterized as Radical SAM core.
+At position 888 to 986, the domain is characterized as GTD-binding.
+At position 17 to 240, the domain is characterized as Peptidase S1.
+At position 254 to 423, the domain is characterized as PCI.
+At position 91 to 291, the domain is characterized as AH.
+At position 282 to 527, the domain is characterized as MHD.
+At position 9 to 71, the domain is characterized as Histone-fold.
+At position 347 to 411, the domain is characterized as SAM.
+At position 416 to 487, the domain is characterized as U-box.
+At position 240 to 531, the domain is characterized as Protein kinase.
+At position 1 to 44, the domain is characterized as KRAB.
+At position 2 to 150, the domain is characterized as MGS-like.
+At position 1129 to 1201, the domain is characterized as S1 motif.
+At position 1239 to 1349, the domain is characterized as SH2.
+At position 387 to 462, the domain is characterized as B5.
+At position 49 to 333, the domain is characterized as Protein kinase.
+At position 17 to 60, the domain is characterized as CUE.
+At position 57 to 311, the domain is characterized as Protein kinase.
+At position 366 to 387, the domain is characterized as NAF.
+At position 283 to 563, the domain is characterized as Protein kinase.
+At position 64 to 137, the domain is characterized as U-box.
+At position 22 to 72, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 82 to 132, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 355 to 434, the domain is characterized as OCT.
+At position 344 to 398, the domain is characterized as Myb-like.
+At position 241 to 625, the domain is characterized as Peptidase S53.
+At position 635 to 722, the domain is characterized as PKD.
+At position 94 to 173, the domain is characterized as S4 RNA-binding.
+At position 553 to 614, the domain is characterized as KH.
+At position 3 to 167, the domain is characterized as DHFR.
+At position 202 to 504, the domain is characterized as CP-type G.
+At position 48 to 137, the domain is characterized as Ig-like C2-type 1.
+At position 142 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 329 to 415, the domain is characterized as Ig-like C2-type 4.
+At position 200 to 618, the domain is characterized as Protein kinase.
+At position 142 to 231, the domain is characterized as Ig-like C1-type.
+At position 284 to 333, the domain is characterized as bHLH.
+At position 328 to 609, the domain is characterized as Protein kinase.
+At position 51 to 356, the domain is characterized as ABC transmembrane type-1 1.
+At position 709 to 998, the domain is characterized as ABC transmembrane type-1 2.
+At position 238 to 322, the domain is characterized as PDZ.
+At position 83 to 240, the domain is characterized as Helicase ATP-binding.
+At position 412 to 565, the domain is characterized as Helicase C-terminal.
+At position 596 to 728, the domain is characterized as Toprim.
+At position 11 to 62, the domain is characterized as LIM zinc-binding.
+At position 186 to 237, the domain is characterized as HAMP.
+At position 245 to 448, the domain is characterized as Histidine kinase.
+At position 556 to 612, the domain is characterized as LIM zinc-binding 1.
+At position 621 to 672, the domain is characterized as LIM zinc-binding 2.
+At position 5 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 217 to 247, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 252 to 281, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 319 to 404, the domain is characterized as B5.
+At position 626 to 719, the domain is characterized as FDX-ACB.
+At position 179 to 574, the domain is characterized as Peptidase S53.
+At position 90 to 148, the domain is characterized as S4 RNA-binding.
+At position 123 to 238, the domain is characterized as PilZ.
+At position 153 to 250, the domain is characterized as CRM 1.
+At position 352 to 449, the domain is characterized as CRM 2.
+At position 564 to 664, the domain is characterized as CRM 3.
+At position 358 to 495, the domain is characterized as YTH.
+At position 50 to 114, the domain is characterized as S4 RNA-binding.
+At position 73 to 526, the domain is characterized as IF rod.
+At position 395 to 456, the domain is characterized as LIM zinc-binding 1.
+At position 460 to 520, the domain is characterized as LIM zinc-binding 2.
+At position 521 to 589, the domain is characterized as LIM zinc-binding 3.
+At position 5 to 134, the domain is characterized as Galectin.
+At position 35 to 260, the domain is characterized as Peptidase S1.
+At position 78 to 301, the domain is characterized as Glutamine amidotransferase type-1.
+At position 294 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 28 to 202, the domain is characterized as Helicase ATP-binding.
+At position 229 to 380, the domain is characterized as Helicase C-terminal.
+At position 1705 to 1887, the domain is characterized as VWFA.
+At position 1 to 95, the domain is characterized as Ig-like 1.
+At position 121 to 213, the domain is characterized as Ig-like 2.
+At position 227 to 322, the domain is characterized as Ig-like 3.
+At position 330 to 432, the domain is characterized as Ig-like 4.
+At position 207 to 260, the domain is characterized as HAMP.
+At position 268 to 480, the domain is characterized as Histidine kinase.
+At position 4 to 301, the domain is characterized as Helicase ATP-binding.
+At position 272 to 307, the domain is characterized as EF-hand 3.
+At position 273 to 363, the domain is characterized as EH 3.
+At position 308 to 341, the domain is characterized as EF-hand 4.
+At position 863 to 882, the domain is characterized as UIM 1.
+At position 889 to 907, the domain is characterized as UIM 2.
+At position 119 to 247, the domain is characterized as Thioredoxin.
+At position 168 to 274, the domain is characterized as HTH araC/xylS-type.
+At position 227 to 268, the domain is characterized as LDL-receptor class A 1.
+At position 270 to 379, the domain is characterized as CUB 1.
+At position 387 to 549, the domain is characterized as MAM.
+At position 569 to 679, the domain is characterized as CUB 2.
+At position 686 to 724, the domain is characterized as LDL-receptor class A 2.
+At position 723 to 816, the domain is characterized as SRCR.
+At position 830 to 1069, the domain is characterized as Peptidase S1.
+At position 33 to 212, the domain is characterized as FAD-binding PCMH-type.
+At position 38 to 200, the domain is characterized as SIS.
+At position 88 to 195, the domain is characterized as Calponin-homology (CH) 1.
+At position 255 to 362, the domain is characterized as Calponin-homology (CH) 2.
+At position 156 to 281, the domain is characterized as Fatty acid hydroxylase.
+At position 22 to 70, the domain is characterized as F-box.
+At position 431 to 551, the domain is characterized as Ricin B-type lectin.
+At position 103 to 219, the domain is characterized as OmpA-like.
+At position 3 to 79, the domain is characterized as HTH rpiR-type.
+At position 123 to 264, the domain is characterized as SIS.
+At position 71 to 146, the domain is characterized as ACT.
+At position 45 to 337, the domain is characterized as tr-type G.
+At position 549 to 607, the domain is characterized as KH.
+At position 617 to 679, the domain is characterized as S1 motif.
+At position 58 to 328, the domain is characterized as Protein kinase.
+At position 486 to 616, the domain is characterized as MATH.
+At position 655 to 722, the domain is characterized as BTB.
+At position 604 to 710, the domain is characterized as Cadherin 5.
+At position 592 to 752, the domain is characterized as GGDEF.
+At position 171 to 238, the domain is characterized as KH.
+At position 204 to 392, the domain is characterized as PNPLA.
+At position 20 to 211, the domain is characterized as NodB homology.
+At position 325 to 502, the domain is characterized as Helicase C-terminal.
+At position 193 to 393, the domain is characterized as HIN-200 1.
+At position 566 to 765, the domain is characterized as HIN-200 2.
+At position 15 to 39, the domain is characterized as Chitin-binding type R&R.
+At position 10 to 241, the domain is characterized as Nudix hydrolase.
+At position 142 to 177, the domain is characterized as EF-hand.
+At position 213 to 281, the domain is characterized as SAM.
+At position 51 to 129, the domain is characterized as Biotinyl-binding.
+At position 16 to 284, the domain is characterized as Protein kinase.
+At position 5 to 90, the domain is characterized as NAB.
+At position 289 to 445, the domain is characterized as Helicase ATP-binding.
+At position 545 to 736, the domain is characterized as Helicase C-terminal.
+At position 30 to 212, the domain is characterized as tr-type G.
+At position 1 to 53, the domain is characterized as H15.
+At position 593 to 669, the domain is characterized as BRCT.
+At position 22 to 84, the domain is characterized as LCN-type CS-alpha/beta.
+At position 429 to 465, the domain is characterized as QLQ.
+At position 704 to 776, the domain is characterized as HSA.
+At position 881 to 1046, the domain is characterized as Helicase ATP-binding.
+At position 1191 to 1354, the domain is characterized as Helicase C-terminal.
+At position 1536 to 1606, the domain is characterized as Bromo.
+At position 41 to 283, the domain is characterized as HBM.
+At position 310 to 362, the domain is characterized as HAMP.
+At position 367 to 603, the domain is characterized as Methyl-accepting transducer.
+At position 187 to 308, the domain is characterized as Ferric oxidoreductase.
+At position 337 to 454, the domain is characterized as FAD-binding FR-type.
+At position 115 to 310, the domain is characterized as ATP-grasp.
+At position 291 to 565, the domain is characterized as Protein kinase.
+At position 67 to 287, the domain is characterized as BURP.
+At position 45 to 80, the domain is characterized as Pacifastin.
+At position 74 to 328, the domain is characterized as Protein kinase.
+At position 382 to 406, the domain is characterized as NAF.
+At position 33 to 241, the domain is characterized as tr-type G.
+At position 56 to 288, the domain is characterized as Radical SAM core.
+At position 565 to 792, the domain is characterized as MIF4G.
+At position 1241 to 1363, the domain is characterized as MI.
+At position 1433 to 1599, the domain is characterized as W2.
+At position 977 to 1099, the domain is characterized as RCK N-terminal.
+At position 844 to 1104, the domain is characterized as PKS/mFAS DH.
+At position 2112 to 2192, the domain is characterized as Carrier.
+At position 55 to 163, the domain is characterized as THUMP.
+At position 9 to 62, the domain is characterized as F-box.
+At position 327 to 378, the domain is characterized as FBD.
+At position 423 to 557, the domain is characterized as Plastocyanin-like 3.
+At position 25 to 151, the domain is characterized as VOC.
+At position 191 to 254, the domain is characterized as R3H.
+At position 127 to 486, the domain is characterized as PTS EIIC type-1.
+At position 44 to 235, the domain is characterized as RNase H type-2.
+At position 12 to 199, the domain is characterized as RNase H type-2.
+At position 22 to 129, the domain is characterized as CUB.
+At position 53 to 129, the domain is characterized as Lipoyl-binding.
+At position 50 to 242, the domain is characterized as Cupin type-1 1.
+At position 294 to 443, the domain is characterized as Cupin type-1 2.
+At position 56 to 131, the domain is characterized as EMI.
+At position 814 to 864, the domain is characterized as Collagen-like.
+At position 866 to 1013, the domain is characterized as C1q.
+At position 405 to 613, the domain is characterized as Rab-GAP TBC.
+At position 26 to 126, the domain is characterized as Glutaredoxin.
+At position 71 to 200, the domain is characterized as THUMP.
+At position 84 to 374, the domain is characterized as Radical SAM core.
+At position 398 to 549, the domain is characterized as N-acetyltransferase.
+At position 17 to 135, the domain is characterized as Rhodanese 1.
+At position 165 to 278, the domain is characterized as Rhodanese 2.
+At position 1720 to 1749, the domain is characterized as IQ.
+At position 39 to 92, the domain is characterized as PSI.
+At position 220 to 382, the domain is characterized as TrmE-type G.
+At position 253 to 413, the domain is characterized as Helicase C-terminal.
+At position 619 to 734, the domain is characterized as SMC hinge.
+At position 163 to 253, the domain is characterized as SH2 2.
+At position 364 to 624, the domain is characterized as Protein kinase.
+At position 53 to 208, the domain is characterized as Flavodoxin-like.
+At position 267 to 514, the domain is characterized as FAD-binding FR-type.
+At position 152 to 201, the domain is characterized as bHLH.
+At position 176 to 227, the domain is characterized as LRRCT.
+At position 299 to 420, the domain is characterized as CBM6.
+At position 424 to 492, the domain is characterized as Dockerin.
+At position 512 to 833, the domain is characterized as GH10.
+At position 163 to 247, the domain is characterized as Glutaredoxin.
+At position 13 to 73, the domain is characterized as v-SNARE coiled-coil homology.
+At position 4 to 469, the domain is characterized as SAM-dependent MTase C5-type.
+At position 10 to 156, the domain is characterized as UBC core.
+At position 13 to 282, the domain is characterized as Protein kinase.
+At position 76 to 170, the domain is characterized as Fe2OG dioxygenase.
+At position 177 to 501, the domain is characterized as Kinesin motor.
+At position 692 to 752, the domain is characterized as KH.
+At position 762 to 831, the domain is characterized as S1 motif.
+At position 414 to 612, the domain is characterized as MAGE.
+At position 489 to 611, the domain is characterized as HD.
+At position 840 to 919, the domain is characterized as ACT 2.
+At position 36 to 264, the domain is characterized as MIF4G.
+At position 3 to 131, the domain is characterized as VOC.
+At position 28 to 171, the domain is characterized as SIS.
+At position 15 to 80, the domain is characterized as HMA 1.
+At position 82 to 147, the domain is characterized as HMA 2.
+At position 73 to 188, the domain is characterized as PINc.
+At position 304 to 363, the domain is characterized as CBS 1.
+At position 367 to 427, the domain is characterized as CBS 2.
+At position 121 to 416, the domain is characterized as PI3K/PI4K catalytic.
+At position 112 to 307, the domain is characterized as ATP-grasp.
+At position 539 to 716, the domain is characterized as W2.
+At position 118 to 178, the domain is characterized as Sushi 2.
+At position 179 to 242, the domain is characterized as Sushi 3.
+At position 243 to 301, the domain is characterized as Sushi 4.
+At position 302 to 357, the domain is characterized as Sushi 5.
+At position 358 to 415, the domain is characterized as Sushi 6.
+At position 22 to 79, the domain is characterized as Ig-like V-type 1.
+At position 114 to 171, the domain is characterized as Ig-like V-type 2.
+At position 191 to 288, the domain is characterized as Ig-like V-type 3.
+At position 118 to 432, the domain is characterized as PPM-type phosphatase.
+At position 1227 to 1300, the domain is characterized as U-box.
+At position 614 to 696, the domain is characterized as Smr.
+At position 305 to 451, the domain is characterized as C-CAP/cofactor C-like.
+At position 16 to 285, the domain is characterized as tr-type G.
+At position 1893 to 1922, the domain is characterized as IQ.
+At position 234 to 286, the domain is characterized as KBD.
+At position 23 to 128, the domain is characterized as Thioredoxin 1.
+At position 323 to 462, the domain is characterized as Thioredoxin 2.
+At position 19 to 116, the domain is characterized as Ig-like.
+At position 672 to 877, the domain is characterized as MRH.
+At position 216 to 270, the domain is characterized as bHLH.
+At position 61 to 108, the domain is characterized as G-patch.
+At position 121 to 203, the domain is characterized as REM-1 2.
+At position 204 to 284, the domain is characterized as REM-1 3.
+At position 352 to 472, the domain is characterized as C2.
+At position 656 to 915, the domain is characterized as Protein kinase.
+At position 916 to 983, the domain is characterized as AGC-kinase C-terminal.
+At position 102 to 338, the domain is characterized as Lon N-terminal.
+At position 734 to 918, the domain is characterized as Lon proteolytic.
+At position 80 to 157, the domain is characterized as Cytochrome b5 heme-binding.
+At position 182 to 542, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 185 to 234, the domain is characterized as F-box.
+At position 427 to 692, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 43 to 419, the domain is characterized as PIPK.
+At position 294 to 439, the domain is characterized as JmjC.
+At position 18 to 274, the domain is characterized as UmuC.
+At position 187 to 198, the domain is characterized as EGF-like 1.
+At position 234 to 260, the domain is characterized as EGF-like 2.
+At position 265 to 291, the domain is characterized as EGF-like 3.
+At position 327 to 419, the domain is characterized as Fibronectin type-III 1.
+At position 420 to 504, the domain is characterized as Fibronectin type-III 2.
+At position 505 to 594, the domain is characterized as Fibronectin type-III 3.
+At position 595 to 686, the domain is characterized as Fibronectin type-III 4.
+At position 687 to 776, the domain is characterized as Fibronectin type-III 5.
+At position 777 to 863, the domain is characterized as Fibronectin type-III 6.
+At position 864 to 952, the domain is characterized as Fibronectin type-III 7.
+At position 953 to 1037, the domain is characterized as Fibronectin type-III 8.
+At position 1038 to 1126, the domain is characterized as Fibronectin type-III 9.
+At position 1124 to 1339, the domain is characterized as Fibrinogen C-terminal.
+At position 10 to 99, the domain is characterized as BRCT 1.
+At position 627 to 717, the domain is characterized as BRCT 2.
+At position 738 to 820, the domain is characterized as BRCT 3.
+At position 96 to 324, the domain is characterized as Radical SAM core.
+At position 1536 to 1679, the domain is characterized as NTR.
+At position 178 to 243, the domain is characterized as SEP.
+At position 291 to 367, the domain is characterized as UBX.
+At position 69 to 184, the domain is characterized as I-type lysozyme.
+At position 433 to 444, the domain is characterized as EGF-like.
+At position 40 to 129, the domain is characterized as S1 motif.
+At position 458 to 581, the domain is characterized as Thioredoxin.
+At position 66 to 320, the domain is characterized as GB1/RHD3-type G.
+At position 583 to 796, the domain is characterized as SEC7.
+At position 26 to 202, the domain is characterized as N-acetyltransferase.
+At position 34 to 187, the domain is characterized as SIS.
+At position 4 to 127, the domain is characterized as VOC 1.
+At position 132 to 251, the domain is characterized as VOC 2.
+At position 439 to 561, the domain is characterized as HD.
+At position 788 to 856, the domain is characterized as ACT 2.
+At position 574 to 650, the domain is characterized as Ubiquitin-like.
+At position 1679 to 1749, the domain is characterized as Bromo.
+At position 50 to 165, the domain is characterized as Expansin-like EG45.
+At position 175 to 254, the domain is characterized as Expansin-like CBD.
+At position 177 to 353, the domain is characterized as TNase-like.
+At position 29 to 76, the domain is characterized as WAP.
+At position 3 to 175, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1775 to 2042, the domain is characterized as Protein kinase.
+At position 260 to 306, the domain is characterized as RPE3 insert.
+At position 41 to 353, the domain is characterized as GH26.
+At position 35 to 259, the domain is characterized as Radical SAM core.
+At position 292 to 540, the domain is characterized as Glutamine amidotransferase type-1.
+At position 104 to 473, the domain is characterized as USP.
+At position 32 to 255, the domain is characterized as Fibrinogen C-terminal.
+At position 259 to 541, the domain is characterized as ABC transmembrane type-1 1.
+At position 595 to 821, the domain is characterized as ABC transporter 1.
+At position 974 to 1173, the domain is characterized as ABC transmembrane type-1 2.
+At position 1210 to 1441, the domain is characterized as ABC transporter 2.
+At position 21 to 164, the domain is characterized as NAC.
+At position 614 to 1124, the domain is characterized as USP.
+At position 293 to 404, the domain is characterized as EH.
+At position 3 to 88, the domain is characterized as GST N-terminal.
+At position 90 to 206, the domain is characterized as GST C-terminal.
+At position 51 to 399, the domain is characterized as IF rod.
+At position 509 to 622, the domain is characterized as LTD.
+At position 62 to 222, the domain is characterized as PPIase cyclophilin-type.
+At position 595 to 832, the domain is characterized as ABC transporter.
+At position 49 to 204, the domain is characterized as C-CAP/cofactor C-like.
+At position 74 to 264, the domain is characterized as MACPF.
+At position 25 to 138, the domain is characterized as Ig-like V-type.
+At position 145 to 234, the domain is characterized as Ig-like C2-type.
+At position 22 to 292, the domain is characterized as Protein kinase.
+At position 75 to 349, the domain is characterized as Pyruvate carboxyltransferase.
+At position 18 to 81, the domain is characterized as LCN-type CS-alpha/beta.
+At position 19 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 476 to 559, the domain is characterized as Disintegrin.
+At position 854 to 905, the domain is characterized as TSP type-1 2.
+At position 19 to 135, the domain is characterized as I-type lysozyme.
+At position 110 to 171, the domain is characterized as SH3.
+At position 230 to 351, the domain is characterized as C2 1.
+At position 362 to 495, the domain is characterized as C2 2.
+At position 40 to 233, the domain is characterized as Lon N-terminal.
+At position 621 to 802, the domain is characterized as Lon proteolytic.
+At position 587 to 624, the domain is characterized as EGF-like 1.
+At position 626 to 665, the domain is characterized as EGF-like 2; calcium-binding.
+At position 50 to 220, the domain is characterized as Helicase ATP-binding.
+At position 231 to 392, the domain is characterized as Helicase C-terminal.
+At position 23 to 114, the domain is characterized as UPAR/Ly6 1.
+At position 115 to 213, the domain is characterized as UPAR/Ly6 2.
+At position 214 to 305, the domain is characterized as UPAR/Ly6 3.
+At position 9 to 109, the domain is characterized as LIM zinc-binding 1.
+At position 110 to 167, the domain is characterized as LIM zinc-binding 2.
+At position 504 to 663, the domain is characterized as C2 1.
+At position 771 to 903, the domain is characterized as C2 2.
+At position 969 to 1131, the domain is characterized as C2 3.
+At position 1155 to 1323, the domain is characterized as C2 4.
+At position 1383 to 1517, the domain is characterized as C2 5.
+At position 1598 to 1726, the domain is characterized as C2 6.
+At position 3 to 140, the domain is characterized as PINc.
+At position 35 to 153, the domain is characterized as DSCP-N.
+At position 160 to 182, the domain is characterized as Follistatin-like 1.
+At position 195 to 217, the domain is characterized as Follistatin-like 2.
+At position 229 to 251, the domain is characterized as Follistatin-like 3.
+At position 257 to 280, the domain is characterized as Follistatin-like 4.
+At position 287 to 309, the domain is characterized as Follistatin-like 5.
+At position 318 to 340, the domain is characterized as Follistatin-like 6.
+At position 435 to 458, the domain is characterized as Follistatin-like 7.
+At position 215 to 383, the domain is characterized as PCI.
+At position 605 to 902, the domain is characterized as Protein kinase.
+At position 5 to 168, the domain is characterized as 3'-5' exonuclease.
+At position 208 to 288, the domain is characterized as HRDC.
+At position 238 to 297, the domain is characterized as SH3.
+At position 97 to 214, the domain is characterized as PB1.
+At position 41 to 267, the domain is characterized as Radical SAM core.
+At position 292 to 536, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1167 to 1187, the domain is characterized as WH2 1.
+At position 1207 to 1227, the domain is characterized as WH2 2.
+At position 1297 to 1317, the domain is characterized as WH2 3.
+At position 51 to 239, the domain is characterized as GH11.
+At position 68 to 433, the domain is characterized as Protein kinase.
+At position 108 to 178, the domain is characterized as BTB.
+At position 383 to 400, the domain is characterized as WH2.
+At position 312 to 597, the domain is characterized as Protein kinase.
+At position 50 to 370, the domain is characterized as Peptidase A1.
+At position 171 to 462, the domain is characterized as Protein kinase.
+At position 65 to 258, the domain is characterized as ABC transmembrane type-1.
+At position 390 to 647, the domain is characterized as PPM-type phosphatase.
+At position 646 to 736, the domain is characterized as BRCT 2.
+At position 757 to 839, the domain is characterized as BRCT 3.
+At position 43 to 151, the domain is characterized as PH.
+At position 161 to 355, the domain is characterized as Rho-GAP.
+At position 613 to 883, the domain is characterized as Protein kinase.
+At position 384 to 580, the domain is characterized as Helicase ATP-binding.
+At position 716 to 876, the domain is characterized as Helicase C-terminal.
+At position 352 to 415, the domain is characterized as SH3.
+At position 408 to 584, the domain is characterized as Exonuclease.
+At position 71 to 93, the domain is characterized as EF-hand 2.
+At position 25 to 122, the domain is characterized as Ig-like.
+At position 159 to 332, the domain is characterized as Helicase ATP-binding.
+At position 361 to 510, the domain is characterized as Helicase C-terminal.
+At position 118 to 178, the domain is characterized as S4 RNA-binding.
+At position 127 to 193, the domain is characterized as Ig-like C2-type 2.
+At position 230 to 295, the domain is characterized as Ig-like C2-type 3.
+At position 323 to 376, the domain is characterized as Ig-like C2-type 4.
+At position 410 to 463, the domain is characterized as Ig-like C2-type 5.
+At position 21 to 223, the domain is characterized as AIG1-type G.
+At position 6 to 119, the domain is characterized as Response regulatory.
+At position 36 to 109, the domain is characterized as IGFBP N-terminal.
+At position 88 to 154, the domain is characterized as Kazal-like.
+At position 383 to 474, the domain is characterized as PDZ.
+At position 18 to 52, the domain is characterized as WW.
+At position 176 to 350, the domain is characterized as Helicase ATP-binding.
+At position 379 to 523, the domain is characterized as Helicase C-terminal.
+At position 79 to 151, the domain is characterized as RRM 1.
+At position 153 to 234, the domain is characterized as RRM 2.
+At position 163 to 456, the domain is characterized as GT92.
+At position 48 to 79, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 9 to 229, the domain is characterized as Radical SAM core.
+At position 1 to 225, the domain is characterized as SMP-LTD.
+At position 10 to 205, the domain is characterized as Lon N-terminal.
+At position 593 to 774, the domain is characterized as Lon proteolytic.
+At position 537 to 613, the domain is characterized as Carrier 1.
+At position 1584 to 1660, the domain is characterized as Carrier 2.
+At position 962 to 1067, the domain is characterized as Calponin-homology (CH).
+At position 12 to 314, the domain is characterized as Protein kinase.
+At position 408 to 443, the domain is characterized as EF-hand 1.
+At position 444 to 479, the domain is characterized as EF-hand 2.
+At position 359 to 391, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 398 to 428, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 576 to 634, the domain is characterized as Prospero-type homeo.
+At position 635 to 734, the domain is characterized as Prospero.
+At position 122 to 155, the domain is characterized as WW 1.
+At position 163 to 196, the domain is characterized as WW 2.
+At position 317 to 599, the domain is characterized as Protein kinase.
+At position 205 to 398, the domain is characterized as Peptidase M12B.
+At position 13 to 73, the domain is characterized as HTH tetR-type.
+At position 5 to 107, the domain is characterized as BTB.
+At position 182 to 195, the domain is characterized as CRIB.
+At position 145 to 324, the domain is characterized as Helicase ATP-binding.
+At position 349 to 500, the domain is characterized as Helicase C-terminal.
+At position 142 to 209, the domain is characterized as GRAM 1.
+At position 288 to 356, the domain is characterized as GRAM 2.
+At position 509 to 696, the domain is characterized as Rab-GAP TBC.
+At position 880 to 915, the domain is characterized as EF-hand.
+At position 1119 to 1657, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 381 to 710, the domain is characterized as Kinesin motor.
+At position 33 to 107, the domain is characterized as Ig-like.
+At position 82 to 397, the domain is characterized as IF rod.
+At position 8 to 65, the domain is characterized as CBS 1.
+At position 73 to 131, the domain is characterized as CBS 2.
+At position 11 to 221, the domain is characterized as Peptidase M12B.
+At position 233 to 303, the domain is characterized as Disintegrin.
+At position 313 to 368, the domain is characterized as TSP type-1.
+At position 358 to 480, the domain is characterized as C2 1.
+At position 509 to 635, the domain is characterized as C2 2.
+At position 225 to 488, the domain is characterized as F-BAR.
+At position 737 to 950, the domain is characterized as Rho-GAP.
+At position 486 to 919, the domain is characterized as USP.
+At position 970 to 1142, the domain is characterized as Exonuclease.
+At position 14 to 74, the domain is characterized as HTH tetR-type.
+At position 24 to 77, the domain is characterized as Tudor-knot.
+At position 255 to 533, the domain is characterized as MYST-type HAT.
+At position 39 to 283, the domain is characterized as Zn-dependent PLC.
+At position 67 to 316, the domain is characterized as Radical SAM core.
+At position 9 to 66, the domain is characterized as HTH lysR-type.
+At position 131 to 379, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 209 to 382, the domain is characterized as EngA-type G 2.
+At position 383 to 467, the domain is characterized as KH-like.
+At position 101 to 287, the domain is characterized as ATP-grasp.
+At position 210 to 237, the domain is characterized as PLD phosphodiesterase 1.
+At position 484 to 511, the domain is characterized as PLD phosphodiesterase 2.
+At position 11 to 234, the domain is characterized as Glutamine amidotransferase type-2.
+At position 103 to 211, the domain is characterized as tRNA-binding.
+At position 15 to 181, the domain is characterized as Miro 1.
+At position 197 to 232, the domain is characterized as EF-hand 1.
+At position 317 to 352, the domain is characterized as EF-hand 2.
+At position 429 to 592, the domain is characterized as Miro 2.
+At position 110 to 400, the domain is characterized as ABC transmembrane type-1.
+At position 435 to 671, the domain is characterized as ABC transporter.
+At position 46 to 78, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 30 to 212, the domain is characterized as CNNM transmembrane.
+At position 231 to 291, the domain is characterized as CBS 1.
+At position 296 to 356, the domain is characterized as CBS 2.
+At position 357 to 426, the domain is characterized as CBS 3.
+At position 24 to 508, the domain is characterized as TROVE.
+At position 23 to 1049, the domain is characterized as Zinc-hook.
+At position 45 to 291, the domain is characterized as Peptidase S1.
+At position 19 to 283, the domain is characterized as ZP.
+At position 1 to 77, the domain is characterized as NAB.
+At position 166 to 378, the domain is characterized as C2.
+At position 412 to 671, the domain is characterized as Protein kinase.
+At position 672 to 748, the domain is characterized as AGC-kinase C-terminal.
+At position 173 to 288, the domain is characterized as CRC.
+At position 178 to 217, the domain is characterized as EGF-like 1.
+At position 218 to 263, the domain is characterized as EGF-like 2; calcium-binding.
+At position 264 to 309, the domain is characterized as EGF-like 3; calcium-binding.
+At position 310 to 357, the domain is characterized as EGF-like 4; calcium-binding.
+At position 358 to 400, the domain is characterized as EGF-like 5; calcium-binding.
+At position 401 to 442, the domain is characterized as EGF-like 6; calcium-binding.
+At position 443 to 482, the domain is characterized as EGF-like 7; calcium-binding.
+At position 483 to 526, the domain is characterized as EGF-like 8; calcium-binding.
+At position 527 to 580, the domain is characterized as EGF-like 9; calcium-binding.
+At position 29 to 125, the domain is characterized as CS.
+At position 119 to 313, the domain is characterized as AMMECR1.
+At position 404 to 502, the domain is characterized as Fibronectin type-III.
+At position 38 to 343, the domain is characterized as RHD.
+At position 104 to 498, the domain is characterized as PPM-type phosphatase.
+At position 26 to 118, the domain is characterized as UPAR/Ly6.
+At position 258 to 482, the domain is characterized as NR LBD.
+At position 84 to 150, the domain is characterized as Chitin-binding type R&R.
+At position 253 to 440, the domain is characterized as GATase cobBQ-type.
+At position 45 to 156, the domain is characterized as SRCR 1.
+At position 161 to 260, the domain is characterized as SRCR 2.
+At position 265 to 361, the domain is characterized as SRCR 3.
+At position 31 to 230, the domain is characterized as Velvet.
+At position 453 to 598, the domain is characterized as SIS 2.
+At position 321 to 489, the domain is characterized as tr-type G.
+At position 109 to 218, the domain is characterized as SET.
+At position 5 to 226, the domain is characterized as ABC transporter.
+At position 4 to 82, the domain is characterized as ACT.
+At position 91 to 167, the domain is characterized as PRC barrel.
+At position 81 to 183, the domain is characterized as PA.
+At position 60 to 112, the domain is characterized as SANT.
+At position 349 to 434, the domain is characterized as SWIRM.
+At position 789 to 1144, the domain is characterized as G-alpha.
+At position 327 to 376, the domain is characterized as bHLH.
+At position 111 to 412, the domain is characterized as USP.
+At position 145 to 534, the domain is characterized as Protein kinase.
+At position 281 to 406, the domain is characterized as AB hydrolase-1.
+At position 348 to 494, the domain is characterized as ELMO.
+At position 12 to 255, the domain is characterized as Lon N-terminal.
+At position 689 to 874, the domain is characterized as Lon proteolytic.
+At position 71 to 260, the domain is characterized as RNase H type-2.
+At position 217 to 372, the domain is characterized as TrmE-type G.
+At position 5 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 551 to 667, the domain is characterized as sHSP.
+At position 495 to 668, the domain is characterized as tr-type G.
+At position 173 to 271, the domain is characterized as PpiC 1.
+At position 280 to 380, the domain is characterized as PpiC 2.
+At position 125 to 281, the domain is characterized as PID.
+At position 539 to 725, the domain is characterized as Rab-GAP TBC.
+At position 15 to 145, the domain is characterized as VHS.
+At position 217 to 276, the domain is characterized as SH3.
+At position 185 to 372, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 141, the domain is characterized as Toprim.
+At position 114 to 193, the domain is characterized as PDZ 1.
+At position 198 to 273, the domain is characterized as PDZ 2.
+At position 1 to 134, the domain is characterized as B12-binding.
+At position 261 to 320, the domain is characterized as SH3.
+At position 38 to 115, the domain is characterized as Inhibitor I9.
+At position 119 to 595, the domain is characterized as Peptidase S8.
+At position 136 to 422, the domain is characterized as tr-type G.
+At position 178 to 501, the domain is characterized as USP.
+At position 3 to 131, the domain is characterized as CMP/dCMP-type deaminase.
+At position 571 to 666, the domain is characterized as SH2.
+At position 74 to 273, the domain is characterized as TLDc.
+At position 96 to 135, the domain is characterized as Agouti.
+At position 7 to 162, the domain is characterized as Exonuclease.
+At position 250 to 510, the domain is characterized as Helicase ATP-binding.
+At position 741 to 897, the domain is characterized as Helicase C-terminal.
+At position 1 to 418, the domain is characterized as PTS EIIC type-1.
+At position 449 to 527, the domain is characterized as PTS EIIB type-1.
+At position 292 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 203 to 493, the domain is characterized as Protein kinase.
+At position 24 to 99, the domain is characterized as KRAB.
+At position 167 to 420, the domain is characterized as MHD.
+At position 159 to 302, the domain is characterized as PPC.
+At position 315 to 531, the domain is characterized as Histidine kinase.
+At position 56 to 481, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 981 to 1287, the domain is characterized as PKS/mFAS DH.
+At position 2457 to 2534, the domain is characterized as Carrier.
+At position 138 to 441, the domain is characterized as NB-ARC.
+At position 332 to 413, the domain is characterized as Death.
+At position 148 to 204, the domain is characterized as BTB.
+At position 26 to 66, the domain is characterized as LRRNT.
+At position 336 to 365, the domain is characterized as IQ.
+At position 27 to 252, the domain is characterized as ABC transporter.
+At position 45 to 172, the domain is characterized as Nudix hydrolase.
+At position 60 to 333, the domain is characterized as Dynamin-type G.
+At position 567 to 655, the domain is characterized as GED.
+At position 246 to 404, the domain is characterized as Helicase ATP-binding.
+At position 422 to 578, the domain is characterized as Helicase C-terminal.
+At position 22 to 131, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 207 to 320, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 89 to 222, the domain is characterized as GST C-terminal.
+At position 25 to 136, the domain is characterized as Thioredoxin 1.
+At position 154 to 269, the domain is characterized as Thioredoxin 2.
+At position 272 to 314, the domain is characterized as UBA.
+At position 45 to 337, the domain is characterized as ABC transmembrane type-1 1.
+At position 373 to 609, the domain is characterized as ABC transporter 1.
+At position 678 to 969, the domain is characterized as ABC transmembrane type-1 2.
+At position 1035 to 1321, the domain is characterized as ABC transporter 2.
+At position 135 to 196, the domain is characterized as PWWP.
+At position 72 to 189, the domain is characterized as C-type lectin.
+At position 176 to 356, the domain is characterized as Glutamine amidotransferase type-1.
+At position 416 to 629, the domain is characterized as Protein kinase 2.
+At position 9 to 331, the domain is characterized as Kinesin motor.
+At position 256 to 501, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 47 to 151, the domain is characterized as Cyclin N-terminal.
+At position 18 to 73, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 86 to 139, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 156 to 317, the domain is characterized as SUN.
+At position 165 to 221, the domain is characterized as BSD 1.
+At position 243 to 295, the domain is characterized as BSD 2.
+At position 387 to 512, the domain is characterized as IPT/TIG.
+At position 350 to 428, the domain is characterized as PB1.
+At position 456 to 515, the domain is characterized as SH3 2.
+At position 1842 to 1918, the domain is characterized as Carrier 2.
+At position 223 to 247, the domain is characterized as Pentapeptide repeat 1.
+At position 253 to 292, the domain is characterized as Pentapeptide repeat 2.
+At position 293 to 327, the domain is characterized as Pentapeptide repeat 3.
+At position 16 to 255, the domain is characterized as ABC transporter.
+At position 403 to 621, the domain is characterized as tr-type G.
+At position 469 to 519, the domain is characterized as DHHC.
+At position 50 to 326, the domain is characterized as Protein kinase.
+At position 24 to 151, the domain is characterized as C-type lectin.
+At position 35 to 301, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 295 to 548, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 250 to 445, the domain is characterized as GATase cobBQ-type.
+At position 499 to 599, the domain is characterized as PH.
+At position 1138 to 1385, the domain is characterized as PPM-type phosphatase.
+At position 45 to 393, the domain is characterized as Peptidase A1.
+At position 24 to 64, the domain is characterized as Chitin-binding type-1.
+At position 42 to 277, the domain is characterized as ABC transporter.
+At position 188 to 273, the domain is characterized as RCK C-terminal 1.
+At position 319 to 509, the domain is characterized as Rho-GAP.
+At position 7 to 59, the domain is characterized as PQ-loop.
+At position 611 to 682, the domain is characterized as MBD.
+At position 744 to 817, the domain is characterized as Pre-SET.
+At position 820 to 1282, the domain is characterized as SET.
+At position 1291 to 1307, the domain is characterized as Post-SET.
+At position 15 to 218, the domain is characterized as FAD-binding PCMH-type.
+At position 1808 to 1899, the domain is characterized as Fibronectin type-III 2.
+At position 1901 to 2017, the domain is characterized as Fibronectin type-III 3.
+At position 44 to 126, the domain is characterized as Lipoyl-binding.
+At position 1085 to 1147, the domain is characterized as SH3.
+At position 672 to 848, the domain is characterized as PCI.
+At position 89 to 209, the domain is characterized as PX.
+At position 8 to 63, the domain is characterized as DEK-C.
+At position 320 to 392, the domain is characterized as ACT 1.
+At position 14 to 185, the domain is characterized as Velvet.
+At position 113 to 148, the domain is characterized as QLQ.
+At position 179 to 223, the domain is characterized as WRC.
+At position 189 to 252, the domain is characterized as FHA.
+At position 24 to 127, the domain is characterized as SWIRM.
+At position 242 to 293, the domain is characterized as SANT.
+At position 224 to 407, the domain is characterized as PCI.
+At position 151 to 259, the domain is characterized as CUB 1.
+At position 261 to 320, the domain is characterized as Sushi 1.
+At position 322 to 436, the domain is characterized as CUB 2.
+At position 439 to 500, the domain is characterized as Sushi 2.
+At position 502 to 613, the domain is characterized as CUB 3.
+At position 617 to 676, the domain is characterized as Sushi 3.
+At position 678 to 741, the domain is characterized as Sushi 4.
+At position 744 to 805, the domain is characterized as Sushi 5.
+At position 172 to 200, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 201 to 230, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 14 to 78, the domain is characterized as SAM.
+At position 323 to 487, the domain is characterized as Helicase ATP-binding.
+At position 551 to 731, the domain is characterized as Helicase C-terminal.
+At position 82 to 194, the domain is characterized as Rieske.
+At position 189 to 284, the domain is characterized as RRM 1.
+At position 154 to 253, the domain is characterized as PpiC.
+At position 1 to 142, the domain is characterized as SPX.
+At position 37 to 495, the domain is characterized as Sema.
+At position 497 to 544, the domain is characterized as PSI.
+At position 574 to 632, the domain is characterized as Ig-like C2-type.
+At position 246 to 500, the domain is characterized as EAL.
+At position 1577 to 1659, the domain is characterized as Ig-like.
+At position 1702 to 1934, the domain is characterized as Alpha-type protein kinase.
+At position 395 to 466, the domain is characterized as TRAM.
+At position 558 to 622, the domain is characterized as SAM 1.
+At position 630 to 693, the domain is characterized as SAM 2.
+At position 718 to 783, the domain is characterized as SAM 3.
+At position 41 to 162, the domain is characterized as MATH.
+At position 201 to 269, the domain is characterized as BTB.
+At position 11 to 99, the domain is characterized as Acylphosphatase-like.
+At position 27 to 69, the domain is characterized as CAP-Gly.
+At position 115 to 161, the domain is characterized as F-box.
+At position 76 to 123, the domain is characterized as WAP 1.
+At position 127 to 177, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 179 to 226, the domain is characterized as WAP 2.
+At position 228 to 272, the domain is characterized as WAP 3.
+At position 48 to 156, the domain is characterized as Cadherin 1.
+At position 157 to 266, the domain is characterized as Cadherin 2.
+At position 267 to 386, the domain is characterized as Cadherin 3.
+At position 383 to 494, the domain is characterized as Cadherin 4.
+At position 210 to 540, the domain is characterized as Kinesin motor.
+At position 40 to 245, the domain is characterized as BPL/LPL catalytic.
+At position 153 to 465, the domain is characterized as IF rod.
+At position 10 to 81, the domain is characterized as J.
+At position 92 to 147, the domain is characterized as DPH-type MB.
+At position 253 to 441, the domain is characterized as GATase cobBQ-type.
+At position 355 to 399, the domain is characterized as LysM.
+At position 750 to 823, the domain is characterized as Carrier 1.
+At position 1819 to 1895, the domain is characterized as Carrier 2.
+At position 3 to 111, the domain is characterized as SSB.
+At position 300 to 374, the domain is characterized as HTH OST-type 3.
+At position 530 to 589, the domain is characterized as Tudor.
+At position 317 to 357, the domain is characterized as UBA 2.
+At position 124 to 192, the domain is characterized as H15.
+At position 1 to 133, the domain is characterized as DAGKc.
+At position 30 to 698, the domain is characterized as PFL.
+At position 705 to 828, the domain is characterized as Glycine radical.
+At position 3 to 203, the domain is characterized as HORMA.
+At position 31 to 205, the domain is characterized as Exonuclease.
+At position 563 to 660, the domain is characterized as tRNA-binding.
+At position 166 to 252, the domain is characterized as Toprim.
+At position 57 to 143, the domain is characterized as Doublecortin 1.
+At position 186 to 269, the domain is characterized as Doublecortin 2.
+At position 390 to 647, the domain is characterized as Protein kinase.
+At position 4 to 278, the domain is characterized as tr-type G.
+At position 9 to 118, the domain is characterized as Longin.
+At position 133 to 193, the domain is characterized as v-SNARE coiled-coil homology.
+At position 1516 to 1585, the domain is characterized as Pre-SET.
+At position 1590 to 1750, the domain is characterized as SET.
+At position 1800 to 1816, the domain is characterized as Post-SET.
+At position 260 to 359, the domain is characterized as BACK.
+At position 347 to 425, the domain is characterized as OCT.
+At position 499 to 565, the domain is characterized as FHA.
+At position 32 to 112, the domain is characterized as Ig-like.
+At position 178 to 205, the domain is characterized as ITAM.
+At position 1 to 142, the domain is characterized as IF rod.
+At position 119 to 433, the domain is characterized as IF rod.
+At position 180 to 366, the domain is characterized as Glutamine amidotransferase type-1.
+At position 516 to 708, the domain is characterized as ATP-grasp 1.
+At position 1054 to 1245, the domain is characterized as ATP-grasp 2.
+At position 1318 to 1474, the domain is characterized as MGS-like.
+At position 97 to 254, the domain is characterized as Tyrosine-protein phosphatase.
+At position 109 to 199, the domain is characterized as Cytochrome c 1.
+At position 604 to 683, the domain is characterized as BRCT.
+At position 53 to 94, the domain is characterized as Gla.
+At position 116 to 154, the domain is characterized as EGF-like 1; calcium-binding.
+At position 156 to 196, the domain is characterized as EGF-like 2; calcium-binding.
+At position 197 to 237, the domain is characterized as EGF-like 3; calcium-binding.
+At position 238 to 278, the domain is characterized as EGF-like 4; calcium-binding.
+At position 298 to 470, the domain is characterized as Laminin G-like 1.
+At position 477 to 670, the domain is characterized as Laminin G-like 2.
+At position 42 to 107, the domain is characterized as Collagen-like.
+At position 108 to 244, the domain is characterized as C1q.
+At position 339 to 431, the domain is characterized as PH.
+At position 454 to 577, the domain is characterized as Arf-GAP.
+At position 381 to 554, the domain is characterized as tr-type G.
+At position 196 to 408, the domain is characterized as Helicase ATP-binding.
+At position 442 to 631, the domain is characterized as Helicase C-terminal.
+At position 24 to 135, the domain is characterized as Ig-like V-type 1.
+At position 294 to 536, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 226, the domain is characterized as ATLF-like.
+At position 242 to 470, the domain is characterized as TR mART core.
+At position 176 to 255, the domain is characterized as RRM 2.
+At position 282 to 354, the domain is characterized as RRM 3.
+At position 191 to 271, the domain is characterized as KH.
+At position 24 to 68, the domain is characterized as CAP-Gly.
+At position 335 to 377, the domain is characterized as LRRCT.
+At position 153 to 300, the domain is characterized as TRUD.
+At position 28 to 103, the domain is characterized as Ubiquitin-like.
+At position 102 to 175, the domain is characterized as Ubiquitin-like.
+At position 40 to 215, the domain is characterized as tr-type G.
+At position 86 to 155, the domain is characterized as SH3.
+At position 19 to 356, the domain is characterized as Kinesin motor.
+At position 140 to 433, the domain is characterized as JmjC.
+At position 47 to 161, the domain is characterized as sHSP.
+At position 89 to 118, the domain is characterized as IQ 1.
+At position 907 to 932, the domain is characterized as IQ 2.
+At position 928 to 955, the domain is characterized as IQ 3.
+At position 952 to 979, the domain is characterized as IQ 4.
+At position 1091 to 1119, the domain is characterized as IQ 5.
+At position 1114 to 1143, the domain is characterized as IQ 6.
+At position 21 to 74, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 11 to 127, the domain is characterized as MTTase N-terminal.
+At position 150 to 378, the domain is characterized as Radical SAM core.
+At position 381 to 449, the domain is characterized as TRAM.
+At position 7 to 66, the domain is characterized as TRAM.
+At position 413 to 578, the domain is characterized as PID 1.
+At position 584 to 736, the domain is characterized as PID 2.
+At position 168 to 463, the domain is characterized as IF rod.
+At position 324 to 409, the domain is characterized as PDZ.
+At position 40 to 81, the domain is characterized as Collagen-like.
+At position 15 to 170, the domain is characterized as Thioredoxin.
+At position 10 to 212, the domain is characterized as tr-type G.
+At position 688 to 810, the domain is characterized as N-terminal Ras-GEF.
+At position 840 to 1064, the domain is characterized as Ras-GEF.
+At position 118 to 307, the domain is characterized as ATP-grasp.
+At position 181 to 295, the domain is characterized as SRCR 2.
+At position 319 to 418, the domain is characterized as SRCR 3.
+At position 428 to 537, the domain is characterized as SRCR 4.
+At position 51 to 300, the domain is characterized as Peptidase S6.
+At position 35 to 280, the domain is characterized as AB hydrolase-1.
+At position 493 to 700, the domain is characterized as MCM.
+At position 53 to 127, the domain is characterized as H15.
+At position 110 to 293, the domain is characterized as tr-type G.
+At position 1 to 647, the domain is characterized as Peptidase M13.
+At position 113 to 312, the domain is characterized as Peptidase M12A.
+At position 306 to 345, the domain is characterized as EGF-like.
+At position 371 to 487, the domain is characterized as CUB.
+At position 628 to 676, the domain is characterized as TSP type-1.
+At position 32 to 137, the domain is characterized as Ig-like V-type.
+At position 148 to 247, the domain is characterized as Ig-like C1-type 1.
+At position 254 to 348, the domain is characterized as Ig-like C1-type 2.
+At position 32 to 79, the domain is characterized as KH.
+At position 3 to 385, the domain is characterized as BRO1.
+At position 79 to 141, the domain is characterized as CBS 1.
+At position 144 to 201, the domain is characterized as CBS 2.
+At position 57 to 117, the domain is characterized as SH3 1.
+At position 183 to 243, the domain is characterized as SH3 2.
+At position 287 to 352, the domain is characterized as SH3 3.
+At position 34 to 249, the domain is characterized as MIF4G.
+At position 17 to 57, the domain is characterized as EGF-like 1.
+At position 60 to 98, the domain is characterized as EGF-like 2.
+At position 99 to 137, the domain is characterized as EGF-like 3; calcium-binding.
+At position 139 to 179, the domain is characterized as EGF-like 4.
+At position 178 to 214, the domain is characterized as EGF-like 5.
+At position 215 to 254, the domain is characterized as EGF-like 6; calcium-binding.
+At position 27 to 219, the domain is characterized as Helicase ATP-binding.
+At position 244 to 386, the domain is characterized as Helicase C-terminal.
+At position 18 to 202, the domain is characterized as ABC transmembrane type-1.
+At position 8 to 224, the domain is characterized as Radical SAM core.
+At position 51 to 142, the domain is characterized as SH2.
+At position 134 to 590, the domain is characterized as Urease.
+At position 579 to 649, the domain is characterized as Dockerin.
+At position 1 to 66, the domain is characterized as Disintegrin.
+At position 29 to 106, the domain is characterized as IGFBP N-terminal.
+At position 328 to 385, the domain is characterized as VWFC 1.
+At position 395 to 451, the domain is characterized as VWFC 2.
+At position 463 to 492, the domain is characterized as Antistasin-like 1.
+At position 499 to 526, the domain is characterized as Antistasin-like 2.
+At position 533 to 558, the domain is characterized as Antistasin-like 3.
+At position 561 to 586, the domain is characterized as Antistasin-like 4.
+At position 601 to 658, the domain is characterized as VWFC 3.
+At position 672 to 730, the domain is characterized as VWFC 4.
+At position 746 to 804, the domain is characterized as VWFC 5.
+At position 810 to 867, the domain is characterized as VWFC 6.
+At position 81 to 381, the domain is characterized as AB hydrolase-1.
+At position 332 to 460, the domain is characterized as RRM 4.
+At position 419 to 629, the domain is characterized as FtsK.
+At position 67 to 341, the domain is characterized as Pyruvate carboxyltransferase.
+At position 5 to 354, the domain is characterized as Kinesin motor.
+At position 516 to 572, the domain is characterized as FHA.
+At position 1580 to 1678, the domain is characterized as PH.
+At position 77 to 204, the domain is characterized as TBDR plug.
+At position 212 to 999, the domain is characterized as TBDR beta-barrel.
+At position 350 to 631, the domain is characterized as Protein kinase.
+At position 1 to 272, the domain is characterized as Protein kinase.
+At position 9 to 64, the domain is characterized as HTH lacI-type.
+At position 19 to 230, the domain is characterized as tr-type G.
+At position 39 to 113, the domain is characterized as Lipoyl-binding.
+At position 2 to 89, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 124 to 158, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 178 to 209, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 163 to 273, the domain is characterized as SET.
+At position 42 to 196, the domain is characterized as Tyrosine-protein phosphatase.
+At position 316 to 365, the domain is characterized as bHLH.
+At position 25 to 251, the domain is characterized as ABC transmembrane type-2.
+At position 135 to 381, the domain is characterized as Radical SAM core.
+At position 126 to 440, the domain is characterized as Peptidase S8.
+At position 449 to 581, the domain is characterized as P/Homo B.
+At position 24 to 94, the domain is characterized as KH type-2.
+At position 18 to 215, the domain is characterized as Ch-type lysozyme.
+At position 6 to 112, the domain is characterized as Longin.
+At position 62 to 209, the domain is characterized as Nudix hydrolase.
+At position 706 to 791, the domain is characterized as Fibronectin type-III 1.
+At position 797 to 887, the domain is characterized as Fibronectin type-III 2.
+At position 897 to 984, the domain is characterized as Fibronectin type-III 3.
+At position 983 to 1090, the domain is characterized as CBM2.
+At position 25 to 157, the domain is characterized as N-terminal Ras-GEF.
+At position 1194 to 1434, the domain is characterized as Ras-GEF.
+At position 288 to 371, the domain is characterized as PDZ.
+At position 56 to 440, the domain is characterized as Peptidase A1.
+At position 27 to 130, the domain is characterized as Ig-like V-type.
+At position 375 to 650, the domain is characterized as Protein kinase.
+At position 48 to 315, the domain is characterized as Pyruvate carboxyltransferase.
+At position 45 to 217, the domain is characterized as Laminin G-like 1.
+At position 224 to 390, the domain is characterized as Laminin G-like 2.
+At position 38 to 289, the domain is characterized as AB hydrolase-1.
+At position 151 to 339, the domain is characterized as Helicase ATP-binding.
+At position 370 to 561, the domain is characterized as Helicase C-terminal.
+At position 181 to 247, the domain is characterized as KH.
+At position 307 to 400, the domain is characterized as HD.
+At position 22 to 115, the domain is characterized as Ig-like 1.
+At position 76 to 208, the domain is characterized as ADD.
+At position 298 to 361, the domain is characterized as WWE 1.
+At position 364 to 458, the domain is characterized as WWE 2.
+At position 484 to 698, the domain is characterized as PARP catalytic.
+At position 235 to 360, the domain is characterized as CBM21.
+At position 55 to 243, the domain is characterized as RNase H type-2.
+At position 938 to 1198, the domain is characterized as Protein kinase.
+At position 319 to 527, the domain is characterized as AB hydrolase-1.
+At position 290 to 526, the domain is characterized as NR LBD.
+At position 193 to 266, the domain is characterized as RRM 1.
+At position 278 to 351, the domain is characterized as RRM 2.
+At position 18 to 345, the domain is characterized as Kinesin motor.
+At position 105 to 133, the domain is characterized as IQ 1.
+At position 134 to 156, the domain is characterized as IQ 2.
+At position 65 to 292, the domain is characterized as OBG-type G.
+At position 292 to 369, the domain is characterized as TGS.
+At position 361 to 639, the domain is characterized as Protein kinase.
+At position 140 to 223, the domain is characterized as PDZ 1.
+At position 279 to 361, the domain is characterized as PDZ 2.
+At position 816 to 899, the domain is characterized as PDZ 3.
+At position 19 to 213, the domain is characterized as Lon N-terminal.
+At position 77 to 193, the domain is characterized as OmpA-like.
+At position 58 to 280, the domain is characterized as BURP.
+At position 99 to 176, the domain is characterized as PRC barrel.
+At position 169 to 295, the domain is characterized as C-type lectin.
+At position 32 to 222, the domain is characterized as RNase H type-2.
+At position 228 to 392, the domain is characterized as PCI.
+At position 45 to 129, the domain is characterized as RRM.
+At position 122 to 153, the domain is characterized as EGF-like 2.
+At position 148 to 182, the domain is characterized as EGF-like 3.
+At position 183 to 212, the domain is characterized as EGF-like 4.
+At position 213 to 241, the domain is characterized as EGF-like 5.
+At position 236 to 270, the domain is characterized as EGF-like 6.
+At position 372 to 403, the domain is characterized as EGF-like 7.
+At position 337 to 489, the domain is characterized as VPS9.
+At position 3 to 283, the domain is characterized as DegV.
+At position 278 to 364, the domain is characterized as RRM.
+At position 1734 to 2021, the domain is characterized as Autotransporter.
+At position 390 to 507, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 508 to 611, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 439 to 638, the domain is characterized as EXS.
+At position 53 to 185, the domain is characterized as RUN.
+At position 585 to 634, the domain is characterized as Myb-like 1.
+At position 634 to 718, the domain is characterized as Myb-like 2.
+At position 26 to 61, the domain is characterized as EF-hand.
+At position 58 to 158, the domain is characterized as SRCR 1.
+At position 189 to 289, the domain is characterized as SRCR 2.
+At position 344 to 444, the domain is characterized as SRCR 3.
+At position 473 to 573, the domain is characterized as SRCR 4.
+At position 282 to 417, the domain is characterized as Fido.
+At position 1551 to 1642, the domain is characterized as Olduvai.
+At position 246 to 437, the domain is characterized as GATase cobBQ-type.
+At position 272 to 677, the domain is characterized as USP.
+At position 402 to 492, the domain is characterized as BRCT.
+At position 53 to 185, the domain is characterized as Jacalin-type lectin.
+At position 61 to 298, the domain is characterized as Radical SAM core.
+At position 70 to 113, the domain is characterized as CUE.
+At position 364 to 507, the domain is characterized as RCK N-terminal.
+At position 29 to 119, the domain is characterized as Ig-like 1.
+At position 309 to 398, the domain is characterized as Ig-like 2.
+At position 454 to 539, the domain is characterized as Ig-like 3.
+At position 646 to 741, the domain is characterized as Fibronectin type-III 1.
+At position 746 to 845, the domain is characterized as Fibronectin type-III 2.
+At position 847 to 942, the domain is characterized as Fibronectin type-III 3.
+At position 946 to 1030, the domain is characterized as Ig-like 4.
+At position 1043 to 1137, the domain is characterized as Fibronectin type-III 4.
+At position 1151 to 1245, the domain is characterized as Ig-like 5.
+At position 21 to 190, the domain is characterized as SprT-like.
+At position 33 to 323, the domain is characterized as ABC transmembrane type-1 1.
+At position 360 to 596, the domain is characterized as ABC transporter 1.
+At position 676 to 964, the domain is characterized as ABC transmembrane type-1 2.
+At position 998 to 1236, the domain is characterized as ABC transporter 2.
+At position 44 to 133, the domain is characterized as PPIase FKBP-type.
+At position 479 to 540, the domain is characterized as LIM zinc-binding 1.
+At position 544 to 603, the domain is characterized as LIM zinc-binding 2.
+At position 604 to 673, the domain is characterized as LIM zinc-binding 3.
+At position 233 to 322, the domain is characterized as EH 1.
+At position 266 to 301, the domain is characterized as EF-hand 1.
+At position 576 to 665, the domain is characterized as EH 2.
+At position 609 to 644, the domain is characterized as EF-hand 2.
+At position 1599 to 1616, the domain is characterized as WH2.
+At position 221 to 382, the domain is characterized as TrmE-type G.
+At position 41 to 211, the domain is characterized as Rab-GAP TBC.
+At position 56 to 193, the domain is characterized as MPN.
+At position 59 to 101, the domain is characterized as LDL-receptor class A.
+At position 102 to 202, the domain is characterized as SRCR.
+At position 203 to 432, the domain is characterized as Peptidase S1.
+At position 180 to 395, the domain is characterized as CP-type G.
+At position 223 to 432, the domain is characterized as Cytochrome c.
+At position 44 to 129, the domain is characterized as Cytochrome c.
+At position 46 to 326, the domain is characterized as YjeF C-terminal.
+At position 357 to 510, the domain is characterized as SEFIR.
+At position 23 to 408, the domain is characterized as Helicase ATP-binding.
+At position 1363 to 1445, the domain is characterized as SH2.
+At position 54 to 307, the domain is characterized as TSP type-1 1.
+At position 378 to 478, the domain is characterized as SWIRM.
+At position 20 to 130, the domain is characterized as HIT.
+At position 47 to 310, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 18 to 187, the domain is characterized as uDENN.
+At position 8 to 180, the domain is characterized as Clp R.
+At position 71 to 165, the domain is characterized as Fibronectin type-III 1.
+At position 298 to 395, the domain is characterized as Fibronectin type-III 2.
+At position 401 to 491, the domain is characterized as Fibronectin type-III 3.
+At position 563 to 819, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 850 to 1129, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 126 to 224, the domain is characterized as Fibronectin type-III.
+At position 259 to 453, the domain is characterized as GATase cobBQ-type.
+At position 40 to 260, the domain is characterized as ABC transporter.
+At position 4 to 56, the domain is characterized as HTH myb-type 1.
+At position 57 to 111, the domain is characterized as HTH myb-type 2.
+At position 820 to 893, the domain is characterized as Carrier.
+At position 81 to 203, the domain is characterized as GST C-terminal.
+At position 32 to 124, the domain is characterized as Ig-like.
+At position 50 to 113, the domain is characterized as HMA.
+At position 497 to 532, the domain is characterized as EF-hand 4.
+At position 32 to 203, the domain is characterized as BPL/LPL catalytic.
+At position 297 to 485, the domain is characterized as Helicase ATP-binding 1.
+At position 516 to 735, the domain is characterized as Helicase C-terminal 1.
+At position 795 to 1100, the domain is characterized as SEC63 1.
+At position 1149 to 1324, the domain is characterized as Helicase ATP-binding 2.
+At position 1355 to 1550, the domain is characterized as Helicase C-terminal 2.
+At position 1626 to 1776, the domain is characterized as SEC63 2.
+At position 560 to 619, the domain is characterized as CBS 1.
+At position 788 to 845, the domain is characterized as CBS 2.
+At position 11 to 226, the domain is characterized as tr-type G.
+At position 84 to 342, the domain is characterized as Protein kinase.
+At position 495 to 525, the domain is characterized as EF-hand 4.
+At position 241 to 314, the domain is characterized as SPOR.
+At position 75 to 333, the domain is characterized as Protein kinase.
+At position 448 to 483, the domain is characterized as EF-hand 3.
+At position 484 to 519, the domain is characterized as EF-hand 4.
+At position 287 to 426, the domain is characterized as N-acetyltransferase.
+At position 129 to 313, the domain is characterized as FAD-binding PCMH-type.
+At position 223 to 417, the domain is characterized as TrmE-type G.
+At position 102 to 176, the domain is characterized as Cytochrome b5 heme-binding.
+At position 11 to 213, the domain is characterized as ABC transporter.
+At position 131 to 211, the domain is characterized as COMM.
+At position 168 to 345, the domain is characterized as Glutamine amidotransferase type-1.
+At position 45 to 304, the domain is characterized as Protein kinase.
+At position 424 to 513, the domain is characterized as SH2.
+At position 82 to 192, the domain is characterized as Expansin-like EG45.
+At position 205 to 287, the domain is characterized as Expansin-like CBD.
+At position 31 to 153, the domain is characterized as Bulb-type lectin.
+At position 347 to 428, the domain is characterized as PAN.
+At position 526 to 807, the domain is characterized as Protein kinase.
+At position 29 to 146, the domain is characterized as MTTase N-terminal.
+At position 408 to 467, the domain is characterized as TRAM.
+At position 48 to 265, the domain is characterized as Radical SAM core.
+At position 81 to 205, the domain is characterized as RGS 1.
+At position 214 to 337, the domain is characterized as RGS 2.
+At position 179 to 359, the domain is characterized as Helicase ATP-binding.
+At position 391 to 537, the domain is characterized as Helicase C-terminal.
+At position 237 to 394, the domain is characterized as VLRF1.
+At position 139 to 367, the domain is characterized as Rho-GAP.
+At position 285 to 337, the domain is characterized as bHLH.
+At position 14 to 146, the domain is characterized as CMP/dCMP-type deaminase.
+At position 148 to 322, the domain is characterized as CRAL-TRIO.
+At position 153 to 394, the domain is characterized as NR LBD.
+At position 67 to 217, the domain is characterized as HD.
+At position 169 to 405, the domain is characterized as Radical SAM core.
+At position 408 to 475, the domain is characterized as TRAM.
+At position 37 to 133, the domain is characterized as HD.
+At position 113 to 436, the domain is characterized as Protein kinase.
+At position 437 to 499, the domain is characterized as AGC-kinase C-terminal.
+At position 57 to 606, the domain is characterized as PLA2c.
+At position 2 to 134, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 25 to 98, the domain is characterized as Importin N-terminal.
+At position 1 to 18, the domain is characterized as EF-hand 1.
+At position 19 to 54, the domain is characterized as EF-hand 2.
+At position 56 to 91, the domain is characterized as EF-hand 3.
+At position 92 to 124, the domain is characterized as EF-hand 4.
+At position 29 to 188, the domain is characterized as Helicase ATP-binding.
+At position 11 to 187, the domain is characterized as Ku.
+At position 33 to 89, the domain is characterized as Kazal-like.
+At position 260 to 356, the domain is characterized as Cytochrome c.
+At position 537 to 660, the domain is characterized as STAS.
+At position 71 to 120, the domain is characterized as CWF21.
+At position 119 to 288, the domain is characterized as tr-type G.
+At position 142 to 324, the domain is characterized as Helicase ATP-binding.
+At position 336 to 498, the domain is characterized as Helicase C-terminal.
+At position 31 to 213, the domain is characterized as Eph LBD.
+At position 344 to 452, the domain is characterized as Fibronectin type-III 1.
+At position 453 to 548, the domain is characterized as Fibronectin type-III 2.
+At position 637 to 900, the domain is characterized as Protein kinase.
+At position 281 to 347, the domain is characterized as MIT 1.
+At position 376 to 444, the domain is characterized as MIT 2.
+At position 449 to 620, the domain is characterized as tr-type G.
+At position 442 to 565, the domain is characterized as Ricin B-type lectin.
+At position 804 to 907, the domain is characterized as Cytochrome c 1.
+At position 949 to 1057, the domain is characterized as Cytochrome c 2.
+At position 1075 to 1163, the domain is characterized as Cytochrome c 3.
+At position 274 to 341, the domain is characterized as DRBM 2.
+At position 408 to 735, the domain is characterized as A to I editase.
+At position 7 to 261, the domain is characterized as Chorismate mutase.
+At position 326 to 361, the domain is characterized as EF-hand 1.
+At position 362 to 397, the domain is characterized as EF-hand 2.
+At position 398 to 433, the domain is characterized as EF-hand 3.
+At position 437 to 467, the domain is characterized as EF-hand 4.
+At position 6 to 129, the domain is characterized as C2.
+At position 325 to 359, the domain is characterized as WW 1.
+At position 519 to 552, the domain is characterized as WW 2.
+At position 33 to 99, the domain is characterized as KH.
+At position 10 to 122, the domain is characterized as MTTase N-terminal.
+At position 372 to 446, the domain is characterized as TRAM.
+At position 185 to 439, the domain is characterized as AB hydrolase-1.
+At position 216 to 370, the domain is characterized as TrmE-type G.
+At position 146 to 188, the domain is characterized as LRRCT.
+At position 35 to 263, the domain is characterized as Cupin type-1 1.
+At position 266 to 470, the domain is characterized as Peptidase M12B.
+At position 561 to 616, the domain is characterized as TSP type-1 1.
+At position 854 to 912, the domain is characterized as TSP type-1 2.
+At position 914 to 971, the domain is characterized as TSP type-1 3.
+At position 975 to 1029, the domain is characterized as TSP type-1 4.
+At position 62 to 293, the domain is characterized as OBG-type G.
+At position 293 to 368, the domain is characterized as TGS.
+At position 528 to 823, the domain is characterized as Protein kinase.
+At position 20 to 112, the domain is characterized as ARID.
+At position 230 to 329, the domain is characterized as Fe2OG dioxygenase.
+At position 169 to 329, the domain is characterized as Integrase catalytic.
+At position 21 to 60, the domain is characterized as EGF-like 1.
+At position 61 to 112, the domain is characterized as EGF-like 2.
+At position 115 to 152, the domain is characterized as EGF-like 3.
+At position 153 to 189, the domain is characterized as EGF-like 4.
+At position 191 to 229, the domain is characterized as EGF-like 5; calcium-binding.
+At position 231 to 271, the domain is characterized as EGF-like 6.
+At position 273 to 309, the domain is characterized as EGF-like 7; calcium-binding.
+At position 311 to 350, the domain is characterized as EGF-like 8; calcium-binding.
+At position 352 to 388, the domain is characterized as EGF-like 9; calcium-binding.
+At position 389 to 427, the domain is characterized as EGF-like 10.
+At position 429 to 470, the domain is characterized as EGF-like 11; calcium-binding.
+At position 472 to 508, the domain is characterized as EGF-like 12; calcium-binding.
+At position 510 to 546, the domain is characterized as EGF-like 13; calcium-binding.
+At position 548 to 584, the domain is characterized as EGF-like 14; calcium-binding.
+At position 586 to 622, the domain is characterized as EGF-like 15; calcium-binding.
+At position 623 to 656, the domain is characterized as EGF-like 16.
+At position 658 to 686, the domain is characterized as EGF-like 17.
+At position 688 to 724, the domain is characterized as EGF-like 18.
+At position 726 to 762, the domain is characterized as EGF-like 19.
+At position 764 to 800, the domain is characterized as EGF-like 20.
+At position 803 to 839, the domain is characterized as EGF-like 21.
+At position 841 to 877, the domain is characterized as EGF-like 22.
+At position 878 to 924, the domain is characterized as EGF-like 23.
+At position 1002 to 1040, the domain is characterized as EGF-like 26.
+At position 1042 to 1081, the domain is characterized as EGF-like 27.
+At position 1083 to 1122, the domain is characterized as EGF-like 28.
+At position 1126 to 1167, the domain is characterized as EGF-like 29.
+At position 157 to 403, the domain is characterized as ABC transporter.
+At position 498 to 707, the domain is characterized as ABC transmembrane type-2.
+At position 55 to 85, the domain is characterized as EF-hand 2.
+At position 136 to 159, the domain is characterized as EF-hand 4.
+At position 593 to 673, the domain is characterized as BRCT.
+At position 124 to 438, the domain is characterized as FH2.
+At position 302 to 379, the domain is characterized as B5.
+At position 73 to 314, the domain is characterized as PPM-type phosphatase.
+At position 177 to 381, the domain is characterized as Histidine kinase.
+At position 88 to 284, the domain is characterized as Helicase ATP-binding.
+At position 555 to 712, the domain is characterized as Toprim.
+At position 339 to 450, the domain is characterized as PLAT.
+At position 133 to 224, the domain is characterized as Ig-like C2-type.
+At position 81 to 239, the domain is characterized as Thioredoxin.
+At position 10 to 295, the domain is characterized as tr-type G.
+At position 97 to 314, the domain is characterized as Radical SAM core.
+At position 52 to 121, the domain is characterized as POTRA.
+At position 466 to 584, the domain is characterized as LTD.
+At position 1 to 217, the domain is characterized as YjeF N-terminal.
+At position 300 to 551, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 194, the domain is characterized as TCTP.
+At position 18 to 210, the domain is characterized as Lon N-terminal.
+At position 63 to 336, the domain is characterized as Dynamin-type G.
+At position 569 to 657, the domain is characterized as GED.
+At position 171 to 277, the domain is characterized as Fe2OG dioxygenase.
+At position 45 to 77, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 87 to 116, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 528 to 605, the domain is characterized as PABC.
+At position 10 to 229, the domain is characterized as Peptidase S1.
+At position 1506 to 1634, the domain is characterized as MaoC-like.
+At position 546 to 587, the domain is characterized as Collagen-like 3.
+At position 1072 to 1127, the domain is characterized as Collagen-like 4.
+At position 1128 to 1172, the domain is characterized as Collagen-like 5.
+At position 1444 to 1499, the domain is characterized as Collagen-like 6.
+At position 107 to 453, the domain is characterized as GS catalytic.
+At position 281 to 380, the domain is characterized as Fibronectin type-III 1.
+At position 384 to 476, the domain is characterized as Fibronectin type-III 2.
+At position 480 to 573, the domain is characterized as Fibronectin type-III 3.
+At position 577 to 672, the domain is characterized as Fibronectin type-III 4.
+At position 676 to 768, the domain is characterized as Fibronectin type-III 5.
+At position 769 to 862, the domain is characterized as Fibronectin type-III 6.
+At position 874 to 960, the domain is characterized as Fibronectin type-III 7.
+At position 961 to 1055, the domain is characterized as Fibronectin type-III 8.
+At position 1059 to 1156, the domain is characterized as Fibronectin type-III 9.
+At position 487 to 527, the domain is characterized as EF-hand 2.
+At position 528 to 563, the domain is characterized as EF-hand 3.
+At position 564 to 602, the domain is characterized as EF-hand 4.
+At position 195 to 423, the domain is characterized as ABC transmembrane type-1.
+At position 86 to 166, the domain is characterized as PDZ.
+At position 36 to 118, the domain is characterized as GS beta-grasp.
+At position 135 to 382, the domain is characterized as GS catalytic.
+At position 20 to 85, the domain is characterized as J.
+At position 163 to 476, the domain is characterized as IF rod.
+At position 217 to 287, the domain is characterized as PAH 1.
+At position 404 to 474, the domain is characterized as PAH 2.
+At position 656 to 727, the domain is characterized as PAH 3.
+At position 23 to 112, the domain is characterized as HTH La-type RNA-binding.
+At position 123 to 216, the domain is characterized as RRM.
+At position 4 to 225, the domain is characterized as ABC transporter.
+At position 515 to 659, the domain is characterized as RUN.
+At position 835 to 893, the domain is characterized as SH3.
+At position 119 to 148, the domain is characterized as EF-hand 3.
+At position 605 to 684, the domain is characterized as Cytochrome c.
+At position 167 to 410, the domain is characterized as NR LBD.
+At position 209 to 275, the domain is characterized as KH.
+At position 76 to 110, the domain is characterized as SAP.
+At position 130 to 306, the domain is characterized as Exonuclease.
+At position 7 to 57, the domain is characterized as Myosin N-terminal SH3-like.
+At position 61 to 840, the domain is characterized as Myosin motor.
+At position 843 to 872, the domain is characterized as IQ 1.
+At position 866 to 895, the domain is characterized as IQ 2.
+At position 940 to 969, the domain is characterized as IQ 3.
+At position 1427 to 1695, the domain is characterized as Dilute.
+At position 692 to 785, the domain is characterized as PB1.
+At position 38 to 76, the domain is characterized as EGF-like.
+At position 744 to 1083, the domain is characterized as HECT.
+At position 107 to 353, the domain is characterized as PPM-type phosphatase.
+At position 1204 to 1273, the domain is characterized as S1 motif.
+At position 1316 to 1426, the domain is characterized as SH2.
+At position 3 to 176, the domain is characterized as Miro 1.
+At position 192 to 227, the domain is characterized as EF-hand 1.
+At position 881 to 955, the domain is characterized as Carrier.
+At position 549 to 819, the domain is characterized as Ras-GEF.
+At position 169 to 257, the domain is characterized as Sm.
+At position 34 to 155, the domain is characterized as OTU.
+At position 458 to 547, the domain is characterized as Pre-SET.
+At position 550 to 679, the domain is characterized as SET.
+At position 690 to 706, the domain is characterized as Post-SET.
+At position 72 to 188, the domain is characterized as RGS.
+At position 145 to 387, the domain is characterized as Radical SAM core.
+At position 389 to 461, the domain is characterized as TRAM.
+At position 21 to 104, the domain is characterized as UPAR/Ly6.
+At position 17 to 206, the domain is characterized as Glutamine amidotransferase type-1.
+At position 60 to 198, the domain is characterized as Flavodoxin-like.
+At position 241 to 399, the domain is characterized as FAD-binding FR-type.
+At position 486 to 656, the domain is characterized as tr-type G.
+At position 50 to 93, the domain is characterized as CUE.
+At position 17 to 269, the domain is characterized as BAR.
+At position 407 to 466, the domain is characterized as SH3.
+At position 246 to 318, the domain is characterized as Bromo 1.
+At position 408 to 480, the domain is characterized as Bromo 2.
+At position 570 to 650, the domain is characterized as NET.
+At position 16 to 293, the domain is characterized as Helicase ATP-binding.
+At position 514 to 692, the domain is characterized as Helicase C-terminal.
+At position 1 to 131, the domain is characterized as TIR.
+At position 187 to 279, the domain is characterized as RRM.
+At position 136 to 246, the domain is characterized as Cadherin 2.
+At position 247 to 353, the domain is characterized as Cadherin 3.
+At position 359 to 472, the domain is characterized as Cadherin 4.
+At position 473 to 576, the domain is characterized as Cadherin 5.
+At position 573 to 688, the domain is characterized as Cadherin 6.
+At position 703 to 784, the domain is characterized as BRCT.
+At position 167 to 307, the domain is characterized as OTU.
+At position 2 to 298, the domain is characterized as Glutamine amidotransferase type-2.
+At position 53 to 137, the domain is characterized as RRM.
+At position 27 to 143, the domain is characterized as CMP/dCMP-type deaminase.
+At position 53 to 194, the domain is characterized as PI-PLC X-box.
+At position 126 to 192, the domain is characterized as DRBM 1.
+At position 284 to 348, the domain is characterized as DRBM 2.
+At position 415 to 742, the domain is characterized as A to I editase.
+At position 19 to 148, the domain is characterized as VHS.
+At position 262 to 281, the domain is characterized as UIM 1.
+At position 293 to 312, the domain is characterized as UIM 2.
+At position 357 to 390, the domain is characterized as CBM10 1.
+At position 395 to 424, the domain is characterized as CBM10 2.
+At position 23 to 398, the domain is characterized as GH18.
+At position 495 to 553, the domain is characterized as Chitin-binding type-2.
+At position 325 to 617, the domain is characterized as BEACH.
+At position 410 to 530, the domain is characterized as TFIIS central.
+At position 688 to 791, the domain is characterized as SPOC.
+At position 814 to 956, the domain is characterized as Peptidase S59.
+At position 98 to 132, the domain is characterized as EF-hand 1; atypical.
+At position 141 to 174, the domain is characterized as EF-hand 2.
+At position 207 to 235, the domain is characterized as EF-hand 4.
+At position 236 to 270, the domain is characterized as EF-hand 5.
+At position 19 to 134, the domain is characterized as MTTase N-terminal.
+At position 390 to 460, the domain is characterized as TRAM.
+At position 259 to 325, the domain is characterized as PAS 2.
+At position 334 to 377, the domain is characterized as PAC.
+At position 18 to 86, the domain is characterized as Sm.
+At position 498 to 612, the domain is characterized as Toprim.
+At position 1 to 71, the domain is characterized as HTH gntR-type.
+At position 275 to 348, the domain is characterized as PUA.
+At position 19 to 72, the domain is characterized as ClpX-type ZB.
+At position 159 to 353, the domain is characterized as ABC transmembrane type-1.
+At position 1041 to 1294, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 307, the domain is characterized as tRNA-binding.
+At position 50 to 83, the domain is characterized as ShKT.
+At position 232 to 322, the domain is characterized as BRCT.
+At position 742 to 1067, the domain is characterized as Reverse transcriptase.
+At position 203 to 452, the domain is characterized as NR LBD.
+At position 4 to 138, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 146 to 246, the domain is characterized as Fibronectin type-III.
+At position 180 to 382, the domain is characterized as Pentraxin (PTX).
+At position 545 to 837, the domain is characterized as Protein kinase.
+At position 895 to 1025, the domain is characterized as Guanylate cyclase.
+At position 112 to 140, the domain is characterized as IQ 1.
+At position 141 to 163, the domain is characterized as IQ 2.
+At position 164 to 188, the domain is characterized as IQ 3.
+At position 3 to 105, the domain is characterized as Thioredoxin.
+At position 118 to 186, the domain is characterized as COMM.
+At position 39 to 273, the domain is characterized as Cupin type-1 1.
+At position 337 to 486, the domain is characterized as Cupin type-1 2.
+At position 291 to 450, the domain is characterized as SSD.
+At position 91 to 166, the domain is characterized as Smr.
+At position 138 to 190, the domain is characterized as bHLH.
+At position 124 to 216, the domain is characterized as PH.
+At position 275 to 324, the domain is characterized as bHLH.
+At position 116 to 337, the domain is characterized as Radical SAM core.
+At position 106 to 138, the domain is characterized as EF-hand 4.
+At position 133 to 170, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 742 to 840, the domain is characterized as BRCT 1.
+At position 936 to 1049, the domain is characterized as BRCT 2.
+At position 175 to 272, the domain is characterized as CRM.
+At position 45 to 126, the domain is characterized as Fibronectin type-III 1.
+At position 330 to 429, the domain is characterized as Fibronectin type-III 2.
+At position 430 to 529, the domain is characterized as Fibronectin type-III 3.
+At position 533 to 624, the domain is characterized as Fibronectin type-III 4.
+At position 622 to 714, the domain is characterized as Fibronectin type-III 5.
+At position 719 to 828, the domain is characterized as Fibronectin type-III 6.
+At position 1 to 111, the domain is characterized as C2.
+At position 211 to 236, the domain is characterized as WW 1.
+At position 294 to 319, the domain is characterized as WW 2.
+At position 351 to 376, the domain is characterized as WW 3.
+At position 463 to 767, the domain is characterized as HECT.
+At position 105 to 310, the domain is characterized as ATP-grasp.
+At position 14 to 65, the domain is characterized as bHLH.
+At position 8 to 71, the domain is characterized as HMA.
+At position 25 to 138, the domain is characterized as Bulb-type lectin.
+At position 16 to 325, the domain is characterized as ABC transmembrane type-1.
+At position 365 to 611, the domain is characterized as ABC transporter.
+At position 30 to 99, the domain is characterized as BTB.
+At position 134 to 236, the domain is characterized as BACK.
+At position 43 to 115, the domain is characterized as POTRA.
+At position 100 to 133, the domain is characterized as EGF-like 1.
+At position 135 to 251, the domain is characterized as CUB.
+At position 249 to 286, the domain is characterized as EGF-like 2.
+At position 706 to 751, the domain is characterized as PSI 1.
+At position 758 to 797, the domain is characterized as PSI 2.
+At position 798 to 922, the domain is characterized as C-type lectin.
+At position 935 to 986, the domain is characterized as PSI 3.
+At position 989 to 1064, the domain is characterized as PSI 4.
+At position 1066 to 1111, the domain is characterized as Laminin EGF-like 1.
+At position 1112 to 1160, the domain is characterized as Laminin EGF-like 2.
+At position 75 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 434 to 587, the domain is characterized as Helicase C-terminal.
+At position 54 to 221, the domain is characterized as FAD-binding PCMH-type.
+At position 497 to 772, the domain is characterized as Reverse transcriptase.
+At position 1242 to 1260, the domain is characterized as DUF1725.
+At position 28 to 100, the domain is characterized as Importin N-terminal.
+At position 449 to 480, the domain is characterized as EF-hand 3.
+At position 565 to 813, the domain is characterized as NR LBD.
+At position 8 to 100, the domain is characterized as HTH arsR-type.
+At position 190 to 382, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 193 to 306, the domain is characterized as PH.
+At position 417 to 515, the domain is characterized as SH2.
+At position 237 to 502, the domain is characterized as NR LBD.
+At position 158 to 382, the domain is characterized as Histidine kinase.
+At position 72 to 150, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 150 to 189, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 287 to 343, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 608 to 786, the domain is characterized as Helicase ATP-binding.
+At position 817 to 961, the domain is characterized as Helicase C-terminal.
+At position 32 to 166, the domain is characterized as Thioredoxin.
+At position 7 to 168, the domain is characterized as Flavodoxin-like.
+At position 224 to 491, the domain is characterized as FAD-binding FR-type.
+At position 65 to 219, the domain is characterized as N-acetyltransferase.
+At position 328 to 498, the domain is characterized as tr-type G.
+At position 41 to 106, the domain is characterized as Inhibitor I9.
+At position 116 to 388, the domain is characterized as Peptidase S8.
+At position 82 to 148, the domain is characterized as HMA 2.
+At position 79 to 280, the domain is characterized as ABC transmembrane type-1.
+At position 45 to 238, the domain is characterized as SMP-LBD.
+At position 241 to 357, the domain is characterized as C2.
+At position 16 to 107, the domain is characterized as HIG1.
+At position 538 to 613, the domain is characterized as Cytochrome b5 heme-binding.
+At position 654 to 767, the domain is characterized as FAD-binding FR-type.
+At position 6 to 36, the domain is characterized as Pentraxin (PTX).
+At position 212 to 325, the domain is characterized as CMP/dCMP-type deaminase.
+At position 584 to 690, the domain is characterized as Cadherin 5.
+At position 9 to 99, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 572 to 696, the domain is characterized as PH.
+At position 730 to 823, the domain is characterized as GED.
+At position 315 to 403, the domain is characterized as BRCT 1.
+At position 3 to 239, the domain is characterized as GP-PDE.
+At position 1 to 107, the domain is characterized as Pyrin.
+At position 229 to 558, the domain is characterized as NACHT.
+At position 375 to 449, the domain is characterized as HTH OST-type 3.
+At position 586 to 645, the domain is characterized as Tudor.
+At position 150 to 406, the domain is characterized as NR LBD.
+At position 1 to 68, the domain is characterized as NAC-A/B.
+At position 8 to 238, the domain is characterized as Glutamine amidotransferase type-1.
+At position 85 to 332, the domain is characterized as Glutamine amidotransferase type-1.
+At position 171 to 259, the domain is characterized as EH 1.
+At position 203 to 238, the domain is characterized as EF-hand 1.
+At position 460 to 549, the domain is characterized as EH 2.
+At position 493 to 528, the domain is characterized as EF-hand 2.
+At position 1401 to 1418, the domain is characterized as WH2.
+At position 764 to 902, the domain is characterized as PH.
+At position 526 to 636, the domain is characterized as OCEL.
+At position 50 to 316, the domain is characterized as Protein kinase.
+At position 80 to 202, the domain is characterized as GST C-terminal.
+At position 75 to 394, the domain is characterized as Kinesin motor.
+At position 566 to 645, the domain is characterized as KIX.
+At position 1067 to 1139, the domain is characterized as Bromo.
+At position 1287 to 1663, the domain is characterized as CBP/p300-type HAT.
+At position 49 to 199, the domain is characterized as PADR1 zinc-binding.
+At position 200 to 290, the domain is characterized as BRCT.
+At position 338 to 439, the domain is characterized as WGR.
+At position 466 to 585, the domain is characterized as PARP alpha-helical.
+At position 594 to 827, the domain is characterized as PARP catalytic.
+At position 97 to 287, the domain is characterized as ATP-grasp.
+At position 395 to 534, the domain is characterized as TIR.
+At position 8 to 203, the domain is characterized as Lon N-terminal.
+At position 1 to 165, the domain is characterized as Macro.
+At position 61 to 128, the domain is characterized as BTB.
+At position 163 to 255, the domain is characterized as BACK.
+At position 1749 to 1848, the domain is characterized as Calx-beta.
+At position 2072 to 2186, the domain is characterized as C-type lectin.
+At position 4 to 405, the domain is characterized as Kinesin motor.
+At position 1 to 153, the domain is characterized as N-acetyltransferase.
+At position 152 to 378, the domain is characterized as NR LBD.
+At position 615 to 721, the domain is characterized as tRNA-binding.
+At position 569 to 655, the domain is characterized as Dicer dsRNA-binding fold.
+At position 827 to 942, the domain is characterized as PAZ.
+At position 969 to 1124, the domain is characterized as RNase III 1.
+At position 1161 to 1308, the domain is characterized as RNase III 2.
+At position 1334 to 1400, the domain is characterized as DRBM.
+At position 1 to 314, the domain is characterized as GT23.
+At position 80 to 296, the domain is characterized as Radical SAM core.
+At position 153 to 365, the domain is characterized as TLC.
+At position 1 to 361, the domain is characterized as SMP-LTD.
+At position 1716 to 1788, the domain is characterized as RRM.
+At position 74 to 291, the domain is characterized as Peptidase M12B.
+At position 295 to 388, the domain is characterized as Disintegrin.
+At position 389 to 444, the domain is characterized as TSP type-1 1.
+At position 687 to 746, the domain is characterized as TSP type-1 2.
+At position 747 to 810, the domain is characterized as TSP type-1 3.
+At position 808 to 871, the domain is characterized as TSP type-1 4.
+At position 904 to 957, the domain is characterized as TSP type-1 5.
+At position 958 to 1019, the domain is characterized as TSP type-1 6.
+At position 1020 to 1078, the domain is characterized as TSP type-1 7.
+At position 1079 to 1137, the domain is characterized as TSP type-1 8.
+At position 1195 to 1302, the domain is characterized as CUB 1.
+At position 1293 to 1426, the domain is characterized as CUB 2.
+At position 47 to 377, the domain is characterized as G-alpha.
+At position 11 to 441, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 926 to 1231, the domain is characterized as PKS/mFAS DH.
+At position 2459 to 2537, the domain is characterized as Carrier.
+At position 45 to 291, the domain is characterized as AB hydrolase-1.
+At position 146 to 221, the domain is characterized as Rho RNA-BD.
+At position 16 to 428, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 898 to 1182, the domain is characterized as PKS/mFAS DH.
+At position 2005 to 2081, the domain is characterized as Carrier.
+At position 499 to 671, the domain is characterized as tr-type G.
+At position 221 to 584, the domain is characterized as PPM-type phosphatase.
+At position 218 to 487, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 114 to 197, the domain is characterized as ACT 2.
+At position 245 to 324, the domain is characterized as ACT 3.
+At position 1 to 17, the domain is characterized as Peptidase S1.
+At position 22 to 259, the domain is characterized as Glutamine amidotransferase type-2.
+At position 51 to 128, the domain is characterized as BTB.
+At position 268 to 607, the domain is characterized as NPH3.
+At position 620 to 710, the domain is characterized as PDZ 1.
+At position 705 to 796, the domain is characterized as PDZ 2.
+At position 1350 to 1429, the domain is characterized as PDZ 3.
+At position 1501 to 1582, the domain is characterized as PDZ 4.
+At position 1593 to 1661, the domain is characterized as SH3.
+At position 1722 to 1905, the domain is characterized as Guanylate kinase-like.
+At position 518 to 648, the domain is characterized as Ricin B-type lectin.
+At position 1 to 299, the domain is characterized as BRO1.
+At position 95 to 173, the domain is characterized as GRAM.
+At position 1490 to 1888, the domain is characterized as HECT.
+At position 200 to 366, the domain is characterized as Helicase ATP-binding.
+At position 648 to 703, the domain is characterized as HTH myb-type.
+At position 173 to 228, the domain is characterized as PAC.
+At position 217 to 280, the domain is characterized as Ubiquitin-like.
+At position 645 to 726, the domain is characterized as S1 motif.
+At position 32 to 61, the domain is characterized as IQ.
+At position 108 to 169, the domain is characterized as LIM zinc-binding 1.
+At position 171 to 232, the domain is characterized as LIM zinc-binding 2.
+At position 27 to 172, the domain is characterized as 6-Cys 1.
+At position 175 to 305, the domain is characterized as 6-Cys 2.
+At position 474 to 529, the domain is characterized as Kazal-like.
+At position 62 to 112, the domain is characterized as Sushi 1.
+At position 113 to 171, the domain is characterized as Sushi 2.
+At position 170 to 254, the domain is characterized as HYR.
+At position 255 to 314, the domain is characterized as Sushi 3.
+At position 579 to 633, the domain is characterized as SOCS box.
+At position 241 to 410, the domain is characterized as tr-type G.
+At position 19 to 123, the domain is characterized as CBM39.
+At position 211 to 481, the domain is characterized as GH16.
+At position 31 to 206, the domain is characterized as SIS.
+At position 83 to 503, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 972 to 1257, the domain is characterized as PKS/mFAS DH.
+At position 2472 to 2550, the domain is characterized as Carrier.
+At position 431 to 554, the domain is characterized as HD.
+At position 651 to 736, the domain is characterized as ACT 1.
+At position 765 to 835, the domain is characterized as ACT 2.
+At position 16 to 74, the domain is characterized as CpcD-like.
+At position 65 to 92, the domain is characterized as EGF-like 1.
+At position 94 to 203, the domain is characterized as CUB.
+At position 204 to 232, the domain is characterized as EGF-like 2.
+At position 235 to 270, the domain is characterized as EGF-like 3.
+At position 945 to 999, the domain is characterized as Laminin EGF-like 1.
+At position 952 to 998, the domain is characterized as EGF-like 4.
+At position 1000 to 1047, the domain is characterized as Laminin EGF-like 2.
+At position 486 to 608, the domain is characterized as HD.
+At position 723 to 802, the domain is characterized as ACT 1.
+At position 834 to 912, the domain is characterized as ACT 2.
+At position 1648 to 1720, the domain is characterized as RRM.
+At position 13 to 138, the domain is characterized as RNase III.
+At position 164 to 232, the domain is characterized as DRBM.
+At position 44 to 156, the domain is characterized as SCP2.
+At position 31 to 105, the domain is characterized as U-box.
+At position 183 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 597 to 675, the domain is characterized as Carrier.
+At position 330 to 382, the domain is characterized as PAC.
+At position 397 to 633, the domain is characterized as Methyl-accepting transducer.
+At position 91 to 172, the domain is characterized as Core-binding (CB).
+At position 195 to 373, the domain is characterized as Tyr recombinase.
+At position 220 to 319, the domain is characterized as SH2.
+At position 586 to 854, the domain is characterized as Ras-GEF.
+At position 30 to 470, the domain is characterized as Trm1 methyltransferase.
+At position 74 to 332, the domain is characterized as Protein kinase.
+At position 375 to 410, the domain is characterized as EF-hand 1.
+At position 411 to 446, the domain is characterized as EF-hand 2.
+At position 447 to 482, the domain is characterized as EF-hand 3.
+At position 486 to 516, the domain is characterized as EF-hand 4.
+At position 210 to 491, the domain is characterized as FERM.
+At position 16 to 141, the domain is characterized as DUSP.
+At position 323 to 382, the domain is characterized as USP.
+At position 5 to 242, the domain is characterized as PABS.
+At position 300 to 334, the domain is characterized as NAF.
+At position 35 to 89, the domain is characterized as sHSP.
+At position 60 to 171, the domain is characterized as Thioredoxin.
+At position 174 to 213, the domain is characterized as DSL.
+At position 214 to 247, the domain is characterized as EGF-like 1.
+At position 272 to 308, the domain is characterized as EGF-like 2.
+At position 310 to 349, the domain is characterized as EGF-like 3.
+At position 351 to 387, the domain is characterized as EGF-like 4.
+At position 389 to 425, the domain is characterized as EGF-like 5.
+At position 427 to 463, the domain is characterized as EGF-like 6.
+At position 829 to 895, the domain is characterized as SAM 1.
+At position 944 to 1008, the domain is characterized as SAM 2.
+At position 1032 to 1101, the domain is characterized as SAM 3.
+At position 27 to 118, the domain is characterized as DEP.
+At position 380 to 805, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1309 to 1629, the domain is characterized as PKS/mFAS DH.
+At position 1681 to 1755, the domain is characterized as Carrier 1.
+At position 1787 to 1865, the domain is characterized as Carrier 2.
+At position 515 to 576, the domain is characterized as SAM.
+At position 172 to 375, the domain is characterized as B30.2/SPRY.
+At position 13 to 141, the domain is characterized as Ferritin-like diiron.
+At position 232 to 464, the domain is characterized as Sigma-54 factor interaction.
+At position 14 to 57, the domain is characterized as UBA-like.
+At position 97 to 116, the domain is characterized as UIM 1.
+At position 123 to 140, the domain is characterized as UIM 2.
+At position 169 to 658, the domain is characterized as USP.
+At position 29 to 173, the domain is characterized as Ig-like V-type 1.
+At position 176 to 308, the domain is characterized as Ig-like V-type 2.
+At position 21 to 225, the domain is characterized as Velvet.
+At position 29 to 258, the domain is characterized as Peptidase S1.
+At position 29 to 88, the domain is characterized as Sushi 1.
+At position 89 to 150, the domain is characterized as Sushi 2.
+At position 151 to 215, the domain is characterized as Sushi 3.
+At position 216 to 275, the domain is characterized as Sushi 4.
+At position 276 to 342, the domain is characterized as Sushi 5.
+At position 343 to 408, the domain is characterized as Sushi 6.
+At position 409 to 467, the domain is characterized as Sushi 7.
+At position 192 to 388, the domain is characterized as Peptidase M12B.
+At position 554 to 788, the domain is characterized as NR LBD.
+At position 164 to 346, the domain is characterized as Glutamine amidotransferase type-1.
+At position 521 to 576, the domain is characterized as SOCS box.
+At position 630 to 698, the domain is characterized as S1 motif.
+At position 18 to 443, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 918 to 1191, the domain is characterized as PKS/mFAS DH.
+At position 1686 to 1761, the domain is characterized as Carrier.
+At position 173 to 245, the domain is characterized as Bromo.
+At position 304 to 386, the domain is characterized as NET.
+At position 49 to 357, the domain is characterized as AB hydrolase-1.
+At position 41 to 113, the domain is characterized as EMI.
+At position 118 to 148, the domain is characterized as EGF-like 1.
+At position 156 to 191, the domain is characterized as EGF-like 2.
+At position 199 to 233, the domain is characterized as EGF-like 3.
+At position 241 to 276, the domain is characterized as EGF-like 4.
+At position 421 to 458, the domain is characterized as EGF-like 5.
+At position 681 to 716, the domain is characterized as EGF-like 6.
+At position 3 to 225, the domain is characterized as DPCK.
+At position 152 to 235, the domain is characterized as PPIase FKBP-type.
+At position 42 to 166, the domain is characterized as tRNA-binding.
+At position 421 to 496, the domain is characterized as B5.
+At position 745 to 838, the domain is characterized as FDX-ACB.
+At position 79 to 136, the domain is characterized as Sushi.
+At position 136 to 172, the domain is characterized as EGF-like 1; calcium-binding.
+At position 224 to 269, the domain is characterized as EGF-like 2; calcium-binding.
+At position 270 to 319, the domain is characterized as EGF-like 3; calcium-binding.
+At position 31 to 269, the domain is characterized as ABC transporter.
+At position 2011 to 2128, the domain is characterized as C2.
+At position 195 to 276, the domain is characterized as HSA.
+At position 469 to 529, the domain is characterized as Myb-like.
+At position 350 to 588, the domain is characterized as Histidine kinase.
+At position 614 to 731, the domain is characterized as Response regulatory.
+At position 291 to 484, the domain is characterized as B30.2/SPRY.
+At position 1 to 110, the domain is characterized as Thioredoxin.
+At position 192 to 802, the domain is characterized as USP.
+At position 42 to 76, the domain is characterized as ShKT.
+At position 247 to 347, the domain is characterized as Fe2OG dioxygenase.
+At position 69 to 175, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 742 to 828, the domain is characterized as SUEL-type lectin.
+At position 22 to 149, the domain is characterized as 6-Cys 1.
+At position 153 to 301, the domain is characterized as 6-Cys 2.
+At position 170 to 342, the domain is characterized as OBG-type G.
+At position 20 to 211, the domain is characterized as ABC transmembrane type-1.
+At position 211 to 299, the domain is characterized as Ig-like C1-type.
+At position 46 to 469, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 30 to 288, the domain is characterized as Protein kinase.
+At position 36 to 171, the domain is characterized as Nudix hydrolase.
+At position 21 to 160, the domain is characterized as SprT-like.
+At position 989 to 1192, the domain is characterized as MyTH4 1.
+At position 1197 to 1506, the domain is characterized as FERM 1.
+At position 1501 to 1567, the domain is characterized as SH3.
+At position 1644 to 1793, the domain is characterized as MyTH4 2.
+At position 1799 to 2102, the domain is characterized as FERM 2.
+At position 399 to 567, the domain is characterized as Helicase ATP-binding.
+At position 765 to 922, the domain is characterized as Helicase C-terminal.
+At position 123 to 202, the domain is characterized as Death.
+At position 411 to 578, the domain is characterized as PA14.
+At position 95 to 247, the domain is characterized as Exonuclease.
+At position 141 to 375, the domain is characterized as SMP-LTD.
+At position 62 to 118, the domain is characterized as Tudor 1.
+At position 291 to 350, the domain is characterized as Tudor 2.
+At position 527 to 584, the domain is characterized as Tudor 3.
+At position 757 to 816, the domain is characterized as Tudor 4.
+At position 974 to 1030, the domain is characterized as Tudor 5.
+At position 1282 to 1340, the domain is characterized as Tudor 6.
+At position 1485 to 1543, the domain is characterized as Tudor 7.
+At position 1799 to 1916, the domain is characterized as SET.
+At position 1922 to 1938, the domain is characterized as Post-SET.
+At position 50 to 99, the domain is characterized as WAP.
+At position 405 to 483, the domain is characterized as ACT 1.
+At position 484 to 560, the domain is characterized as ACT 2.
+At position 3 to 133, the domain is characterized as RNase III.
+At position 15 to 158, the domain is characterized as YEATS.
+At position 469 to 583, the domain is characterized as PAZ.
+At position 749 to 1040, the domain is characterized as Piwi.
+At position 16 to 127, the domain is characterized as RWD.
+At position 235 to 511, the domain is characterized as Protein kinase 1.
+At position 556 to 928, the domain is characterized as Protein kinase 2.
+At position 60 to 268, the domain is characterized as MARVEL.
+At position 413 to 521, the domain is characterized as OCEL.
+At position 186 to 264, the domain is characterized as Thyroglobulin type-1.
+At position 80 to 132, the domain is characterized as bHLH.
+At position 44 to 125, the domain is characterized as EMI.
+At position 124 to 159, the domain is characterized as EGF-like 1.
+At position 161 to 201, the domain is characterized as EGF-like 2; calcium-binding.
+At position 206 to 242, the domain is characterized as EGF-like 3.
+At position 238 to 284, the domain is characterized as EGF-like 4.
+At position 285 to 325, the domain is characterized as EGF-like 5; calcium-binding.
+At position 335 to 370, the domain is characterized as EGF-like 6.
+At position 375 to 411, the domain is characterized as EGF-like 7.
+At position 412 to 452, the domain is characterized as EGF-like 8; calcium-binding.
+At position 516 to 552, the domain is characterized as EGF-like 9.
+At position 560 to 595, the domain is characterized as EGF-like 10.
+At position 603 to 638, the domain is characterized as EGF-like 11.
+At position 736 to 770, the domain is characterized as EGF-like 12.
+At position 783 to 814, the domain is characterized as EGF-like 13.
+At position 822 to 857, the domain is characterized as EGF-like 14.
+At position 865 to 901, the domain is characterized as EGF-like 15.
+At position 909 to 944, the domain is characterized as EGF-like 16.
+At position 955 to 987, the domain is characterized as EGF-like 17.
+At position 995 to 1030, the domain is characterized as EGF-like 18.
+At position 1038 to 1073, the domain is characterized as EGF-like 19.
+At position 1081 to 1116, the domain is characterized as EGF-like 20.
+At position 1124 to 1159, the domain is characterized as EGF-like 21.
+At position 1211 to 1246, the domain is characterized as EGF-like 22.
+At position 1254 to 1289, the domain is characterized as EGF-like 23.
+At position 1297 to 1332, the domain is characterized as EGF-like 24.
+At position 1345 to 1375, the domain is characterized as EGF-like 25.
+At position 1383 to 1418, the domain is characterized as EGF-like 26.
+At position 1469 to 1504, the domain is characterized as EGF-like 27.
+At position 14 to 132, the domain is characterized as Response regulatory.
+At position 188 to 381, the domain is characterized as CheB-type methylesterase.
+At position 22 to 312, the domain is characterized as Protein kinase.
+At position 212 to 313, the domain is characterized as Fibronectin type-III 1.
+At position 317 to 409, the domain is characterized as Fibronectin type-III 2.
+At position 413 to 506, the domain is characterized as Fibronectin type-III 3.
+At position 510 to 604, the domain is characterized as Fibronectin type-III 4.
+At position 608 to 701, the domain is characterized as Fibronectin type-III 5.
+At position 705 to 795, the domain is characterized as Fibronectin type-III 6.
+At position 805 to 894, the domain is characterized as Fibronectin type-III 7.
+At position 895 to 989, the domain is characterized as Fibronectin type-III 8.
+At position 990 to 1095, the domain is characterized as Fibronectin type-III 9.
+At position 18 to 137, the domain is characterized as Bulb-type lectin.
+At position 271 to 307, the domain is characterized as EGF-like; atypical.
+At position 326 to 408, the domain is characterized as PAN.
+At position 478 to 763, the domain is characterized as Protein kinase.
+At position 373 to 440, the domain is characterized as PASTA 1.
+At position 441 to 509, the domain is characterized as PASTA 2.
+At position 510 to 575, the domain is characterized as PASTA 3.
+At position 20 to 106, the domain is characterized as Sm.
+At position 178 to 269, the domain is characterized as SH2 1.
+At position 276 to 338, the domain is characterized as SH3.
+At position 348 to 438, the domain is characterized as SH2 2.
+At position 471 to 574, the domain is characterized as PH.
+At position 574 to 687, the domain is characterized as C2.
+At position 745 to 939, the domain is characterized as Ras-GAP.
+At position 213 to 286, the domain is characterized as RRM.
+At position 397 to 483, the domain is characterized as PPIase FKBP-type.
+At position 112 to 148, the domain is characterized as EGF-like 2; calcium-binding.
+At position 150 to 186, the domain is characterized as EGF-like 3; calcium-binding.
+At position 188 to 225, the domain is characterized as EGF-like 4; calcium-binding.
+At position 227 to 263, the domain is characterized as EGF-like 5.
+At position 265 to 322, the domain is characterized as EGF-like 6.
+At position 324 to 360, the domain is characterized as EGF-like 7; calcium-binding.
+At position 362 to 398, the domain is characterized as EGF-like 8; calcium-binding.
+At position 400 to 440, the domain is characterized as EGF-like 9.
+At position 444 to 607, the domain is characterized as Laminin G-like 1.
+At position 609 to 645, the domain is characterized as EGF-like 10.
+At position 649 to 808, the domain is characterized as Laminin G-like 2.
+At position 810 to 846, the domain is characterized as EGF-like 11.
+At position 872 to 1051, the domain is characterized as Laminin G-like 3.
+At position 1053 to 1089, the domain is characterized as EGF-like 12.
+At position 1091 to 1127, the domain is characterized as EGF-like 13.
+At position 1131 to 1168, the domain is characterized as EGF-like 14.
+At position 1170 to 1206, the domain is characterized as EGF-like 15.
+At position 64 to 167, the domain is characterized as FAD-binding FR-type.
+At position 134 to 333, the domain is characterized as MAGE.
+At position 590 to 672, the domain is characterized as BRCT.
+At position 240 to 349, the domain is characterized as CUB 1.
+At position 357 to 519, the domain is characterized as MAM.
+At position 539 to 649, the domain is characterized as CUB 2.
+At position 656 to 694, the domain is characterized as LDL-receptor class A 2.
+At position 693 to 786, the domain is characterized as SRCR.
+At position 800 to 1034, the domain is characterized as Peptidase S1.
+At position 51 to 180, the domain is characterized as MsrB.
+At position 91 to 249, the domain is characterized as Nudix hydrolase.
+At position 408 to 525, the domain is characterized as SET.
+At position 1 to 139, the domain is characterized as RNase H type-1.
+At position 43 to 343, the domain is characterized as Protein kinase.
+At position 67 to 165, the domain is characterized as Plastocyanin-like.
+At position 91 to 181, the domain is characterized as RRM.
+At position 386 to 460, the domain is characterized as HSA.
+At position 684 to 744, the domain is characterized as Myb-like.
+At position 45 to 97, the domain is characterized as bHLH.
+At position 301 to 331, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 350 to 379, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 172 to 232, the domain is characterized as bZIP.
+At position 19 to 70, the domain is characterized as Rubredoxin-like.
+At position 534 to 615, the domain is characterized as PABC.
+At position 17 to 137, the domain is characterized as G.
+At position 45 to 289, the domain is characterized as Radical SAM core.
+At position 149 to 276, the domain is characterized as MH1.
+At position 332 to 495, the domain is characterized as MH2.
+At position 994 to 1062, the domain is characterized as R3H.
+At position 49 to 275, the domain is characterized as Radical SAM core.
+At position 17 to 272, the domain is characterized as Protein kinase.
+At position 299 to 353, the domain is characterized as NAF.
+At position 121 to 229, the domain is characterized as CBM21.
+At position 34 to 167, the domain is characterized as MARVEL.
+At position 115 to 181, the domain is characterized as DRBM.
+At position 261 to 582, the domain is characterized as A to I editase.
+At position 1 to 234, the domain is characterized as Peptidase S1.
+At position 698 to 716, the domain is characterized as WH2 1.
+At position 728 to 745, the domain is characterized as WH2 2.
+At position 140 to 393, the domain is characterized as SMP-LTD.
+At position 147 to 393, the domain is characterized as TLDc.
+At position 16 to 70, the domain is characterized as HTH lacI-type.
+At position 33 to 68, the domain is characterized as LDL-receptor class A 1.
+At position 71 to 229, the domain is characterized as MAM 1.
+At position 433 to 471, the domain is characterized as LDL-receptor class A 2.
+At position 474 to 637, the domain is characterized as MAM 3.
+At position 652 to 816, the domain is characterized as MAM 4.
+At position 822 to 860, the domain is characterized as LDL-receptor class A 3.
+At position 863 to 1024, the domain is characterized as MAM 5.
+At position 1049 to 1086, the domain is characterized as LDL-receptor class A 4.
+At position 1088 to 1256, the domain is characterized as MAM 6.
+At position 1263 to 1301, the domain is characterized as LDL-receptor class A 5.
+At position 1305 to 1465, the domain is characterized as MAM 7.
+At position 1482 to 1518, the domain is characterized as LDL-receptor class A 6.
+At position 1519 to 1676, the domain is characterized as MAM 8.
+At position 1683 to 1720, the domain is characterized as LDL-receptor class A 7.
+At position 1727 to 1892, the domain is characterized as MAM 9.
+At position 1902 to 1939, the domain is characterized as LDL-receptor class A 8.
+At position 1946 to 1982, the domain is characterized as LDL-receptor class A 9.
+At position 1985 to 2023, the domain is characterized as LDL-receptor class A 10.
+At position 2024 to 2057, the domain is characterized as EGF-like.
+At position 34 to 178, the domain is characterized as Thioredoxin.
+At position 167 to 222, the domain is characterized as HTH myb-type.
+At position 467 to 556, the domain is characterized as EH 2.
+At position 500 to 535, the domain is characterized as EF-hand 2.
+At position 1411 to 1428, the domain is characterized as WH2.
+At position 440 to 720, the domain is characterized as Protein kinase.
+At position 256 to 501, the domain is characterized as ABC transporter 2.
+At position 35 to 153, the domain is characterized as sHSP.
+At position 165 to 235, the domain is characterized as S1 motif.
+At position 340 to 410, the domain is characterized as KH.
+At position 188 to 220, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 166 to 296, the domain is characterized as PAS 1.
+At position 314 to 416, the domain is characterized as PAS 2.
+At position 332 to 355, the domain is characterized as DAZ 1.
+At position 356 to 379, the domain is characterized as DAZ 2.
+At position 380 to 403, the domain is characterized as DAZ 3.
+At position 404 to 427, the domain is characterized as DAZ 4.
+At position 428 to 451, the domain is characterized as DAZ 5.
+At position 452 to 475, the domain is characterized as DAZ 6.
+At position 476 to 499, the domain is characterized as DAZ 7.
+At position 500 to 523, the domain is characterized as DAZ 8.
+At position 524 to 547, the domain is characterized as DAZ 9.
+At position 113 to 268, the domain is characterized as N-acetyltransferase.
+At position 357 to 427, the domain is characterized as Bromo.
+At position 23 to 96, the domain is characterized as TB.
+At position 87 to 110, the domain is characterized as Follistatin-like 1.
+At position 105 to 159, the domain is characterized as Kazal-like 1.
+At position 160 to 183, the domain is characterized as Follistatin-like 2.
+At position 179 to 234, the domain is characterized as Kazal-like 2.
+At position 237 to 261, the domain is characterized as Follistatin-like 3.
+At position 254 to 311, the domain is characterized as Kazal-like 3.
+At position 167 to 213, the domain is characterized as G-patch.
+At position 177 to 363, the domain is characterized as CheB-type methylesterase.
+At position 792 to 949, the domain is characterized as HNH Cas9-type.
+At position 429 to 539, the domain is characterized as SCP2.
+At position 413 to 503, the domain is characterized as Smr.
+At position 812 to 901, the domain is characterized as Fibronectin type-III 3.
+At position 2193 to 2286, the domain is characterized as Fibronectin type-III 17.
+At position 147 to 228, the domain is characterized as BAG.
+At position 120 to 352, the domain is characterized as ATP-grasp.
+At position 695 to 744, the domain is characterized as KA1.
+At position 19 to 135, the domain is characterized as Ig-like V-type.
+At position 287 to 361, the domain is characterized as U-box.
+At position 1 to 97, the domain is characterized as EamA 1.
+At position 116 to 237, the domain is characterized as EamA 2.
+At position 28 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 1 to 47, the domain is characterized as Kazal-like.
+At position 92 to 148, the domain is characterized as CBS 1.
+At position 152 to 209, the domain is characterized as CBS 2.
+At position 50 to 290, the domain is characterized as Peptidase S1.
+At position 31 to 213, the domain is characterized as SIS.
+At position 42 to 88, the domain is characterized as F-box.
+At position 508 to 582, the domain is characterized as Bromo.
+At position 453 to 649, the domain is characterized as FtsK.
+At position 13 to 265, the domain is characterized as Protein kinase.
+At position 603 to 652, the domain is characterized as KA1.
+At position 121 to 215, the domain is characterized as Rhodanese.
+At position 31 to 126, the domain is characterized as IGFBP N-terminal.
+At position 215 to 297, the domain is characterized as Thyroglobulin type-1.
+At position 20 to 381, the domain is characterized as GH18.
+At position 54 to 302, the domain is characterized as Glutamine amidotransferase type-2.
+At position 2 to 115, the domain is characterized as MTTase N-terminal.
+At position 397 to 466, the domain is characterized as TRAM.
+At position 33 to 74, the domain is characterized as Anaphylatoxin-like 1.
+At position 75 to 109, the domain is characterized as Anaphylatoxin-like 2.
+At position 110 to 142, the domain is characterized as Anaphylatoxin-like 3.
+At position 177 to 216, the domain is characterized as EGF-like 1.
+At position 217 to 262, the domain is characterized as EGF-like 2; calcium-binding.
+At position 263 to 308, the domain is characterized as EGF-like 3; calcium-binding.
+At position 309 to 356, the domain is characterized as EGF-like 4; calcium-binding.
+At position 357 to 399, the domain is characterized as EGF-like 5; calcium-binding.
+At position 400 to 441, the domain is characterized as EGF-like 6; calcium-binding.
+At position 442 to 481, the domain is characterized as EGF-like 7; calcium-binding.
+At position 482 to 525, the domain is characterized as EGF-like 8; calcium-binding.
+At position 526 to 579, the domain is characterized as EGF-like 9; calcium-binding.
+At position 40 to 222, the domain is characterized as FAD-binding PCMH-type.
+At position 689 to 924, the domain is characterized as VLIG-type G.
+At position 96 to 254, the domain is characterized as FCP1 homology.
+At position 633 to 667, the domain is characterized as SAP.
+At position 11 to 45, the domain is characterized as PPIase cyclophilin-type.
+At position 103 to 161, the domain is characterized as S4 RNA-binding.
+At position 548 to 641, the domain is characterized as PB1.
+At position 7 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 52 to 276, the domain is characterized as L-type lectin-like.
+At position 22 to 203, the domain is characterized as NodB homology.
+At position 124 to 238, the domain is characterized as sHSP.
+At position 113 to 179, the domain is characterized as HMA 1.
+At position 198 to 264, the domain is characterized as HMA 2.
+At position 309 to 375, the domain is characterized as HMA 3.
+At position 400 to 466, the domain is characterized as HMA 4.
+At position 529 to 595, the domain is characterized as HMA 5.
+At position 605 to 671, the domain is characterized as HMA 6.
+At position 728 to 821, the domain is characterized as BRCT 1.
+At position 900 to 989, the domain is characterized as BRCT 2.
+At position 48 to 276, the domain is characterized as Helicase ATP-binding.
+At position 308 to 482, the domain is characterized as Helicase C-terminal.
+At position 147 to 210, the domain is characterized as S5 DRBM.
+At position 13 to 129, the domain is characterized as MTTase N-terminal.
+At position 152 to 388, the domain is characterized as Radical SAM core.
+At position 391 to 462, the domain is characterized as TRAM.
+At position 153 to 186, the domain is characterized as WW 1.
+At position 212 to 245, the domain is characterized as WW 2.
+At position 28 to 490, the domain is characterized as Sema.
+At position 429 to 544, the domain is characterized as Toprim.
+At position 27 to 302, the domain is characterized as Protein kinase.
+At position 193 to 390, the domain is characterized as Peptidase M12B.
+At position 521 to 678, the domain is characterized as C2 1.
+At position 787 to 919, the domain is characterized as C2 2.
+At position 985 to 1147, the domain is characterized as C2 3.
+At position 1171 to 1339, the domain is characterized as C2 4.
+At position 1403 to 1533, the domain is characterized as C2 5.
+At position 1617 to 1745, the domain is characterized as C2 6.
+At position 756 to 857, the domain is characterized as tRNA-binding.
+At position 566 to 843, the domain is characterized as Protein kinase.
+At position 77 to 225, the domain is characterized as Cupin type-1.
+At position 36 to 138, the domain is characterized as LOB.
+At position 47 to 283, the domain is characterized as GB1/RHD3-type G.
+At position 170 to 235, the domain is characterized as HTH luxR-type.
+At position 335 to 428, the domain is characterized as Fibronectin type-III 1.
+At position 529 to 623, the domain is characterized as Fibronectin type-III 3.
+At position 625 to 736, the domain is characterized as Fibronectin type-III 4.
+At position 169 to 261, the domain is characterized as AB hydrolase-1.
+At position 1 to 50, the domain is characterized as Thioredoxin.
+At position 414 to 577, the domain is characterized as Helicase ATP-binding.
+At position 599 to 775, the domain is characterized as Helicase C-terminal.
+At position 28 to 74, the domain is characterized as CHCH.
+At position 319 to 411, the domain is characterized as ARID.
+At position 1 to 123, the domain is characterized as PIK helical.
+At position 558 to 836, the domain is characterized as PI3K/PI4K catalytic.
+At position 30 to 115, the domain is characterized as Sm.
+At position 205 to 286, the domain is characterized as Peptidase A2.
+At position 638 to 812, the domain is characterized as PCI.
+At position 13 to 368, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 1 to 217, the domain is characterized as Radical SAM core.
+At position 3 to 130, the domain is characterized as Nudix hydrolase.
+At position 244 to 297, the domain is characterized as Protein kinase.
+At position 53 to 109, the domain is characterized as WHEP-TRS.
+At position 82 to 158, the domain is characterized as Lipoyl-binding 1.
+At position 208 to 284, the domain is characterized as Lipoyl-binding 2.
+At position 346 to 651, the domain is characterized as Protein kinase.
+At position 1 to 232, the domain is characterized as KaiC 1.
+At position 246 to 501, the domain is characterized as KaiC 2.
+At position 190 to 279, the domain is characterized as Olduvai 1.
+At position 280 to 391, the domain is characterized as Olduvai 2.
+At position 3 to 35, the domain is characterized as ShKT.
+At position 546 to 729, the domain is characterized as N-acetyltransferase.
+At position 96 to 344, the domain is characterized as ABC transporter.
+At position 121 to 435, the domain is characterized as Peptidase S8.
+At position 444 to 576, the domain is characterized as P/Homo B.
+At position 204 to 373, the domain is characterized as PCI.
+At position 192 to 278, the domain is characterized as PDZ.
+At position 256 to 420, the domain is characterized as DOD-type homing endonuclease.
+At position 278 to 448, the domain is characterized as Helicase ATP-binding.
+At position 470 to 628, the domain is characterized as Helicase C-terminal.
+At position 29 to 84, the domain is characterized as TIL.
+At position 60 to 233, the domain is characterized as HD.
+At position 151 to 480, the domain is characterized as SAC.
+At position 263 to 303, the domain is characterized as EGF-like.
+At position 58 to 225, the domain is characterized as FCP1 homology.
+At position 8 to 231, the domain is characterized as BAR.
+At position 15 to 111, the domain is characterized as SH2.
+At position 1203 to 1266, the domain is characterized as SAM.
+At position 41 to 288, the domain is characterized as AB hydrolase-1.
+At position 1290 to 1573, the domain is characterized as Protein kinase.
+At position 149 to 457, the domain is characterized as PPM-type phosphatase.
+At position 4 to 194, the domain is characterized as DPCK.
+At position 23 to 114, the domain is characterized as Ig-like.
+At position 21 to 152, the domain is characterized as ENTH.
+At position 487 to 597, the domain is characterized as CNA-B 1.
+At position 598 to 708, the domain is characterized as CNA-B 2.
+At position 38 to 213, the domain is characterized as VWFA.
+At position 239 to 427, the domain is characterized as Laminin G-like.
+At position 481 to 520, the domain is characterized as Collagen-like 1.
+At position 526 to 565, the domain is characterized as Collagen-like 2.
+At position 566 to 625, the domain is characterized as Collagen-like 3.
+At position 657 to 708, the domain is characterized as Collagen-like 4.
+At position 714 to 773, the domain is characterized as Collagen-like 5.
+At position 774 to 833, the domain is characterized as Collagen-like 6.
+At position 868 to 922, the domain is characterized as Collagen-like 7.
+At position 925 to 984, the domain is characterized as Collagen-like 8.
+At position 1047 to 1095, the domain is characterized as Collagen-like 9.
+At position 1118 to 1155, the domain is characterized as Collagen-like 10.
+At position 1156 to 1215, the domain is characterized as Collagen-like 11.
+At position 1249 to 1308, the domain is characterized as Collagen-like 12.
+At position 1315 to 1374, the domain is characterized as Collagen-like 13.
+At position 1387 to 1446, the domain is characterized as Collagen-like 14.
+At position 1495 to 1550, the domain is characterized as Collagen-like 15.
+At position 1575 to 1604, the domain is characterized as Collagen-like 16.
+At position 23 to 199, the domain is characterized as EngB-type G.
+At position 30 to 133, the domain is characterized as Ig-like V-type.
+At position 26 to 290, the domain is characterized as GH16.
+At position 263 to 342, the domain is characterized as ACT 1.
+At position 344 to 405, the domain is characterized as ACT 2.
+At position 14 to 297, the domain is characterized as Radical SAM core.
+At position 75 to 103, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 60 to 82, the domain is characterized as GoLoco 1.
+At position 102 to 124, the domain is characterized as GoLoco 2.
+At position 130 to 153, the domain is characterized as GoLoco 3.
+At position 55 to 98, the domain is characterized as SMB 1.
+At position 99 to 143, the domain is characterized as SMB 2.
+At position 110 to 289, the domain is characterized as Tyr recombinase.
+At position 390 to 456, the domain is characterized as TRAM.
+At position 15 to 210, the domain is characterized as DPCK.
+At position 423 to 459, the domain is characterized as CBM1.
+At position 19 to 133, the domain is characterized as Response regulatory.
+At position 39 to 263, the domain is characterized as ABC transporter.
+At position 7 to 96, the domain is characterized as CS.
+At position 20 to 273, the domain is characterized as F-BAR.
+At position 866 to 927, the domain is characterized as SH3.
+At position 7 to 404, the domain is characterized as BRO1.
+At position 1083 to 1371, the domain is characterized as Autotransporter.
+At position 22 to 139, the domain is characterized as Thioredoxin 1.
+At position 138 to 254, the domain is characterized as Thioredoxin 2.
+At position 480 to 609, the domain is characterized as Thioredoxin 3.
+At position 1 to 29, the domain is characterized as C-type lectin.
+At position 49 to 146, the domain is characterized as Glutaredoxin.
+At position 248 to 449, the domain is characterized as Helicase C-terminal.
+At position 178 to 238, the domain is characterized as SH3.
+At position 246 to 344, the domain is characterized as SH2.
+At position 369 to 622, the domain is characterized as Protein kinase.
+At position 105 to 482, the domain is characterized as USP.
+At position 12 to 392, the domain is characterized as Kinesin motor.
+At position 15 to 87, the domain is characterized as GRAM.
+At position 194 to 381, the domain is characterized as Glutamine amidotransferase type-1.
+At position 270 to 290, the domain is characterized as ELK.
+At position 640 to 718, the domain is characterized as BRCT.
+At position 46 to 301, the domain is characterized as OBG-type G.
+At position 322 to 405, the domain is characterized as TGS.
+At position 1 to 183, the domain is characterized as GMPS ATP-PPase.
+At position 104 to 156, the domain is characterized as bHLH.
+At position 178 to 241, the domain is characterized as bZIP.
+At position 337 to 379, the domain is characterized as LRRCT.
+At position 3 to 258, the domain is characterized as F-BAR.
+At position 332 to 389, the domain is characterized as SH3.
+At position 77 to 493, the domain is characterized as Peptidase A1.
+At position 307 to 407, the domain is characterized as Saposin B-type.
+At position 128 to 379, the domain is characterized as Protein kinase.
+At position 398 to 440, the domain is characterized as UBA.
+At position 1039 to 1088, the domain is characterized as KA1.
+At position 4 to 115, the domain is characterized as STAS.
+At position 8 to 172, the domain is characterized as Exonuclease.
+At position 339 to 388, the domain is characterized as bHLH.
+At position 73 to 164, the domain is characterized as Ig-like C2-type 1.
+At position 173 to 270, the domain is characterized as Ig-like C2-type 2.
+At position 382 to 672, the domain is characterized as Protein kinase.
+At position 841 to 1123, the domain is characterized as Protein kinase.
+At position 656 to 834, the domain is characterized as MOSC.
+At position 82 to 190, the domain is characterized as THUMP.
+At position 435 to 693, the domain is characterized as Protein kinase.
+At position 290 to 537, the domain is characterized as FAD-binding FR-type.
+At position 46 to 317, the domain is characterized as Septin-type G.
+At position 1 to 57, the domain is characterized as Peptidase M12B.
+At position 65 to 146, the domain is characterized as Disintegrin.
+At position 22 to 106, the domain is characterized as Saposin B-type.
+At position 378 to 492, the domain is characterized as Response regulatory.
+At position 69 to 349, the domain is characterized as Protein kinase.
+At position 92 to 124, the domain is characterized as LisH.
+At position 636 to 722, the domain is characterized as Thioredoxin.
+At position 108 to 143, the domain is characterized as EF-hand 2.
+At position 95 to 159, the domain is characterized as S4 RNA-binding.
+At position 375 to 634, the domain is characterized as Protein kinase.
+At position 635 to 704, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 329, the domain is characterized as PUM-HD.
+At position 1 to 84, the domain is characterized as ACB.
+At position 49 to 183, the domain is characterized as Galectin 1.
+At position 212 to 336, the domain is characterized as Galectin 2.
+At position 138 to 260, the domain is characterized as MPN.
+At position 326 to 532, the domain is characterized as MCM.
+At position 1 to 237, the domain is characterized as Lon N-terminal.
+At position 627 to 805, the domain is characterized as Lon proteolytic.
+At position 152 to 327, the domain is characterized as Helicase ATP-binding.
+At position 355 to 502, the domain is characterized as Helicase C-terminal.
+At position 19 to 187, the domain is characterized as NAC.
+At position 144 to 192, the domain is characterized as EF-hand 1.
+At position 198 to 223, the domain is characterized as EF-hand 2.
+At position 224 to 259, the domain is characterized as EF-hand 3.
+At position 260 to 300, the domain is characterized as EF-hand 4.
+At position 301 to 332, the domain is characterized as EF-hand 5.
+At position 210 to 288, the domain is characterized as RRM.
+At position 403 to 481, the domain is characterized as B5.
+At position 697 to 793, the domain is characterized as FDX-ACB.
+At position 133 to 265, the domain is characterized as Fatty acid hydroxylase.
+At position 1337 to 1500, the domain is characterized as JmjC.
+At position 21 to 115, the domain is characterized as CBM39.
+At position 179 to 461, the domain is characterized as GH16.
+At position 254 to 474, the domain is characterized as Histidine kinase.
+At position 140 to 317, the domain is characterized as Prephenate dehydratase.
+At position 331 to 422, the domain is characterized as ACT.
+At position 15 to 212, the domain is characterized as Lon N-terminal.
+At position 613 to 794, the domain is characterized as Lon proteolytic.
+At position 312 to 463, the domain is characterized as PI-PLC X-box.
+At position 546 to 662, the domain is characterized as PI-PLC Y-box.
+At position 662 to 790, the domain is characterized as C2.
+At position 438 to 471, the domain is characterized as EGF-like.
+At position 53 to 286, the domain is characterized as FAD-binding PCMH-type.
+At position 667 to 700, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 267 to 409, the domain is characterized as Ricin B-type lectin 1.
+At position 413 to 560, the domain is characterized as Ricin B-type lectin 2.
+At position 564 to 707, the domain is characterized as Ricin B-type lectin 3.
+At position 213 to 279, the domain is characterized as KH.
+At position 27 to 155, the domain is characterized as GST C-terminal.
+At position 202 to 503, the domain is characterized as CP-type G.
+At position 29 to 146, the domain is characterized as SCP.
+At position 814 to 1102, the domain is characterized as Autotransporter.
+At position 195 to 244, the domain is characterized as KBD.
+At position 296 to 407, the domain is characterized as SPR.
+At position 424 to 584, the domain is characterized as SSD.
+At position 271 to 317, the domain is characterized as G-patch.
+At position 589 to 863, the domain is characterized as Protein kinase.
+At position 15 to 207, the domain is characterized as NodB homology.
+At position 3 to 279, the domain is characterized as DegV.
+At position 69 to 299, the domain is characterized as Radical SAM core.
+At position 695 to 843, the domain is characterized as uDENN.
+At position 865 to 998, the domain is characterized as cDENN.
+At position 1000 to 1093, the domain is characterized as dDENN.
+At position 416 to 575, the domain is characterized as Exonuclease.
+At position 619 to 697, the domain is characterized as BRCT.
+At position 111 to 237, the domain is characterized as MRH.
+At position 524 to 579, the domain is characterized as SOCS box.
+At position 133 to 262, the domain is characterized as Fatty acid hydroxylase.
+At position 128 to 196, the domain is characterized as POTRA.
+At position 315 to 393, the domain is characterized as UBX.
+At position 41 to 313, the domain is characterized as Protein kinase.
+At position 200 to 439, the domain is characterized as ABC transporter.
+At position 83 to 236, the domain is characterized as Ferritin-like diiron.
+At position 17 to 54, the domain is characterized as EGF-like.
+At position 199 to 476, the domain is characterized as NPH3.
+At position 825 to 1094, the domain is characterized as Protein kinase.
+At position 65 to 135, the domain is characterized as Bromo 1.
+At position 197 to 267, the domain is characterized as Bromo 2.
+At position 398 to 468, the domain is characterized as Bromo 3.
+At position 536 to 606, the domain is characterized as Bromo 4.
+At position 674 to 744, the domain is characterized as Bromo 5.
+At position 790 to 860, the domain is characterized as Bromo 6.
+At position 954 to 1072, the domain is characterized as BAH 1.
+At position 1155 to 1271, the domain is characterized as BAH 2.
+At position 32 to 96, the domain is characterized as SH3.
+At position 571 to 769, the domain is characterized as Histidine kinase.
+At position 3 to 50, the domain is characterized as LysM 1.
+At position 54 to 101, the domain is characterized as LysM 2.
+At position 105 to 152, the domain is characterized as LysM 3.
+At position 82 to 282, the domain is characterized as Laminin G-like.
+At position 43 to 141, the domain is characterized as PH.
+At position 619 to 811, the domain is characterized as Rab-GAP TBC.
+At position 99 to 140, the domain is characterized as CHCH.
+At position 360 to 621, the domain is characterized as Pterin-binding.
+At position 652 to 749, the domain is characterized as B12-binding N-terminal.
+At position 762 to 897, the domain is characterized as B12-binding.
+At position 927 to 1273, the domain is characterized as AdoMet activation.
+At position 12 to 168, the domain is characterized as NAC.
+At position 24 to 80, the domain is characterized as L27 1.
+At position 87 to 137, the domain is characterized as L27 2.
+At position 154 to 235, the domain is characterized as PDZ.
+At position 242 to 312, the domain is characterized as SH3.
+At position 427 to 616, the domain is characterized as Guanylate kinase-like.
+At position 54 to 144, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 36 to 103, the domain is characterized as BTB.
+At position 196 to 466, the domain is characterized as NPH3.
+At position 54 to 273, the domain is characterized as Radical SAM core.
+At position 542 to 809, the domain is characterized as MHD.
+At position 353 to 473, the domain is characterized as C2.
+At position 657 to 916, the domain is characterized as Protein kinase.
+At position 917 to 984, the domain is characterized as AGC-kinase C-terminal.
+At position 293 to 478, the domain is characterized as VWFA 1.
+At position 495 to 668, the domain is characterized as VWFA 2.
+At position 44 to 104, the domain is characterized as EMI.
+At position 105 to 145, the domain is characterized as EGF-like 1.
+At position 164 to 204, the domain is characterized as EGF-like 2; calcium-binding.
+At position 205 to 244, the domain is characterized as EGF-like 3.
+At position 245 to 285, the domain is characterized as EGF-like 4; calcium-binding.
+At position 445 to 481, the domain is characterized as EGF-like 5.
+At position 236 to 567, the domain is characterized as Protein kinase.
+At position 321 to 638, the domain is characterized as DOT1.
+At position 10 to 78, the domain is characterized as Sm.
+At position 15 to 231, the domain is characterized as Radical SAM core.
+At position 702 to 1002, the domain is characterized as Protein kinase.
+At position 568 to 738, the domain is characterized as Helicase ATP-binding.
+At position 875 to 1034, the domain is characterized as Helicase C-terminal.
+At position 28 to 133, the domain is characterized as DUSP.
+At position 257 to 889, the domain is characterized as USP.
+At position 1 to 110, the domain is characterized as Ig-like.
+At position 589 to 958, the domain is characterized as Protein kinase.
+At position 959 to 1057, the domain is characterized as AGC-kinase C-terminal.
+At position 426 to 497, the domain is characterized as PAS.
+At position 64 to 134, the domain is characterized as Bromo 1.
+At position 200 to 270, the domain is characterized as Bromo 2.
+At position 400 to 470, the domain is characterized as Bromo 3.
+At position 538 to 608, the domain is characterized as Bromo 4.
+At position 676 to 746, the domain is characterized as Bromo 5.
+At position 792 to 862, the domain is characterized as Bromo 6.
+At position 956 to 1074, the domain is characterized as BAH 1.
+At position 1156 to 1272, the domain is characterized as BAH 2.
+At position 21 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 144 to 237, the domain is characterized as Ig-like C2-type 2.
+At position 460 to 739, the domain is characterized as Protein kinase.
+At position 68 to 327, the domain is characterized as Protein kinase 1.
+At position 328 to 397, the domain is characterized as AGC-kinase C-terminal.
+At position 422 to 679, the domain is characterized as Protein kinase 2.
+At position 2 to 85, the domain is characterized as Glutaredoxin.
+At position 617 to 1081, the domain is characterized as Rab-GAP TBC.
+At position 441 to 557, the domain is characterized as HD.
+At position 680 to 763, the domain is characterized as ACT 1.
+At position 792 to 861, the domain is characterized as ACT 2.
+At position 145 to 218, the domain is characterized as HTH crp-type.
+At position 104 to 278, the domain is characterized as Helicase ATP-binding.
+At position 291 to 453, the domain is characterized as Helicase C-terminal.
+At position 20 to 174, the domain is characterized as CP-type G.
+At position 468 to 531, the domain is characterized as SAM 1.
+At position 537 to 601, the domain is characterized as SAM 2.
+At position 665 to 844, the domain is characterized as MOSC.
+At position 1351 to 1502, the domain is characterized as Nudix hydrolase.
+At position 174 to 205, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 207 to 236, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 413 to 609, the domain is characterized as B30.2/SPRY.
+At position 111 to 427, the domain is characterized as Protein kinase.
+At position 428 to 484, the domain is characterized as AGC-kinase C-terminal.
+At position 170 to 398, the domain is characterized as tr-type G.
+At position 220 to 309, the domain is characterized as EH 2.
+At position 253 to 288, the domain is characterized as EF-hand 2.
+At position 732 to 793, the domain is characterized as SH3 1.
+At position 897 to 955, the domain is characterized as SH3 2.
+At position 986 to 1044, the domain is characterized as SH3 3.
+At position 1058 to 1122, the domain is characterized as SH3 4.
+At position 1139 to 1198, the domain is characterized as SH3 5.
+At position 1221 to 1407, the domain is characterized as DH.
+At position 1446 to 1555, the domain is characterized as PH.
+At position 1563 to 1679, the domain is characterized as C2.
+At position 673 to 776, the domain is characterized as SRCR.
+At position 29 to 98, the domain is characterized as BTB.
+At position 134 to 234, the domain is characterized as BACK.
+At position 135 to 237, the domain is characterized as Gnk2-homologous 2.
+At position 331 to 621, the domain is characterized as Protein kinase.
+At position 417 to 547, the domain is characterized as C2.
+At position 573 to 683, the domain is characterized as PH.
+At position 970 to 1157, the domain is characterized as MHD1.
+At position 300 to 503, the domain is characterized as Helicase ATP-binding.
+At position 514 to 677, the domain is characterized as Helicase C-terminal.
+At position 104 to 134, the domain is characterized as EF-hand 3.
+At position 112 to 174, the domain is characterized as S4 RNA-binding.
+At position 168 to 449, the domain is characterized as ABC transmembrane type-1 1.
+At position 499 to 722, the domain is characterized as ABC transporter 1.
+At position 793 to 1079, the domain is characterized as ABC transmembrane type-1 2.
+At position 1119 to 1352, the domain is characterized as ABC transporter 2.
+At position 82 to 232, the domain is characterized as PPIase cyclophilin-type.
+At position 269 to 437, the domain is characterized as Senescence.
+At position 220 to 284, the domain is characterized as S5 DRBM.
+At position 26 to 137, the domain is characterized as PWI.
+At position 124 to 294, the domain is characterized as Era-type G.
+At position 325 to 402, the domain is characterized as KH type-2.
+At position 473 to 594, the domain is characterized as RCK N-terminal.
+At position 561 to 818, the domain is characterized as Protein kinase.
+At position 71 to 301, the domain is characterized as Radical SAM core.
+At position 199 to 384, the domain is characterized as Glutamine amidotransferase type-1.
+At position 340 to 471, the domain is characterized as NlpC/P60.
+At position 326 to 607, the domain is characterized as Helicase ATP-binding.
+At position 650 to 797, the domain is characterized as Helicase C-terminal.
+At position 34 to 116, the domain is characterized as GOLD.
+At position 44 to 105, the domain is characterized as KH; atypical.
+At position 602 to 691, the domain is characterized as BRCT.
+At position 295 to 358, the domain is characterized as bZIP.
+At position 28 to 131, the domain is characterized as SRCR 1.
+At position 134 to 234, the domain is characterized as SRCR 2.
+At position 239 to 340, the domain is characterized as SRCR 3.
+At position 376 to 476, the domain is characterized as SRCR 4.
+At position 481 to 581, the domain is characterized as SRCR 5.
+At position 586 to 686, the domain is characterized as SRCR 6.
+At position 689 to 789, the domain is characterized as SRCR 7.
+At position 794 to 895, the domain is characterized as SRCR 8.
+At position 931 to 1031, the domain is characterized as SRCR 9.
+At position 1155 to 1255, the domain is characterized as SRCR 11.
+At position 1046 to 1108, the domain is characterized as FIP-RBD.
+At position 14 to 75, the domain is characterized as TRAM.
+At position 7 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 551 to 914, the domain is characterized as UvrD-like helicase C-terminal.
+At position 68 to 177, the domain is characterized as Thioredoxin.
+At position 217 to 461, the domain is characterized as CN hydrolase.
+At position 112 to 197, the domain is characterized as Core-binding (CB).
+At position 220 to 402, the domain is characterized as Tyr recombinase.
+At position 122 to 315, the domain is characterized as JmjC.
+At position 744 to 1005, the domain is characterized as PPM-type phosphatase.
+At position 5 to 83, the domain is characterized as RRM 1.
+At position 107 to 185, the domain is characterized as RRM 2.
+At position 277 to 386, the domain is characterized as RRM 3.
+At position 486 to 579, the domain is characterized as RRM 4.
+At position 205 to 346, the domain is characterized as Nudix hydrolase.
+At position 639 to 721, the domain is characterized as BRCT.
+At position 374 to 544, the domain is characterized as tr-type G.
+At position 440 to 457, the domain is characterized as WH2.
+At position 100 to 318, the domain is characterized as Fibrinogen C-terminal.
+At position 33 to 107, the domain is characterized as Ubiquitin-like.
+At position 178 to 206, the domain is characterized as STI1 1.
+At position 208 to 247, the domain is characterized as STI1 2.
+At position 379 to 426, the domain is characterized as STI1 3.
+At position 430 to 462, the domain is characterized as STI1 4.
+At position 581 to 621, the domain is characterized as UBA.
+At position 1 to 400, the domain is characterized as Glutamine amidotransferase type-2.
+At position 2107 to 2170, the domain is characterized as HP.
+At position 7 to 149, the domain is characterized as N-acetyltransferase.
+At position 39 to 139, the domain is characterized as Ig-like V-type 1.
+At position 142 to 231, the domain is characterized as Ig-like V-type 2.
+At position 64 to 262, the domain is characterized as Exonuclease.
+At position 524 to 579, the domain is characterized as LRRCT.
+At position 638 to 779, the domain is characterized as TIR.
+At position 16 to 260, the domain is characterized as NR LBD.
+At position 261 to 438, the domain is characterized as Helicase C-terminal.
+At position 395 to 624, the domain is characterized as NR LBD.
+At position 201 to 299, the domain is characterized as HTH araC/xylS-type.
+At position 1 to 178, the domain is characterized as PTS EIIB type-5.
+At position 28 to 230, the domain is characterized as AIG1-type G.
+At position 233 to 262, the domain is characterized as IQ.
+At position 1 to 54, the domain is characterized as POU-specific.
+At position 1369 to 1522, the domain is characterized as PINc.
+At position 1120 to 1182, the domain is characterized as SH3.
+At position 251 to 328, the domain is characterized as TFIIS N-terminal.
+At position 174 to 358, the domain is characterized as Glutamine amidotransferase type-1.
+At position 496 to 634, the domain is characterized as Ricin B-type lectin.
+At position 587 to 666, the domain is characterized as BRCT.
+At position 22 to 61, the domain is characterized as SMB 1.
+At position 62 to 105, the domain is characterized as SMB 2.
+At position 112 to 385, the domain is characterized as EndoU.
+At position 324 to 469, the domain is characterized as VPS9.
+At position 3 to 140, the domain is characterized as TIR.
+At position 124 to 408, the domain is characterized as Peptidase S1.
+At position 332 to 374, the domain is characterized as LRRNT.
+At position 530 to 581, the domain is characterized as LRRCT 2.
+At position 315 to 601, the domain is characterized as ABC transporter 1.
+At position 621 to 950, the domain is characterized as ABC transporter 2.
+At position 26 to 149, the domain is characterized as Thioredoxin 1.
+At position 369 to 488, the domain is characterized as Thioredoxin 2.
+At position 5 to 151, the domain is characterized as UBC core.
+At position 546 to 597, the domain is characterized as GYF.
+At position 149 to 248, the domain is characterized as PB1.
+At position 341 to 384, the domain is characterized as LysM 1.
+At position 400 to 448, the domain is characterized as LysM 2.
+At position 6 to 97, the domain is characterized as CS.
+At position 44 to 333, the domain is characterized as ABC transmembrane type-1 1.
+At position 700 to 988, the domain is characterized as ABC transmembrane type-1 2.
+At position 1024 to 1260, the domain is characterized as ABC transporter 2.
+At position 37 to 105, the domain is characterized as KH type-2.
+At position 454 to 466, the domain is characterized as CRIB.
+At position 958 to 996, the domain is characterized as UBA.
+At position 707 to 987, the domain is characterized as Autotransporter.
+At position 46 to 312, the domain is characterized as PPM-type phosphatase.
+At position 1363 to 1886, the domain is characterized as FAT.
+At position 1993 to 2309, the domain is characterized as PI3K/PI4K catalytic.
+At position 2293 to 2325, the domain is characterized as FATC.
+At position 136 to 514, the domain is characterized as MACPF.
+At position 515 to 545, the domain is characterized as EGF-like.
+At position 411 to 593, the domain is characterized as RHD.
+At position 229 to 303, the domain is characterized as U-box.
+At position 149 to 335, the domain is characterized as CNNM transmembrane.
+At position 354 to 415, the domain is characterized as CBS 1.
+At position 421 to 479, the domain is characterized as CBS 2.
+At position 419 to 572, the domain is characterized as GAF 1.
+At position 604 to 754, the domain is characterized as GAF 2.
+At position 783 to 1107, the domain is characterized as PDEase.
+At position 27 to 87, the domain is characterized as v-SNARE coiled-coil homology.
+At position 610 to 950, the domain is characterized as PUM-HD.
+At position 306 to 366, the domain is characterized as SH3.
+At position 581 to 659, the domain is characterized as BRCT.
+At position 110 to 139, the domain is characterized as IQ.
+At position 73 to 197, the domain is characterized as THUMP.
+At position 289 to 664, the domain is characterized as GH16.
+At position 41 to 236, the domain is characterized as Cupin type-1 1.
+At position 295 to 444, the domain is characterized as Cupin type-1 2.
+At position 744 to 859, the domain is characterized as GAE.
+At position 47 to 193, the domain is characterized as Tyrosine-protein phosphatase.
+At position 516 to 609, the domain is characterized as BRCT 3.
+At position 616 to 704, the domain is characterized as BRCT 4.
+At position 781 to 862, the domain is characterized as BRCT 5.
+At position 883 to 924, the domain is characterized as BRCT 6.
+At position 8 to 187, the domain is characterized as Guanylate kinase-like.
+At position 165 to 199, the domain is characterized as SAP.
+At position 56 to 110, the domain is characterized as TCP.
+At position 955 to 1187, the domain is characterized as Ras-GEF.
+At position 27 to 133, the domain is characterized as Cadherin 1.
+At position 568 to 676, the domain is characterized as Cadherin 6.
+At position 43 to 115, the domain is characterized as Bromo 1.
+At position 286 to 358, the domain is characterized as Bromo 2.
+At position 124 to 324, the domain is characterized as TLDc.
+At position 37 to 262, the domain is characterized as Cache.
+At position 301 to 355, the domain is characterized as HAMP.
+At position 360 to 596, the domain is characterized as Methyl-accepting transducer.
+At position 1 to 79, the domain is characterized as Glutaredoxin.
+At position 53 to 197, the domain is characterized as C2 B9-type.
+At position 4 to 258, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1 to 30, the domain is characterized as C-type lectin.
+At position 207 to 292, the domain is characterized as Ig-like C1-type.
+At position 420 to 455, the domain is characterized as UVR.
+At position 73 to 354, the domain is characterized as Protein kinase.
+At position 2 to 91, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 136 to 251, the domain is characterized as CMP/dCMP-type deaminase.
+At position 415 to 578, the domain is characterized as Miro 2.
+At position 49 to 205, the domain is characterized as PPIase cyclophilin-type.
+At position 19 to 184, the domain is characterized as Exonuclease.
+At position 1767 to 1796, the domain is characterized as IQ.
+At position 171 to 200, the domain is characterized as GS.
+At position 201 to 491, the domain is characterized as Protein kinase.
+At position 88 to 368, the domain is characterized as Protein kinase.
+At position 545 to 588, the domain is characterized as TSP type-1 2.
+At position 5 to 116, the domain is characterized as Response regulatory.
+At position 239 to 326, the domain is characterized as PKD.
+At position 5 to 212, the domain is characterized as ABC transporter.
+At position 79 to 186, the domain is characterized as Ras-associating.
+At position 187 to 234, the domain is characterized as SARAH.
+At position 184 to 452, the domain is characterized as MHD.
+At position 333 to 502, the domain is characterized as tr-type G.
+At position 22 to 57, the domain is characterized as CBM1.
+At position 663 to 738, the domain is characterized as Biotinyl-binding.
+At position 258 to 344, the domain is characterized as PNT.
+At position 1 to 35, the domain is characterized as Myosin motor.
+At position 113 to 181, the domain is characterized as SAM.
+At position 405 to 564, the domain is characterized as PA14.
+At position 96 to 384, the domain is characterized as Protein kinase.
+At position 186 to 251, the domain is characterized as KH 1.
+At position 267 to 334, the domain is characterized as KH 2.
+At position 420 to 485, the domain is characterized as KH 3.
+At position 502 to 568, the domain is characterized as KH 4.
+At position 141 to 443, the domain is characterized as NB-ARC.
+At position 102 to 478, the domain is characterized as PPM-type phosphatase.
+At position 73 to 95, the domain is characterized as EF-hand 2.
+At position 42 to 175, the domain is characterized as MPN.
+At position 84 to 505, the domain is characterized as Peptidase A1.
+At position 314 to 419, the domain is characterized as Saposin B-type.
+At position 35 to 159, the domain is characterized as AB hydrolase-1.
+At position 340 to 426, the domain is characterized as PPIase FKBP-type.
+At position 1111 to 1244, the domain is characterized as TIR.
+At position 7 to 101, the domain is characterized as HTH arsR-type.
+At position 129 to 218, the domain is characterized as Rhodanese.
+At position 223 to 261, the domain is characterized as LRRCT.
+At position 3 to 232, the domain is characterized as Radical SAM core.
+At position 54 to 232, the domain is characterized as Helicase ATP-binding.
+At position 274 to 430, the domain is characterized as Helicase C-terminal.
+At position 200 to 251, the domain is characterized as bHLH.
+At position 161 to 200, the domain is characterized as UBA.
+At position 271 to 432, the domain is characterized as EF-1-gamma C-terminal.
+At position 29 to 103, the domain is characterized as ACT.
+At position 168 to 434, the domain is characterized as AB hydrolase-1.
+At position 3 to 56, the domain is characterized as TIL.
+At position 57 to 91, the domain is characterized as SAP.
+At position 33 to 175, the domain is characterized as Clp R.
+At position 447 to 482, the domain is characterized as UVR.
+At position 1 to 141, the domain is characterized as C2 1.
+At position 159 to 295, the domain is characterized as C2 2.
+At position 338 to 557, the domain is characterized as VWFA.
+At position 83 to 398, the domain is characterized as IF rod.
+At position 8 to 248, the domain is characterized as ABC transporter 1.
+At position 309 to 542, the domain is characterized as ABC transporter 2.
+At position 67 to 124, the domain is characterized as CTLH.
+At position 472 to 554, the domain is characterized as PDZ 2.
+At position 643 to 721, the domain is characterized as PDZ 3.
+At position 813 to 895, the domain is characterized as PDZ 4.
+At position 970 to 1066, the domain is characterized as PDZ 5.
+At position 1124 to 1206, the domain is characterized as PDZ 6.
+At position 26 to 121, the domain is characterized as BTB.
+At position 269 to 402, the domain is characterized as SHD.
+At position 407 to 710, the domain is characterized as MHD.
+At position 351 to 450, the domain is characterized as BRCT.
+At position 8 to 131, the domain is characterized as MATH.
+At position 77 to 222, the domain is characterized as Tyrosine-protein phosphatase.
+At position 152 to 395, the domain is characterized as Radical SAM core.
+At position 102 to 183, the domain is characterized as PRC barrel.
+At position 125 to 233, the domain is characterized as CBM21.
+At position 20 to 103, the domain is characterized as Toprim.
+At position 36 to 278, the domain is characterized as ATP-grasp.
+At position 27 to 178, the domain is characterized as NAC.
+At position 71 to 186, the domain is characterized as C-type lectin.
+At position 34 to 387, the domain is characterized as Rab-GAP TBC.
+At position 585 to 783, the domain is characterized as Tyrosine-protein phosphatase.
+At position 76 to 292, the domain is characterized as Radical SAM core.
+At position 22 to 325, the domain is characterized as SET.
+At position 495 to 549, the domain is characterized as Kazal-like.
+At position 26 to 81, the domain is characterized as F-box.
+At position 26 to 128, the domain is characterized as Gnk2-homologous 1.
+At position 134 to 244, the domain is characterized as Gnk2-homologous 2.
+At position 19 to 152, the domain is characterized as Cyclin N-terminal.
+At position 154 to 254, the domain is characterized as Fe2OG dioxygenase.
+At position 8 to 111, the domain is characterized as HIT.
+At position 752 to 803, the domain is characterized as HTH myb-type 1.
+At position 804 to 858, the domain is characterized as HTH myb-type 2.
+At position 363 to 505, the domain is characterized as Response regulatory.
+At position 6 to 213, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 253, the domain is characterized as Deacetylase sirtuin-type.
+At position 69 to 210, the domain is characterized as GAF.
+At position 252 to 480, the domain is characterized as Sigma-54 factor interaction.
+At position 10 to 252, the domain is characterized as KaiC 1.
+At position 253 to 485, the domain is characterized as KaiC 2.
+At position 164 to 228, the domain is characterized as t-SNARE coiled-coil homology.
+At position 92 to 125, the domain is characterized as WW 1.
+At position 133 to 166, the domain is characterized as WW 2.
+At position 276 to 330, the domain is characterized as FF 1.
+At position 340 to 397, the domain is characterized as FF 2.
+At position 410 to 470, the domain is characterized as FF 3.
+At position 490 to 550, the domain is characterized as FF 4.
+At position 554 to 610, the domain is characterized as FF 5.
+At position 625 to 682, the domain is characterized as FF 6.
+At position 21 to 200, the domain is characterized as Helicase ATP-binding.
+At position 335 to 501, the domain is characterized as Helicase C-terminal.
+At position 528 to 622, the domain is characterized as Dicer dsRNA-binding fold.
+At position 874 to 1014, the domain is characterized as RNase III 1.
+At position 1056 to 1250, the domain is characterized as RNase III 2.
+At position 168 to 335, the domain is characterized as OBG-type G.
+At position 105 to 268, the domain is characterized as Integrase catalytic.
+At position 241 to 337, the domain is characterized as CRM 1.
+At position 359 to 455, the domain is characterized as CRM 2.
+At position 44 to 106, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 179 to 241, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 439 to 563, the domain is characterized as Ricin B-type lectin 2.
+At position 35 to 111, the domain is characterized as Inhibitor I9.
+At position 116 to 589, the domain is characterized as Peptidase S8.
+At position 362 to 433, the domain is characterized as PA.
+At position 623 to 690, the domain is characterized as S1 motif.
+At position 21 to 112, the domain is characterized as UPAR/Ly6 1.
+At position 113 to 208, the domain is characterized as UPAR/Ly6 2.
+At position 209 to 300, the domain is characterized as UPAR/Ly6 3.
+At position 34 to 211, the domain is characterized as Plastocyanin-like 1.
+At position 212 to 376, the domain is characterized as Plastocyanin-like 2.
+At position 21 to 278, the domain is characterized as Alpha-carbonic anhydrase.
+At position 205 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 15 to 284, the domain is characterized as Protein kinase.
+At position 70 to 111, the domain is characterized as CWF21.
+At position 12 to 87, the domain is characterized as PAS.
+At position 88 to 138, the domain is characterized as PAC.
+At position 147 to 258, the domain is characterized as STAS.
+At position 372 to 462, the domain is characterized as HTH La-type RNA-binding.
+At position 187 to 245, the domain is characterized as bZIP.
+At position 228 to 453, the domain is characterized as SMP-LTD.
+At position 451 to 576, the domain is characterized as C2 1.
+At position 636 to 781, the domain is characterized as C2 2.
+At position 138 to 290, the domain is characterized as N-acetyltransferase.
+At position 154 to 267, the domain is characterized as SPR.
+At position 228 to 273, the domain is characterized as TSP type-1.
+At position 286 to 360, the domain is characterized as CTCK.
+At position 64 to 197, the domain is characterized as TNase-like.
+At position 26 to 178, the domain is characterized as N-acetyltransferase.
+At position 33 to 336, the domain is characterized as PPM-type phosphatase.
+At position 46 to 79, the domain is characterized as EF-hand 2.
+At position 92 to 150, the domain is characterized as CBS 1.
+At position 151 to 207, the domain is characterized as CBS 2.
+At position 4 to 215, the domain is characterized as HD Cas3-type.
+At position 39 to 155, the domain is characterized as HD.
+At position 231 to 427, the domain is characterized as HD-GYP.
+At position 481 to 598, the domain is characterized as Toprim.
+At position 30 to 105, the domain is characterized as REM-1.
+At position 306 to 413, the domain is characterized as PH.
+At position 592 to 652, the domain is characterized as CBS 1.
+At position 704 to 761, the domain is characterized as CBS 2.
+At position 5 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 197 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 156 to 278, the domain is characterized as C2 1.
+At position 290 to 425, the domain is characterized as C2 2.
+At position 151 to 186, the domain is characterized as Tify.
+At position 450 to 515, the domain is characterized as SAM 1.
+At position 528 to 592, the domain is characterized as SAM 2.
+At position 616 to 683, the domain is characterized as SAM 3.
+At position 366 to 653, the domain is characterized as Protein kinase.
+At position 615 to 736, the domain is characterized as MSP.
+At position 38 to 139, the domain is characterized as LOB.
+At position 3 to 74, the domain is characterized as S4 RNA-binding.
+At position 173 to 323, the domain is characterized as N-acetyltransferase.
+At position 376 to 555, the domain is characterized as VWFA.
+At position 99 to 184, the domain is characterized as MANSC.
+At position 210 to 305, the domain is characterized as PKD.
+At position 309 to 345, the domain is characterized as LDL-receptor class A.
+At position 262 to 435, the domain is characterized as tr-type G.
+At position 1 to 133, the domain is characterized as FAD-binding FR-type.
+At position 388 to 515, the domain is characterized as PINc.
+At position 15 to 107, the domain is characterized as CARD.
+At position 568 to 658, the domain is characterized as PDZ.
+At position 807 to 990, the domain is characterized as Guanylate kinase-like.
+At position 7 to 67, the domain is characterized as HTH iclR-type.
+At position 227 to 300, the domain is characterized as HSA.
+At position 570 to 735, the domain is characterized as Helicase ATP-binding.
+At position 1196 to 1342, the domain is characterized as Helicase C-terminal.
+At position 11 to 199, the domain is characterized as DPCK.
+At position 368 to 434, the domain is characterized as PDZ 3.
+At position 464 to 541, the domain is characterized as SH3.
+At position 573 to 754, the domain is characterized as Guanylate kinase-like.
+At position 51 to 146, the domain is characterized as Cyclin N-terminal.
+At position 87 to 364, the domain is characterized as Protein kinase.
+At position 19 to 172, the domain is characterized as MRH.
+At position 177 to 203, the domain is characterized as PLD phosphodiesterase 1.
+At position 4 to 133, the domain is characterized as PINc.
+At position 35 to 202, the domain is characterized as N-acetyltransferase.
+At position 100 to 305, the domain is characterized as Peptidase M12A.
+At position 307 to 419, the domain is characterized as CUB 1.
+At position 420 to 531, the domain is characterized as CUB 2.
+At position 532 to 573, the domain is characterized as EGF-like; calcium-binding.
+At position 521 to 640, the domain is characterized as SMC hinge.
+At position 33 to 164, the domain is characterized as Thioredoxin.
+At position 25 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 142, the domain is characterized as C2 NT-type.
+At position 33 to 62, the domain is characterized as LRRNT.
+At position 192 to 246, the domain is characterized as LRRCT.
+At position 160 to 330, the domain is characterized as Helicase ATP-binding.
+At position 359 to 504, the domain is characterized as Helicase C-terminal.
+At position 198 to 494, the domain is characterized as Protein kinase.
+At position 57 to 158, the domain is characterized as SRCR 1.
+At position 187 to 301, the domain is characterized as SRCR 2.
+At position 325 to 424, the domain is characterized as SRCR 3.
+At position 434 to 543, the domain is characterized as SRCR 4.
+At position 26 to 108, the domain is characterized as RRM 1.
+At position 111 to 190, the domain is characterized as RRM 2.
+At position 27 to 242, the domain is characterized as Peptidase S1.
+At position 407 to 658, the domain is characterized as Protein kinase.
+At position 161 to 446, the domain is characterized as FIIND.
+At position 446 to 536, the domain is characterized as CARD.
+At position 622 to 701, the domain is characterized as BRCT.
+At position 107 to 353, the domain is characterized as AB hydrolase-1.
+At position 9 to 259, the domain is characterized as Pyruvate carboxyltransferase.
+At position 270 to 424, the domain is characterized as NHR 2.
+At position 25 to 173, the domain is characterized as Ferritin-like diiron.
+At position 377 to 424, the domain is characterized as GPS.
+At position 19 to 166, the domain is characterized as MRH.
+At position 642 to 721, the domain is characterized as BRCT.
+At position 5 to 65, the domain is characterized as J.
+At position 25 to 74, the domain is characterized as F-box.
+At position 120 to 259, the domain is characterized as PPC.
+At position 32 to 160, the domain is characterized as ENTH.
+At position 771 to 1012, the domain is characterized as I/LWEQ.
+At position 1 to 191, the domain is characterized as BPL/LPL catalytic.
+At position 39 to 117, the domain is characterized as KH type-2.
+At position 14 to 74, the domain is characterized as HTH iclR-type.
+At position 89 to 262, the domain is characterized as IclR-ED.
+At position 1 to 100, the domain is characterized as MSS4.
+At position 37 to 129, the domain is characterized as Fibronectin type-III 1.
+At position 130 to 222, the domain is characterized as Fibronectin type-III 2.
+At position 218 to 305, the domain is characterized as Fibronectin type-III 3.
+At position 306 to 388, the domain is characterized as Fibronectin type-III 4.
+At position 393 to 454, the domain is characterized as Fibronectin type-III 5.
+At position 475 to 569, the domain is characterized as Fibronectin type-III 6.
+At position 565 to 654, the domain is characterized as Fibronectin type-III 7.
+At position 655 to 749, the domain is characterized as Fibronectin type-III 8.
+At position 744 to 831, the domain is characterized as Fibronectin type-III 9.
+At position 832 to 926, the domain is characterized as Fibronectin type-III 10.
+At position 1150 to 1409, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1427 to 1695, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 119 to 230, the domain is characterized as Fe2OG dioxygenase.
+At position 4 to 34, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 62 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 94 to 123, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 8 to 92, the domain is characterized as KRAB.
+At position 4 to 307, the domain is characterized as Protein kinase.
+At position 75 to 181, the domain is characterized as Expansin-like EG45.
+At position 194 to 281, the domain is characterized as Expansin-like CBD.
+At position 1 to 194, the domain is characterized as AMMECR1.
+At position 176 to 260, the domain is characterized as Death.
+At position 407 to 492, the domain is characterized as PDZ 1.
+At position 42 to 103, the domain is characterized as Chitin-binding type R&R.
+At position 191 to 254, the domain is characterized as Nudix hydrolase.
+At position 124 to 328, the domain is characterized as Alpha-type protein kinase.
+At position 392 to 599, the domain is characterized as MCM.
+At position 248 to 329, the domain is characterized as Toprim.
+At position 27 to 138, the domain is characterized as Ig-like V-type 1.
+At position 389 to 571, the domain is characterized as RHD.
+At position 17 to 124, the domain is characterized as Rhodanese.
+At position 134 to 618, the domain is characterized as Peptidase S8.
+At position 33 to 430, the domain is characterized as FERM.
+At position 449 to 529, the domain is characterized as SH2; atypical.
+At position 589 to 866, the domain is characterized as Protein kinase 1.
+At position 894 to 1166, the domain is characterized as Protein kinase 2.
+At position 344 to 402, the domain is characterized as GYF.
+At position 240 to 628, the domain is characterized as GRAS.
+At position 39 to 147, the domain is characterized as Gnk2-homologous 1.
+At position 160 to 267, the domain is characterized as Gnk2-homologous 2.
+At position 184 to 448, the domain is characterized as MHD.
+At position 169 to 391, the domain is characterized as Histidine kinase.
+At position 115 to 294, the domain is characterized as SMP-LTD.
+At position 293 to 413, the domain is characterized as C2 1.
+At position 442 to 563, the domain is characterized as C2 2.
+At position 710 to 832, the domain is characterized as C2 3.
+At position 246 to 310, the domain is characterized as Z-binding 2.
+At position 456 to 524, the domain is characterized as DRBM 1.
+At position 567 to 635, the domain is characterized as DRBM 2.
+At position 675 to 743, the domain is characterized as DRBM 3.
+At position 835 to 1170, the domain is characterized as A to I editase.
+At position 17 to 131, the domain is characterized as MTTase N-terminal.
+At position 145 to 253, the domain is characterized as Gnk2-homologous 2.
+At position 249 to 428, the domain is characterized as Helicase ATP-binding.
+At position 613 to 779, the domain is characterized as Helicase C-terminal.
+At position 795 to 928, the domain is characterized as RLR CTR.
+At position 383 to 482, the domain is characterized as SprT-like.
+At position 30 to 216, the domain is characterized as FAD-binding PCMH-type.
+At position 1064 to 1302, the domain is characterized as Glutamine amidotransferase type-1.
+At position 29 to 157, the domain is characterized as PX.
+At position 324 to 409, the domain is characterized as SCD.
+At position 47 to 450, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 714 to 1015, the domain is characterized as PKS/mFAS DH.
+At position 2246 to 2322, the domain is characterized as Carrier.
+At position 4 to 230, the domain is characterized as Protein kinase.
+At position 241 to 299, the domain is characterized as Collagen-like 1.
+At position 350 to 409, the domain is characterized as Collagen-like 2.
+At position 430 to 469, the domain is characterized as Collagen-like 3.
+At position 493 to 526, the domain is characterized as Collagen-like 4.
+At position 527 to 586, the domain is characterized as Collagen-like 5.
+At position 621 to 680, the domain is characterized as Collagen-like 6.
+At position 681 to 740, the domain is characterized as Collagen-like 7.
+At position 10 to 77, the domain is characterized as Histone-fold.
+At position 205 to 424, the domain is characterized as RMT2.
+At position 6 to 211, the domain is characterized as DPCK.
+At position 20 to 145, the domain is characterized as C-type lysozyme.
+At position 31 to 545, the domain is characterized as Sema.
+At position 605 to 695, the domain is characterized as Ig-like C2-type.
+At position 224 to 461, the domain is characterized as NR LBD.
+At position 154 to 448, the domain is characterized as Dynamin-type G.
+At position 825 to 916, the domain is characterized as GED.
+At position 125 to 357, the domain is characterized as Radical SAM core.
+At position 32 to 134, the domain is characterized as Ig-like V-type.
+At position 139 to 367, the domain is characterized as Sigma-54 factor interaction.
+At position 116 to 410, the domain is characterized as AB hydrolase-1.
+At position 229 to 565, the domain is characterized as Protein kinase.
+At position 472 to 565, the domain is characterized as PSP1 C-terminal.
+At position 134 to 319, the domain is characterized as Helicase ATP-binding.
+At position 510 to 660, the domain is characterized as Helicase C-terminal.
+At position 358 to 390, the domain is characterized as EGF-like.
+At position 929 to 1025, the domain is characterized as BRCT.
+At position 13 to 248, the domain is characterized as ABC transporter.
+At position 1 to 20, the domain is characterized as LCN-type CS-alpha/beta.
+At position 92 to 186, the domain is characterized as GST C-terminal.
+At position 8 to 413, the domain is characterized as BRO1.
+At position 128 to 266, the domain is characterized as SIS.
+At position 56 to 182, the domain is characterized as Thioredoxin 1.
+At position 407 to 524, the domain is characterized as Thioredoxin 2.
+At position 137 to 235, the domain is characterized as HTH araC/xylS-type.
+At position 70 to 323, the domain is characterized as AB hydrolase-1.
+At position 21 to 159, the domain is characterized as Ig-like V-type.
+At position 381 to 805, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1280 to 1581, the domain is characterized as PKS/mFAS DH.
+At position 1640 to 1724, the domain is characterized as Carrier.
+At position 199 to 299, the domain is characterized as SRCR 2.
+At position 305 to 405, the domain is characterized as SRCR 3.
+At position 464 to 565, the domain is characterized as SRCR 4.
+At position 758 to 858, the domain is characterized as SRCR 5.
+At position 21 to 101, the domain is characterized as UPAR/Ly6.
+At position 35 to 105, the domain is characterized as S1 motif 1.
+At position 120 to 183, the domain is characterized as S1 motif 2.
+At position 204 to 272, the domain is characterized as S1 motif 3.
+At position 289 to 359, the domain is characterized as S1 motif 4.
+At position 377 to 444, the domain is characterized as S1 motif 5.
+At position 461 to 525, the domain is characterized as S1 motif 6.
+At position 28 to 342, the domain is characterized as Septin-type G.
+At position 240 to 362, the domain is characterized as C2 1.
+At position 402 to 517, the domain is characterized as C2 2.
+At position 15 to 161, the domain is characterized as NAC.
+At position 8 to 334, the domain is characterized as Protein kinase.
+At position 32 to 133, the domain is characterized as LOB.
+At position 71 to 240, the domain is characterized as Helicase ATP-binding.
+At position 265 to 445, the domain is characterized as Helicase C-terminal.
+At position 412 to 507, the domain is characterized as Toprim.
+At position 44 to 147, the domain is characterized as FAD-binding FR-type.
+At position 136 to 199, the domain is characterized as bZIP.
+At position 139 to 273, the domain is characterized as Ig-like C1-type 1.
+At position 278 to 382, the domain is characterized as Ig-like C1-type 2.
+At position 363 to 793, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1641 to 1718, the domain is characterized as Carrier.
+At position 222 to 458, the domain is characterized as PPM-type phosphatase.
+At position 23 to 150, the domain is characterized as Cyclin N-terminal.
+At position 41 to 116, the domain is characterized as Rho RNA-BD.
+At position 50 to 89, the domain is characterized as ShKT 1.
+At position 107 to 134, the domain is characterized as ShKT 2.
+At position 140 to 182, the domain is characterized as ShKT 3.
+At position 139 to 222, the domain is characterized as SPOR.
+At position 226 to 474, the domain is characterized as FAD-binding FR-type.
+At position 28 to 151, the domain is characterized as Thioredoxin.
+At position 124 to 178, the domain is characterized as AWS.
+At position 180 to 297, the domain is characterized as SET.
+At position 304 to 320, the domain is characterized as Post-SET.
+At position 46 to 105, the domain is characterized as LIM zinc-binding 1.
+At position 105 to 169, the domain is characterized as LIM zinc-binding 2.
+At position 95 to 375, the domain is characterized as ABC transmembrane type-1.
+At position 418 to 660, the domain is characterized as ABC transporter.
+At position 196 to 264, the domain is characterized as POTRA.
+At position 219 to 361, the domain is characterized as TrmE-type G.
+At position 23 to 79, the domain is characterized as L27 1.
+At position 86 to 136, the domain is characterized as L27 2.
+At position 153 to 234, the domain is characterized as PDZ.
+At position 241 to 311, the domain is characterized as SH3.
+At position 426 to 615, the domain is characterized as Guanylate kinase-like.
+At position 153 to 331, the domain is characterized as Helicase ATP-binding.
+At position 378 to 523, the domain is characterized as Helicase C-terminal.
+At position 102 to 154, the domain is characterized as Myb-like 1.
+At position 459 to 526, the domain is characterized as Myb-like 2.
+At position 322 to 467, the domain is characterized as JmjC.
+At position 104 to 441, the domain is characterized as Kinesin motor.
+At position 28 to 152, the domain is characterized as PX.
+At position 130 to 565, the domain is characterized as Urease.
+At position 192 to 425, the domain is characterized as RMT2.
+At position 270 to 385, the domain is characterized as Cadherin 3.
+At position 386 to 497, the domain is characterized as Cadherin 4.
+At position 19 to 55, the domain is characterized as CBM1.
+At position 1 to 136, the domain is characterized as Thioredoxin.
+At position 202 to 320, the domain is characterized as SET.
+At position 10 to 232, the domain is characterized as ABC transporter.
+At position 12 to 339, the domain is characterized as Transferrin-like 1.
+At position 351 to 680, the domain is characterized as Transferrin-like 2.
+At position 259 to 377, the domain is characterized as YkuD.
+At position 112 to 274, the domain is characterized as CP-type G.
+At position 261 to 296, the domain is characterized as DMA.
+At position 878 to 1055, the domain is characterized as PIK helical.
+At position 1127 to 1396, the domain is characterized as PI3K/PI4K catalytic.
+At position 162 to 330, the domain is characterized as Helicase ATP-binding.
+At position 506 to 665, the domain is characterized as Helicase C-terminal.
+At position 93 to 286, the domain is characterized as DH.
+At position 303 to 462, the domain is characterized as PH.
+At position 488 to 616, the domain is characterized as C2.
+At position 650 to 848, the domain is characterized as Rho-GAP.
+At position 357 to 406, the domain is characterized as bHLH.
+At position 247 to 424, the domain is characterized as FCP1 homology.
+At position 137 to 256, the domain is characterized as RGS.
+At position 59 to 127, the domain is characterized as SH2.
+At position 277 to 468, the domain is characterized as Rho-GAP.
+At position 1 to 403, the domain is characterized as Helicase ATP-binding.
+At position 32 to 168, the domain is characterized as Arf-GAP.
+At position 4 to 187, the domain is characterized as Lon N-terminal.
+At position 581 to 762, the domain is characterized as Lon proteolytic.
+At position 72 to 164, the domain is characterized as DEP.
+At position 2 to 97, the domain is characterized as HTH arsR-type.
+At position 278 to 446, the domain is characterized as Helicase ATP-binding.
+At position 614 to 790, the domain is characterized as Helicase C-terminal.
+At position 49 to 258, the domain is characterized as YjeF N-terminal.
+At position 1749 to 1844, the domain is characterized as Fibronectin type-III 3.
+At position 1843 to 1927, the domain is characterized as Fibronectin type-III 4.
+At position 1934 to 2029, the domain is characterized as Fibronectin type-III 5.
+At position 2030 to 2118, the domain is characterized as Fibronectin type-III 6.
+At position 346 to 400, the domain is characterized as EGF-like.
+At position 6 to 190, the domain is characterized as Flavodoxin-like.
+At position 64 to 201, the domain is characterized as N-terminal Ras-GEF.
+At position 248 to 503, the domain is characterized as Ras-GEF.
+At position 612 to 699, the domain is characterized as Ras-associating.
+At position 1 to 93, the domain is characterized as Glutaredoxin.
+At position 133 to 335, the domain is characterized as ATP-grasp 1.
+At position 3 to 91, the domain is characterized as DM10.
+At position 115 to 346, the domain is characterized as ATP-grasp.
+At position 146 to 208, the domain is characterized as t-SNARE coiled-coil homology.
+At position 302 to 398, the domain is characterized as SH2.
+At position 419 to 478, the domain is characterized as SH3.
+At position 544 to 787, the domain is characterized as Peptidase S1.
+At position 206 to 329, the domain is characterized as MsrB.
+At position 26 to 103, the domain is characterized as RRM 1.
+At position 147 to 225, the domain is characterized as RRM 2.
+At position 290 to 383, the domain is characterized as RRM 3.
+At position 462 to 612, the domain is characterized as RRM 4.
+At position 51 to 342, the domain is characterized as Protein kinase.
+At position 155 to 207, the domain is characterized as bHLH.
+At position 28 to 102, the domain is characterized as REM-1 1.
+At position 242 to 322, the domain is characterized as REM-1 3.
+At position 359 to 515, the domain is characterized as C2.
+At position 863 to 1122, the domain is characterized as Protein kinase.
+At position 1123 to 1190, the domain is characterized as AGC-kinase C-terminal.
+At position 16 to 167, the domain is characterized as PPIase cyclophilin-type.
+At position 49 to 377, the domain is characterized as Protein kinase.
+At position 147 to 191, the domain is characterized as bZIP.
+At position 208 to 444, the domain is characterized as DOG1.
+At position 50 to 90, the domain is characterized as LDL-receptor class A.
+At position 23 to 45, the domain is characterized as GoLoco 1.
+At position 63 to 85, the domain is characterized as GoLoco 2.
+At position 12 to 343, the domain is characterized as PTS EIIC type-2.
+At position 379 to 475, the domain is characterized as PTS EIIB type-2.
+At position 496 to 638, the domain is characterized as PTS EIIA type-2.
+At position 140 to 199, the domain is characterized as SH3.
+At position 138 to 312, the domain is characterized as MRG.
+At position 310 to 332, the domain is characterized as RRM.
+At position 8 to 63, the domain is characterized as HTH cro/C1-type 1.
+At position 234 to 290, the domain is characterized as HTH cro/C1-type 2.
+At position 2 to 80, the domain is characterized as Sm.
+At position 30 to 97, the domain is characterized as HTH gntR-type.
+At position 82 to 188, the domain is characterized as SH2.
+At position 205 to 253, the domain is characterized as SOCS box.
+At position 166 to 445, the domain is characterized as Protein kinase.
+At position 25 to 448, the domain is characterized as SET.
+At position 185 to 382, the domain is characterized as ATP-grasp.
+At position 268 to 426, the domain is characterized as Helicase ATP-binding.
+At position 427 to 595, the domain is characterized as Helicase C-terminal.
+At position 572 to 696, the domain is characterized as C2.
+At position 729 to 923, the domain is characterized as Rho-GAP.
+At position 102 to 286, the domain is characterized as Helicase ATP-binding.
+At position 321 to 554, the domain is characterized as Helicase C-terminal.
+At position 507 to 611, the domain is characterized as Calponin-homology (CH).
+At position 681 to 743, the domain is characterized as LIM zinc-binding.
+At position 905 to 1048, the domain is characterized as bMERB.
+At position 71 to 147, the domain is characterized as Cytochrome b5 heme-binding.
+At position 228 to 315, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 11 to 268, the domain is characterized as Protein kinase.
+At position 48 to 160, the domain is characterized as FAD-binding FR-type.
+At position 1691 to 1726, the domain is characterized as EF-hand.
+At position 1 to 247, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 134 to 321, the domain is characterized as Reticulon.
+At position 25 to 1224, the domain is characterized as Zinc-hook.
+At position 555 to 671, the domain is characterized as SMC hinge.
+At position 52 to 188, the domain is characterized as RGS.
+At position 203 to 470, the domain is characterized as Protein kinase.
+At position 480 to 545, the domain is characterized as AGC-kinase C-terminal.
+At position 133 to 245, the domain is characterized as Cadherin 2.
+At position 246 to 358, the domain is characterized as Cadherin 3.
+At position 473 to 669, the domain is characterized as Cadherin 5.
+At position 670 to 774, the domain is characterized as Cadherin 6.
+At position 775 to 878, the domain is characterized as Cadherin 7.
+At position 879 to 998, the domain is characterized as Cadherin 8.
+At position 999 to 1103, the domain is characterized as Cadherin 9.
+At position 1104 to 1211, the domain is characterized as Cadherin 10.
+At position 1212 to 1318, the domain is characterized as Cadherin 11.
+At position 1319 to 1431, the domain is characterized as Cadherin 12.
+At position 1432 to 1553, the domain is characterized as Cadherin 13.
+At position 1554 to 1677, the domain is characterized as Cadherin 14.
+At position 22 to 109, the domain is characterized as HPr.
+At position 91 to 318, the domain is characterized as Reverse transcriptase.
+At position 65 to 208, the domain is characterized as DAGKc.
+At position 21 to 124, the domain is characterized as MaoC-like.
+At position 14 to 268, the domain is characterized as uDENN.
+At position 289 to 429, the domain is characterized as cDENN.
+At position 431 to 565, the domain is characterized as dDENN.
+At position 1340 to 1415, the domain is characterized as Death.
+At position 33 to 289, the domain is characterized as Protein kinase.
+At position 156 to 277, the domain is characterized as LRAT.
+At position 159 to 548, the domain is characterized as GRAS.
+At position 402 to 604, the domain is characterized as N-acetyltransferase.
+At position 654 to 785, the domain is characterized as SEC7.
+At position 13 to 206, the domain is characterized as ABC transmembrane type-1.
+At position 178 to 306, the domain is characterized as NTR.
+At position 28 to 79, the domain is characterized as F-box.
+At position 298 to 568, the domain is characterized as Protein kinase.
+At position 52 to 224, the domain is characterized as CRAL-TRIO.
+At position 631 to 811, the domain is characterized as DH.
+At position 829 to 945, the domain is characterized as PH.
+At position 1055 to 1116, the domain is characterized as SH3.
+At position 79 to 389, the domain is characterized as IF rod.
+At position 38 to 278, the domain is characterized as ABC transporter.
+At position 5 to 82, the domain is characterized as Carrier.
+At position 16 to 261, the domain is characterized as Protein kinase.
+At position 1121 to 1238, the domain is characterized as SET.
+At position 1247 to 1263, the domain is characterized as Post-SET.
+At position 28 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 119 to 203, the domain is characterized as Ig-like C2-type 2.
+At position 224 to 305, the domain is characterized as Ig-like C2-type 3.
+At position 573 to 674, the domain is characterized as Fibronectin type-III 1.
+At position 720 to 815, the domain is characterized as Fibronectin type-III 2.
+At position 823 to 923, the domain is characterized as Fibronectin type-III 3.
+At position 40 to 98, the domain is characterized as TSP type-1 1.
+At position 102 to 177, the domain is characterized as TSP type-1 2.
+At position 179 to 233, the domain is characterized as TSP type-1 3.
+At position 336 to 392, the domain is characterized as TSP type-1 4.
+At position 399 to 482, the domain is characterized as TSP type-1 5.
+At position 484 to 543, the domain is characterized as TSP type-1 6.
+At position 601 to 661, the domain is characterized as TSP type-1 7.
+At position 662 to 735, the domain is characterized as TSP type-1 8.
+At position 737 to 796, the domain is characterized as TSP type-1 9.
+At position 797 to 869, the domain is characterized as TSP type-1 10.
+At position 871 to 924, the domain is characterized as TSP type-1 11.
+At position 925 to 998, the domain is characterized as TSP type-1 12.
+At position 1000 to 1125, the domain is characterized as TSP type-1 13.
+At position 1127 to 1181, the domain is characterized as TSP type-1 14.
+At position 1182 to 1245, the domain is characterized as TSP type-1 15.
+At position 1247 to 1302, the domain is characterized as TSP type-1 16.
+At position 1303 to 1368, the domain is characterized as TSP type-1 17.
+At position 1370 to 1431, the domain is characterized as TSP type-1 18.
+At position 5 to 149, the domain is characterized as N-acetyltransferase.
+At position 5 to 280, the domain is characterized as CN hydrolase.
+At position 17 to 104, the domain is characterized as HPr.
+At position 53 to 174, the domain is characterized as TBDR plug.
+At position 185 to 921, the domain is characterized as TBDR beta-barrel.
+At position 286 to 422, the domain is characterized as SIS 1.
+At position 445 to 580, the domain is characterized as SIS 2.
+At position 83 to 475, the domain is characterized as Peptidase A1.
+At position 33 to 429, the domain is characterized as Alpha-carbonic anhydrase.
+At position 4 to 60, the domain is characterized as F-box.
+At position 340 to 390, the domain is characterized as FBD.
+At position 243 to 645, the domain is characterized as PPM-type phosphatase.
+At position 7 to 296, the domain is characterized as RHD.
+At position 135 to 254, the domain is characterized as PPIase FKBP-type.
+At position 104 to 363, the domain is characterized as Protein kinase 1.
+At position 364 to 433, the domain is characterized as AGC-kinase C-terminal.
+At position 454 to 712, the domain is characterized as Protein kinase 2.
+At position 17 to 319, the domain is characterized as ABC transmembrane type-1.
+At position 349 to 564, the domain is characterized as ABC transporter.
+At position 622 to 699, the domain is characterized as Cytochrome c.
+At position 592 to 757, the domain is characterized as Helicase ATP-binding.
+At position 778 to 932, the domain is characterized as Helicase C-terminal.
+At position 19 to 229, the domain is characterized as tr-type G.
+At position 30 to 152, the domain is characterized as RNase III.
+At position 177 to 246, the domain is characterized as DRBM.
+At position 496 to 548, the domain is characterized as PSI.
+At position 573 to 631, the domain is characterized as Ig-like C2-type.
+At position 133 to 334, the domain is characterized as ATP-grasp.
+At position 169 to 265, the domain is characterized as PAZ.
+At position 507 to 671, the domain is characterized as Piwi.
+At position 217 to 332, the domain is characterized as Calponin-homology (CH).
+At position 1437 to 1571, the domain is characterized as CKK.
+At position 2 to 251, the domain is characterized as Glutamine amidotransferase type-2.
+At position 29 to 260, the domain is characterized as ABC transporter.
+At position 311 to 363, the domain is characterized as HAMP 1.
+At position 398 to 451, the domain is characterized as HAMP 2.
+At position 470 to 706, the domain is characterized as Methyl-accepting transducer.
+At position 257 to 458, the domain is characterized as NACHT.
+At position 977 to 1252, the domain is characterized as FIIND.
+At position 1278 to 1354, the domain is characterized as CARD.
+At position 23 to 135, the domain is characterized as sHSP.
+At position 164 to 265, the domain is characterized as PpiC 1.
+At position 275 to 374, the domain is characterized as PpiC 2.
+At position 41 to 349, the domain is characterized as AB hydrolase-1.
+At position 1 to 144, the domain is characterized as ABC transmembrane type-1.
+At position 146 to 187, the domain is characterized as JmjN.
+At position 361 to 527, the domain is characterized as JmjC.
+At position 974 to 1032, the domain is characterized as FYR N-terminal.
+At position 1034 to 1124, the domain is characterized as FYR C-terminal.
+At position 845 to 1107, the domain is characterized as PKS/mFAS DH.
+At position 2123 to 2200, the domain is characterized as Carrier.
+At position 159 to 245, the domain is characterized as Doublecortin 1.
+At position 315 to 398, the domain is characterized as Doublecortin 2.
+At position 479 to 737, the domain is characterized as Protein kinase.
+At position 300 to 388, the domain is characterized as B5.
+At position 612 to 705, the domain is characterized as FDX-ACB.
+At position 110 to 172, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 357 to 419, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 240 to 358, the domain is characterized as C2 1.
+At position 404 to 521, the domain is characterized as C2 2.
+At position 555 to 676, the domain is characterized as C2 3.
+At position 93 to 165, the domain is characterized as PRC barrel.
+At position 77 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 596 to 675, the domain is characterized as BRCT.
+At position 4 to 90, the domain is characterized as Core-binding (CB).
+At position 323 to 410, the domain is characterized as Fibronectin type-III 1.
+At position 411 to 504, the domain is characterized as Fibronectin type-III 2.
+At position 505 to 583, the domain is characterized as Fibronectin type-III 3.
+At position 585 to 665, the domain is characterized as Fibronectin type-III 4.
+At position 1974 to 2052, the domain is characterized as BRCT 1.
+At position 2073 to 2164, the domain is characterized as BRCT 2.
+At position 597 to 698, the domain is characterized as VRR-NUC.
+At position 28 to 132, the domain is characterized as Gnk2-homologous 1.
+At position 140 to 251, the domain is characterized as Gnk2-homologous 2.
+At position 1078 to 1151, the domain is characterized as BIG2.
+At position 399 to 645, the domain is characterized as Roc.
+At position 10 to 91, the domain is characterized as PB1.
+At position 840 to 965, the domain is characterized as DBINO.
+At position 1090 to 1262, the domain is characterized as Helicase ATP-binding.
+At position 1663 to 1818, the domain is characterized as Helicase C-terminal.
+At position 5 to 428, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 896 to 1181, the domain is characterized as PKS/mFAS DH.
+At position 2025 to 2100, the domain is characterized as Carrier.
+At position 90 to 246, the domain is characterized as Helicase ATP-binding.
+At position 323 to 524, the domain is characterized as Helicase C-terminal.
+At position 34 to 174, the domain is characterized as Peptidase C51.
+At position 28 to 494, the domain is characterized as Sema.
+At position 1 to 435, the domain is characterized as SMP-LTD.
+At position 18 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 118 to 204, the domain is characterized as Ig-like C2-type 2.
+At position 307 to 392, the domain is characterized as Ig-like C2-type 4.
+At position 427 to 521, the domain is characterized as Fibronectin type-III 1.
+At position 527 to 617, the domain is characterized as Fibronectin type-III 2.
+At position 622 to 716, the domain is characterized as Fibronectin type-III 3.
+At position 726 to 816, the domain is characterized as Fibronectin type-III 4.
+At position 841 to 937, the domain is characterized as Fibronectin type-III 5.
+At position 942 to 1039, the domain is characterized as Fibronectin type-III 6.
+At position 58 to 111, the domain is characterized as J.
+At position 1294 to 1647, the domain is characterized as HECT.
+At position 68 to 151, the domain is characterized as SH2.
+At position 445 to 587, the domain is characterized as VPS9.
+At position 613 to 695, the domain is characterized as Ras-associating.
+At position 438 to 485, the domain is characterized as SARAH.
+At position 268 to 362, the domain is characterized as Ig-like V-type.
+At position 48 to 149, the domain is characterized as Ig-like C2-type 1.
+At position 249 to 338, the domain is characterized as Ig-like C2-type 2.
+At position 339 to 429, the domain is characterized as Ig-like C2-type 3.
+At position 430 to 530, the domain is characterized as Ig-like C2-type 4.
+At position 531 to 630, the domain is characterized as Ig-like C2-type 5.
+At position 633 to 729, the domain is characterized as Fibronectin type-III 1.
+At position 731 to 826, the domain is characterized as Fibronectin type-III 2.
+At position 830 to 923, the domain is characterized as Ig-like C2-type 6.
+At position 926 to 1022, the domain is characterized as Fibronectin type-III 3.
+At position 1039 to 1132, the domain is characterized as Ig-like C2-type 7.
+At position 535 to 603, the domain is characterized as LRRCT.
+At position 26 to 111, the domain is characterized as Disintegrin.
+At position 194 to 274, the domain is characterized as SAND.
+At position 20 to 341, the domain is characterized as ABC transporter.
+At position 68 to 178, the domain is characterized as Thioredoxin.
+At position 243 to 305, the domain is characterized as t-SNARE coiled-coil homology.
+At position 32 to 258, the domain is characterized as Radical SAM core.
+At position 90 to 248, the domain is characterized as DAGKc.
+At position 12 to 157, the domain is characterized as SprT-like.
+At position 7 to 279, the domain is characterized as tr-type G.
+At position 210 to 401, the domain is characterized as Albumin 2.
+At position 8 to 327, the domain is characterized as DhaK.
+At position 356 to 548, the domain is characterized as DhaL.
+At position 56 to 339, the domain is characterized as Protein kinase.
+At position 429 to 553, the domain is characterized as Thioredoxin.
+At position 212 to 400, the domain is characterized as MIF4G.
+At position 502 to 633, the domain is characterized as MI.
+At position 42 to 295, the domain is characterized as SET.
+At position 1 to 29, the domain is characterized as LCN-type CS-alpha/beta.
+At position 71 to 162, the domain is characterized as DEP.
+At position 12 to 67, the domain is characterized as HTH lacI-type.
+At position 39 to 221, the domain is characterized as tr-type G.
+At position 151 to 381, the domain is characterized as Radical SAM core.
+At position 247 to 428, the domain is characterized as GATase cobBQ-type.
+At position 164 to 254, the domain is characterized as 5'-3' exonuclease.
+At position 1 to 70, the domain is characterized as SH2.
+At position 95 to 348, the domain is characterized as Protein kinase.
+At position 6 to 143, the domain is characterized as SprT-like.
+At position 2 to 50, the domain is characterized as Kazal-like.
+At position 41 to 90, the domain is characterized as F-box.
+At position 20 to 221, the domain is characterized as WLM.
+At position 248 to 566, the domain is characterized as Protein kinase.
+At position 11 to 46, the domain is characterized as EF-hand.
+At position 228 to 252, the domain is characterized as HhH.
+At position 83 to 217, the domain is characterized as PPC.
+At position 2 to 101, the domain is characterized as Phytocyanin.
+At position 125 to 479, the domain is characterized as PTS EIIC type-1.
+At position 2 to 441, the domain is characterized as F-BAR.
+At position 218 to 298, the domain is characterized as DEP.
+At position 475 to 704, the domain is characterized as Rho-GAP.
+At position 156 to 254, the domain is characterized as Fibronectin type-III.
+At position 49 to 106, the domain is characterized as SMP 1.
+At position 115 to 171, the domain is characterized as SMP 2.
+At position 290 to 539, the domain is characterized as Glutamine amidotransferase type-1.
+At position 101 to 229, the domain is characterized as Runt.
+At position 84 to 249, the domain is characterized as Bms1-type G.
+At position 39 to 116, the domain is characterized as GRAM.
+At position 181 to 556, the domain is characterized as Myotubularin phosphatase.
+At position 13 to 81, the domain is characterized as Sm.
+At position 12 to 487, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 514 to 808, the domain is characterized as UvrD-like helicase C-terminal.
+At position 4 to 128, the domain is characterized as RCK N-terminal.
+At position 8 to 204, the domain is characterized as DPCK.
+At position 499 to 665, the domain is characterized as Helicase ATP-binding.
+At position 690 to 842, the domain is characterized as Helicase C-terminal.
+At position 1098 to 1177, the domain is characterized as HRDC.
+At position 3 to 97, the domain is characterized as Stress-response A/B barrel.
+At position 127 to 326, the domain is characterized as Peptidase M12A.
+At position 349 to 361, the domain is characterized as EGF-like.
+At position 490 to 540, the domain is characterized as TSP type-1.
+At position 496 to 649, the domain is characterized as N-acetyltransferase.
+At position 738 to 808, the domain is characterized as Bromo.
+At position 180 to 280, the domain is characterized as BTB.
+At position 45 to 124, the domain is characterized as RRM 1.
+At position 11 to 121, the domain is characterized as C-type lectin.
+At position 257 to 689, the domain is characterized as Protein kinase.
+At position 468 to 518, the domain is characterized as DHHC.
+At position 1654 to 2196, the domain is characterized as FAT.
+At position 2306 to 2614, the domain is characterized as PI3K/PI4K catalytic.
+At position 2622 to 2654, the domain is characterized as FATC.
+At position 125 to 178, the domain is characterized as BRCT.
+At position 28 to 173, the domain is characterized as FZ.
+At position 9 to 231, the domain is characterized as ATP-grasp.
+At position 255 to 499, the domain is characterized as ABC transporter 2.
+At position 41 to 93, the domain is characterized as bHLH.
+At position 7 to 68, the domain is characterized as HTH asnC-type.
+At position 749 to 841, the domain is characterized as Ras-associating.
+At position 1552 to 1828, the domain is characterized as PPM-type phosphatase.
+At position 1892 to 2029, the domain is characterized as Guanylate cyclase.
+At position 141 to 290, the domain is characterized as FAS1.
+At position 173 to 343, the domain is characterized as EngA-type G 2.
+At position 344 to 428, the domain is characterized as KH-like.
+At position 104 to 274, the domain is characterized as CP-type G.
+At position 108 to 152, the domain is characterized as LEM.
+At position 74 to 261, the domain is characterized as Macro.
+At position 541 to 576, the domain is characterized as EF-hand 1.
+At position 585 to 618, the domain is characterized as EF-hand 2.
+At position 615 to 650, the domain is characterized as EF-hand 3.
+At position 680 to 714, the domain is characterized as EF-hand 4.
+At position 43 to 149, the domain is characterized as Calponin-homology (CH) 1.
+At position 166 to 269, the domain is characterized as Calponin-homology (CH) 2.
+At position 1 to 131, the domain is characterized as GOLD.
+At position 149 to 243, the domain is characterized as PH.
+At position 17 to 117, the domain is characterized as PilZ.
+At position 77 to 265, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 75, the domain is characterized as Cytochrome b5 heme-binding.
+At position 464 to 515, the domain is characterized as Rubredoxin-like.
+At position 380 to 440, the domain is characterized as PP1-binding.
+At position 160 to 371, the domain is characterized as TRUD.
+At position 31 to 74, the domain is characterized as sHSP.
+At position 322 to 490, the domain is characterized as MurNAc-LAA.
+At position 658 to 781, the domain is characterized as C2.
+At position 63 to 132, the domain is characterized as BTB.
+At position 169 to 269, the domain is characterized as BACK.
+At position 49 to 167, the domain is characterized as sHSP.
+At position 49 to 99, the domain is characterized as Myosin N-terminal SH3-like.
+At position 103 to 790, the domain is characterized as Myosin motor.
+At position 793 to 822, the domain is characterized as IQ.
+At position 149 to 413, the domain is characterized as Protein kinase.
+At position 27 to 223, the domain is characterized as Glutamine amidotransferase type-1.
+At position 81 to 175, the domain is characterized as Fe2OG dioxygenase.
+At position 26 to 85, the domain is characterized as TRAM.
+At position 1 to 147, the domain is characterized as uDENN.
+At position 169 to 309, the domain is characterized as cDENN.
+At position 311 to 366, the domain is characterized as dDENN.
+At position 161 to 348, the domain is characterized as Rho-GAP.
+At position 124 to 208, the domain is characterized as Ig-like C2-type 2.
+At position 229 to 310, the domain is characterized as Ig-like C2-type 3.
+At position 469 to 566, the domain is characterized as Fibronectin type-III 1.
+At position 603 to 698, the domain is characterized as Fibronectin type-III 2.
+At position 707 to 807, the domain is characterized as Fibronectin type-III 3.
+At position 9 to 122, the domain is characterized as Response regulatory.
+At position 182 to 264, the domain is characterized as 5'-3' exonuclease.
+At position 4 to 369, the domain is characterized as Trm1 methyltransferase.
+At position 29 to 214, the domain is characterized as AMMECR1.
+At position 901 to 966, the domain is characterized as HP.
+At position 236 to 557, the domain is characterized as PDEase.
+At position 119 to 389, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 341 to 575, the domain is characterized as ABC transporter.
+At position 91 to 213, the domain is characterized as B12-binding.
+At position 49 to 357, the domain is characterized as PPM-type phosphatase.
+At position 100 to 266, the domain is characterized as CRAL-TRIO.
+At position 164 to 338, the domain is characterized as OBG-type G.
+At position 362 to 440, the domain is characterized as OCT.
+At position 349 to 392, the domain is characterized as P-type 1.
+At position 396 to 439, the domain is characterized as P-type 2.
+At position 292 to 370, the domain is characterized as RRM 3.
+At position 221 to 373, the domain is characterized as TrmE-type G.
+At position 35 to 118, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 148 to 402, the domain is characterized as ABC transporter 1.
+At position 857 to 1101, the domain is characterized as ABC transporter 2.
+At position 450 to 641, the domain is characterized as Helicase C-terminal.
+At position 24 to 162, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 45 to 119, the domain is characterized as Ubiquitin-like.
+At position 138 to 216, the domain is characterized as BAG.
+At position 13 to 67, the domain is characterized as ClpX-type ZB.
+At position 17 to 182, the domain is characterized as Exonuclease.
+At position 263 to 429, the domain is characterized as JmjC.
+At position 726 to 784, the domain is characterized as FYR N-terminal.
+At position 786 to 876, the domain is characterized as FYR C-terminal.
+At position 632 to 812, the domain is characterized as DH.
+At position 830 to 946, the domain is characterized as PH.
+At position 129 to 225, the domain is characterized as PB1.
+At position 38 to 339, the domain is characterized as Protein kinase.
+At position 137 to 227, the domain is characterized as PpiC.
+At position 508 to 600, the domain is characterized as PB1.
+At position 159 to 211, the domain is characterized as bHLH.
+At position 228 to 413, the domain is characterized as FAD-binding PCMH-type.
+At position 54 to 133, the domain is characterized as Core-binding (CB).
+At position 168 to 331, the domain is characterized as Tyr recombinase.
+At position 225 to 277, the domain is characterized as HAMP.
+At position 286 to 356, the domain is characterized as PAS.
+At position 421 to 651, the domain is characterized as Histidine kinase.
+At position 23 to 303, the domain is characterized as Peptidase S8.
+At position 395 to 468, the domain is characterized as PWWP 1.
+At position 1049 to 1111, the domain is characterized as PWWP 2.
+At position 1182 to 1232, the domain is characterized as AWS.
+At position 1234 to 1351, the domain is characterized as SET.
+At position 1359 to 1375, the domain is characterized as Post-SET.
+At position 12 to 206, the domain is characterized as AMMECR1.
+At position 152 to 261, the domain is characterized as Cystatin fetuin-B-type 2.
+At position 144 to 328, the domain is characterized as FAD-binding PCMH-type.
+At position 3 to 117, the domain is characterized as Response regulatory 1.
+At position 121 to 228, the domain is characterized as Response regulatory 2.
+At position 72 to 145, the domain is characterized as RRM 1.
+At position 154 to 235, the domain is characterized as RRM 2.
+At position 321 to 398, the domain is characterized as RRM 3.
+At position 715 to 792, the domain is characterized as PABC.
+At position 274 to 446, the domain is characterized as Helicase ATP-binding.
+At position 497 to 689, the domain is characterized as Helicase C-terminal.
+At position 676 to 910, the domain is characterized as NR LBD.
+At position 164 to 231, the domain is characterized as SH3 1.
+At position 294 to 387, the domain is characterized as Fibronectin type-III 1.
+At position 390 to 471, the domain is characterized as Fibronectin type-III 2.
+At position 486 to 587, the domain is characterized as Fibronectin type-III 3.
+At position 95 to 387, the domain is characterized as ABC transmembrane type-1.
+At position 475 to 730, the domain is characterized as ABC transporter.
+At position 1 to 53, the domain is characterized as Ig-like C2-type 1.
+At position 54 to 142, the domain is characterized as Ig-like C2-type 2.
+At position 144 to 241, the domain is characterized as Ig-like C2-type 3.
+At position 244 to 343, the domain is characterized as Fibronectin type-III 1.
+At position 344 to 459, the domain is characterized as Fibronectin type-III 2.
+At position 459 to 553, the domain is characterized as Ig-like C2-type 4.
+At position 556 to 621, the domain is characterized as Fibronectin type-III 3.
+At position 518 to 691, the domain is characterized as N-acetyltransferase.
+At position 24 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 148 to 197, the domain is characterized as bHLH.
+At position 26 to 137, the domain is characterized as CFEM.
+At position 63 to 200, the domain is characterized as MPN.
+At position 48 to 138, the domain is characterized as G.
+At position 906 to 985, the domain is characterized as RRM.
+At position 4 to 150, the domain is characterized as Clp R.
+At position 2 to 365, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 382 to 775, the domain is characterized as PIPK.
+At position 39 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 90 to 286, the domain is characterized as Peptidase M12A.
+At position 288 to 400, the domain is characterized as CUB 1.
+At position 402 to 513, the domain is characterized as CUB 2.
+At position 20 to 154, the domain is characterized as MPN.
+At position 167 to 364, the domain is characterized as ABC transmembrane type-1.
+At position 2 to 62, the domain is characterized as MADS-box.
+At position 29 to 87, the domain is characterized as TRAM.
+At position 31 to 220, the domain is characterized as GH16.
+At position 18 to 106, the domain is characterized as PDZ.
+At position 125 to 345, the domain is characterized as Radical SAM core.
+At position 332 to 492, the domain is characterized as UBC core.
+At position 40 to 624, the domain is characterized as Peptidase M2 1.
+At position 643 to 1222, the domain is characterized as Peptidase M2 2.
+At position 105 to 187, the domain is characterized as Toprim.
+At position 32 to 131, the domain is characterized as SRCR.
+At position 164 to 231, the domain is characterized as BTB.
+At position 270 to 372, the domain is characterized as BACK.
+At position 5 to 236, the domain is characterized as Radical SAM core.
+At position 3 to 106, the domain is characterized as HTH La-type RNA-binding.
+At position 115 to 192, the domain is characterized as RRM.
+At position 269 to 399, the domain is characterized as xRRM.
+At position 664 to 985, the domain is characterized as PDEase.
+At position 22 to 168, the domain is characterized as RNase III.
+At position 24 to 348, the domain is characterized as Asparaginase/glutaminase.
+At position 57 to 194, the domain is characterized as Nudix hydrolase.
+At position 116 to 237, the domain is characterized as MI 1.
+At position 280 to 401, the domain is characterized as MI 2.
+At position 414 to 535, the domain is characterized as MI 3.
+At position 577 to 697, the domain is characterized as MI 4.
+At position 35 to 155, the domain is characterized as sHSP.
+At position 91 to 257, the domain is characterized as Helicase ATP-binding.
+At position 262 to 456, the domain is characterized as Helicase C-terminal.
+At position 88 to 401, the domain is characterized as PPM-type phosphatase.
+At position 16 to 70, the domain is characterized as HTH cro/C1-type.
+At position 120 to 207, the domain is characterized as IPT/TIG 1.
+At position 293 to 380, the domain is characterized as IPT/TIG 2.
+At position 74 to 191, the domain is characterized as Plastocyanin-like 1.
+At position 197 to 353, the domain is characterized as Plastocyanin-like 2.
+At position 413 to 547, the domain is characterized as Plastocyanin-like 3.
+At position 19 to 83, the domain is characterized as S4 RNA-binding.
+At position 224 to 311, the domain is characterized as PDZ 1.
+At position 319 to 406, the domain is characterized as PDZ 2.
+At position 715 to 890, the domain is characterized as Guanylate kinase-like.
+At position 4 to 221, the domain is characterized as Radical SAM core.
+At position 61 to 135, the domain is characterized as S1 motif.
+At position 141 to 200, the domain is characterized as KH.
+At position 102 to 223, the domain is characterized as MsrB.
+At position 21 to 66, the domain is characterized as Gla.
+At position 159 to 243, the domain is characterized as Ig-like C2-type.
+At position 399 to 672, the domain is characterized as Protein kinase.
+At position 673 to 745, the domain is characterized as AGC-kinase C-terminal.
+At position 968 to 1058, the domain is characterized as PDZ.
+At position 31 to 194, the domain is characterized as MAM.
+At position 196 to 281, the domain is characterized as Ig-like C2-type.
+At position 294 to 389, the domain is characterized as Fibronectin type-III 1.
+At position 392 to 488, the domain is characterized as Fibronectin type-III 2.
+At position 491 to 595, the domain is characterized as Fibronectin type-III 3.
+At position 597 to 680, the domain is characterized as Fibronectin type-III 4.
+At position 887 to 1141, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1173 to 1435, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 16 to 95, the domain is characterized as S4 RNA-binding.
+At position 603 to 692, the domain is characterized as BRCT.
+At position 201 to 353, the domain is characterized as GST C-terminal.
+At position 132 to 259, the domain is characterized as Thioredoxin 1.
+At position 268 to 382, the domain is characterized as Thioredoxin 2.
+At position 376 to 504, the domain is characterized as Thioredoxin 3.
+At position 14 to 349, the domain is characterized as Kinesin motor.
+At position 583 to 662, the domain is characterized as BRCT.
+At position 556 to 854, the domain is characterized as Protein kinase.
+At position 145 to 272, the domain is characterized as Fatty acid hydroxylase.
+At position 137 to 449, the domain is characterized as IF rod.
+At position 707 to 782, the domain is characterized as Ubiquitin-like.
+At position 342 to 511, the domain is characterized as tr-type G.
+At position 21 to 124, the domain is characterized as Inhibitor I9.
+At position 120 to 671, the domain is characterized as Peptidase S8.
+At position 397 to 501, the domain is characterized as PA.
+At position 31 to 275, the domain is characterized as ABC transporter.
+At position 1 to 312, the domain is characterized as SMP-LTD.
+At position 108 to 155, the domain is characterized as LysM 1.
+At position 172 to 216, the domain is characterized as LysM 2.
+At position 261 to 381, the domain is characterized as C2 2.
+At position 421 to 546, the domain is characterized as C2 3.
+At position 587 to 709, the domain is characterized as C2 4.
+At position 290 to 367, the domain is characterized as TFIIS N-terminal.
+At position 14 to 85, the domain is characterized as Sm.
+At position 14 to 100, the domain is characterized as Core-binding (CB).
+At position 121 to 303, the domain is characterized as Tyr recombinase.
+At position 53 to 426, the domain is characterized as GH18.
+At position 478 to 534, the domain is characterized as Chitin-binding type-2 1.
+At position 563 to 617, the domain is characterized as Chitin-binding type-2 2.
+At position 29 to 132, the domain is characterized as Cadherin 1.
+At position 587 to 689, the domain is characterized as Cadherin 6.
+At position 52 to 87, the domain is characterized as EGF-like 1.
+At position 89 to 128, the domain is characterized as EGF-like 2; calcium-binding.
+At position 132 to 168, the domain is characterized as EGF-like 3.
+At position 169 to 213, the domain is characterized as EGF-like 4; calcium-binding.
+At position 214 to 254, the domain is characterized as EGF-like 5; calcium-binding.
+At position 420 to 563, the domain is characterized as MAM.
+At position 10 to 222, the domain is characterized as Radical SAM core.
+At position 25 to 154, the domain is characterized as EamA 1.
+At position 230 to 448, the domain is characterized as Histidine kinase.
+At position 192 to 456, the domain is characterized as Protein kinase.
+At position 100 to 357, the domain is characterized as Protein kinase.
+At position 358 to 433, the domain is characterized as AGC-kinase C-terminal.
+At position 117 to 130, the domain is characterized as CRIB.
+At position 162 to 342, the domain is characterized as Rho-GAP.
+At position 29 to 197, the domain is characterized as FAD-binding PCMH-type.
+At position 47 to 149, the domain is characterized as HD.
+At position 213 to 271, the domain is characterized as Collagen-like.
+At position 10 to 128, the domain is characterized as VOC.
+At position 80 to 253, the domain is characterized as Helicase ATP-binding.
+At position 277 to 426, the domain is characterized as Helicase C-terminal.
+At position 68 to 256, the domain is characterized as Reticulon.
+At position 104 to 220, the domain is characterized as DOMON.
+At position 440 to 953, the domain is characterized as KAP NTPase.
+At position 3 to 169, the domain is characterized as PfpI endopeptidase.
+At position 125 to 376, the domain is characterized as Tyrosine-protein phosphatase.
+At position 125 to 179, the domain is characterized as AWS.
+At position 181 to 298, the domain is characterized as SET.
+At position 305 to 321, the domain is characterized as Post-SET.
+At position 196 to 299, the domain is characterized as Pre-SET.
+At position 302 to 435, the domain is characterized as SET.
+At position 446 to 462, the domain is characterized as Post-SET.
+At position 99 to 220, the domain is characterized as MRH.
+At position 69 to 198, the domain is characterized as FAD-binding FR-type.
+At position 24 to 110, the domain is characterized as REM-1.
+At position 20 to 219, the domain is characterized as Cytochrome b561.
+At position 131 to 418, the domain is characterized as Protein kinase.
+At position 10 to 127, the domain is characterized as MTTase N-terminal.
+At position 150 to 381, the domain is characterized as Radical SAM core.
+At position 109 to 427, the domain is characterized as Peptidase A1.
+At position 73 to 232, the domain is characterized as Thioredoxin.
+At position 3 to 178, the domain is characterized as Prephenate dehydratase.
+At position 193 to 271, the domain is characterized as ACT.
+At position 1 to 38, the domain is characterized as Link 1.
+At position 44 to 140, the domain is characterized as Link 2.
+At position 718 to 754, the domain is characterized as EGF-like 1.
+At position 756 to 792, the domain is characterized as EGF-like 2; calcium-binding.
+At position 805 to 862, the domain is characterized as C-type lectin.
+At position 19 to 174, the domain is characterized as N-acetyltransferase.
+At position 379 to 436, the domain is characterized as PP1-binding.
+At position 43 to 115, the domain is characterized as KH type-2.
+At position 40 to 231, the domain is characterized as KIND.
+At position 305 to 323, the domain is characterized as WH2 1.
+At position 369 to 386, the domain is characterized as WH2 2.
+At position 35 to 253, the domain is characterized as Radical SAM core.
+At position 304 to 551, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1589 to 1736, the domain is characterized as NTR.
+At position 78 to 149, the domain is characterized as HMA.
+At position 172 to 359, the domain is characterized as Helicase ATP-binding.
+At position 396 to 553, the domain is characterized as Helicase C-terminal.
+At position 82 to 170, the domain is characterized as Fibronectin type-III 1.
+At position 171 to 259, the domain is characterized as Fibronectin type-III 2.
+At position 260 to 343, the domain is characterized as Fibronectin type-III 3.
+At position 346 to 437, the domain is characterized as Fibronectin type-III 4.
+At position 438 to 523, the domain is characterized as Fibronectin type-III 5.
+At position 524 to 614, the domain is characterized as Fibronectin type-III 6.
+At position 615 to 703, the domain is characterized as Fibronectin type-III 7.
+At position 704 to 793, the domain is characterized as Fibronectin type-III 8.
+At position 794 to 888, the domain is characterized as Fibronectin type-III 9.
+At position 887 to 979, the domain is characterized as Fibronectin type-III 10.
+At position 1110 to 1367, the domain is characterized as Tyrosine-protein phosphatase.
+At position 16 to 307, the domain is characterized as Protein kinase.
+At position 413 to 424, the domain is characterized as EGF-like.
+At position 22 to 212, the domain is characterized as GH16.
+At position 16 to 87, the domain is characterized as S1 motif.
+At position 143 to 466, the domain is characterized as ABC transmembrane type-1 1.
+At position 525 to 751, the domain is characterized as ABC transporter 1.
+At position 816 to 1093, the domain is characterized as ABC transmembrane type-1 2.
+At position 1131 to 1380, the domain is characterized as ABC transporter 2.
+At position 163 to 399, the domain is characterized as Radical SAM core.
+At position 402 to 470, the domain is characterized as TRAM.
+At position 40 to 118, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 118 to 157, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 259 to 315, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 151 to 379, the domain is characterized as START.
+At position 343 to 381, the domain is characterized as EGF-like 1.
+At position 386 to 564, the domain is characterized as Laminin G-like 1.
+At position 565 to 602, the domain is characterized as EGF-like 2.
+At position 609 to 788, the domain is characterized as Laminin G-like 2.
+At position 784 to 820, the domain is characterized as EGF-like 3.
+At position 835 to 1014, the domain is characterized as Laminin G-like 3.
+At position 63 to 387, the domain is characterized as Kinesin motor.
+At position 119 to 237, the domain is characterized as EamA 1.
+At position 268 to 388, the domain is characterized as EamA 2.
+At position 615 to 696, the domain is characterized as BRCT.
+At position 262 to 453, the domain is characterized as Helicase ATP-binding.
+At position 465 to 626, the domain is characterized as Helicase C-terminal.
+At position 143 to 466, the domain is characterized as NACHT.
+At position 245 to 362, the domain is characterized as Sox C-terminal.
+At position 132 to 290, the domain is characterized as FCP1 homology.
+At position 4 to 118, the domain is characterized as PINc.
+At position 502 to 619, the domain is characterized as SMC hinge.
+At position 80 to 150, the domain is characterized as BTB.
+At position 678 to 871, the domain is characterized as ATP-grasp 2.
+At position 952 to 1085, the domain is characterized as MGS-like.
+At position 224 to 393, the domain is characterized as tr-type G.
+At position 117 to 279, the domain is characterized as Integrase catalytic.
+At position 217 to 277, the domain is characterized as KH.
+At position 205 to 270, the domain is characterized as KH 1.
+At position 286 to 353, the domain is characterized as KH 2.
+At position 418 to 483, the domain is characterized as KH 3.
+At position 500 to 566, the domain is characterized as KH 4.
+At position 244 to 448, the domain is characterized as DH.
+At position 496 to 606, the domain is characterized as PH.
+At position 656 to 824, the domain is characterized as N-terminal Ras-GEF.
+At position 897 to 1164, the domain is characterized as Ras-GEF.
+At position 35 to 362, the domain is characterized as Protein kinase.
+At position 5 to 194, the domain is characterized as ABC transporter.
+At position 403 to 480, the domain is characterized as B5.
+At position 695 to 791, the domain is characterized as FDX-ACB.
+At position 99 to 298, the domain is characterized as ATP-grasp.
+At position 9 to 158, the domain is characterized as Ferritin-like diiron.
+At position 2 to 322, the domain is characterized as Asparaginase/glutaminase.
+At position 415 to 506, the domain is characterized as ACB.
+At position 3 to 87, the domain is characterized as Carrier.
+At position 277 to 315, the domain is characterized as LRRCT.
+At position 141 to 339, the domain is characterized as Rho-GAP.
+At position 8 to 91, the domain is characterized as DIX.
+At position 252 to 324, the domain is characterized as PDZ.
+At position 404 to 478, the domain is characterized as DEP.
+At position 226 to 406, the domain is characterized as Helicase ATP-binding.
+At position 438 to 589, the domain is characterized as Helicase C-terminal.
+At position 291 to 477, the domain is characterized as PCI.
+At position 141 to 213, the domain is characterized as Bromo.
+At position 270 to 351, the domain is characterized as NET.
+At position 22 to 297, the domain is characterized as Protein kinase.
+At position 343 to 613, the domain is characterized as Protein kinase.
+At position 148 to 414, the domain is characterized as Radical SAM core.
+At position 101 to 287, the domain is characterized as DCUN1.
+At position 103 to 387, the domain is characterized as Protein kinase.
+At position 2 to 89, the domain is characterized as RRM 1.
+At position 301 to 379, the domain is characterized as RRM 2.
+At position 485 to 557, the domain is characterized as RRM 3.
+At position 605 to 688, the domain is characterized as RRM 4.
+At position 703 to 780, the domain is characterized as RRM 5.
+At position 227 to 317, the domain is characterized as RRM.
+At position 129 to 167, the domain is characterized as F-box.
+At position 116 to 447, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 147, the domain is characterized as RPW8.
+At position 180 to 242, the domain is characterized as NB-ARC 1.
+At position 312 to 437, the domain is characterized as NB-ARC 2.
+At position 20 to 42, the domain is characterized as EF-hand 1.
+At position 7 to 225, the domain is characterized as MurNAc-LAA.
+At position 53 to 135, the domain is characterized as SCAN box.
+At position 221 to 317, the domain is characterized as KRAB.
+At position 177 to 445, the domain is characterized as MHD.
+At position 263 to 492, the domain is characterized as Methyl-accepting transducer.
+At position 37 to 105, the domain is characterized as Chitin-binding type R&R.
+At position 82 to 318, the domain is characterized as Bin3-type SAM.
+At position 41 to 232, the domain is characterized as RNase H type-2.
+At position 141 to 214, the domain is characterized as PRC barrel.
+At position 25 to 53, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 54 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 82 to 111, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 123 to 152, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 152 to 181, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 191 to 219, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 220 to 249, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 259 to 291, the domain is characterized as 4Fe-4S ferredoxin-type 9.
+At position 300 to 331, the domain is characterized as 4Fe-4S ferredoxin-type 10.
+At position 339 to 368, the domain is characterized as 4Fe-4S ferredoxin-type 11.
+At position 158 to 366, the domain is characterized as CP-type G.
+At position 217 to 321, the domain is characterized as PB1.
+At position 35 to 67, the domain is characterized as LisH.
+At position 25 to 102, the domain is characterized as RRM.
+At position 195 to 232, the domain is characterized as GRAM 1.
+At position 246 to 343, the domain is characterized as PH.
+At position 590 to 656, the domain is characterized as GRAM 2.
+At position 96 to 267, the domain is characterized as Helicase ATP-binding.
+At position 294 to 438, the domain is characterized as Helicase C-terminal.
+At position 180 to 246, the domain is characterized as HMA.
+At position 115 to 182, the domain is characterized as BTB 1.
+At position 272 to 346, the domain is characterized as BTB 2.
+At position 7 to 321, the domain is characterized as Cbl-PTB.
+At position 1 to 89, the domain is characterized as HTH arsR-type.
+At position 158 to 378, the domain is characterized as TRUD.
+At position 187 to 269, the domain is characterized as PDZ.
+At position 55 to 116, the domain is characterized as HTH iclR-type.
+At position 131 to 300, the domain is characterized as IclR-ED.
+At position 228 to 256, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 730 to 823, the domain is characterized as Fibronectin type-III 2.
+At position 828 to 930, the domain is characterized as Fibronectin type-III 3.
+At position 934 to 1030, the domain is characterized as Fibronectin type-III 4.
+At position 1114 to 1206, the domain is characterized as Fibronectin type-III 5.
+At position 151 to 481, the domain is characterized as Kinesin motor.
+At position 2 to 131, the domain is characterized as Nudix hydrolase.
+At position 401 to 646, the domain is characterized as Protein kinase.
+At position 255 to 338, the domain is characterized as IPT/TIG.
+At position 440 to 600, the domain is characterized as OTU.
+At position 212 to 271, the domain is characterized as SH3.
+At position 74 to 253, the domain is characterized as Helicase ATP-binding.
+At position 264 to 489, the domain is characterized as Helicase C-terminal.
+At position 6 to 43, the domain is characterized as EF-hand 1.
+At position 36 to 357, the domain is characterized as Kinesin motor.
+At position 112 to 234, the domain is characterized as MPN.
+At position 38 to 163, the domain is characterized as C-type lectin.
+At position 83 to 231, the domain is characterized as FAS1.
+At position 504 to 644, the domain is characterized as Flavodoxin-like.
+At position 676 to 905, the domain is characterized as FAD-binding FR-type.
+At position 230 to 293, the domain is characterized as KH 1.
+At position 302 to 368, the domain is characterized as KH 2.
+At position 494 to 585, the domain is characterized as ARID.
+At position 686 to 786, the domain is characterized as sHSP.
+At position 276 to 375, the domain is characterized as PpiC 2.
+At position 376 to 492, the domain is characterized as PI-PLC Y-box.
+At position 492 to 615, the domain is characterized as C2.
+At position 158 to 226, the domain is characterized as DRBM 2.
+At position 292 to 360, the domain is characterized as DRBM 3.
+At position 28 to 87, the domain is characterized as 4Fe-4S.
+At position 28 to 119, the domain is characterized as Fibronectin type-III 1.
+At position 179 to 354, the domain is characterized as VWFA.
+At position 379 to 468, the domain is characterized as Fibronectin type-III 2.
+At position 469 to 559, the domain is characterized as Fibronectin type-III 3.
+At position 560 to 647, the domain is characterized as Fibronectin type-III 4.
+At position 649 to 738, the domain is characterized as Fibronectin type-III 5.
+At position 743 to 833, the domain is characterized as Fibronectin type-III 6.
+At position 842 to 1037, the domain is characterized as Laminin G-like.
+At position 1071 to 1127, the domain is characterized as Collagen-like 1.
+At position 1133 to 1190, the domain is characterized as Collagen-like 2.
+At position 357 to 646, the domain is characterized as Clu.
+At position 35 to 72, the domain is characterized as EGF-like 1.
+At position 73 to 112, the domain is characterized as EGF-like 2; calcium-binding.
+At position 125 to 162, the domain is characterized as EGF-like 3; calcium-binding.
+At position 177 to 236, the domain is characterized as Sushi 1.
+At position 237 to 296, the domain is characterized as Sushi 2.
+At position 10 to 66, the domain is characterized as F-box.
+At position 31 to 62, the domain is characterized as bZIP.
+At position 273 to 339, the domain is characterized as Myb-like 1.
+At position 340 to 391, the domain is characterized as HTH myb-type.
+At position 392 to 486, the domain is characterized as Myb-like 2.
+At position 493 to 549, the domain is characterized as Myb-like 3.
+At position 308 to 568, the domain is characterized as Protein kinase.
+At position 25 to 215, the domain is characterized as RNase H type-2.
+At position 162 to 334, the domain is characterized as OBG-type G.
+At position 178 to 280, the domain is characterized as AB hydrolase-1.
+At position 18 to 166, the domain is characterized as Nudix hydrolase.
+At position 12 to 242, the domain is characterized as ABC transporter.
+At position 480 to 579, the domain is characterized as Fibronectin type-III.
+At position 78 to 385, the domain is characterized as GH18.
+At position 2 to 92, the domain is characterized as BRCT 1.
+At position 96 to 185, the domain is characterized as BRCT 2.
+At position 298 to 384, the domain is characterized as BRCT 3.
+At position 392 to 486, the domain is characterized as BRCT 4.
+At position 93 to 178, the domain is characterized as PB1.
+At position 21 to 151, the domain is characterized as Rhodanese.
+At position 175 to 318, the domain is characterized as Tyrosine-protein phosphatase.
+At position 131 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 332, the domain is characterized as Fibronectin type-III 1.
+At position 334 to 435, the domain is characterized as Fibronectin type-III 2.
+At position 439 to 547, the domain is characterized as Fibronectin type-III 3.
+At position 893 to 1156, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1187 to 1450, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 1 to 208, the domain is characterized as Deacetylase sirtuin-type.
+At position 28 to 258, the domain is characterized as ATP-grasp.
+At position 230 to 289, the domain is characterized as SH3.
+At position 4 to 143, the domain is characterized as Ricin B-type lectin.
+At position 135 to 186, the domain is characterized as BACK.
+At position 36 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 87 to 245, the domain is characterized as DAGKc.
+At position 223 to 342, the domain is characterized as GAF.
+At position 343 to 554, the domain is characterized as Histidine kinase.
+At position 25 to 89, the domain is characterized as HMA.
+At position 24 to 102, the domain is characterized as RRM 1.
+At position 221 to 299, the domain is characterized as RRM 2.
+At position 417 to 489, the domain is characterized as RRM 3.
+At position 535 to 618, the domain is characterized as RRM 4.
+At position 640 to 723, the domain is characterized as RRM 5.
+At position 1 to 305, the domain is characterized as Deacetylase sirtuin-type.
+At position 580 to 656, the domain is characterized as BRCT.
+At position 128 to 236, the domain is characterized as RRM 1.
+At position 227 to 314, the domain is characterized as RRM 2.
+At position 29 to 86, the domain is characterized as Kazal-like 1.
+At position 106 to 162, the domain is characterized as Kazal-like 2.
+At position 149 to 468, the domain is characterized as Peptidase S8.
+At position 476 to 616, the domain is characterized as P/Homo B.
+At position 899 to 937, the domain is characterized as PLAC.
+At position 62 to 158, the domain is characterized as Rieske.
+At position 93 to 106, the domain is characterized as CRIB.
+At position 138 to 319, the domain is characterized as Rho-GAP.
+At position 276 to 519, the domain is characterized as ABC transporter 1.
+At position 594 to 809, the domain is characterized as ABC transporter 2.
+At position 1398 to 1456, the domain is characterized as Prospero-type homeo.
+At position 1457 to 1556, the domain is characterized as Prospero.
+At position 43 to 294, the domain is characterized as ABC transporter.
+At position 23 to 167, the domain is characterized as VOC.
+At position 187 to 219, the domain is characterized as EGF-like 1.
+At position 399 to 431, the domain is characterized as EGF-like 2.
+At position 557 to 609, the domain is characterized as TB 1.
+At position 626 to 663, the domain is characterized as EGF-like 3; calcium-binding.
+At position 677 to 729, the domain is characterized as TB 2.
+At position 873 to 910, the domain is characterized as EGF-like 4; calcium-binding.
+At position 915 to 956, the domain is characterized as EGF-like 5; calcium-binding.
+At position 957 to 997, the domain is characterized as EGF-like 6; calcium-binding.
+At position 998 to 1037, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1038 to 1078, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1079 to 1119, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1120 to 1160, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1161 to 1201, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1202 to 1243, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1244 to 1281, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1286 to 1328, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1347 to 1401, the domain is characterized as TB 3.
+At position 1424 to 1466, the domain is characterized as EGF-like 15; calcium-binding.
+At position 1467 to 1503, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1524 to 1577, the domain is characterized as TB 4.
+At position 1621 to 1657, the domain is characterized as EGF-like 17.
+At position 1662 to 1706, the domain is characterized as EGF-like 18; calcium-binding.
+At position 95 to 252, the domain is characterized as Upf1 CH-rich.
+At position 47 to 100, the domain is characterized as bHLH.
+At position 173 to 250, the domain is characterized as Toprim.
+At position 74 to 143, the domain is characterized as HTH iclR-type.
+At position 149 to 300, the domain is characterized as DDE Tnp4.
+At position 70 to 167, the domain is characterized as Inhibitor I9.
+At position 177 to 478, the domain is characterized as Peptidase S8.
+At position 43 to 170, the domain is characterized as SCP.
+At position 206 to 239, the domain is characterized as ShKT.
+At position 194 to 367, the domain is characterized as EngA-type G 2.
+At position 368 to 452, the domain is characterized as KH-like.
+At position 329 to 491, the domain is characterized as Helicase ATP-binding.
+At position 546 to 704, the domain is characterized as Helicase C-terminal.
+At position 23 to 196, the domain is characterized as EngB-type G.
+At position 11 to 101, the domain is characterized as EH 1.
+At position 141 to 230, the domain is characterized as EH 2.
+At position 194 to 229, the domain is characterized as EF-hand 2.
+At position 434 to 568, the domain is characterized as DAGKc.
+At position 198 to 411, the domain is characterized as CHASE.
+At position 479 to 760, the domain is characterized as Histidine kinase.
+At position 786 to 920, the domain is characterized as Response regulatory 1.
+At position 946 to 1071, the domain is characterized as Response regulatory 2.
+At position 40 to 363, the domain is characterized as G-alpha.
+At position 653 to 720, the domain is characterized as SH3 1.
+At position 791 to 882, the domain is characterized as Fibronectin type-III 1.
+At position 884 to 976, the domain is characterized as Fibronectin type-III 2.
+At position 981 to 1081, the domain is characterized as Fibronectin type-III 3.
+At position 1625 to 1693, the domain is characterized as SH3 2.
+At position 1764 to 1831, the domain is characterized as SH3 3.
+At position 10 to 244, the domain is characterized as PABS.
+At position 75 to 181, the domain is characterized as TBDR plug.
+At position 186 to 720, the domain is characterized as TBDR beta-barrel.
+At position 19 to 215, the domain is characterized as Peptidase M12B.
+At position 427 to 610, the domain is characterized as Flavodoxin-like.
+At position 660 to 903, the domain is characterized as FAD-binding FR-type.
+At position 79 to 143, the domain is characterized as SH3b.
+At position 199 to 242, the domain is characterized as LysM 2.
+At position 349 to 467, the domain is characterized as NlpC/P60.
+At position 20 to 198, the domain is characterized as Thioredoxin.
+At position 202 to 437, the domain is characterized as PABS.
+At position 36 to 154, the domain is characterized as MTTase N-terminal.
+At position 177 to 407, the domain is characterized as Radical SAM core.
+At position 410 to 471, the domain is characterized as TRAM.
+At position 1 to 108, the domain is characterized as HPt.
+At position 480 to 725, the domain is characterized as Histidine kinase.
+At position 727 to 864, the domain is characterized as CheW-like.
+At position 3 to 484, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 522 to 867, the domain is characterized as UvrD-like helicase C-terminal.
+At position 13 to 141, the domain is characterized as VHS.
+At position 263 to 282, the domain is characterized as UIM.
+At position 165 to 244, the domain is characterized as PPIase FKBP-type.
+At position 218 to 391, the domain is characterized as PCI.
+At position 141 to 334, the domain is characterized as Peptidase M12B.
+At position 346 to 434, the domain is characterized as Disintegrin.
+At position 581 to 615, the domain is characterized as EGF-like; calcium-binding.
+At position 172 to 288, the domain is characterized as TFIIS central.
+At position 132 to 420, the domain is characterized as Tyr recombinase Flp-type.
+At position 748 to 804, the domain is characterized as Sushi.
+At position 804 to 847, the domain is characterized as EGF-like; calcium-binding.
+At position 58 to 127, the domain is characterized as S1 motif.
+At position 135 to 193, the domain is characterized as KH.
+At position 691 to 726, the domain is characterized as Anaphylatoxin-like.
+At position 1516 to 1659, the domain is characterized as NTR.
+At position 1 to 113, the domain is characterized as Tyrosine-protein phosphatase.
+At position 417 to 489, the domain is characterized as ACT 1.
+At position 498 to 575, the domain is characterized as ACT 2.
+At position 8 to 134, the domain is characterized as RNase III.
+At position 622 to 695, the domain is characterized as SH3.
+At position 213 to 379, the domain is characterized as Integrase catalytic.
+At position 191 to 385, the domain is characterized as Rho-GAP.
+At position 148 to 369, the domain is characterized as Radical SAM core.
+At position 104 to 248, the domain is characterized as PPC.
+At position 368 to 537, the domain is characterized as Helicase C-terminal.
+At position 920 to 1060, the domain is characterized as RNase III 1.
+At position 1099 to 1282, the domain is characterized as RNase III 2.
+At position 372 to 805, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1340 to 1658, the domain is characterized as PKS/mFAS DH.
+At position 1733 to 1812, the domain is characterized as Carrier 1.
+At position 1877 to 1953, the domain is characterized as Carrier 2.
+At position 2020 to 2099, the domain is characterized as Carrier 3.
+At position 353 to 590, the domain is characterized as ABC transporter.
+At position 100 to 179, the domain is characterized as RRM.
+At position 365 to 526, the domain is characterized as NTF2.
+At position 576 to 628, the domain is characterized as TAP-C.
+At position 642 to 719, the domain is characterized as Carrier.
+At position 37 to 167, the domain is characterized as Ig-like V-type.
+At position 168 to 252, the domain is characterized as Ig-like C2-type 1.
+At position 265 to 343, the domain is characterized as Ig-like C2-type 2.
+At position 348 to 419, the domain is characterized as Ig-like C2-type 3.
+At position 119 to 261, the domain is characterized as PA14.
+At position 1 to 564, the domain is characterized as Peptidase M13.
+At position 573 to 784, the domain is characterized as ATP-grasp.
+At position 295 to 345, the domain is characterized as FBD.
+At position 40 to 172, the domain is characterized as EamA 1.
+At position 219 to 338, the domain is characterized as EamA 2.
+At position 25 to 257, the domain is characterized as Phosphagen kinase C-terminal.
+At position 23 to 116, the domain is characterized as Ig-like V-type.
+At position 124 to 221, the domain is characterized as Ig-like C2-type 1.
+At position 227 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 270 to 289, the domain is characterized as UIM 1.
+At position 317 to 336, the domain is characterized as UIM 2.
+At position 3 to 90, the domain is characterized as GST N-terminal.
+At position 96 to 234, the domain is characterized as GST C-terminal.
+At position 65 to 385, the domain is characterized as Peptidase A1.
+At position 68 to 137, the domain is characterized as Chromo 1.
+At position 271 to 332, the domain is characterized as Chromo 2.
+At position 321 to 379, the domain is characterized as Chromo 3.
+At position 182 to 258, the domain is characterized as U-box.
+At position 504 to 652, the domain is characterized as CBM3.
+At position 678 to 770, the domain is characterized as Fibronectin type-III.
+At position 771 to 880, the domain is characterized as CBM2.
+At position 54 to 188, the domain is characterized as MsrB.
+At position 38 to 280, the domain is characterized as ABC transporter.
+At position 234 to 310, the domain is characterized as SWIB/MDM2.
+At position 23 to 328, the domain is characterized as Protein kinase.
+At position 19 to 313, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 314 to 610, the domain is characterized as UvrD-like helicase C-terminal.
+At position 82 to 211, the domain is characterized as GST C-terminal.
+At position 24 to 61, the domain is characterized as LDL-receptor class A 1.
+At position 66 to 103, the domain is characterized as LDL-receptor class A 2.
+At position 108 to 144, the domain is characterized as LDL-receptor class A 3.
+At position 1182 to 1251, the domain is characterized as S1 motif.
+At position 1299 to 1388, the domain is characterized as SH2.
+At position 9 to 77, the domain is characterized as HTH merR-type.
+At position 147 to 222, the domain is characterized as Carrier.
+At position 1120 to 1660, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 29 to 257, the domain is characterized as Peptidase S1.
+At position 190 to 379, the domain is characterized as Helicase ATP-binding.
+At position 406 to 550, the domain is characterized as Helicase C-terminal.
+At position 113 to 165, the domain is characterized as bHLH.
+At position 1128 to 1363, the domain is characterized as Fibrillar collagen NC1.
+At position 19 to 87, the domain is characterized as DRBM.
+At position 93 to 204, the domain is characterized as HTH La-type RNA-binding.
+At position 186 to 419, the domain is characterized as VWFA.
+At position 3 to 126, the domain is characterized as PINc.
+At position 21 to 197, the domain is characterized as EngB-type G.
+At position 3 to 625, the domain is characterized as PFL.
+At position 632 to 760, the domain is characterized as Glycine radical.
+At position 196 to 360, the domain is characterized as PA14.
+At position 4 to 147, the domain is characterized as MPN.
+At position 853 to 1126, the domain is characterized as Protein kinase.
+At position 130 to 304, the domain is characterized as PXA.
+At position 336 to 468, the domain is characterized as RGS.
+At position 570 to 690, the domain is characterized as PX.
+At position 88 to 207, the domain is characterized as Ferric oxidoreductase.
+At position 237 to 366, the domain is characterized as FAD-binding FR-type.
+At position 43 to 157, the domain is characterized as Expansin-like EG45.
+At position 167 to 246, the domain is characterized as Expansin-like CBD.
+At position 69 to 145, the domain is characterized as RRM.
+At position 122 to 157, the domain is characterized as EF-hand 2.
+At position 157 to 189, the domain is characterized as EF-hand 3.
+At position 298 to 707, the domain is characterized as USP.
+At position 78 to 215, the domain is characterized as EamA 1.
+At position 253 to 379, the domain is characterized as EamA 2.
+At position 592 to 765, the domain is characterized as tr-type G.
+At position 252 to 355, the domain is characterized as Helicase C-terminal.
+At position 297 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 66 to 109, the domain is characterized as CUE.
+At position 351 to 447, the domain is characterized as Rhodanese.
+At position 560 to 831, the domain is characterized as Protein kinase.
+At position 132 to 195, the domain is characterized as bZIP.
+At position 9 to 157, the domain is characterized as N-acetyltransferase.
+At position 16 to 272, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 275 to 521, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 140 to 447, the domain is characterized as Peptidase A1.
+At position 1 to 82, the domain is characterized as IGFBP N-terminal.
+At position 113 to 328, the domain is characterized as ATP-grasp.
+At position 35 to 423, the domain is characterized as Helicase ATP-binding.
+At position 440 to 602, the domain is characterized as Helicase C-terminal.
+At position 474 to 596, the domain is characterized as HD.
+At position 715 to 796, the domain is characterized as ACT 1.
+At position 822 to 896, the domain is characterized as ACT 2.
+At position 30 to 107, the domain is characterized as EMI.
+At position 101 to 136, the domain is characterized as EGF-like 1.
+At position 144 to 179, the domain is characterized as EGF-like 2.
+At position 187 to 222, the domain is characterized as EGF-like 3.
+At position 230 to 265, the domain is characterized as EGF-like 4.
+At position 278 to 308, the domain is characterized as EGF-like 5.
+At position 316 to 351, the domain is characterized as EGF-like 6.
+At position 405 to 440, the domain is characterized as EGF-like 7.
+At position 453 to 483, the domain is characterized as EGF-like 8.
+At position 491 to 526, the domain is characterized as EGF-like 9.
+At position 539 to 569, the domain is characterized as EGF-like 10.
+At position 577 to 612, the domain is characterized as EGF-like 11.
+At position 665 to 700, the domain is characterized as EGF-like 12.
+At position 713 to 743, the domain is characterized as EGF-like 13.
+At position 751 to 786, the domain is characterized as EGF-like 14.
+At position 799 to 829, the domain is characterized as EGF-like 15.
+At position 166 to 397, the domain is characterized as GB1/RHD3-type G.
+At position 426 to 1145, the domain is characterized as GH81.
+At position 45 to 103, the domain is characterized as TCP.
+At position 572 to 697, the domain is characterized as DBINO.
+At position 812 to 984, the domain is characterized as Helicase ATP-binding.
+At position 1381 to 1535, the domain is characterized as Helicase C-terminal.
+At position 436 to 606, the domain is characterized as tr-type G.
+At position 35 to 835, the domain is characterized as Protein kinase.
+At position 836 to 879, the domain is characterized as AGC-kinase C-terminal.
+At position 165 to 228, the domain is characterized as bZIP.
+At position 173 to 264, the domain is characterized as CS.
+At position 281 to 392, the domain is characterized as FAD-binding FR-type.
+At position 543 to 842, the domain is characterized as Peptidase M60.
+At position 695 to 755, the domain is characterized as RAP.
+At position 11 to 276, the domain is characterized as tr-type G.
+At position 123 to 155, the domain is characterized as LisH.
+At position 156 to 231, the domain is characterized as CTLH.
+At position 84 to 209, the domain is characterized as HotDog ACOT-type 1.
+At position 289 to 401, the domain is characterized as HotDog ACOT-type 2.
+At position 8 to 148, the domain is characterized as DAC.
+At position 280 to 351, the domain is characterized as RRM.
+At position 62 to 167, the domain is characterized as Expansin-like EG45.
+At position 181 to 261, the domain is characterized as Expansin-like CBD.
+At position 148 to 347, the domain is characterized as Peptidase M12A.
+At position 349 to 461, the domain is characterized as CUB 1.
+At position 462 to 574, the domain is characterized as CUB 2.
+At position 574 to 615, the domain is characterized as EGF-like 1; calcium-binding.
+At position 618 to 730, the domain is characterized as CUB 3.
+At position 730 to 770, the domain is characterized as EGF-like 2; calcium-binding.
+At position 774 to 886, the domain is characterized as CUB 4.
+At position 887 to 1003, the domain is characterized as CUB 5.
+At position 763 to 1004, the domain is characterized as I/LWEQ.
+At position 27 to 91, the domain is characterized as J.
+At position 7 to 258, the domain is characterized as ABC transporter.
+At position 9 to 447, the domain is characterized as Helicase ATP-binding.
+At position 16 to 137, the domain is characterized as MH1.
+At position 349 to 546, the domain is characterized as MH2.
+At position 17 to 180, the domain is characterized as PPIase cyclophilin-type.
+At position 12 to 91, the domain is characterized as RRM 1.
+At position 167 to 241, the domain is characterized as RRM 2.
+At position 20 to 250, the domain is characterized as RNase H type-2.
+At position 5 to 194, the domain is characterized as Cytochrome c.
+At position 135 to 313, the domain is characterized as SMP-LTD.
+At position 312 to 433, the domain is characterized as C2 1.
+At position 460 to 580, the domain is characterized as C2 2.
+At position 627 to 751, the domain is characterized as C2 3.
+At position 777 to 899, the domain is characterized as C2 4.
+At position 971 to 1093, the domain is characterized as C2 5.
+At position 505 to 734, the domain is characterized as AIG1-type G.
+At position 37 to 118, the domain is characterized as GST N-terminal.
+At position 126 to 256, the domain is characterized as GST C-terminal.
+At position 89 to 210, the domain is characterized as PX.
+At position 234 to 437, the domain is characterized as BAR.
+At position 512 to 587, the domain is characterized as Cytochrome b5 heme-binding.
+At position 616 to 729, the domain is characterized as FAD-binding FR-type.
+At position 176 to 362, the domain is characterized as Glutamine amidotransferase type-1.
+At position 863 to 950, the domain is characterized as Fibronectin type-III 7.
+At position 1049 to 1151, the domain is characterized as Fibronectin type-III 9.
+At position 344 to 622, the domain is characterized as ABC transmembrane type-1 1.
+At position 785 to 1014, the domain is characterized as ABC transporter 1.
+At position 1421 to 1715, the domain is characterized as ABC transmembrane type-1 2.
+At position 1930 to 2165, the domain is characterized as ABC transporter 2.
+At position 157 to 214, the domain is characterized as CBS 2.
+At position 26 to 56, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 67 to 99, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 26 to 99, the domain is characterized as H15.
+At position 294 to 514, the domain is characterized as TLDc.
+At position 32 to 82, the domain is characterized as bHLH.
+At position 332 to 670, the domain is characterized as TTL.
+At position 26 to 126, the domain is characterized as Cytochrome c.
+At position 9 to 133, the domain is characterized as MaoC-like.
+At position 33 to 94, the domain is characterized as SH3.
+At position 100 to 200, the domain is characterized as SH2.
+At position 220 to 482, the domain is characterized as Protein kinase.
+At position 842 to 891, the domain is characterized as KA1.
+At position 1 to 70, the domain is characterized as HTH gntR-type.
+At position 455 to 562, the domain is characterized as MRH.
+At position 73 to 318, the domain is characterized as GB1/RHD3-type G.
+At position 37 to 220, the domain is characterized as Thioredoxin.
+At position 28 to 69, the domain is characterized as CHCH 1.
+At position 70 to 108, the domain is characterized as CHCH 2.
+At position 60 to 109, the domain is characterized as AWS.
+At position 111 to 228, the domain is characterized as SET.
+At position 4 to 165, the domain is characterized as DHFR.
+At position 80 to 140, the domain is characterized as Tudor.
+At position 2 to 175, the domain is characterized as PRELI/MSF1.
+At position 306 to 482, the domain is characterized as CRAL-TRIO.
+At position 509 to 653, the domain is characterized as GOLD.
+At position 61 to 250, the domain is characterized as RNase H type-2.
+At position 93 to 307, the domain is characterized as RNase H type-2.
+At position 1030 to 1212, the domain is characterized as Rho-GAP.
+At position 316 to 490, the domain is characterized as Helicase ATP-binding.
+At position 517 to 674, the domain is characterized as Helicase C-terminal.
+At position 218 to 445, the domain is characterized as Ras-GAP.
+At position 73 to 184, the domain is characterized as sHSP.
+At position 4 to 26, the domain is characterized as Response regulatory.
+At position 190 to 480, the domain is characterized as Protein kinase.
+At position 139 to 217, the domain is characterized as HARP.
+At position 256 to 412, the domain is characterized as Helicase ATP-binding.
+At position 527 to 681, the domain is characterized as Helicase C-terminal.
+At position 347 to 628, the domain is characterized as Protein kinase.
+At position 199 to 284, the domain is characterized as KH.
+At position 115 to 194, the domain is characterized as PDZ 1.
+At position 199 to 273, the domain is characterized as PDZ 2.
+At position 227 to 366, the domain is characterized as PA14.
+At position 280 to 344, the domain is characterized as Mop.
+At position 110 to 180, the domain is characterized as PAS 1.
+At position 274 to 341, the domain is characterized as PAS 2.
+At position 347 to 385, the domain is characterized as PAC.
+At position 41 to 184, the domain is characterized as SIS.
+At position 226 to 271, the domain is characterized as RPE1 insert.
+At position 316 to 358, the domain is characterized as CCT.
+At position 27 to 355, the domain is characterized as Protein kinase.
+At position 321 to 747, the domain is characterized as FH2.
+At position 142 to 218, the domain is characterized as Carrier.
+At position 996 to 1539, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 43 to 102, the domain is characterized as TRAM.
+At position 656 to 784, the domain is characterized as C2.
+At position 105 to 343, the domain is characterized as Radical SAM core.
+At position 56 to 298, the domain is characterized as Radical SAM core.
+At position 31 to 457, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 948 to 1234, the domain is characterized as PKS/mFAS DH.
+At position 2299 to 2376, the domain is characterized as Carrier.
+At position 71 to 134, the domain is characterized as S5 DRBM.
+At position 198 to 378, the domain is characterized as CRAL-TRIO.
+At position 1 to 30, the domain is characterized as Inhibitor I9.
+At position 39 to 342, the domain is characterized as Peptidase S8.
+At position 102 to 337, the domain is characterized as Radical SAM core.
+At position 51 to 106, the domain is characterized as F-box.
+At position 203 to 374, the domain is characterized as EngA-type G 2.
+At position 178 to 266, the domain is characterized as GAT.
+At position 48 to 198, the domain is characterized as TNase-like.
+At position 106 to 156, the domain is characterized as LysM 1.
+At position 56 to 110, the domain is characterized as HTH myb-type.
+At position 171 to 310, the domain is characterized as PX.
+At position 25 to 101, the domain is characterized as Inhibitor I9.
+At position 103 to 582, the domain is characterized as Peptidase S8.
+At position 367 to 441, the domain is characterized as PA.
+At position 30 to 144, the domain is characterized as Plastocyanin-like 1.
+At position 173 to 353, the domain is characterized as Plastocyanin-like 2.
+At position 450 to 581, the domain is characterized as Plastocyanin-like 3.
+At position 21 to 838, the domain is characterized as Vitellogenin.
+At position 1518 to 1703, the domain is characterized as VWFD.
+At position 12 to 279, the domain is characterized as Pyruvate carboxyltransferase.
+At position 322 to 491, the domain is characterized as tr-type G.
+At position 70 to 328, the domain is characterized as GH16.
+At position 9 to 228, the domain is characterized as MIF4G.
+At position 14 to 111, the domain is characterized as Ig-like C2-type 1.
+At position 123 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 216 to 306, the domain is characterized as Ig-like C2-type 3.
+At position 310 to 399, the domain is characterized as Ig-like C2-type 4.
+At position 270 to 333, the domain is characterized as SAM.
+At position 32 to 98, the domain is characterized as KH.
+At position 118 to 236, the domain is characterized as EamA.
+At position 24 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 148 to 484, the domain is characterized as Protein kinase.
+At position 30 to 247, the domain is characterized as Peptidase S1.
+At position 109 to 309, the domain is characterized as Thioredoxin.
+At position 19 to 147, the domain is characterized as VHS.
+At position 173 to 192, the domain is characterized as UIM.
+At position 219 to 278, the domain is characterized as SH3.
+At position 366 to 383, the domain is characterized as ITAM.
+At position 2 to 152, the domain is characterized as KaiA N-terminal.
+At position 162 to 270, the domain is characterized as KaiA C-terminal.
+At position 447 to 635, the domain is characterized as Helicase ATP-binding.
+At position 900 to 999, the domain is characterized as Tudor 2.
+At position 858 to 975, the domain is characterized as SET.
+At position 984 to 1000, the domain is characterized as Post-SET.
+At position 30 to 78, the domain is characterized as F-box.
+At position 39 to 100, the domain is characterized as Chitin-binding type R&R.
+At position 766 to 850, the domain is characterized as PB1.
+At position 106 to 358, the domain is characterized as GS catalytic.
+At position 513 to 552, the domain is characterized as STI1.
+At position 87 to 223, the domain is characterized as BAH.
+At position 224 to 327, the domain is characterized as ELM2.
+At position 332 to 384, the domain is characterized as SANT.
+At position 49 to 122, the domain is characterized as KRAB.
+At position 38 to 132, the domain is characterized as HTH arsR-type.
+At position 154 to 242, the domain is characterized as Ig-like C2-type 2.
+At position 251 to 353, the domain is characterized as Ig-like C2-type 3.
+At position 108 to 303, the domain is characterized as ATP-grasp.
+At position 3 to 208, the domain is characterized as DPCK.
+At position 15 to 290, the domain is characterized as CN hydrolase.
+At position 261 to 373, the domain is characterized as C-type lectin.
+At position 66 to 220, the domain is characterized as Flavodoxin-like.
+At position 276 to 537, the domain is characterized as FAD-binding FR-type.
+At position 8 to 59, the domain is characterized as Rubredoxin-like.
+At position 12 to 113, the domain is characterized as Longin.
+At position 52 to 131, the domain is characterized as Ig-like C2-type.
+At position 372 to 440, the domain is characterized as ACT 1.
+At position 446 to 510, the domain is characterized as ACT 2.
+At position 49 to 250, the domain is characterized as TR mART core.
+At position 11 to 152, the domain is characterized as SprT-like.
+At position 6 to 255, the domain is characterized as Helicase ATP-binding.
+At position 449 to 638, the domain is characterized as Helicase C-terminal.
+At position 22 to 127, the domain is characterized as Thioredoxin.
+At position 614 to 696, the domain is characterized as BRCT.
+At position 96 to 263, the domain is characterized as TNase-like.
+At position 5 to 70, the domain is characterized as LCN-type CS-alpha/beta.
+At position 118 to 432, the domain is characterized as IF rod.
+At position 107 to 521, the domain is characterized as Peptidase A1.
+At position 95 to 312, the domain is characterized as RNase H type-2.
+At position 182 to 373, the domain is characterized as Glutamine amidotransferase type-1.
+At position 197 to 493, the domain is characterized as SF4 helicase.
+At position 342 to 543, the domain is characterized as Protein kinase.
+At position 79 to 150, the domain is characterized as POTRA.
+At position 219 to 381, the domain is characterized as TrmE-type G.
+At position 568 to 603, the domain is characterized as EF-hand 1.
+At position 652 to 687, the domain is characterized as EF-hand 2.
+At position 692 to 727, the domain is characterized as EF-hand 3.
+At position 89 to 408, the domain is characterized as Calpain catalytic.
+At position 102 to 327, the domain is characterized as HD Cas3-type.
+At position 26 to 363, the domain is characterized as G-alpha.
+At position 336 to 528, the domain is characterized as DH.
+At position 584 to 684, the domain is characterized as PH.
+At position 342 to 509, the domain is characterized as tr-type G.
+At position 11 to 226, the domain is characterized as Radical SAM core.
+At position 4 to 409, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 930 to 1236, the domain is characterized as PKS/mFAS DH.
+At position 2214 to 2292, the domain is characterized as Carrier.
+At position 168 to 361, the domain is characterized as MARVEL.
+At position 1 to 33, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 138 to 422, the domain is characterized as Protein kinase.
+At position 6 to 248, the domain is characterized as Glutamine amidotransferase type-1.
+At position 310 to 520, the domain is characterized as Rab-GAP TBC.
+At position 3 to 438, the domain is characterized as Helicase ATP-binding.
+At position 31 to 143, the domain is characterized as Ig-like V-type.
+At position 147 to 236, the domain is characterized as Ig-like C2-type 1.
+At position 247 to 330, the domain is characterized as Ig-like C2-type 2.
+At position 4 to 37, the domain is characterized as F-box.
+At position 243 to 314, the domain is characterized as PAS.
+At position 498 to 805, the domain is characterized as Histidine kinase.
+At position 1244 to 1364, the domain is characterized as Response regulatory.
+At position 219 to 315, the domain is characterized as PH 1.
+At position 417 to 511, the domain is characterized as PH 2.
+At position 239 to 322, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 384 to 445, the domain is characterized as S4 RNA-binding.
+At position 30 to 280, the domain is characterized as Protein kinase.
+At position 133 to 241, the domain is characterized as CBM21.
+At position 1 to 145, the domain is characterized as PPIase cyclophilin-type.
+At position 62 to 116, the domain is characterized as FHA.
+At position 160 to 421, the domain is characterized as Protein kinase.
+At position 29 to 201, the domain is characterized as FAD-binding PCMH-type.
+At position 97 to 165, the domain is characterized as S4 RNA-binding.
+At position 48 to 85, the domain is characterized as EF-hand 1.
+At position 151 to 251, the domain is characterized as Fe2OG dioxygenase.
+At position 633 to 792, the domain is characterized as Cytochrome c.
+At position 21 to 211, the domain is characterized as NodB homology.
+At position 179 to 289, the domain is characterized as Death.
+At position 100 to 159, the domain is characterized as OVATE.
+At position 325 to 360, the domain is characterized as UVR.
+At position 27 to 422, the domain is characterized as Helicase ATP-binding.
+At position 443 to 609, the domain is characterized as Helicase C-terminal.
+At position 214 to 374, the domain is characterized as Tyrosine-protein phosphatase.
+At position 10 to 261, the domain is characterized as ABC transporter.
+At position 12 to 177, the domain is characterized as NAC.
+At position 46 to 125, the domain is characterized as UPAR/Ly6.
+At position 133 to 365, the domain is characterized as Radical SAM core.
+At position 368 to 429, the domain is characterized as TRAM.
+At position 128 to 357, the domain is characterized as Radical SAM core.
+At position 360 to 427, the domain is characterized as TRAM.
+At position 89 to 285, the domain is characterized as ABC transporter 1.
+At position 351 to 554, the domain is characterized as ABC transporter 2.
+At position 49 to 151, the domain is characterized as HD.
+At position 79 to 246, the domain is characterized as Helicase ATP-binding.
+At position 258 to 416, the domain is characterized as Helicase C-terminal.
+At position 89 to 211, the domain is characterized as PX.
+At position 10 to 73, the domain is characterized as bZIP.
+At position 80 to 141, the domain is characterized as CBS 1.
+At position 467 to 615, the domain is characterized as Helicase C-terminal.
+At position 161 to 302, the domain is characterized as MRH.
+At position 80 to 142, the domain is characterized as TGS.
+At position 214 to 415, the domain is characterized as Peptidase M12B.
+At position 422 to 509, the domain is characterized as Disintegrin.
+At position 658 to 686, the domain is characterized as EGF-like.
+At position 25 to 260, the domain is characterized as ABC transporter 1.
+At position 260 to 511, the domain is characterized as ABC transporter 2.
+At position 499 to 668, the domain is characterized as tr-type G.
+At position 81 to 310, the domain is characterized as Radical SAM core.
+At position 1 to 213, the domain is characterized as SPX.
+At position 872 to 1217, the domain is characterized as GP-PDE.
+At position 4 to 83, the domain is characterized as Cytochrome b5 heme-binding.
+At position 40 to 306, the domain is characterized as Septin-type G.
+At position 408 to 542, the domain is characterized as Plastocyanin-like 3.
+At position 765 to 903, the domain is characterized as N-terminal Ras-GEF.
+At position 938 to 1170, the domain is characterized as Ras-GEF.
+At position 67 to 80, the domain is characterized as CRIB.
+At position 295 to 546, the domain is characterized as Protein kinase.
+At position 13 to 267, the domain is characterized as Protein kinase.
+At position 302 to 329, the domain is characterized as NAF.
+At position 67 to 198, the domain is characterized as MATH.
+At position 155 to 253, the domain is characterized as CRM 1.
+At position 275 to 371, the domain is characterized as CRM 2.
+At position 22 to 122, the domain is characterized as Gnk2-homologous 1.
+At position 19 to 146, the domain is characterized as EamA.
+At position 38 to 91, the domain is characterized as HTH cro/C1-type.
+At position 285 to 417, the domain is characterized as Nop.
+At position 222 to 319, the domain is characterized as PH 2.
+At position 99 to 290, the domain is characterized as ABC transmembrane type-1.
+At position 82 to 133, the domain is characterized as bHLH.
+At position 19 to 63, the domain is characterized as F-box.
+At position 29 to 259, the domain is characterized as Peptidase S1.
+At position 383 to 478, the domain is characterized as PTS EIIB type-2.
+At position 19 to 131, the domain is characterized as Response regulatory.
+At position 156 to 229, the domain is characterized as PAS.
+At position 230 to 284, the domain is characterized as PAC.
+At position 285 to 454, the domain is characterized as GAF.
+At position 617 to 668, the domain is characterized as HTH bat-type.
+At position 529 to 600, the domain is characterized as Olduvai 3.
+At position 601 to 692, the domain is characterized as Olduvai 4.
+At position 695 to 750, the domain is characterized as Olduvai 5.
+At position 751 to 843, the domain is characterized as Olduvai 6.
+At position 844 to 919, the domain is characterized as Olduvai 7.
+At position 920 to 1012, the domain is characterized as Olduvai 8.
+At position 1013 to 1111, the domain is characterized as Olduvai 9.
+At position 9 to 97, the domain is characterized as Tudor-knot.
+At position 193 to 368, the domain is characterized as MRG.
+At position 139 to 258, the domain is characterized as C-type lectin.
+At position 142 to 248, the domain is characterized as Rhodanese.
+At position 422 to 510, the domain is characterized as PI3K-RBD.
+At position 1559 to 1678, the domain is characterized as C2.
+At position 21 to 119, the domain is characterized as Plastocyanin-like.
+At position 1199 to 1323, the domain is characterized as C2 1.
+At position 1633 to 1776, the domain is characterized as MHD1.
+At position 1882 to 2024, the domain is characterized as MHD2.
+At position 2038 to 2165, the domain is characterized as C2 2.
+At position 12 to 65, the domain is characterized as MEIS N-terminal.
+At position 33 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 373 to 520, the domain is characterized as TIR.
+At position 50 to 178, the domain is characterized as WIF.
+At position 317 to 590, the domain is characterized as Protein kinase.
+At position 149 to 243, the domain is characterized as TonB C-terminal.
+At position 25 to 113, the domain is characterized as Link.
+At position 20 to 156, the domain is characterized as HTH marR-type.
+At position 6 to 79, the domain is characterized as PAS.
+At position 80 to 133, the domain is characterized as PAC.
+At position 142 to 253, the domain is characterized as STAS.
+At position 254 to 434, the domain is characterized as PCI.
+At position 29 to 130, the domain is characterized as SRCR 1.
+At position 159 to 270, the domain is characterized as SRCR 2.
+At position 294 to 393, the domain is characterized as SRCR 3.
+At position 403 to 512, the domain is characterized as SRCR 4.
+At position 35 to 132, the domain is characterized as Ig-like V-type 1.
+At position 166 to 259, the domain is characterized as Ig-like V-type 2.
+At position 270 to 378, the domain is characterized as Ig-like V-type 3.
+At position 392 to 498, the domain is characterized as Ig-like V-type 4.
+At position 509 to 615, the domain is characterized as Ig-like V-type 5.
+At position 642 to 733, the domain is characterized as Ig-like V-type 6.
+At position 746 to 851, the domain is characterized as Ig-like V-type 7.
+At position 859 to 943, the domain is characterized as Ig-like C2-type 1.
+At position 33 to 167, the domain is characterized as Ig-like V-type.
+At position 152 to 323, the domain is characterized as Helicase ATP-binding.
+At position 395 to 552, the domain is characterized as Helicase C-terminal.
+At position 72 to 370, the domain is characterized as Protein kinase.
+At position 12 to 141, the domain is characterized as C2.
+At position 456 to 516, the domain is characterized as PAP-associated.
+At position 415 to 548, the domain is characterized as Ricin B-type lectin.
+At position 1 to 273, the domain is characterized as Protein kinase.
+At position 7 to 211, the domain is characterized as Glutamine amidotransferase type-1.
+At position 241 to 526, the domain is characterized as Helicase ATP-binding.
+At position 804 to 976, the domain is characterized as Helicase C-terminal.
+At position 335 to 415, the domain is characterized as UBX.
+At position 872 to 995, the domain is characterized as PINc.
+At position 69 to 182, the domain is characterized as THUMP.
+At position 217 to 433, the domain is characterized as TrmE-type G.
+At position 331 to 550, the domain is characterized as TLDc.
+At position 726 to 784, the domain is characterized as Tudor 1.
+At position 962 to 1021, the domain is characterized as Tudor 2.
+At position 1228 to 1285, the domain is characterized as Tudor 3.
+At position 1479 to 1539, the domain is characterized as Tudor 4.
+At position 414 to 521, the domain is characterized as SCP2.
+At position 91 to 131, the domain is characterized as DHHC.
+At position 19 to 163, the domain is characterized as Reelin.
+At position 374 to 520, the domain is characterized as MATH.
+At position 52 to 122, the domain is characterized as POTRA.
+At position 66 to 170, the domain is characterized as EamA.
+At position 9 to 260, the domain is characterized as Pyruvate carboxyltransferase.
+At position 107 to 182, the domain is characterized as Rho RNA-BD.
+At position 995 to 1282, the domain is characterized as CNH.
+At position 28 to 117, the domain is characterized as Cystatin.
+At position 24 to 273, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 134 to 315, the domain is characterized as Helicase ATP-binding.
+At position 460 to 619, the domain is characterized as Helicase C-terminal.
+At position 652 to 742, the domain is characterized as Dicer dsRNA-binding fold.
+At position 892 to 1020, the domain is characterized as PAZ.
+At position 1044 to 1203, the domain is characterized as RNase III 1.
+At position 1254 to 1406, the domain is characterized as RNase III 2.
+At position 1440 to 1508, the domain is characterized as DRBM.
+At position 14 to 107, the domain is characterized as GS beta-grasp.
+At position 114 to 446, the domain is characterized as GS catalytic.
+At position 1 to 204, the domain is characterized as RNase H type-2.
+At position 710 to 1019, the domain is characterized as Protein kinase.
+At position 688 to 877, the domain is characterized as SEC7.
+At position 26 to 136, the domain is characterized as Calponin-homology (CH).
+At position 56 to 300, the domain is characterized as ABC transporter.
+At position 373 to 621, the domain is characterized as ABC transmembrane type-2.
+At position 295 to 595, the domain is characterized as Protein kinase 1.
+At position 860 to 1128, the domain is characterized as Protein kinase 2.
+At position 102 to 388, the domain is characterized as Protein kinase.
+At position 26 to 178, the domain is characterized as 6-Cys 1.
+At position 278 to 409, the domain is characterized as 6-Cys 2.
+At position 473 to 587, the domain is characterized as Toprim.
+At position 43 to 122, the domain is characterized as GIY-YIG.
+At position 3 to 327, the domain is characterized as FERM.
+At position 367 to 631, the domain is characterized as Protein kinase.
+At position 313 to 399, the domain is characterized as Rhodanese.
+At position 24 to 130, the domain is characterized as Gnk2-homologous 1.
+At position 136 to 245, the domain is characterized as Gnk2-homologous 2.
+At position 339 to 616, the domain is characterized as Protein kinase.
+At position 24 to 101, the domain is characterized as RRM 1.
+At position 115 to 192, the domain is characterized as RRM 2.
+At position 176 to 277, the domain is characterized as PpiC 1.
+At position 353 to 519, the domain is characterized as RCK N-terminal.
+At position 93 to 398, the domain is characterized as tr-type G.
+At position 11 to 682, the domain is characterized as PFL.
+At position 689 to 810, the domain is characterized as Glycine radical.
+At position 1886 to 1915, the domain is characterized as IQ.
+At position 370 to 427, the domain is characterized as COS.
+At position 429 to 528, the domain is characterized as Fibronectin type-III.
+At position 513 to 747, the domain is characterized as B30.2/SPRY.
+At position 16 to 320, the domain is characterized as FERM.
+At position 416 to 599, the domain is characterized as Macro.
+At position 79 to 148, the domain is characterized as PAH 1.
+At position 162 to 232, the domain is characterized as PAH 2.
+At position 216 to 287, the domain is characterized as KRAB.
+At position 55 to 372, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 115 to 382, the domain is characterized as Peptidase S8.
+At position 48 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 214 to 276, the domain is characterized as t-SNARE coiled-coil homology.
+At position 94 to 143, the domain is characterized as bHLH; atypical.
+At position 368 to 522, the domain is characterized as Helicase C-terminal.
+At position 295 to 440, the domain is characterized as JmjC.
+At position 156 to 275, the domain is characterized as C-type lectin.
+At position 55 to 113, the domain is characterized as Cyclin N-terminal.
+At position 6 to 133, the domain is characterized as MATH.
+At position 259 to 468, the domain is characterized as Ku.
+At position 591 to 625, the domain is characterized as SAP.
+At position 481 to 642, the domain is characterized as CBM3 1.
+At position 836 to 986, the domain is characterized as CBM3 2.
+At position 105 to 257, the domain is characterized as Nudix hydrolase.
+At position 547 to 566, the domain is characterized as UIM 1.
+At position 583 to 602, the domain is characterized as UIM 2.
+At position 651 to 668, the domain is characterized as UIM 3.
+At position 141 to 468, the domain is characterized as IF rod.
+At position 5 to 106, the domain is characterized as PINc.
+At position 592 to 677, the domain is characterized as Smr.
+At position 23 to 154, the domain is characterized as Thioredoxin.
+At position 39 to 74, the domain is characterized as Tify.
+At position 147 to 398, the domain is characterized as ABC transporter 1.
+At position 890 to 1034, the domain is characterized as TIR.
+At position 107 to 471, the domain is characterized as GS catalytic.
+At position 6 to 152, the domain is characterized as N-acetyltransferase.
+At position 36 to 84, the domain is characterized as F-box.
+At position 490 to 712, the domain is characterized as Histidine kinase.
+At position 27 to 97, the domain is characterized as POTRA.
+At position 1 to 69, the domain is characterized as HTH OST-type 1.
+At position 218 to 288, the domain is characterized as HTH OST-type 2.
+At position 30 to 281, the domain is characterized as ABC transporter 1.
+At position 729 to 971, the domain is characterized as ABC transporter 2.
+At position 239 to 438, the domain is characterized as Peptidase M12B.
+At position 444 to 531, the domain is characterized as Disintegrin.
+At position 675 to 712, the domain is characterized as EGF-like.
+At position 21 to 227, the domain is characterized as ABC transporter.
+At position 26 to 155, the domain is characterized as EamA.
+At position 216 to 318, the domain is characterized as PB1.
+At position 8 to 375, the domain is characterized as PPM-type phosphatase.
+At position 1087 to 1325, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 194, the domain is characterized as UmuC.
+At position 509 to 590, the domain is characterized as PB1.
+At position 33 to 455, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1423 to 1498, the domain is characterized as Carrier.
+At position 82 to 253, the domain is characterized as Tyrosine-protein phosphatase.
+At position 33 to 166, the domain is characterized as HTH marR-type.
+At position 115 to 287, the domain is characterized as ATP-grasp.
+At position 215 to 377, the domain is characterized as Helicase ATP-binding.
+At position 431 to 589, the domain is characterized as Helicase C-terminal.
+At position 1 to 239, the domain is characterized as Radical SAM core.
+At position 58 to 196, the domain is characterized as RNase H type-1.
+At position 154 to 246, the domain is characterized as Ig-like C2-type 1.
+At position 269 to 362, the domain is characterized as Ig-like C2-type 2.
+At position 376 to 471, the domain is characterized as Fibronectin type-III 1.
+At position 504 to 599, the domain is characterized as Fibronectin type-III 2.
+At position 605 to 698, the domain is characterized as Fibronectin type-III 3.
+At position 704 to 799, the domain is characterized as Fibronectin type-III 4.
+At position 806 to 901, the domain is characterized as Fibronectin type-III 5.
+At position 1122 to 1207, the domain is characterized as Ig-like C2-type 3.
+At position 1336 to 1425, the domain is characterized as Ig-like C2-type 4.
+At position 273 to 344, the domain is characterized as Collagen-like.
+At position 353 to 453, the domain is characterized as SRCR.
+At position 109 to 289, the domain is characterized as Tyr recombinase.
+At position 12 to 80, the domain is characterized as HTH gntR-type.
+At position 975 to 1041, the domain is characterized as BIG2.
+At position 67 to 566, the domain is characterized as Myosin motor.
+At position 33 to 235, the domain is characterized as Radical SAM core.
+At position 79 to 149, the domain is characterized as HTH iclR-type.
+At position 36 to 258, the domain is characterized as Radical SAM core.
+At position 11 to 90, the domain is characterized as GST N-terminal.
+At position 96 to 228, the domain is characterized as GST C-terminal.
+At position 35 to 117, the domain is characterized as Doublecortin 1.
+At position 157 to 236, the domain is characterized as Doublecortin 2.
+At position 560 to 729, the domain is characterized as C2 DOCK-type.
+At position 1632 to 2066, the domain is characterized as DOCKER.
+At position 1 to 184, the domain is characterized as B30.2/SPRY.
+At position 26 to 357, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 252 to 420, the domain is characterized as PCI.
+At position 122 to 233, the domain is characterized as sHSP 1.
+At position 251 to 354, the domain is characterized as sHSP 2.
+At position 18 to 295, the domain is characterized as Protein kinase.
+At position 23 to 193, the domain is characterized as Laminin G-like.
+At position 26 to 73, the domain is characterized as WAP; atypical.
+At position 70 to 128, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 32 to 66, the domain is characterized as EGF-like 1.
+At position 336 to 587, the domain is characterized as ZP.
+At position 304 to 573, the domain is characterized as Clu.
+At position 165 to 390, the domain is characterized as TRUD.
+At position 262 to 344, the domain is characterized as IPT/TIG.
+At position 20 to 107, the domain is characterized as Ig-like V-type.
+At position 147 to 235, the domain is characterized as Ig-like C1-type.
+At position 40 to 109, the domain is characterized as Importin N-terminal.
+At position 21 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 109 to 195, the domain is characterized as Ig-like C2-type 2.
+At position 6 to 142, the domain is characterized as RNase III.
+At position 272 to 341, the domain is characterized as DRBM.
+At position 17 to 237, the domain is characterized as NB-ARC.
+At position 711 to 775, the domain is characterized as HMA.
+At position 25 to 91, the domain is characterized as BTB.
+At position 47 to 77, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 102 to 403, the domain is characterized as Protein kinase.
+At position 36 to 135, the domain is characterized as Ig-like C2-type 1.
+At position 20 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 100 to 139, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 238 to 294, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 1 to 200, the domain is characterized as Macro.
+At position 229 to 461, the domain is characterized as Ku.
+At position 32 to 302, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 114 to 206, the domain is characterized as Ig-like C1-type.
+At position 39 to 103, the domain is characterized as S1 motif 1.
+At position 121 to 187, the domain is characterized as S1 motif 2.
+At position 208 to 276, the domain is characterized as S1 motif 3.
+At position 293 to 363, the domain is characterized as S1 motif 4.
+At position 380 to 450, the domain is characterized as S1 motif 5.
+At position 467 to 536, the domain is characterized as S1 motif 6.
+At position 83 to 206, the domain is characterized as GST C-terminal.
+At position 38 to 232, the domain is characterized as Lon N-terminal.
+At position 634 to 815, the domain is characterized as Lon proteolytic.
+At position 150 to 200, the domain is characterized as DHHC.
+At position 171 to 364, the domain is characterized as Galectin.
+At position 513 to 661, the domain is characterized as Ricin B-type lectin.
+At position 281 to 375, the domain is characterized as BRCT.
+At position 577 to 714, the domain is characterized as C2 1.
+At position 773 to 897, the domain is characterized as C2 2.
+At position 9 to 317, the domain is characterized as Protein kinase 1.
+At position 379 to 654, the domain is characterized as Protein kinase 2.
+At position 24 to 95, the domain is characterized as H15.
+At position 532 to 766, the domain is characterized as NR LBD.
+At position 902 to 976, the domain is characterized as RRM 2.
+At position 304 to 548, the domain is characterized as ABC transporter 1.
+At position 625 to 840, the domain is characterized as ABC transporter 2.
+At position 45 to 221, the domain is characterized as Collagen-like.
+At position 259 to 374, the domain is characterized as C-type lectin.
+At position 212 to 286, the domain is characterized as RRM.
+At position 168 to 343, the domain is characterized as Helicase ATP-binding.
+At position 371 to 518, the domain is characterized as Helicase C-terminal.
+At position 90 to 277, the domain is characterized as Helicase ATP-binding.
+At position 574 to 736, the domain is characterized as Toprim.
+At position 69 to 214, the domain is characterized as SCP.
+At position 607 to 714, the domain is characterized as CBS 1.
+At position 768 to 815, the domain is characterized as CBS 2.
+At position 1 to 247, the domain is characterized as ABC transporter.
+At position 193 to 304, the domain is characterized as HD.
+At position 626 to 839, the domain is characterized as FtsK.
+At position 404 to 573, the domain is characterized as tr-type G.
+At position 21 to 83, the domain is characterized as S1 motif 1.
+At position 101 to 167, the domain is characterized as S1 motif 2.
+At position 188 to 256, the domain is characterized as S1 motif 3.
+At position 273 to 343, the domain is characterized as S1 motif 4.
+At position 360 to 430, the domain is characterized as S1 motif 5.
+At position 447 to 516, the domain is characterized as S1 motif 6.
+At position 335 to 612, the domain is characterized as BEACH.
+At position 347 to 516, the domain is characterized as tr-type G.
+At position 5 to 228, the domain is characterized as Radical SAM core.
+At position 23 to 267, the domain is characterized as AB hydrolase-1.
+At position 291 to 529, the domain is characterized as Glutamine amidotransferase type-1.
+At position 35 to 278, the domain is characterized as ATP-grasp.
+At position 22 to 224, the domain is characterized as tr-type G.
+At position 23 to 109, the domain is characterized as Fibronectin type-III 1.
+At position 113 to 206, the domain is characterized as Fibronectin type-III 2.
+At position 207 to 291, the domain is characterized as Fibronectin type-III 3.
+At position 292 to 384, the domain is characterized as Fibronectin type-III 4.
+At position 378 to 466, the domain is characterized as Fibronectin type-III 5.
+At position 470 to 556, the domain is characterized as Fibronectin type-III 6.
+At position 557 to 642, the domain is characterized as Fibronectin type-III 7.
+At position 643 to 733, the domain is characterized as Fibronectin type-III 8.
+At position 734 to 821, the domain is characterized as Fibronectin type-III 9.
+At position 822 to 913, the domain is characterized as Fibronectin type-III 10.
+At position 908 to 994, the domain is characterized as Fibronectin type-III 11.
+At position 995 to 1088, the domain is characterized as Fibronectin type-III 12.
+At position 1086 to 1173, the domain is characterized as Fibronectin type-III 13.
+At position 1176 to 1263, the domain is characterized as Fibronectin type-III 14.
+At position 1264 to 1357, the domain is characterized as Fibronectin type-III 15.
+At position 1358 to 1449, the domain is characterized as Fibronectin type-III 16.
+At position 1449 to 1551, the domain is characterized as Fibronectin type-III 17.
+At position 1704 to 1964, the domain is characterized as Tyrosine-protein phosphatase.
+At position 93 to 165, the domain is characterized as Kringle.
+At position 170 to 271, the domain is characterized as SRCR 1.
+At position 280 to 381, the domain is characterized as SRCR 2.
+At position 387 to 487, the domain is characterized as SRCR 3.
+At position 500 to 601, the domain is characterized as SRCR 4.
+At position 631 to 874, the domain is characterized as Peptidase S1.
+At position 1 to 106, the domain is characterized as HSR.
+At position 182 to 282, the domain is characterized as SAND.
+At position 276 to 326, the domain is characterized as bHLH.
+At position 187 to 234, the domain is characterized as F-box.
+At position 214 to 374, the domain is characterized as Hflx-type G.
+At position 291 to 405, the domain is characterized as Cyclin N-terminal.
+At position 659 to 756, the domain is characterized as HTH araC/xylS-type.
+At position 6 to 81, the domain is characterized as U-box.
+At position 609 to 655, the domain is characterized as UBA.
+At position 162 to 343, the domain is characterized as CheB-type methylesterase.
+At position 57 to 357, the domain is characterized as ABC transmembrane type-1.
+At position 390 to 587, the domain is characterized as ABC transporter.
+At position 24 to 96, the domain is characterized as UPAR/Ly6.
+At position 403 to 471, the domain is characterized as S4 RNA-binding.
+At position 1 to 258, the domain is characterized as Pterin-binding.
+At position 849 to 1124, the domain is characterized as Protein kinase 2.
+At position 31 to 276, the domain is characterized as Peptidase S1.
+At position 7 to 56, the domain is characterized as SpoVT-AbrB 1.
+At position 85 to 128, the domain is characterized as SpoVT-AbrB 2.
+At position 52 to 149, the domain is characterized as Ig-like.
+At position 151 to 242, the domain is characterized as Ig-like C2-type.
+At position 250 to 304, the domain is characterized as TSP type-1 1.
+At position 306 to 358, the domain is characterized as TSP type-1 2.
+At position 545 to 685, the domain is characterized as ZU5.
+At position 862 to 939, the domain is characterized as Death.
+At position 82 to 189, the domain is characterized as Calponin-homology (CH).
+At position 1202 to 1215, the domain is characterized as CRIB.
+At position 1376 to 1647, the domain is characterized as Protein kinase.
+At position 150 to 241, the domain is characterized as PPIase FKBP-type.
+At position 237 to 283, the domain is characterized as F-box.
+At position 80 to 402, the domain is characterized as PDEase.
+At position 8 to 136, the domain is characterized as N-acetyltransferase 1.
+At position 149 to 301, the domain is characterized as N-acetyltransferase 2.
+At position 1 to 126, the domain is characterized as NTR.
+At position 46 to 75, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 344 to 568, the domain is characterized as ABC transporter 2.
+At position 116 to 192, the domain is characterized as PRC barrel.
+At position 167 to 248, the domain is characterized as PRC barrel.
+At position 84 to 232, the domain is characterized as UBC core.
+At position 330 to 380, the domain is characterized as bHLH.
+At position 1 to 54, the domain is characterized as H15.
+At position 322 to 551, the domain is characterized as MH2.
+At position 256 to 449, the domain is characterized as GATase cobBQ-type.
+At position 280 to 579, the domain is characterized as NB-ARC.
+At position 346 to 428, the domain is characterized as Fibronectin type-III.
+At position 403 to 827, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1294 to 1608, the domain is characterized as PKS/mFAS DH.
+At position 1666 to 1743, the domain is characterized as Carrier.
+At position 280 to 356, the domain is characterized as PUA.
+At position 43 to 472, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 948 to 1219, the domain is characterized as PKS/mFAS DH.
+At position 1703 to 1777, the domain is characterized as Carrier.
+At position 38 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 139 to 221, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 313, the domain is characterized as Ig-like C2-type 3.
+At position 127 to 556, the domain is characterized as Urease.
+At position 104 to 226, the domain is characterized as SET.
+At position 14 to 136, the domain is characterized as Rhodanese.
+At position 113 to 177, the domain is characterized as J.
+At position 65 to 175, the domain is characterized as Thioredoxin.
+At position 93 to 392, the domain is characterized as Protein kinase.
+At position 393 to 467, the domain is characterized as AGC-kinase C-terminal.
+At position 528 to 673, the domain is characterized as Helicase C-terminal.
+At position 389 to 478, the domain is characterized as STAS.
+At position 91 to 194, the domain is characterized as PB1.
+At position 13 to 73, the domain is characterized as F-box.
+At position 54 to 87, the domain is characterized as WW 1.
+At position 101 to 134, the domain is characterized as WW 2.
+At position 32 to 269, the domain is characterized as PABS.
+At position 93 to 313, the domain is characterized as VWFA.
+At position 134 to 259, the domain is characterized as FZ 1.
+At position 268 to 304, the domain is characterized as LDL-receptor class A 1.
+At position 305 to 340, the domain is characterized as LDL-receptor class A 2.
+At position 341 to 377, the domain is characterized as LDL-receptor class A 3.
+At position 378 to 415, the domain is characterized as LDL-receptor class A 4.
+At position 450 to 573, the domain is characterized as FZ 2.
+At position 579 to 614, the domain is characterized as LDL-receptor class A 5.
+At position 615 to 653, the domain is characterized as LDL-receptor class A 6.
+At position 654 to 689, the domain is characterized as LDL-receptor class A 7.
+At position 690 to 801, the domain is characterized as SRCR.
+At position 802 to 1035, the domain is characterized as Peptidase S1.
+At position 300 to 413, the domain is characterized as CRC.
+At position 8 to 72, the domain is characterized as SH3.
+At position 78 to 170, the domain is characterized as SH2.
+At position 191 to 445, the domain is characterized as Protein kinase.
+At position 230 to 396, the domain is characterized as Hflx-type G.
+At position 177 to 343, the domain is characterized as PCI.
+At position 71 to 123, the domain is characterized as bHLH.
+At position 172 to 438, the domain is characterized as MHD.
+At position 3 to 256, the domain is characterized as Chorismate mutase.
+At position 1186 to 1230, the domain is characterized as LEM.
+At position 182 to 268, the domain is characterized as Toprim.
+At position 45 to 134, the domain is characterized as SUEL-type lectin.
+At position 725 to 772, the domain is characterized as GPS.
+At position 8 to 102, the domain is characterized as ABM.
+At position 93 to 252, the domain is characterized as Helicase ATP-binding.
+At position 639 to 802, the domain is characterized as Toprim.
+At position 250 to 442, the domain is characterized as GATase cobBQ-type.
+At position 23 to 130, the domain is characterized as SprT-like.
+At position 12 to 88, the domain is characterized as GIY-YIG.
+At position 671 to 700, the domain is characterized as IQ 1.
+At position 713 to 742, the domain is characterized as IQ 2.
+At position 159 to 349, the domain is characterized as CheB-type methylesterase.
+At position 493 to 527, the domain is characterized as EF-hand 4.
+At position 5 to 90, the domain is characterized as Ras-associating 1.
+At position 132 to 223, the domain is characterized as PH.
+At position 277 to 384, the domain is characterized as Calponin-homology (CH) 1.
+At position 392 to 502, the domain is characterized as Calponin-homology (CH) 2.
+At position 1112 to 1196, the domain is characterized as Ras-associating 2.
+At position 30 to 200, the domain is characterized as FAD-binding PCMH-type.
+At position 291 to 368, the domain is characterized as SWIB/MDM2.
+At position 7 to 263, the domain is characterized as Chorismate mutase.
+At position 133 to 210, the domain is characterized as RRM 2.
+At position 224 to 301, the domain is characterized as RRM 3.
+At position 327 to 404, the domain is characterized as RRM 4.
+At position 573 to 650, the domain is characterized as PABC.
+At position 45 to 418, the domain is characterized as GBD/FH3.
+At position 603 to 1012, the domain is characterized as FH2.
+At position 1030 to 1061, the domain is characterized as DAD.
+At position 71 to 323, the domain is characterized as PPM-type phosphatase.
+At position 12 to 282, the domain is characterized as F-BAR.
+At position 468 to 529, the domain is characterized as SH3 1.
+At position 546 to 609, the domain is characterized as SH3 2.
+At position 1080 to 1380, the domain is characterized as Peptidase M60.
+At position 47 to 193, the domain is characterized as MABP.
+At position 254 to 303, the domain is characterized as UMA.
+At position 120 to 193, the domain is characterized as RRM 2.
+At position 86 to 174, the domain is characterized as PB1.
+At position 417 to 797, the domain is characterized as USP.
+At position 4 to 48, the domain is characterized as LEM.
+At position 216 to 378, the domain is characterized as PCI.
+At position 203 to 293, the domain is characterized as RRM.
+At position 155 to 384, the domain is characterized as NR LBD.
+At position 594 to 677, the domain is characterized as BRCT.
+At position 1 to 96, the domain is characterized as SPX.
+At position 747 to 1066, the domain is characterized as GP-PDE.
+At position 359 to 548, the domain is characterized as Helicase ATP-binding.
+At position 616 to 789, the domain is characterized as Helicase C-terminal.
+At position 69 to 111, the domain is characterized as CUE.
+At position 215 to 722, the domain is characterized as Protein kinase.
+At position 720 to 804, the domain is characterized as PB1.
+At position 23 to 79, the domain is characterized as bHLH.
+At position 10 to 131, the domain is characterized as MaoC-like.
+At position 73 to 156, the domain is characterized as PDZ.
+At position 296 to 421, the domain is characterized as PH.
+At position 60 to 115, the domain is characterized as bHLH.
+At position 14 to 61, the domain is characterized as F-box.
+At position 107 to 335, the domain is characterized as Radical SAM core.
+At position 120 to 359, the domain is characterized as Radical SAM core.
+At position 85 to 146, the domain is characterized as J.
+At position 507 to 611, the domain is characterized as PTS EIIA type-1.
+At position 3 to 45, the domain is characterized as SpoVT-AbrB 1.
+At position 74 to 117, the domain is characterized as SpoVT-AbrB 2.
+At position 8 to 64, the domain is characterized as WHEP-TRS.
+At position 63 to 171, the domain is characterized as MTTase N-terminal.
+At position 199 to 430, the domain is characterized as Radical SAM core.
+At position 430 to 492, the domain is characterized as TRAM.
+At position 11 to 52, the domain is characterized as CHCH.
+At position 218 to 547, the domain is characterized as FERM 1.
+At position 666 to 1103, the domain is characterized as FERM 2.
+At position 234 to 445, the domain is characterized as Helicase ATP-binding.
+At position 494 to 651, the domain is characterized as Helicase C-terminal.
+At position 567 to 778, the domain is characterized as ATP-grasp.
+At position 283 to 378, the domain is characterized as SH2.
+At position 373 to 422, the domain is characterized as SOCS box.
+At position 20 to 161, the domain is characterized as N-acetyltransferase.
+At position 684 to 736, the domain is characterized as NB-ARC 1.
+At position 786 to 830, the domain is characterized as NB-ARC 2.
+At position 1188 to 1252, the domain is characterized as HMA.
+At position 82 to 233, the domain is characterized as Flavodoxin-like.
+At position 289 to 535, the domain is characterized as FAD-binding FR-type.
+At position 209 to 257, the domain is characterized as SOCS box.
+At position 14 to 79, the domain is characterized as SAM.
+At position 30 to 167, the domain is characterized as Thioredoxin.
+At position 21 to 223, the domain is characterized as RNase H type-2.
+At position 623 to 693, the domain is characterized as S1 motif 1.
+At position 707 to 775, the domain is characterized as S1 motif 2.
+At position 36 to 203, the domain is characterized as VWFD 1.
+At position 304 to 360, the domain is characterized as TIL 1.
+At position 398 to 570, the domain is characterized as VWFD 2.
+At position 666 to 723, the domain is characterized as TIL 2.
+At position 782 to 825, the domain is characterized as TIL 3.
+At position 825 to 897, the domain is characterized as VWFC 1.
+At position 863 to 1033, the domain is characterized as VWFD 3.
+At position 1429 to 1613, the domain is characterized as VWFD 4.
+At position 1761 to 1832, the domain is characterized as VWFC 2.
+At position 1870 to 1937, the domain is characterized as VWFC 3.
+At position 2010 to 2104, the domain is characterized as CTCK.
+At position 15 to 160, the domain is characterized as NAC.
+At position 54 to 121, the domain is characterized as BTB.
+At position 156 to 257, the domain is characterized as BACK.
+At position 59 to 123, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 45 to 372, the domain is characterized as SAM-dependent MTase C5-type.
+At position 118 to 399, the domain is characterized as FERM.
+At position 291 to 331, the domain is characterized as UBA.
+At position 445 to 493, the domain is characterized as KA1.
+At position 56 to 158, the domain is characterized as THUMP.
+At position 396 to 479, the domain is characterized as Rhodanese.
+At position 459 to 508, the domain is characterized as GYF.
+At position 439 to 623, the domain is characterized as DH.
+At position 655 to 782, the domain is characterized as PH.
+At position 789 to 850, the domain is characterized as SH3.
+At position 24 to 245, the domain is characterized as ABC transporter.
+At position 286 to 335, the domain is characterized as SOCS box.
+At position 34 to 431, the domain is characterized as Glutamine amidotransferase type-2.
+At position 22 to 137, the domain is characterized as Ig-like C2-type 1.
+At position 149 to 263, the domain is characterized as Ig-like C2-type 2.
+At position 276 to 389, the domain is characterized as Ig-like C2-type 3.
+At position 406 to 536, the domain is characterized as Ig-like C2-type 4.
+At position 544 to 662, the domain is characterized as Ig-like C2-type 5.
+At position 688 to 813, the domain is characterized as Ig-like C2-type 6.
+At position 36 to 215, the domain is characterized as VWFA 1.
+At position 217 to 257, the domain is characterized as EGF-like 1.
+At position 258 to 298, the domain is characterized as EGF-like 2.
+At position 299 to 339, the domain is characterized as EGF-like 3.
+At position 340 to 380, the domain is characterized as EGF-like 4.
+At position 388 to 563, the domain is characterized as VWFA 2.
+At position 2 to 148, the domain is characterized as Toprim.
+At position 435 to 639, the domain is characterized as EXS.
+At position 14 to 90, the domain is characterized as Cytochrome b5 heme-binding.
+At position 760 to 1046, the domain is characterized as Protein kinase.
+At position 8 to 77, the domain is characterized as S1 motif.
+At position 224 to 489, the domain is characterized as FAD-binding FR-type.
+At position 51 to 97, the domain is characterized as TRM112.
+At position 40 to 139, the domain is characterized as Cadherin 1.
+At position 140 to 252, the domain is characterized as Cadherin 2.
+At position 253 to 359, the domain is characterized as Cadherin 3.
+At position 365 to 478, the domain is characterized as Cadherin 4.
+At position 479 to 582, the domain is characterized as Cadherin 5.
+At position 574 to 693, the domain is characterized as Cadherin 6.
+At position 12 to 196, the domain is characterized as Ku.
+At position 131 to 408, the domain is characterized as Peptidase S8.
+At position 383 to 445, the domain is characterized as SAM.
+At position 484 to 688, the domain is characterized as DDHD.
+At position 43 to 104, the domain is characterized as Chitin-binding type R&R.
+At position 239 to 357, the domain is characterized as Nop.
+At position 30 to 156, the domain is characterized as NTR.
+At position 17 to 122, the domain is characterized as CBM20.
+At position 24 to 97, the domain is characterized as KRAB.
+At position 402 to 840, the domain is characterized as Urease.
+At position 58 to 238, the domain is characterized as PH.
+At position 986 to 1309, the domain is characterized as Protein kinase.
+At position 266 to 449, the domain is characterized as GATase cobBQ-type.
+At position 86 to 139, the domain is characterized as Kazal-like 1.
+At position 159 to 214, the domain is characterized as Kazal-like 2.
+At position 232 to 286, the domain is characterized as Kazal-like 3.
+At position 303 to 358, the domain is characterized as Kazal-like 4.
+At position 379 to 431, the domain is characterized as Kazal-like 5.
+At position 442 to 496, the domain is characterized as Kazal-like 6.
+At position 502 to 561, the domain is characterized as Kazal-like 7.
+At position 594 to 647, the domain is characterized as Kazal-like 8.
+At position 688 to 741, the domain is characterized as Laminin EGF-like 1.
+At position 742 to 788, the domain is characterized as Laminin EGF-like 2.
+At position 812 to 866, the domain is characterized as Kazal-like 9.
+At position 1014 to 1136, the domain is characterized as SEA.
+At position 1211 to 1249, the domain is characterized as EGF-like 1.
+At position 1254 to 1430, the domain is characterized as Laminin G-like 1.
+At position 1431 to 1468, the domain is characterized as EGF-like 2.
+At position 1470 to 1507, the domain is characterized as EGF-like 3.
+At position 1517 to 1699, the domain is characterized as Laminin G-like 2.
+At position 1700 to 1739, the domain is characterized as EGF-like 4.
+At position 1775 to 1947, the domain is characterized as Laminin G-like 3.
+At position 27 to 117, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 85 to 201, the domain is characterized as tRNA-binding.
+At position 456 to 538, the domain is characterized as B5.
+At position 869 to 960, the domain is characterized as FDX-ACB.
+At position 455 to 490, the domain is characterized as EF-hand 2.
+At position 37 to 156, the domain is characterized as HD.
+At position 6 to 150, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 515 to 698, the domain is characterized as Helicase ATP-binding 1.
+At position 742 to 946, the domain is characterized as Helicase C-terminal 1.
+At position 1007 to 1308, the domain is characterized as SEC63 1.
+At position 1361 to 1538, the domain is characterized as Helicase ATP-binding 2.
+At position 1575 to 1772, the domain is characterized as Helicase C-terminal 2.
+At position 1840 to 2157, the domain is characterized as SEC63 2.
+At position 728 to 759, the domain is characterized as LRRNT.
+At position 29 to 157, the domain is characterized as RNase III.
+At position 184 to 253, the domain is characterized as DRBM.
+At position 106 to 195, the domain is characterized as RWP-RK.
+At position 220 to 287, the domain is characterized as BTB.
+At position 297 to 416, the domain is characterized as Response regulatory.
+At position 189 to 368, the domain is characterized as Phosphatase tensin-type.
+At position 375 to 502, the domain is characterized as C2 tensin-type.
+At position 31 to 277, the domain is characterized as GB1/RHD3-type G.
+At position 134 to 185, the domain is characterized as BACK.
+At position 65 to 141, the domain is characterized as Ubiquitin-like.
+At position 160 to 238, the domain is characterized as BAG.
+At position 30 to 72, the domain is characterized as CHCH.
+At position 39 to 346, the domain is characterized as Peptidase A1.
+At position 286 to 425, the domain is characterized as SIS 1.
+At position 26 to 167, the domain is characterized as Tyrosine-protein phosphatase.
+At position 15 to 324, the domain is characterized as Helicase ATP-binding.
+At position 308 to 511, the domain is characterized as MCM.
+At position 150 to 225, the domain is characterized as RRM 1.
+At position 247 to 323, the domain is characterized as RRM 2.
+At position 219 to 583, the domain is characterized as Peptidase S53.
+At position 224 to 391, the domain is characterized as Helicase ATP-binding.
+At position 17 to 91, the domain is characterized as H15.
+At position 33 to 293, the domain is characterized as Protein kinase.
+At position 34 to 140, the domain is characterized as Ig-like 1.
+At position 399 to 499, the domain is characterized as Ig-like 4.
+At position 501 to 593, the domain is characterized as Ig-like 5.
+At position 599 to 699, the domain is characterized as Fibronectin type-III.
+At position 101 to 173, the domain is characterized as Bromo 1.
+At position 271 to 343, the domain is characterized as Bromo 2.
+At position 430 to 510, the domain is characterized as NET.
+At position 32 to 80, the domain is characterized as EGF-like 1.
+At position 81 to 132, the domain is characterized as EGF-like 2.
+At position 173 to 221, the domain is characterized as EGF-like 4; calcium-binding.
+At position 222 to 271, the domain is characterized as EGF-like 5; calcium-binding.
+At position 272 to 318, the domain is characterized as EGF-like 6; calcium-binding.
+At position 319 to 367, the domain is characterized as EGF-like 7; calcium-binding.
+At position 592 to 641, the domain is characterized as GPS.
+At position 115 to 188, the domain is characterized as SH3.
+At position 194 to 284, the domain is characterized as SH2.
+At position 311 to 562, the domain is characterized as Protein kinase.
+At position 22 to 83, the domain is characterized as LCN-type CS-alpha/beta.
+At position 22 to 112, the domain is characterized as N-acetyltransferase.
+At position 49 to 168, the domain is characterized as Rieske.
+At position 76 to 151, the domain is characterized as POTRA.
+At position 1 to 219, the domain is characterized as SPX.
+At position 459 to 654, the domain is characterized as EXS.
+At position 198 to 562, the domain is characterized as Peptidase S53.
+At position 46 to 353, the domain is characterized as HAP1 N-terminal.
+At position 2 to 57, the domain is characterized as HTH deoR-type.
+At position 218 to 252, the domain is characterized as Gla.
+At position 200 to 389, the domain is characterized as VWFA.
+At position 103 to 499, the domain is characterized as PPM-type phosphatase.
+At position 2 to 101, the domain is characterized as GST N-terminal.
+At position 107 to 248, the domain is characterized as GST C-terminal.
+At position 11 to 96, the domain is characterized as BMC.
+At position 39 to 145, the domain is characterized as Ig-like V-type.
+At position 54 to 128, the domain is characterized as FHA.
+At position 648 to 921, the domain is characterized as Protein kinase.
+At position 7 to 489, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 553 to 898, the domain is characterized as UvrD-like helicase C-terminal.
+At position 129 to 205, the domain is characterized as Ubiquitin-like.
+At position 197 to 256, the domain is characterized as CBS 2.
+At position 360 to 419, the domain is characterized as CBS 4.
+At position 38 to 193, the domain is characterized as Cytochrome c.
+At position 10 to 131, the domain is characterized as CMP/dCMP-type deaminase.
+At position 623 to 714, the domain is characterized as GED.
+At position 18 to 330, the domain is characterized as GH10.
+At position 73 to 394, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 403 to 436, the domain is characterized as WW.
+At position 48 to 166, the domain is characterized as FZ.
+At position 29 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 134 to 221, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 342, the domain is characterized as Ig-like C2-type 3.
+At position 35 to 130, the domain is characterized as Ig-like C2-type 1.
+At position 138 to 225, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 327, the domain is characterized as Ig-like C2-type 3.
+At position 332 to 419, the domain is characterized as Ig-like C2-type 4.
+At position 424 to 506, the domain is characterized as Ig-like C2-type 5.
+At position 517 to 600, the domain is characterized as Ig-like C2-type 6.
+At position 613 to 711, the domain is characterized as Fibronectin type-III 1.
+At position 716 to 809, the domain is characterized as Fibronectin type-III 2.
+At position 811 to 916, the domain is characterized as Fibronectin type-III 3.
+At position 919 to 1015, the domain is characterized as Fibronectin type-III 4.
+At position 1014 to 1112, the domain is characterized as Fibronectin type-III 5.
+At position 343 to 513, the domain is characterized as tr-type G.
+At position 339 to 400, the domain is characterized as VWFC 1.
+At position 401 to 438, the domain is characterized as VWFC 2.
+At position 439 to 493, the domain is characterized as VWFC 3.
+At position 494 to 553, the domain is characterized as VWFC 4.
+At position 554 to 610, the domain is characterized as VWFC 5.
+At position 611 to 669, the domain is characterized as VWFC 6.
+At position 670 to 728, the domain is characterized as VWFC 7.
+At position 729 to 786, the domain is characterized as VWFC 8.
+At position 787 to 847, the domain is characterized as VWFC 9.
+At position 848 to 907, the domain is characterized as VWFC 10.
+At position 908 to 966, the domain is characterized as VWFC 11.
+At position 967 to 1025, the domain is characterized as VWFC 12.
+At position 1026 to 1083, the domain is characterized as VWFC 13.
+At position 1084 to 1142, the domain is characterized as VWFC 14.
+At position 1146 to 1203, the domain is characterized as VWFC 15.
+At position 1204 to 1260, the domain is characterized as VWFC 16.
+At position 1261 to 1319, the domain is characterized as VWFC 17.
+At position 1321 to 1377, the domain is characterized as VWFC 18.
+At position 1378 to 1439, the domain is characterized as VWFC 19.
+At position 1440 to 1495, the domain is characterized as VWFC 20.
+At position 1496 to 1555, the domain is characterized as VWFC 21.
+At position 1556 to 1614, the domain is characterized as VWFC 22.
+At position 1615 to 1673, the domain is characterized as VWFC 23.
+At position 1674 to 1731, the domain is characterized as VWFC 24.
+At position 1732 to 1799, the domain is characterized as VWFC 25.
+At position 1800 to 1860, the domain is characterized as VWFC 26.
+At position 1861 to 1924, the domain is characterized as VWFC 27.
+At position 1928 to 1988, the domain is characterized as VWFC 28.
+At position 1992 to 2168, the domain is characterized as VWFD.
+At position 2259 to 2319, the domain is characterized as TIL.
+At position 260 to 309, the domain is characterized as bHLH.
+At position 109 to 128, the domain is characterized as HhH.
+At position 610 to 658, the domain is characterized as F-box.
+At position 191 to 291, the domain is characterized as Fe2OG dioxygenase.
+At position 309 to 368, the domain is characterized as CBS 1.
+At position 372 to 432, the domain is characterized as CBS 2.
+At position 46 to 414, the domain is characterized as FERM.
+At position 433 to 539, the domain is characterized as SH2; atypical.
+At position 582 to 843, the domain is characterized as Protein kinase 1.
+At position 892 to 1164, the domain is characterized as Protein kinase 2.
+At position 46 to 161, the domain is characterized as Ig-like C2-type.
+At position 163 to 268, the domain is characterized as Link 1.
+At position 273 to 365, the domain is characterized as Link 2.
+At position 92 to 664, the domain is characterized as Protein kinase.
+At position 13 to 142, the domain is characterized as RNase III.
+At position 8 to 85, the domain is characterized as KRAB.
+At position 410 to 531, the domain is characterized as Ricin B-type lectin.
+At position 733 to 817, the domain is characterized as PB1.
+At position 27 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 58, the domain is characterized as AGC-kinase C-terminal.
+At position 128 to 205, the domain is characterized as REM-1.
+At position 598 to 664, the domain is characterized as RhoBD.
+At position 767 to 966, the domain is characterized as PH.
+At position 488 to 610, the domain is characterized as HD.
+At position 840 to 915, the domain is characterized as ACT 2.
+At position 363 to 449, the domain is characterized as Disintegrin.
+At position 36 to 278, the domain is characterized as SET.
+At position 376 to 436, the domain is characterized as CBS 1.
+At position 437 to 490, the domain is characterized as CBS 2.
+At position 270 to 509, the domain is characterized as Histidine kinase.
+At position 511 to 645, the domain is characterized as CheW-like.
+At position 660 to 776, the domain is characterized as Response regulatory.
+At position 233 to 426, the domain is characterized as MH2.
+At position 27 to 76, the domain is characterized as UBA.
+At position 254 to 319, the domain is characterized as SH3.
+At position 30 to 132, the domain is characterized as Ig-like V-type.
+At position 51 to 247, the domain is characterized as ABC transmembrane type-1.
+At position 734 to 810, the domain is characterized as Carrier 1.
+At position 1816 to 1892, the domain is characterized as Carrier 2.
+At position 33 to 70, the domain is characterized as VM.
+At position 47 to 88, the domain is characterized as RPE1 insert.
+At position 1 to 94, the domain is characterized as Glutamine amidotransferase type-1.
+At position 7 to 18, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 26 to 343, the domain is characterized as Peptidase S6.
+At position 1597 to 1849, the domain is characterized as Autotransporter.
+At position 242 to 456, the domain is characterized as GT92.
+At position 21 to 158, the domain is characterized as NTR.
+At position 166 to 267, the domain is characterized as PH.
+At position 163 to 268, the domain is characterized as AB hydrolase-1.
+At position 540 to 617, the domain is characterized as Carrier.
+At position 569 to 633, the domain is characterized as KH.
+At position 643 to 711, the domain is characterized as S1 motif.
+At position 446 to 763, the domain is characterized as PDEase.
+At position 635 to 928, the domain is characterized as Autotransporter.
+At position 1081 to 1517, the domain is characterized as CBP/p300-type HAT.
+At position 70 to 260, the domain is characterized as RNase H type-2.
+At position 329 to 633, the domain is characterized as USP.
+At position 310 to 541, the domain is characterized as START.
+At position 208 to 435, the domain is characterized as MIF4G.
+At position 627 to 749, the domain is characterized as MI.
+At position 23 to 73, the domain is characterized as LIM zinc-binding 1.
+At position 82 to 135, the domain is characterized as LIM zinc-binding 2.
+At position 3 to 63, the domain is characterized as MADS-box.
+At position 1 to 63, the domain is characterized as IF rod.
+At position 176 to 261, the domain is characterized as PPIase FKBP-type.
+At position 164 to 356, the domain is characterized as CheB-type methylesterase.
+At position 683 to 964, the domain is characterized as Autotransporter.
+At position 311 to 499, the domain is characterized as Histidine kinase.
+At position 21 to 106, the domain is characterized as BMC 1.
+At position 1134 to 1280, the domain is characterized as RUN 2.
+At position 49 to 182, the domain is characterized as C2.
+At position 26 to 108, the domain is characterized as SCAN box.
+At position 208 to 254, the domain is characterized as KRAB.
+At position 179 to 443, the domain is characterized as Protein kinase.
+At position 313 to 438, the domain is characterized as DBINO.
+At position 547 to 718, the domain is characterized as Helicase ATP-binding.
+At position 1160 to 1315, the domain is characterized as Helicase C-terminal.
+At position 407 to 453, the domain is characterized as F-box.
+At position 18 to 252, the domain is characterized as ABC transporter.
+At position 186 to 372, the domain is characterized as Glutamine amidotransferase type-1.
+At position 326 to 422, the domain is characterized as Rhodanese.
+At position 160 to 189, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 188 to 216, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 211 to 407, the domain is characterized as Peptidase M12B.
+At position 431 to 529, the domain is characterized as Disintegrin.
+At position 702 to 751, the domain is characterized as TSP type-1 1.
+At position 757 to 811, the domain is characterized as TSP type-1 2.
+At position 813 to 861, the domain is characterized as TSP type-1 3.
+At position 863 to 911, the domain is characterized as TSP type-1 4.
+At position 915 to 963, the domain is characterized as TSP type-1 5.
+At position 966 to 1015, the domain is characterized as TSP type-1 6.
+At position 36 to 209, the domain is characterized as CP-type G.
+At position 24 to 243, the domain is characterized as RNase H type-2.
+At position 5 to 265, the domain is characterized as ABC transporter.
+At position 280 to 336, the domain is characterized as CBS 1.
+At position 340 to 397, the domain is characterized as CBS 2.
+At position 1240 to 1329, the domain is characterized as EH.
+At position 1273 to 1308, the domain is characterized as EF-hand.
+At position 4 to 121, the domain is characterized as MTTase N-terminal.
+At position 379 to 442, the domain is characterized as TRAM.
+At position 1 to 28, the domain is characterized as GST N-terminal.
+At position 20 to 159, the domain is characterized as Calponin-homology (CH).
+At position 252 to 324, the domain is characterized as GAR.
+At position 1 to 139, the domain is characterized as TCTP.
+At position 10 to 101, the domain is characterized as HIG1.
+At position 33 to 295, the domain is characterized as F-BAR.
+At position 472 to 663, the domain is characterized as Rho-GAP.
+At position 462 to 575, the domain is characterized as CFEM.
+At position 564 to 834, the domain is characterized as Protein kinase.
+At position 49 to 396, the domain is characterized as GH26.
+At position 523 to 703, the domain is characterized as CBM11 1.
+At position 717 to 897, the domain is characterized as CBM11 2.
+At position 137 to 277, the domain is characterized as Fatty acid hydroxylase.
+At position 1 to 93, the domain is characterized as HTH arsR-type.
+At position 136 to 222, the domain is characterized as RRM.
+At position 265 to 503, the domain is characterized as tr-type G.
+At position 38 to 202, the domain is characterized as Exonuclease.
+At position 17 to 169, the domain is characterized as NAC.
+At position 19 to 269, the domain is characterized as Pyruvate carboxyltransferase.
+At position 29 to 155, the domain is characterized as Thioredoxin 1.
+At position 355 to 499, the domain is characterized as Thioredoxin 2.
+At position 2 to 170, the domain is characterized as Miro 1.
+At position 421 to 585, the domain is characterized as Miro 2.
+At position 331 to 860, the domain is characterized as USP.
+At position 647 to 688, the domain is characterized as UBA 1.
+At position 158 to 390, the domain is characterized as Radical SAM core.
+At position 393 to 464, the domain is characterized as TRAM.
+At position 728 to 902, the domain is characterized as SHD.
+At position 906 to 1219, the domain is characterized as MHD.
+At position 280 to 344, the domain is characterized as SAM.
+At position 297 to 350, the domain is characterized as TSP type-1 1.
+At position 352 to 405, the domain is characterized as TSP type-1 2.
+At position 408 to 461, the domain is characterized as TSP type-1 3.
+At position 804 to 856, the domain is characterized as GPS.
+At position 80 to 156, the domain is characterized as Biotinyl-binding.
+At position 54 to 202, the domain is characterized as Tyrosine-protein phosphatase.
+At position 131 to 440, the domain is characterized as NACHT.
+At position 794 to 1077, the domain is characterized as FIIND.
+At position 1087 to 1170, the domain is characterized as CARD.
+At position 42 to 292, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 22 to 211, the domain is characterized as Albumin 1.
+At position 212 to 401, the domain is characterized as Albumin 2.
+At position 402 to 599, the domain is characterized as Albumin 3.
+At position 9 to 127, the domain is characterized as C2 B9-type.
+At position 93 to 296, the domain is characterized as Helicase ATP-binding.
+At position 610 to 774, the domain is characterized as Toprim.
+At position 266 to 407, the domain is characterized as Flavodoxin-like.
+At position 12 to 118, the domain is characterized as MTTase N-terminal.
+At position 141 to 370, the domain is characterized as Radical SAM core.
+At position 373 to 427, the domain is characterized as TRAM.
+At position 167 to 277, the domain is characterized as MATH.
+At position 317 to 380, the domain is characterized as BTB.
+At position 109 to 525, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1012 to 1318, the domain is characterized as PKS/mFAS DH.
+At position 1356 to 1433, the domain is characterized as Carrier 1.
+At position 1472 to 1546, the domain is characterized as Carrier 2.
+At position 424 to 511, the domain is characterized as RRM.
+At position 85 to 389, the domain is characterized as Peptidase A1.
+At position 263 to 446, the domain is characterized as Helicase ATP-binding.
+At position 727 to 890, the domain is characterized as Helicase C-terminal.
+At position 172 to 332, the domain is characterized as Helicase ATP-binding.
+At position 368 to 536, the domain is characterized as Helicase C-terminal.
+At position 34 to 112, the domain is characterized as ACT 1.
+At position 115 to 197, the domain is characterized as ACT 2.
+At position 246 to 322, the domain is characterized as ACT 3.
+At position 324 to 404, the domain is characterized as ACT 4.
+At position 70 to 210, the domain is characterized as RanBD1.
+At position 144 to 375, the domain is characterized as NR LBD.
+At position 18 to 239, the domain is characterized as AB hydrolase-1.
+At position 170 to 297, the domain is characterized as Arf-GAP.
+At position 22 to 153, the domain is characterized as Nudix hydrolase.
+At position 2131 to 2319, the domain is characterized as Rho-GAP.
+At position 581 to 724, the domain is characterized as NTR.
+At position 12 to 194, the domain is characterized as YrdC-like.
+At position 63 to 340, the domain is characterized as tr-type G.
+At position 1 to 420, the domain is characterized as PTS EIIC type-1.
+At position 448 to 530, the domain is characterized as PTS EIIB type-1.
+At position 313 to 506, the domain is characterized as B30.2/SPRY.
+At position 511 to 653, the domain is characterized as HD.
+At position 605 to 713, the domain is characterized as Cadherin 5.
+At position 20 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 417 to 580, the domain is characterized as Miro 2.
+At position 548 to 731, the domain is characterized as N-acetyltransferase.
+At position 40 to 312, the domain is characterized as Deacetylase sirtuin-type.
+At position 46 to 110, the domain is characterized as Ig-like C2-type 1.
+At position 421 to 548, the domain is characterized as Ig-like C2-type 5.
+At position 551 to 660, the domain is characterized as Ig-like C2-type 6.
+At position 667 to 753, the domain is characterized as Ig-like C2-type 7.
+At position 834 to 1162, the domain is characterized as Protein kinase.
+At position 8 to 142, the domain is characterized as MPN.
+At position 35 to 194, the domain is characterized as SIS.
+At position 260 to 287, the domain is characterized as KOW 1.
+At position 412 to 439, the domain is characterized as KOW 2.
+At position 464 to 491, the domain is characterized as KOW 3.
+At position 588 to 615, the domain is characterized as KOW 4.
+At position 683 to 710, the domain is characterized as KOW 5.
+At position 936 to 963, the domain is characterized as KOW 6.
+At position 1 to 198, the domain is characterized as CNNM transmembrane.
+At position 217 to 280, the domain is characterized as CBS 1.
+At position 285 to 342, the domain is characterized as CBS 2.
+At position 33 to 153, the domain is characterized as BTB.
+At position 212 to 281, the domain is characterized as BACK.
+At position 148 to 665, the domain is characterized as USP.
+At position 667 to 760, the domain is characterized as DUSP 1.
+At position 768 to 871, the domain is characterized as DUSP 2.
+At position 329 to 348, the domain is characterized as UIM 3.
+At position 7 to 120, the domain is characterized as HIT.
+At position 318 to 357, the domain is characterized as STI1.
+At position 345 to 471, the domain is characterized as C2 3.
+At position 357 to 636, the domain is characterized as Protein kinase.
+At position 29 to 98, the domain is characterized as S1 motif 1.
+At position 116 to 180, the domain is characterized as S1 motif 2.
+At position 169 to 244, the domain is characterized as RRM 1.
+At position 266 to 341, the domain is characterized as RRM 2.
+At position 33 to 368, the domain is characterized as PPM-type phosphatase.
+At position 4 to 69, the domain is characterized as HMA 1.
+At position 71 to 137, the domain is characterized as HMA 2.
+At position 25 to 85, the domain is characterized as Pre-SET.
+At position 88 to 210, the domain is characterized as SET.
+At position 218 to 234, the domain is characterized as Post-SET.
+At position 25 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 216 to 408, the domain is characterized as GMPS ATP-PPase.
+At position 38 to 109, the domain is characterized as PAS.
+At position 109 to 163, the domain is characterized as PAC.
+At position 6 to 80, the domain is characterized as RRM 1.
+At position 98 to 187, the domain is characterized as RRM 2.
+At position 245 to 319, the domain is characterized as RRM 3.
+At position 355 to 429, the domain is characterized as RRM 4.
+At position 6 to 128, the domain is characterized as MsrB.
+At position 344 to 465, the domain is characterized as Thioredoxin.
+At position 1550 to 1680, the domain is characterized as MaoC-like.
+At position 79 to 237, the domain is characterized as Thioredoxin.
+At position 32 to 123, the domain is characterized as Ubiquitin-like.
+At position 427 to 492, the domain is characterized as KH 3.
+At position 509 to 575, the domain is characterized as KH 4.
+At position 450 to 717, the domain is characterized as Reverse transcriptase.
+At position 539 to 888, the domain is characterized as PUM-HD.
+At position 552 to 721, the domain is characterized as tr-type G.
+At position 103 to 169, the domain is characterized as EamA 1.
+At position 191 to 316, the domain is characterized as EamA 2.
+At position 1224 to 1489, the domain is characterized as Protein kinase.
+At position 1133 to 1332, the domain is characterized as PH.
+At position 512 to 588, the domain is characterized as Carrier.
+At position 86 to 403, the domain is characterized as FERM.
+At position 2292 to 2531, the domain is characterized as I/LWEQ.
+At position 149 to 266, the domain is characterized as C2.
+At position 325 to 583, the domain is characterized as Protein kinase.
+At position 584 to 654, the domain is characterized as AGC-kinase C-terminal.
+At position 123 to 364, the domain is characterized as Radical SAM core.
+At position 33 to 237, the domain is characterized as Eph LBD.
+At position 369 to 486, the domain is characterized as Fibronectin type-III 1.
+At position 487 to 582, the domain is characterized as Fibronectin type-III 2.
+At position 670 to 919, the domain is characterized as Protein kinase.
+At position 948 to 1012, the domain is characterized as SAM.
+At position 7 to 241, the domain is characterized as ABC transporter.
+At position 107 to 298, the domain is characterized as ATP-grasp.
+At position 260 to 378, the domain is characterized as C-type lectin.
+At position 48 to 301, the domain is characterized as GB1/RHD3-type G.
+At position 58 to 176, the domain is characterized as SEA.
+At position 207 to 438, the domain is characterized as Peptidase S1.
+At position 30 to 68, the domain is characterized as EGF-like 1.
+At position 70 to 108, the domain is characterized as EGF-like 2.
+At position 110 to 146, the domain is characterized as EGF-like 3.
+At position 148 to 184, the domain is characterized as EGF-like 4; calcium-binding.
+At position 186 to 222, the domain is characterized as EGF-like 5; calcium-binding.
+At position 224 to 260, the domain is characterized as EGF-like 6; calcium-binding.
+At position 262 to 299, the domain is characterized as EGF-like 7; calcium-binding.
+At position 301 to 337, the domain is characterized as EGF-like 8.
+At position 339 to 395, the domain is characterized as EGF-like 9.
+At position 397 to 439, the domain is characterized as EGF-like 10; calcium-binding.
+At position 441 to 481, the domain is characterized as EGF-like 11.
+At position 485 to 670, the domain is characterized as Laminin G-like 1.
+At position 672 to 708, the domain is characterized as EGF-like 12.
+At position 714 to 885, the domain is characterized as Laminin G-like 2.
+At position 887 to 923, the domain is characterized as EGF-like 13.
+At position 924 to 960, the domain is characterized as EGF-like 14.
+At position 950 to 1137, the domain is characterized as Laminin G-like 3.
+At position 1139 to 1175, the domain is characterized as EGF-like 15.
+At position 1177 to 1212, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1214 to 1250, the domain is characterized as EGF-like 17.
+At position 1255 to 1295, the domain is characterized as EGF-like 18.
+At position 1297 to 1333, the domain is characterized as EGF-like 19; calcium-binding.
+At position 21 to 271, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 91 to 324, the domain is characterized as ATP-grasp.
+At position 67 to 261, the domain is characterized as Peptidase M12A.
+At position 265 to 434, the domain is characterized as MAM.
+At position 435 to 596, the domain is characterized as MATH.
+At position 672 to 712, the domain is characterized as EGF-like.
+At position 63 to 138, the domain is characterized as ACT.
+At position 177 to 312, the domain is characterized as ADF-H 2.
+At position 33 to 168, the domain is characterized as MPN.
+At position 5 to 281, the domain is characterized as tr-type G.
+At position 254 to 415, the domain is characterized as W2.
+At position 294 to 452, the domain is characterized as Obg.
+At position 453 to 621, the domain is characterized as OBG-type G.
+At position 649 to 728, the domain is characterized as OCT.
+At position 41 to 123, the domain is characterized as EMI.
+At position 113 to 148, the domain is characterized as EGF-like 1.
+At position 246 to 276, the domain is characterized as EGF-like 4.
+At position 553 to 587, the domain is characterized as EGF-like 5.
+At position 75 to 110, the domain is characterized as Tify.
+At position 206 to 462, the domain is characterized as GH16.
+At position 224 to 467, the domain is characterized as NR LBD.
+At position 367 to 428, the domain is characterized as SAM.
+At position 221 to 376, the domain is characterized as TrmE-type G.
+At position 1042 to 1099, the domain is characterized as SH3.
+At position 6 to 137, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 21 to 227, the domain is characterized as MARVEL.
+At position 1 to 71, the domain is characterized as Ubiquitin-like.
+At position 101 to 465, the domain is characterized as USP.
+At position 20 to 250, the domain is characterized as HORMA.
+At position 25 to 264, the domain is characterized as ABC transporter.
+At position 9 to 91, the domain is characterized as Doublecortin 1.
+At position 129 to 211, the domain is characterized as Doublecortin 2.
+At position 117 to 289, the domain is characterized as Helicase ATP-binding.
+At position 334 to 511, the domain is characterized as Helicase C-terminal.
+At position 89 to 206, the domain is characterized as C-type lectin.
+At position 20 to 215, the domain is characterized as Lon N-terminal.
+At position 602 to 781, the domain is characterized as Lon proteolytic.
+At position 391 to 489, the domain is characterized as Zinc-hook.
+At position 158 to 343, the domain is characterized as Helicase ATP-binding.
+At position 372 to 528, the domain is characterized as Helicase C-terminal.
+At position 780 to 1213, the domain is characterized as CBP/p300-type HAT.
+At position 474 to 708, the domain is characterized as Glycoamylase-like.
+At position 78 to 253, the domain is characterized as VWFA.
+At position 259 to 300, the domain is characterized as EGF-like 1.
+At position 301 to 342, the domain is characterized as EGF-like 2.
+At position 343 to 384, the domain is characterized as EGF-like 3.
+At position 385 to 426, the domain is characterized as EGF-like 4.
+At position 9 to 88, the domain is characterized as Kringle 5.
+At position 109 to 336, the domain is characterized as Peptidase S1.
+At position 85 to 116, the domain is characterized as LisH.
+At position 130 to 213, the domain is characterized as CTLH.
+At position 76 to 120, the domain is characterized as CHCH.
+At position 114 to 323, the domain is characterized as SMP-LTD.
+At position 305 to 392, the domain is characterized as DIX.
+At position 43 to 90, the domain is characterized as F-box.
+At position 56 to 116, the domain is characterized as SH3.
+At position 122 to 219, the domain is characterized as SH2.
+At position 134 to 331, the domain is characterized as MH2.
+At position 107 to 181, the domain is characterized as POU-specific.
+At position 1 to 370, the domain is characterized as Protein kinase.
+At position 46 to 314, the domain is characterized as Protein kinase.
+At position 7 to 115, the domain is characterized as NTF2.
+At position 943 to 975, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 976 to 1006, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 448 to 617, the domain is characterized as tr-type G.
+At position 84 to 135, the domain is characterized as SANT.
+At position 329 to 518, the domain is characterized as Protein kinase.
+At position 178 to 222, the domain is characterized as bZIP.
+At position 241 to 455, the domain is characterized as DOG1.
+At position 4 to 218, the domain is characterized as tr-type G.
+At position 171 to 444, the domain is characterized as ABC transporter 1.
+At position 867 to 1119, the domain is characterized as ABC transporter 2.
+At position 1192 to 1406, the domain is characterized as ABC transmembrane type-2 2.
+At position 1199 to 1605, the domain is characterized as DOCKER.
+At position 555 to 662, the domain is characterized as PH.
+At position 799 to 1013, the domain is characterized as Rho-GAP.
+At position 14 to 104, the domain is characterized as PDZ GRASP-type 1.
+At position 110 to 198, the domain is characterized as PDZ GRASP-type 2.
+At position 27 to 63, the domain is characterized as CBM1.
+At position 274 to 425, the domain is characterized as N-acetyltransferase.
+At position 51 to 393, the domain is characterized as TTL.
+At position 228 to 305, the domain is characterized as TFIIS N-terminal.
+At position 69 to 211, the domain is characterized as SCP.
+At position 377 to 412, the domain is characterized as EF-hand.
+At position 179 to 264, the domain is characterized as PDZ.
+At position 789 to 908, the domain is characterized as C2.
+At position 948 to 1148, the domain is characterized as Rho-GAP.
+At position 21 to 301, the domain is characterized as GH10.
+At position 1326 to 1636, the domain is characterized as PKS/mFAS DH.
+At position 1725 to 1802, the domain is characterized as Carrier.
+At position 249 to 446, the domain is characterized as GATase cobBQ-type.
+At position 78 to 175, the domain is characterized as Fe2OG dioxygenase.
+At position 220 to 448, the domain is characterized as NR LBD.
+At position 154 to 251, the domain is characterized as HTH araC/xylS-type.
+At position 401 to 450, the domain is characterized as bHLH.
+At position 165 to 398, the domain is characterized as Radical SAM core.
+At position 84 to 224, the domain is characterized as Clp R.
+At position 97 to 175, the domain is characterized as RRM 1.
+At position 191 to 269, the domain is characterized as RRM 2.
+At position 20 to 53, the domain is characterized as CBM1.
+At position 453 to 594, the domain is characterized as SIS 2.
+At position 28 to 60, the domain is characterized as EF-hand 1.
+At position 175 to 210, the domain is characterized as EF-hand 2.
+At position 211 to 246, the domain is characterized as EF-hand 3.
+At position 296 to 410, the domain is characterized as DUSP.
+At position 570 to 1175, the domain is characterized as USP.
+At position 220 to 266, the domain is characterized as F-box.
+At position 62 to 200, the domain is characterized as SCP.
+At position 284 to 379, the domain is characterized as LCCL 1.
+At position 385 to 488, the domain is characterized as LCCL 2.
+At position 676 to 755, the domain is characterized as Ras-associating.
+At position 1357 to 1624, the domain is characterized as PPM-type phosphatase.
+At position 1668 to 1805, the domain is characterized as Guanylate cyclase.
+At position 929 to 995, the domain is characterized as VWFC.
+At position 1062 to 1146, the domain is characterized as CTCK.
+At position 307 to 452, the domain is characterized as JmjC.
+At position 389 to 532, the domain is characterized as RCK N-terminal.
+At position 2 to 232, the domain is characterized as GH18.
+At position 52 to 82, the domain is characterized as EF-hand 2.
+At position 144 to 228, the domain is characterized as RCK C-terminal 1.
+At position 235 to 360, the domain is characterized as RCK N-terminal 2.
+At position 372 to 453, the domain is characterized as RCK C-terminal 2.
+At position 92 to 220, the domain is characterized as FAD-binding FR-type.
+At position 361 to 796, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1290 to 1600, the domain is characterized as PKS/mFAS DH.
+At position 1671 to 1745, the domain is characterized as Carrier.
+At position 55 to 354, the domain is characterized as AB hydrolase-1.
+At position 574 to 785, the domain is characterized as ATP-grasp.
+At position 177 to 321, the domain is characterized as NTR.
+At position 83 to 247, the domain is characterized as TNase-like.
+At position 502 to 606, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 93 to 142, the domain is characterized as bHLH.
+At position 232 to 270, the domain is characterized as EGF-like.
+At position 384 to 494, the domain is characterized as Fibronectin type-III.
+At position 495 to 672, the domain is characterized as B30.2/SPRY.
+At position 61 to 145, the domain is characterized as PA.
+At position 19 to 54, the domain is characterized as EF-hand.
+At position 106 to 250, the domain is characterized as PI-PLC X-box.
+At position 296 to 412, the domain is characterized as PI-PLC Y-box.
+At position 406 to 539, the domain is characterized as C2.
+At position 2 to 186, the domain is characterized as EngB-type G.
+At position 493 to 671, the domain is characterized as Helicase C-terminal.
+At position 1 to 121, the domain is characterized as MSP.
+At position 18 to 287, the domain is characterized as Protein kinase.
+At position 344 to 463, the domain is characterized as C2 1.
+At position 499 to 634, the domain is characterized as C2 2.
+At position 11 to 217, the domain is characterized as ABC transmembrane type-1.
+At position 45 to 197, the domain is characterized as SIS 1.
+At position 215 to 364, the domain is characterized as SIS 2.
+At position 693 to 888, the domain is characterized as ATP-grasp 2.
+At position 957 to 1113, the domain is characterized as MGS-like.
+At position 490 to 643, the domain is characterized as Helicase C-terminal.
+At position 176 to 329, the domain is characterized as Integrase catalytic.
+At position 165 to 216, the domain is characterized as LRRCT 1.
+At position 229 to 270, the domain is characterized as LRRNT.
+At position 352 to 404, the domain is characterized as LRRCT 2.
+At position 168 to 762, the domain is characterized as USP.
+At position 1 to 319, the domain is characterized as Alpha-carbonic anhydrase.
+At position 41 to 158, the domain is characterized as SCP.
+At position 25 to 123, the domain is characterized as Ig-like V-type.
+At position 102 to 178, the domain is characterized as WWE.
+At position 227 to 573, the domain is characterized as USP.
+At position 35 to 363, the domain is characterized as Deacetylase sirtuin-type.
+At position 219 to 307, the domain is characterized as GAT.
+At position 34 to 204, the domain is characterized as FAD-binding PCMH-type.
+At position 146 to 350, the domain is characterized as Histidine kinase.
+At position 11 to 242, the domain is characterized as Glutamine amidotransferase type-1.
+At position 35 to 206, the domain is characterized as FAD-binding PCMH-type.
+At position 172 to 246, the domain is characterized as Toprim.
+At position 535 to 653, the domain is characterized as BRCT.
+At position 41 to 163, the domain is characterized as FZ.
+At position 17 to 119, the domain is characterized as Chorein N-terminal.
+At position 44 to 325, the domain is characterized as GH10.
+At position 27 to 131, the domain is characterized as AB hydrolase-1.
+At position 7 to 160, the domain is characterized as MPN.
+At position 161 to 327, the domain is characterized as OBG-type G.
+At position 9 to 61, the domain is characterized as F-box.
+At position 59 to 262, the domain is characterized as PIK helical.
+At position 554 to 820, the domain is characterized as PI3K/PI4K catalytic.
+At position 27 to 122, the domain is characterized as HPt.
+At position 11 to 63, the domain is characterized as HAMP.
+At position 68 to 138, the domain is characterized as PAS.
+At position 132 to 185, the domain is characterized as PAC.
+At position 189 to 409, the domain is characterized as Histidine kinase.
+At position 1 to 49, the domain is characterized as TGS.
+At position 230 to 280, the domain is characterized as F-box.
+At position 387 to 448, the domain is characterized as TGS.
+At position 631 to 705, the domain is characterized as ACT.
+At position 155 to 335, the domain is characterized as Helicase ATP-binding.
+At position 368 to 542, the domain is characterized as N-acetyltransferase.
+At position 81 to 257, the domain is characterized as CRAL-TRIO.
+At position 55 to 94, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 169 to 318, the domain is characterized as C-CAP/cofactor C-like.
+At position 93 to 394, the domain is characterized as Protein kinase.
+At position 395 to 463, the domain is characterized as AGC-kinase C-terminal.
+At position 79 to 143, the domain is characterized as TGS.
+At position 41 to 112, the domain is characterized as KRAB.
+At position 1 to 60, the domain is characterized as Response regulatory.
+At position 11 to 335, the domain is characterized as YjeF C-terminal.
+At position 3 to 107, the domain is characterized as Phytocyanin.
+At position 89 to 416, the domain is characterized as USP.
+At position 457 to 551, the domain is characterized as DUSP 1.
+At position 567 to 697, the domain is characterized as DUSP 2.
+At position 717 to 830, the domain is characterized as DUSP 3.
+At position 961 to 1012, the domain is characterized as Ubiquitin-like.
+At position 306 to 593, the domain is characterized as Protein kinase.
+At position 22 to 80, the domain is characterized as LCN-type CS-alpha/beta.
+At position 47 to 122, the domain is characterized as RRM.
+At position 60 to 164, the domain is characterized as Cadherin 1.
+At position 165 to 273, the domain is characterized as Cadherin 2.
+At position 274 to 392, the domain is characterized as Cadherin 3.
+At position 389 to 493, the domain is characterized as Cadherin 4.
+At position 493 to 615, the domain is characterized as Cadherin 5.
+At position 59 to 286, the domain is characterized as Radical SAM core.
+At position 22 to 340, the domain is characterized as Protein kinase.
+At position 341 to 404, the domain is characterized as AGC-kinase C-terminal.
+At position 359 to 416, the domain is characterized as S4 RNA-binding.
+At position 132 to 262, the domain is characterized as Galectin.
+At position 47 to 210, the domain is characterized as EngA-type G 1.
+At position 221 to 394, the domain is characterized as EngA-type G 2.
+At position 395 to 477, the domain is characterized as KH-like.
+At position 91 to 163, the domain is characterized as PRC barrel.
+At position 36 to 88, the domain is characterized as Kazal-like.
+At position 91 to 157, the domain is characterized as Thyroglobulin type-1 1.
+At position 234 to 302, the domain is characterized as Thyroglobulin type-1 2.
+At position 406 to 441, the domain is characterized as EF-hand 2.
+At position 230 to 396, the domain is characterized as Helicase ATP-binding.
+At position 487 to 643, the domain is characterized as Helicase C-terminal.
+At position 255 to 329, the domain is characterized as U-box.
+At position 1 to 100, the domain is characterized as HTH arsR-type.
+At position 413 to 481, the domain is characterized as SH3b.
+At position 19 to 108, the domain is characterized as RH1.
+At position 125 to 197, the domain is characterized as RH2.
+At position 625 to 705, the domain is characterized as S1 motif.
+At position 6 to 98, the domain is characterized as Stress-response A/B barrel.
+At position 188 to 305, the domain is characterized as C-type lectin.
+At position 252 to 320, the domain is characterized as FF 1.
+At position 365 to 419, the domain is characterized as FF 2.
+At position 426 to 480, the domain is characterized as FF 3.
+At position 482 to 547, the domain is characterized as FF 4.
+At position 592 to 765, the domain is characterized as pG1 pseudoGTPase.
+At position 766 to 926, the domain is characterized as pG2 pseudoGTPase.
+At position 1349 to 1552, the domain is characterized as Rho-GAP.
+At position 215 to 374, the domain is characterized as TrmE-type G.
+At position 19 to 146, the domain is characterized as Cyclin N-terminal.
+At position 63 to 194, the domain is characterized as VIT.
+At position 346 to 515, the domain is characterized as VWFA.
+At position 29 to 67, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 152 to 296, the domain is characterized as TRUD.
+At position 3 to 237, the domain is characterized as PTS EIIC type-4.
+At position 22 to 106, the domain is characterized as WWE.
+At position 123 to 338, the domain is characterized as PARP catalytic.
+At position 19 to 121, the domain is characterized as Ig-like V-type.
+At position 77 to 225, the domain is characterized as FAS1.
+At position 19 to 116, the domain is characterized as PPIase FKBP-type.
+At position 35 to 85, the domain is characterized as Myosin N-terminal SH3-like.
+At position 89 to 767, the domain is characterized as Myosin motor.
+At position 10 to 353, the domain is characterized as Kinesin motor.
+At position 11 to 278, the domain is characterized as Hcy-binding.
+At position 36 to 327, the domain is characterized as YjeF C-terminal.
+At position 25 to 171, the domain is characterized as PTS EIIA type-2.
+At position 186 to 282, the domain is characterized as PTS EIIB type-2.
+At position 306 to 641, the domain is characterized as PTS EIIC type-2.
+At position 8 to 201, the domain is characterized as Glutamine amidotransferase type-1.
+At position 202 to 393, the domain is characterized as GMPS ATP-PPase.
+At position 205 to 274, the domain is characterized as bHLH.
+At position 243 to 302, the domain is characterized as SH3 1.
+At position 303 to 360, the domain is characterized as SH3 2.
+At position 1032 to 1078, the domain is characterized as F-box.
+At position 306 to 400, the domain is characterized as Fibronectin type-III.
+At position 514 to 775, the domain is characterized as Protein kinase.
+At position 804 to 868, the domain is characterized as SAM.
+At position 22 to 474, the domain is characterized as Biotin carboxylation.
+At position 144 to 341, the domain is characterized as ATP-grasp.
+At position 561 to 828, the domain is characterized as Pyruvate carboxyltransferase.
+At position 92 to 246, the domain is characterized as RNase NYN.
+At position 93 to 186, the domain is characterized as BRICHOS.
+At position 312 to 336, the domain is characterized as NAF.
+At position 294 to 471, the domain is characterized as CRAL-TRIO.
+At position 499 to 646, the domain is characterized as GOLD.
+At position 48 to 158, the domain is characterized as PLAT.
+At position 161 to 334, the domain is characterized as OBG-type G.
+At position 1276 to 1403, the domain is characterized as RNase III 1.
+At position 1661 to 1819, the domain is characterized as RNase III 2.
+At position 1844 to 1909, the domain is characterized as DRBM.
+At position 19 to 128, the domain is characterized as Ig-like.
+At position 18 to 73, the domain is characterized as bHLH.
+At position 89 to 122, the domain is characterized as Orange.
+At position 106 to 357, the domain is characterized as Protein kinase.
+At position 210 to 596, the domain is characterized as Peptidase S53.
+At position 16 to 344, the domain is characterized as SAM-dependent MTase C5-type.
+At position 17 to 298, the domain is characterized as ABC transmembrane type-1.
+At position 321 to 561, the domain is characterized as ABC transporter.
+At position 339 to 526, the domain is characterized as Helicase C-terminal.
+At position 10 to 466, the domain is characterized as Hexokinase.
+At position 616 to 722, the domain is characterized as PH.
+At position 127 to 282, the domain is characterized as N-acetyltransferase.
+At position 369 to 439, the domain is characterized as Bromo.
+At position 83 to 274, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 25 to 151, the domain is characterized as Bulb-type lectin 1.
+At position 154 to 279, the domain is characterized as Bulb-type lectin 2.
+At position 283 to 320, the domain is characterized as EGF-like; atypical.
+At position 332 to 413, the domain is characterized as Apple.
+At position 466 to 764, the domain is characterized as Protein kinase.
+At position 49 to 286, the domain is characterized as Laminin N-terminal.
+At position 287 to 342, the domain is characterized as Laminin EGF-like 1.
+At position 343 to 405, the domain is characterized as Laminin EGF-like 2.
+At position 406 to 455, the domain is characterized as Laminin EGF-like 3.
+At position 474 to 603, the domain is characterized as NTR.
+At position 259 to 376, the domain is characterized as Sox C-terminal.
+At position 194 to 255, the domain is characterized as Thyroglobulin type-1.
+At position 73 to 108, the domain is characterized as EF-hand 1.
+At position 109 to 139, the domain is characterized as EF-hand 2.
+At position 140 to 175, the domain is characterized as EF-hand 3.
+At position 1 to 254, the domain is characterized as Pyruvate carboxyltransferase.
+At position 91 to 219, the domain is characterized as FAD-binding FR-type.
+At position 16 to 76, the domain is characterized as LCN-type CS-alpha/beta.
+At position 121 to 209, the domain is characterized as Fibronectin type-III 1.
+At position 207 to 291, the domain is characterized as Fibronectin type-III 2.
+At position 271 to 364, the domain is characterized as Fibronectin type-III 3.
+At position 368 to 456, the domain is characterized as Fibronectin type-III 4.
+At position 457 to 541, the domain is characterized as Fibronectin type-III 5.
+At position 542 to 623, the domain is characterized as Fibronectin type-III 6.
+At position 625 to 720, the domain is characterized as Fibronectin type-III 7.
+At position 721 to 817, the domain is characterized as Fibronectin type-III 8.
+At position 816 to 902, the domain is characterized as Fibronectin type-III 9.
+At position 1041 to 1298, the domain is characterized as Tyrosine-protein phosphatase.
+At position 36 to 271, the domain is characterized as MIF4G.
+At position 33 to 316, the domain is characterized as Rab-GAP TBC.
+At position 2 to 40, the domain is characterized as Sin.
+At position 156 to 202, the domain is characterized as G-patch.
+At position 1 to 256, the domain is characterized as Deacetylase sirtuin-type.
+At position 477 to 599, the domain is characterized as HD.
+At position 719 to 801, the domain is characterized as ACT 1.
+At position 829 to 904, the domain is characterized as ACT 2.
+At position 5 to 168, the domain is characterized as PPIase cyclophilin-type.
+At position 231 to 342, the domain is characterized as C-type lectin.
+At position 87 to 117, the domain is characterized as Cystatin.
+At position 627 to 689, the domain is characterized as LIM zinc-binding.
+At position 22 to 302, the domain is characterized as SET.
+At position 2 to 202, the domain is characterized as ABC transporter.
+At position 474 to 537, the domain is characterized as SAM 1.
+At position 543 to 607, the domain is characterized as SAM 2.
+At position 364 to 495, the domain is characterized as Nudix hydrolase.
+At position 289 to 468, the domain is characterized as Helicase ATP-binding.
+At position 501 to 645, the domain is characterized as Helicase C-terminal.
+At position 3 to 203, the domain is characterized as DPCK.
+At position 18 to 167, the domain is characterized as Thioredoxin.
+At position 11 to 201, the domain is characterized as RNase H type-2.
+At position 39 to 417, the domain is characterized as Helicase ATP-binding.
+At position 442 to 604, the domain is characterized as Helicase C-terminal.
+At position 153 to 239, the domain is characterized as PDZ 2.
+At position 253 to 337, the domain is characterized as PDZ 3.
+At position 458 to 547, the domain is characterized as PDZ 4.
+At position 559 to 643, the domain is characterized as PDZ 5.
+At position 658 to 740, the domain is characterized as PDZ 6.
+At position 942 to 1024, the domain is characterized as PDZ 7.
+At position 99 to 300, the domain is characterized as ATP-grasp.
+At position 35 to 112, the domain is characterized as IGFBP N-terminal.
+At position 334 to 391, the domain is characterized as VWFC 1.
+At position 401 to 457, the domain is characterized as VWFC 2.
+At position 469 to 498, the domain is characterized as Antistasin-like 1.
+At position 505 to 532, the domain is characterized as Antistasin-like 2.
+At position 539 to 564, the domain is characterized as Antistasin-like 3.
+At position 567 to 592, the domain is characterized as Antistasin-like 4.
+At position 606 to 663, the domain is characterized as VWFC 3.
+At position 677 to 735, the domain is characterized as VWFC 4.
+At position 751 to 809, the domain is characterized as VWFC 5.
+At position 817 to 874, the domain is characterized as VWFC 6.
+At position 25 to 133, the domain is characterized as Ig-like V-type.
+At position 43 to 159, the domain is characterized as Plastocyanin-like 1.
+At position 170 to 323, the domain is characterized as Plastocyanin-like 2.
+At position 408 to 531, the domain is characterized as Plastocyanin-like 3.
+At position 399 to 590, the domain is characterized as PNPLA.
+At position 57 to 305, the domain is characterized as GB1/RHD3-type G.
+At position 889 to 952, the domain is characterized as SAM.
+At position 969 to 1174, the domain is characterized as PARP catalytic.
+At position 411 to 472, the domain is characterized as PWWP.
+At position 37 to 124, the domain is characterized as Thioredoxin.
+At position 37 to 118, the domain is characterized as Saposin B-type.
+At position 132 to 249, the domain is characterized as PilZ.
+At position 119 to 374, the domain is characterized as Deacetylase sirtuin-type.
+At position 181 to 362, the domain is characterized as EXS.
+At position 256 to 425, the domain is characterized as GATase cobBQ-type.
+At position 65 to 131, the domain is characterized as PAS.
+At position 139 to 193, the domain is characterized as PAC.
+At position 218 to 440, the domain is characterized as Histidine kinase 1.
+At position 571 to 686, the domain is characterized as Response regulatory 1.
+At position 747 to 1010, the domain is characterized as Histidine kinase 2.
+At position 1359 to 1483, the domain is characterized as Response regulatory 2.
+At position 61 to 198, the domain is characterized as GAF 1.
+At position 229 to 366, the domain is characterized as GAF 2.
+At position 380 to 573, the domain is characterized as Histidine kinase.
+At position 260 to 484, the domain is characterized as tr-type G.
+At position 255 to 539, the domain is characterized as GT23.
+At position 548 to 609, the domain is characterized as SH3.
+At position 1 to 62, the domain is characterized as HTH asnC-type.
+At position 344 to 404, the domain is characterized as ACT.
+At position 34 to 63, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 64 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 40 to 101, the domain is characterized as KH; atypical.
+At position 528 to 602, the domain is characterized as Carrier.
+At position 447 to 618, the domain is characterized as tr-type G.
+At position 198 to 261, the domain is characterized as KH.
+At position 324 to 417, the domain is characterized as HD.
+At position 221 to 304, the domain is characterized as RRM 1.
+At position 341 to 419, the domain is characterized as RRM 2.
+At position 460 to 546, the domain is characterized as RRM 3.
+At position 25 to 144, the domain is characterized as EamA 1.
+At position 196 to 321, the domain is characterized as EamA 2.
+At position 75 to 264, the domain is characterized as ABC transmembrane type-1.
+At position 219 to 391, the domain is characterized as PCI.
+At position 254 to 445, the domain is characterized as GATase cobBQ-type.
+At position 154 to 300, the domain is characterized as Plastocyanin-like 2.
+At position 362 to 494, the domain is characterized as Plastocyanin-like 3.
+At position 126 to 367, the domain is characterized as Radical SAM core.
+At position 469 to 841, the domain is characterized as FH2.
+At position 29 to 169, the domain is characterized as MATH.
+At position 190 to 500, the domain is characterized as USP.
+At position 203 to 306, the domain is characterized as MaoC-like.
+At position 7 to 111, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 48 to 119, the domain is characterized as FHA.
+At position 7 to 94, the domain is characterized as ATP-cone.
+At position 101 to 270, the domain is characterized as PCI.
+At position 183 to 326, the domain is characterized as FCP1 homology.
+At position 35 to 137, the domain is characterized as FAR1.
+At position 211 to 254, the domain is characterized as MULE.
+At position 355 to 685, the domain is characterized as Transferrin-like 2.
+At position 66 to 127, the domain is characterized as KH 1.
+At position 160 to 221, the domain is characterized as KH 2.
+At position 36 to 112, the domain is characterized as Tudor-knot.
+At position 281 to 552, the domain is characterized as MYST-type HAT.
+At position 303 to 541, the domain is characterized as Glutamine amidotransferase type-1.
+At position 608 to 936, the domain is characterized as ABC transporter 2.
+At position 16 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 326 to 461, the domain is characterized as Fido.
+At position 241 to 330, the domain is characterized as Ig-like 3.
+At position 720 to 800, the domain is characterized as Ig-like 5.
+At position 804 to 891, the domain is characterized as Ig-like 6.
+At position 1078 to 1165, the domain is characterized as Ig-like 9.
+At position 1176 to 1261, the domain is characterized as Ig-like 10.
+At position 1266 to 1442, the domain is characterized as Ig-like 11.
+At position 1536 to 1621, the domain is characterized as Ig-like 12.
+At position 1625 to 1694, the domain is characterized as Ig-like 13.
+At position 1702 to 1798, the domain is characterized as Ig-like 14.
+At position 34 to 112, the domain is characterized as GIY-YIG.
+At position 222 to 257, the domain is characterized as UVR.
+At position 1228 to 1392, the domain is characterized as PNPLA.
+At position 579 to 665, the domain is characterized as Ig-like C2-type.
+At position 223 to 315, the domain is characterized as RRM.
+At position 40 to 315, the domain is characterized as Dynamin-type G.
+At position 654 to 745, the domain is characterized as GED.
+At position 212 to 559, the domain is characterized as USP.
+At position 7 to 319, the domain is characterized as Helicase ATP-binding.
+At position 173 to 205, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 271 to 304, the domain is characterized as KOW 1.
+At position 418 to 449, the domain is characterized as KOW 2.
+At position 470 to 501, the domain is characterized as KOW 3.
+At position 592 to 625, the domain is characterized as KOW 4.
+At position 698 to 731, the domain is characterized as KOW 5.
+At position 1 to 86, the domain is characterized as CARD.
+At position 58 to 567, the domain is characterized as Biotin carboxylation.
+At position 216 to 408, the domain is characterized as ATP-grasp.
+At position 694 to 768, the domain is characterized as Biotinyl-binding.
+At position 1486 to 1822, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1826 to 2141, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 56 to 176, the domain is characterized as RGS.
+At position 455 to 520, the domain is characterized as AGC-kinase C-terminal.
+At position 3 to 118, the domain is characterized as PpiC.
+At position 148 to 197, the domain is characterized as Myb-like.
+At position 285 to 355, the domain is characterized as Plastocyanin-like.
+At position 25 to 128, the domain is characterized as Phytocyanin.
+At position 272 to 346, the domain is characterized as U-box.
+At position 28 to 149, the domain is characterized as VIT.
+At position 275 to 458, the domain is characterized as VWFA.
+At position 352 to 616, the domain is characterized as Protein kinase.
+At position 106 to 360, the domain is characterized as EAL.
+At position 24 to 64, the domain is characterized as Chitin-binding type-1 1.
+At position 5 to 60, the domain is characterized as TIL.
+At position 277 to 347, the domain is characterized as J.
+At position 39 to 90, the domain is characterized as bHLH.
+At position 669 to 900, the domain is characterized as NR LBD.
+At position 219 to 251, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 302 to 331, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 28 to 130, the domain is characterized as Gnk2-homologous 1.
+At position 135 to 246, the domain is characterized as Gnk2-homologous 2.
+At position 318 to 380, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 470 to 532, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 100 to 278, the domain is characterized as Protein kinase.
+At position 263 to 324, the domain is characterized as SH3.
+At position 5 to 162, the domain is characterized as PPIase cyclophilin-type.
+At position 41 to 167, the domain is characterized as Ricin B-type lectin.
+At position 182 to 230, the domain is characterized as Fibronectin type-II.
+At position 244 to 360, the domain is characterized as C-type lectin 1.
+At position 389 to 505, the domain is characterized as C-type lectin 2.
+At position 528 to 644, the domain is characterized as C-type lectin 3.
+At position 678 to 809, the domain is characterized as C-type lectin 4.
+At position 832 to 951, the domain is characterized as C-type lectin 5.
+At position 979 to 1107, the domain is characterized as C-type lectin 6.
+At position 1132 to 1243, the domain is characterized as C-type lectin 7.
+At position 1273 to 1393, the domain is characterized as C-type lectin 8.
+At position 209 to 301, the domain is characterized as ARID.
+At position 404 to 499, the domain is characterized as REKLES.
+At position 41 to 385, the domain is characterized as AB hydrolase-1.
+At position 139 to 189, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 235 to 285, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 51 to 172, the domain is characterized as MsrB.
+At position 28 to 145, the domain is characterized as NTR.
+At position 113 to 177, the domain is characterized as SEP.
+At position 224 to 301, the domain is characterized as UBX.
+At position 194 to 271, the domain is characterized as UBX.
+At position 7 to 225, the domain is characterized as DOG1.
+At position 44 to 173, the domain is characterized as EamA 1.
+At position 216 to 344, the domain is characterized as EamA 2.
+At position 289 to 465, the domain is characterized as Helicase ATP-binding.
+At position 476 to 643, the domain is characterized as Helicase C-terminal.
+At position 11 to 100, the domain is characterized as SUEL-type lectin.
+At position 350 to 476, the domain is characterized as YTH.
+At position 56 to 212, the domain is characterized as FCP1 homology.
+At position 309 to 393, the domain is characterized as BRCT.
+At position 427 to 515, the domain is characterized as Death.
+At position 179 to 368, the domain is characterized as Collagen-like.
+At position 401 to 550, the domain is characterized as Thioredoxin.
+At position 81 to 161, the domain is characterized as GS beta-grasp.
+At position 168 to 434, the domain is characterized as GS catalytic.
+At position 7 to 224, the domain is characterized as Prephenate dehydratase.
+At position 244 to 322, the domain is characterized as ACT.
+At position 103 to 348, the domain is characterized as ABC transporter.
+At position 501 to 658, the domain is characterized as Helicase C-terminal.
+At position 1 to 73, the domain is characterized as U-box.
+At position 82 to 221, the domain is characterized as N-acetyltransferase.
+At position 110 to 182, the domain is characterized as PA.
+At position 217 to 343, the domain is characterized as C2.
+At position 531 to 790, the domain is characterized as Ras-GEF.
+At position 1392 to 1540, the domain is characterized as PI-PLC X-box.
+At position 1730 to 1846, the domain is characterized as PI-PLC Y-box.
+At position 1851 to 1976, the domain is characterized as C2.
+At position 2012 to 2114, the domain is characterized as Ras-associating 1.
+At position 2135 to 2238, the domain is characterized as Ras-associating 2.
+At position 360 to 471, the domain is characterized as PAZ.
+At position 638 to 958, the domain is characterized as Piwi.
+At position 349 to 591, the domain is characterized as NR LBD.
+At position 3 to 114, the domain is characterized as Toprim.
+At position 1 to 206, the domain is characterized as PIK helical.
+At position 895 to 1164, the domain is characterized as PI3K/PI4K catalytic.
+At position 100 to 277, the domain is characterized as FBA.
+At position 50 to 248, the domain is characterized as Peptidase M12A.
+At position 10 to 262, the domain is characterized as Protein kinase.
+At position 30 to 128, the domain is characterized as Cadherin 1.
+At position 129 to 244, the domain is characterized as Cadherin 2.
+At position 245 to 340, the domain is characterized as Cadherin 3.
+At position 341 to 449, the domain is characterized as Cadherin 4.
+At position 450 to 566, the domain is characterized as Cadherin 5.
+At position 567 to 667, the domain is characterized as Cadherin 6.
+At position 668 to 777, the domain is characterized as Cadherin 7.
+At position 24 to 219, the domain is characterized as Rho-GAP.
+At position 24 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 110 to 199, the domain is characterized as Ig-like C2-type 2.
+At position 368 to 464, the domain is characterized as Ig-like C2-type 4.
+At position 469 to 559, the domain is characterized as Ig-like C2-type 5.
+At position 693 to 1031, the domain is characterized as Protein kinase; inactive.
+At position 46 to 113, the domain is characterized as Cytochrome b5 heme-binding.
+At position 511 to 690, the domain is characterized as Macro.
+At position 720 to 829, the domain is characterized as HIT.
+At position 477 to 637, the domain is characterized as CBM3 1.
+At position 703 to 856, the domain is characterized as CBM3 2.
+At position 906 to 1059, the domain is characterized as CBM3 3.
+At position 7 to 66, the domain is characterized as CBS 1.
+At position 78 to 135, the domain is characterized as CBS 2.
+At position 388 to 423, the domain is characterized as EF-hand.
+At position 122 to 295, the domain is characterized as SET.
+At position 28 to 115, the domain is characterized as RRM.
+At position 51 to 164, the domain is characterized as HD.
+At position 10 to 277, the domain is characterized as CN hydrolase.
+At position 33 to 126, the domain is characterized as UPAR/Ly6 1.
+At position 140 to 222, the domain is characterized as UPAR/Ly6 2.
+At position 111 to 314, the domain is characterized as PNPLA.
+At position 28 to 218, the domain is characterized as Glutamine amidotransferase type-1.
+At position 219 to 417, the domain is characterized as GMPS ATP-PPase.
+At position 8 to 73, the domain is characterized as J.
+At position 100 to 408, the domain is characterized as IF rod.
+At position 34 to 288, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 129 to 250, the domain is characterized as TBDR plug.
+At position 255 to 774, the domain is characterized as TBDR beta-barrel.
+At position 23 to 204, the domain is characterized as PNPLA.
+At position 337 to 582, the domain is characterized as Alpha-type protein kinase.
+At position 1 to 63, the domain is characterized as Ubiquitin-like.
+At position 260 to 402, the domain is characterized as Flavodoxin-like.
+At position 1 to 400, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 14 to 178, the domain is characterized as PPIase cyclophilin-type.
+At position 41 to 234, the domain is characterized as PBC.
+At position 96 to 218, the domain is characterized as PLAT.
+At position 221 to 914, the domain is characterized as Lipoxygenase.
+At position 416 to 462, the domain is characterized as Laminin EGF-like 5.
+At position 463 to 517, the domain is characterized as Laminin EGF-like 6.
+At position 518 to 573, the domain is characterized as Laminin EGF-like 7.
+At position 574 to 603, the domain is characterized as Laminin EGF-like 8; truncated.
+At position 46 to 163, the domain is characterized as FZ.
+At position 179 to 301, the domain is characterized as NTR.
+At position 29 to 82, the domain is characterized as bHLH.
+At position 38 to 163, the domain is characterized as TIR.
+At position 73 to 261, the domain is characterized as RNase H type-2.
+At position 20 to 59, the domain is characterized as Chitin-binding type-1.
+At position 1 to 96, the domain is characterized as Jacalin-type lectin 1.
+At position 99 to 241, the domain is characterized as Jacalin-type lectin 2.
+At position 244 to 389, the domain is characterized as Jacalin-type lectin 3.
+At position 403 to 488, the domain is characterized as Jacalin-type lectin 4.
+At position 119 to 404, the domain is characterized as ABC transmembrane type-1 1.
+At position 490 to 710, the domain is characterized as ABC transporter 1.
+At position 744 to 1027, the domain is characterized as ABC transmembrane type-1 2.
+At position 1071 to 1306, the domain is characterized as ABC transporter 2.
+At position 1 to 266, the domain is characterized as Protein kinase.
+At position 30 to 158, the domain is characterized as EamA.
+At position 30 to 149, the domain is characterized as Bulb-type lectin.
+At position 306 to 344, the domain is characterized as EGF-like; atypical.
+At position 360 to 447, the domain is characterized as PAN.
+At position 530 to 810, the domain is characterized as Protein kinase.
+At position 477 to 800, the domain is characterized as Protein kinase.
+At position 185 to 317, the domain is characterized as DCD.
+At position 375 to 413, the domain is characterized as UBA.
+At position 340 to 472, the domain is characterized as NlpC/P60.
+At position 299 to 323, the domain is characterized as NAF.
+At position 57 to 400, the domain is characterized as TTL.
+At position 188 to 394, the domain is characterized as CP-type G.
+At position 95 to 130, the domain is characterized as EF-hand.
+At position 354 to 394, the domain is characterized as EGF-like 1; calcium-binding.
+At position 142 to 386, the domain is characterized as Radical SAM core.
+At position 11 to 142, the domain is characterized as Galectin 1.
+At position 151 to 290, the domain is characterized as Galectin 2.
+At position 464 to 612, the domain is characterized as GST C-terminal.
+At position 80 to 164, the domain is characterized as KH-like.
+At position 517 to 669, the domain is characterized as RNase NYN.
+At position 133 to 442, the domain is characterized as NACHT.
+At position 799 to 1082, the domain is characterized as FIIND.
+At position 1092 to 1175, the domain is characterized as CARD.
+At position 163 to 302, the domain is characterized as NIDO 1.
+At position 409 to 450, the domain is characterized as EGF-like; calcium-binding.
+At position 519 to 659, the domain is characterized as NIDO 2.
+At position 79 to 420, the domain is characterized as YcaO.
+At position 1288 to 1521, the domain is characterized as ABC transporter 2.
+At position 278 to 312, the domain is characterized as SAP.
+At position 77 to 150, the domain is characterized as POTRA.
+At position 512 to 587, the domain is characterized as U-box.
+At position 628 to 753, the domain is characterized as C2 1.
+At position 768 to 897, the domain is characterized as C2 2.
+At position 10 to 37, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 38 to 68, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 169 to 657, the domain is characterized as USP.
+At position 9 to 76, the domain is characterized as NAC-A/B.
+At position 26 to 251, the domain is characterized as YjeF N-terminal.
+At position 10 to 156, the domain is characterized as N-acetyltransferase.
+At position 330 to 379, the domain is characterized as FBD.
+At position 367 to 420, the domain is characterized as TSP type-1.
+At position 24 to 291, the domain is characterized as BAR.
+At position 344 to 404, the domain is characterized as SH3.
+At position 4 to 403, the domain is characterized as BRO1.
+At position 23 to 220, the domain is characterized as GH11.
+At position 288 to 546, the domain is characterized as MHD.
+At position 12 to 64, the domain is characterized as CHCH.
+At position 12 to 84, the domain is characterized as S4 RNA-binding.
+At position 145 to 243, the domain is characterized as Ig-like C2-type 1.
+At position 247 to 334, the domain is characterized as Ig-like C2-type 2.
+At position 2 to 126, the domain is characterized as RCK N-terminal 1.
+At position 138 to 219, the domain is characterized as RCK C-terminal 1.
+At position 224 to 347, the domain is characterized as RCK N-terminal 2.
+At position 356 to 436, the domain is characterized as RCK C-terminal 2.
+At position 155 to 325, the domain is characterized as CheB-type methylesterase.
+At position 13 to 69, the domain is characterized as WHEP-TRS.
+At position 69 to 367, the domain is characterized as ABC transmembrane type-1 1.
+At position 403 to 682, the domain is characterized as ABC transporter 1.
+At position 781 to 1068, the domain is characterized as ABC transmembrane type-1 2.
+At position 1135 to 1374, the domain is characterized as ABC transporter 2.
+At position 121 to 459, the domain is characterized as Peptidase S8.
+At position 642 to 1130, the domain is characterized as Protein kinase.
+At position 51 to 164, the domain is characterized as Thioredoxin.
+At position 239 to 299, the domain is characterized as FF.
+At position 567 to 620, the domain is characterized as bHLH.
+At position 15 to 286, the domain is characterized as Protein kinase.
+At position 28 to 248, the domain is characterized as Peptidase S1.
+At position 153 to 243, the domain is characterized as PPIase FKBP-type.
+At position 281 to 333, the domain is characterized as HAMP.
+At position 368 to 509, the domain is characterized as GGDEF.
+At position 518 to 769, the domain is characterized as EAL.
+At position 92 to 421, the domain is characterized as PI3K/PI4K catalytic.
+At position 638 to 739, the domain is characterized as Fibronectin type-III.
+At position 746 to 921, the domain is characterized as MAM.
+At position 83 to 124, the domain is characterized as Collagen-like.
+At position 125 to 264, the domain is characterized as C1q.
+At position 245 to 280, the domain is characterized as EF-hand 1.
+At position 408 to 565, the domain is characterized as Ferric oxidoreductase.
+At position 599 to 727, the domain is characterized as FAD-binding FR-type.
+At position 22 to 93, the domain is characterized as KRAB.
+At position 7 to 64, the domain is characterized as Kazal-like.
+At position 388 to 650, the domain is characterized as ABC transmembrane type-2.
+At position 1 to 57, the domain is characterized as Myb-like.
+At position 478 to 529, the domain is characterized as FHA.
+At position 1182 to 1296, the domain is characterized as PX.
+At position 116 to 315, the domain is characterized as ATP-grasp.
+At position 19 to 134, the domain is characterized as Thioredoxin 1.
+At position 349 to 474, the domain is characterized as Thioredoxin 2.
+At position 55 to 155, the domain is characterized as SSB.
+At position 1226 to 1781, the domain is characterized as FAT.
+At position 1955 to 2269, the domain is characterized as PI3K/PI4K catalytic.
+At position 2303 to 2335, the domain is characterized as FATC.
+At position 3 to 80, the domain is characterized as ACT.
+At position 84 to 118, the domain is characterized as Oxidoreductase-like.
+At position 42 to 255, the domain is characterized as Cupin type-1 1.
+At position 329 to 478, the domain is characterized as Cupin type-1 2.
+At position 176 to 188, the domain is characterized as EGF-like 1; incomplete.
+At position 188 to 219, the domain is characterized as EGF-like 2.
+At position 219 to 250, the domain is characterized as EGF-like 3.
+At position 250 to 281, the domain is characterized as EGF-like 4.
+At position 281 to 312, the domain is characterized as EGF-like 5.
+At position 312 to 343, the domain is characterized as EGF-like 6.
+At position 343 to 374, the domain is characterized as EGF-like 7.
+At position 374 to 405, the domain is characterized as EGF-like 8.
+At position 405 to 436, the domain is characterized as EGF-like 9.
+At position 436 to 467, the domain is characterized as EGF-like 10.
+At position 467 to 498, the domain is characterized as EGF-like 11.
+At position 498 to 529, the domain is characterized as EGF-like 12.
+At position 529 to 560, the domain is characterized as EGF-like 13.
+At position 560 to 591, the domain is characterized as EGF-like 14.
+At position 595 to 685, the domain is characterized as Fibronectin type-III 1.
+At position 686 to 775, the domain is characterized as Fibronectin type-III 2.
+At position 776 to 866, the domain is characterized as Fibronectin type-III 3.
+At position 867 to 957, the domain is characterized as Fibronectin type-III 4.
+At position 958 to 1046, the domain is characterized as Fibronectin type-III 5.
+At position 1047 to 1138, the domain is characterized as Fibronectin type-III 6.
+At position 1139 to 1228, the domain is characterized as Fibronectin type-III 7.
+At position 1229 to 1318, the domain is characterized as Fibronectin type-III 8.
+At position 1319 to 1408, the domain is characterized as Fibronectin type-III 9.
+At position 1409 to 1495, the domain is characterized as Fibronectin type-III 10.
+At position 1496 to 1584, the domain is characterized as Fibronectin type-III 11.
+At position 1582 to 1797, the domain is characterized as Fibrinogen C-terminal.
+At position 44 to 266, the domain is characterized as Fibrinogen C-terminal.
+At position 39 to 76, the domain is characterized as EF-hand 1.
+At position 118 to 153, the domain is characterized as EF-hand 2.
+At position 153 to 185, the domain is characterized as EF-hand 3.
+At position 105 to 200, the domain is characterized as RRM 1.
+At position 339 to 402, the domain is characterized as S4 RNA-binding.
+At position 46 to 261, the domain is characterized as Radical SAM core.
+At position 11 to 366, the domain is characterized as Kinesin motor.
+At position 1 to 84, the domain is characterized as SEC7.
+At position 193 to 349, the domain is characterized as PH.
+At position 39 to 143, the domain is characterized as Glutaredoxin.
+At position 72 to 107, the domain is characterized as EF-hand 2.
+At position 168 to 203, the domain is characterized as EF-hand 4.
+At position 36 to 228, the domain is characterized as B30.2/SPRY.
+At position 51 to 220, the domain is characterized as Helicase ATP-binding.
+At position 35 to 242, the domain is characterized as GH11 1.
+At position 280 to 487, the domain is characterized as GH11 2.
+At position 523 to 563, the domain is characterized as CBM10 1.
+At position 566 to 606, the domain is characterized as CBM10 2.
+At position 110 to 211, the domain is characterized as PB1.
+At position 79 to 350, the domain is characterized as Radical SAM core.
+At position 401 to 541, the domain is characterized as N-acetyltransferase.
+At position 214 to 470, the domain is characterized as Protein kinase.
+At position 67 to 294, the domain is characterized as Radical SAM core.
+At position 63 to 122, the domain is characterized as Tudor-knot.
+At position 174 to 445, the domain is characterized as MYST-type HAT.
+At position 3 to 147, the domain is characterized as ADF-H.
+At position 67 to 194, the domain is characterized as Nudix hydrolase.
+At position 4 to 144, the domain is characterized as N-acetyltransferase.
+At position 12 to 94, the domain is characterized as GST N-terminal.
+At position 100 to 252, the domain is characterized as GST C-terminal.
+At position 17 to 142, the domain is characterized as Nudix hydrolase.
+At position 78 to 372, the domain is characterized as RHD.
+At position 21 to 141, the domain is characterized as C-type lysozyme.
+At position 135 to 246, the domain is characterized as SET.
+At position 55 to 195, the domain is characterized as N-acetyltransferase.
+At position 22 to 97, the domain is characterized as Ubiquitin-like.
+At position 505 to 563, the domain is characterized as SH3.
+At position 286 to 428, the domain is characterized as SIS 1.
+At position 109 to 330, the domain is characterized as Radical SAM core.
+At position 160 to 225, the domain is characterized as SEP.
+At position 271 to 348, the domain is characterized as UBX.
+At position 207 to 308, the domain is characterized as Fe2OG dioxygenase.
+At position 41 to 301, the domain is characterized as ZP.
+At position 8 to 75, the domain is characterized as NAC-A/B.
+At position 25 to 132, the domain is characterized as Gnk2-homologous 1.
+At position 137 to 234, the domain is characterized as Gnk2-homologous 2.
+At position 1 to 120, the domain is characterized as Thioredoxin.
+At position 468 to 686, the domain is characterized as ABC transporter.
+At position 719 to 803, the domain is characterized as PB1.
+At position 44 to 91, the domain is characterized as WAP 1.
+At position 95 to 145, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 147 to 194, the domain is characterized as WAP 2.
+At position 195 to 240, the domain is characterized as WAP 3.
+At position 35 to 145, the domain is characterized as Ig-like V-type.
+At position 172 to 357, the domain is characterized as Glutamine amidotransferase type-1.
+At position 626 to 855, the domain is characterized as NR LBD.
+At position 1 to 166, the domain is characterized as 3'-5' exonuclease.
+At position 206 to 285, the domain is characterized as HRDC.
+At position 45 to 242, the domain is characterized as Lon N-terminal.
+At position 629 to 811, the domain is characterized as Lon proteolytic.
+At position 479 to 582, the domain is characterized as PTS EIIB type-3.
+At position 16 to 224, the domain is characterized as START.
+At position 4 to 253, the domain is characterized as ABC transporter.
+At position 386 to 807, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1294 to 1601, the domain is characterized as PKS/mFAS DH.
+At position 1651 to 1725, the domain is characterized as Carrier.
+At position 208 to 258, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 28 to 101, the domain is characterized as H15.
+At position 184 to 327, the domain is characterized as Tyrosine-protein phosphatase.
+At position 279 to 370, the domain is characterized as Ig-like C2-type.
+At position 32 to 148, the domain is characterized as FZ.
+At position 988 to 1201, the domain is characterized as FtsK.
+At position 1 to 157, the domain is characterized as RNase H type-1.
+At position 388 to 821, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1316 to 1629, the domain is characterized as PKS/mFAS DH.
+At position 1716 to 1793, the domain is characterized as Carrier.
+At position 13 to 486, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 506 to 806, the domain is characterized as UvrD-like helicase C-terminal.
+At position 15 to 185, the domain is characterized as FAD-binding PCMH-type.
+At position 8 to 150, the domain is characterized as N-acetyltransferase.
+At position 31 to 211, the domain is characterized as BPL/LPL catalytic.
+At position 580 to 770, the domain is characterized as SEC7.
+At position 784 to 895, the domain is characterized as PH.
+At position 32 to 155, the domain is characterized as Avidin-like.
+At position 131 to 310, the domain is characterized as FAD-binding PCMH-type.
+At position 36 to 118, the domain is characterized as GOLD.
+At position 6 to 84, the domain is characterized as PUA.
+At position 909 to 1020, the domain is characterized as Peptidase S74.
+At position 70 to 121, the domain is characterized as HTH myb-type 1.
+At position 122 to 177, the domain is characterized as HTH myb-type 2.
+At position 178 to 228, the domain is characterized as HTH myb-type 3.
+At position 129 to 155, the domain is characterized as HhH.
+At position 1 to 62, the domain is characterized as S4 RNA-binding.
+At position 53 to 297, the domain is characterized as RNase H type-2.
+At position 435 to 626, the domain is characterized as FtsK.
+At position 271 to 590, the domain is characterized as UvrD-like helicase C-terminal.
+At position 251 to 639, the domain is characterized as Asparagine synthetase.
+At position 47 to 271, the domain is characterized as Saposin B-type.
+At position 805 to 1036, the domain is characterized as ABC transporter 1.
+At position 1818 to 2050, the domain is characterized as ABC transporter 2.
+At position 13 to 128, the domain is characterized as MaoC-like.
+At position 96 to 212, the domain is characterized as RGS.
+At position 205 to 292, the domain is characterized as Ig-like.
+At position 42 to 145, the domain is characterized as Cytochrome c 1.
+At position 189 to 304, the domain is characterized as Cytochrome c 2.
+At position 327 to 417, the domain is characterized as Cytochrome c 3.
+At position 1 to 331, the domain is characterized as Alpha-carbonic anhydrase.
+At position 311 to 573, the domain is characterized as Clu.
+At position 280 to 432, the domain is characterized as VPS9.
+At position 36 to 148, the domain is characterized as Cystatin kininogen-type.
+At position 222 to 399, the domain is characterized as Helicase ATP-binding.
+At position 454 to 605, the domain is characterized as Helicase C-terminal.
+At position 414 to 581, the domain is characterized as tr-type G.
+At position 795 to 1124, the domain is characterized as PDEase.
+At position 20 to 835, the domain is characterized as Vitellogenin.
+At position 1512 to 1705, the domain is characterized as VWFD.
+At position 43 to 77, the domain is characterized as SAP.
+At position 139 to 291, the domain is characterized as PINIT.
+At position 6 to 237, the domain is characterized as ABC transporter 1.
+At position 330 to 559, the domain is characterized as ABC transporter 2.
+At position 162 to 291, the domain is characterized as CMP/dCMP-type deaminase.
+At position 482 to 517, the domain is characterized as EF-hand 4.
+At position 187 to 331, the domain is characterized as GAF.
+At position 374 to 614, the domain is characterized as Histidine kinase.
+At position 647 to 766, the domain is characterized as Response regulatory.
+At position 1450 to 1592, the domain is characterized as GAF.
+At position 1760 to 1986, the domain is characterized as Histidine kinase.
+At position 2180 to 2303, the domain is characterized as Response regulatory.
+At position 10 to 250, the domain is characterized as ABC transporter.
+At position 18 to 289, the domain is characterized as CheR-type methyltransferase.
+At position 22 to 146, the domain is characterized as Barwin.
+At position 38 to 161, the domain is characterized as PX.
+At position 138 to 175, the domain is characterized as UBA.
+At position 68 to 506, the domain is characterized as GH18.
+At position 401 to 430, the domain is characterized as IQ.
+At position 57 to 158, the domain is characterized as ULD.
+At position 161 to 234, the domain is characterized as CUTL.
+At position 336 to 538, the domain is characterized as Protein kinase.
+At position 22 to 126, the domain is characterized as Ig-like V-type.
+At position 14 to 173, the domain is characterized as NAC.
+At position 673 to 722, the domain is characterized as KA1.
+At position 35 to 107, the domain is characterized as HSA.
+At position 548 to 713, the domain is characterized as Helicase ATP-binding.
+At position 1076 to 1229, the domain is characterized as Helicase C-terminal.
+At position 1673 to 1727, the domain is characterized as Myb-like.
+At position 56 to 260, the domain is characterized as AH.
+At position 159 to 323, the domain is characterized as GOLD.
+At position 32 to 183, the domain is characterized as MRH.
+At position 127 to 308, the domain is characterized as Reticulon.
+At position 1845 to 1923, the domain is characterized as BRCT 1.
+At position 1944 to 2035, the domain is characterized as BRCT 2.
+At position 248 to 374, the domain is characterized as DOD-type homing endonuclease.
+At position 102 to 273, the domain is characterized as Helicase ATP-binding.
+At position 300 to 444, the domain is characterized as Helicase C-terminal.
+At position 15 to 166, the domain is characterized as N-acetyltransferase.
+At position 384 to 537, the domain is characterized as Cupin type-1 1.
+At position 582 to 754, the domain is characterized as Cupin type-1 2.
+At position 112 to 183, the domain is characterized as S4 RNA-binding.
+At position 457 to 691, the domain is characterized as NR LBD.
+At position 64 to 310, the domain is characterized as PPM-type phosphatase.
+At position 294 to 526, the domain is characterized as Peptidase S1 2.
+At position 216 to 386, the domain is characterized as TrmE-type G.
+At position 250 to 361, the domain is characterized as PX.
+At position 20 to 340, the domain is characterized as Kinesin motor.
+At position 125 to 152, the domain is characterized as PLD phosphodiesterase 1.
+At position 364 to 391, the domain is characterized as PLD phosphodiesterase 2.
+At position 36 to 166, the domain is characterized as N-terminal Ras-GEF.
+At position 209 to 456, the domain is characterized as Ras-GEF.
+At position 33 to 156, the domain is characterized as Ricin B-type lectin.
+At position 652 to 778, the domain is characterized as C-type lectin 4.
+At position 818 to 931, the domain is characterized as C-type lectin 5.
+At position 958 to 1091, the domain is characterized as C-type lectin 6.
+At position 1110 to 1222, the domain is characterized as C-type lectin 7.
+At position 1251 to 1374, the domain is characterized as C-type lectin 8.
+At position 1401 to 1513, the domain is characterized as C-type lectin 9.
+At position 1542 to 1661, the domain is characterized as C-type lectin 10.
+At position 81 to 370, the domain is characterized as ABC transmembrane type-1 1.
+At position 405 to 650, the domain is characterized as ABC transporter 1.
+At position 725 to 1012, the domain is characterized as ABC transmembrane type-1 2.
+At position 1048 to 1285, the domain is characterized as ABC transporter 2.
+At position 422 to 530, the domain is characterized as PAZ.
+At position 709 to 1017, the domain is characterized as Piwi.
+At position 52 to 310, the domain is characterized as Protein kinase.
+At position 158 to 588, the domain is characterized as GH18.
+At position 120 to 508, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 88 to 405, the domain is characterized as GH10.
+At position 11 to 264, the domain is characterized as Protein kinase.
+At position 1 to 245, the domain is characterized as Peptidase S1.
+At position 630 to 700, the domain is characterized as S1 motif.
+At position 263 to 428, the domain is characterized as 3'-5' exonuclease.
+At position 479 to 559, the domain is characterized as HRDC.
+At position 82 to 205, the domain is characterized as GST C-terminal.
+At position 34 to 168, the domain is characterized as PX.
+At position 1 to 94, the domain is characterized as BRCT.
+At position 242 to 370, the domain is characterized as PARP alpha-helical.
+At position 369 to 573, the domain is characterized as PARP catalytic.
+At position 607 to 735, the domain is characterized as VIT.
+At position 876 to 1046, the domain is characterized as VWFA.
+At position 39 to 98, the domain is characterized as Collagen-like.
+At position 10 to 224, the domain is characterized as Glutamine amidotransferase type-2.
+At position 14 to 116, the domain is characterized as LOB.
+At position 139 to 298, the domain is characterized as JmjC.
+At position 980 to 1104, the domain is characterized as PH.
+At position 337 to 366, the domain is characterized as IQ.
+At position 736 to 929, the domain is characterized as SEC7.
+At position 941 to 1075, the domain is characterized as PH.
+At position 298 to 474, the domain is characterized as PCI.
+At position 22 to 138, the domain is characterized as RWD.
+At position 108 to 507, the domain is characterized as Protein kinase 1.
+At position 508 to 999, the domain is characterized as Protein kinase 2.
+At position 103 to 210, the domain is characterized as Cytochrome c.
+At position 379 to 547, the domain is characterized as tr-type G.
+At position 68 to 176, the domain is characterized as THUMP.
+At position 138 to 265, the domain is characterized as NlpC/P60.
+At position 323 to 417, the domain is characterized as Ig-like C2-type 1.
+At position 422 to 521, the domain is characterized as Ig-like C2-type 2.
+At position 529 to 626, the domain is characterized as Ig-like C2-type 3.
+At position 266 to 350, the domain is characterized as Toprim.
+At position 102 to 190, the domain is characterized as PRC barrel.
+At position 97 to 139, the domain is characterized as KH.
+At position 464 to 542, the domain is characterized as POLO box 1.
+At position 563 to 646, the domain is characterized as POLO box 2.
+At position 1 to 64, the domain is characterized as Kazal-like 1.
+At position 65 to 129, the domain is characterized as Kazal-like 2.
+At position 132 to 186, the domain is characterized as Kazal-like 3.
+At position 2 to 34, the domain is characterized as LisH.
+At position 16 to 231, the domain is characterized as ABC transporter.
+At position 590 to 728, the domain is characterized as DOD-type homing endonuclease.
+At position 1 to 72, the domain is characterized as LCN-type CS-alpha/beta.
+At position 13 to 281, the domain is characterized as tr-type G.
+At position 24 to 241, the domain is characterized as tr-type G.
+At position 9 to 130, the domain is characterized as PINc.
+At position 786 to 876, the domain is characterized as PKD.
+At position 577 to 658, the domain is characterized as BRCT.
+At position 272 to 305, the domain is characterized as KOW 1.
+At position 419 to 450, the domain is characterized as KOW 2.
+At position 471 to 502, the domain is characterized as KOW 3.
+At position 593 to 626, the domain is characterized as KOW 4.
+At position 702 to 735, the domain is characterized as KOW 5.
+At position 84 to 243, the domain is characterized as TNase-like.
+At position 78 to 336, the domain is characterized as Protein kinase.
+At position 451 to 485, the domain is characterized as EF-hand 3.
+At position 486 to 521, the domain is characterized as EF-hand 4.
+At position 77 to 376, the domain is characterized as AB hydrolase-1.
+At position 6 to 107, the domain is characterized as Glutaredoxin.
+At position 37 to 291, the domain is characterized as Protein kinase.
+At position 354 to 398, the domain is characterized as NAF.
+At position 414 to 489, the domain is characterized as B5.
+At position 737 to 830, the domain is characterized as FDX-ACB.
+At position 31 to 271, the domain is characterized as Peptidase S1.
+At position 43 to 179, the domain is characterized as PA14.
+At position 295 to 430, the domain is characterized as MPN.
+At position 140 to 177, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 111 to 217, the domain is characterized as HTH APSES-type.
+At position 57 to 165, the domain is characterized as THUMP.
+At position 18 to 77, the domain is characterized as LCN-type CS-alpha/beta.
+At position 514 to 684, the domain is characterized as tr-type G.
+At position 5 to 193, the domain is characterized as Phosphatase tensin-type.
+At position 1247 to 1646, the domain is characterized as FH2.
+At position 730 to 913, the domain is characterized as DDHD.
+At position 16 to 166, the domain is characterized as NAC.
+At position 5 to 249, the domain is characterized as ABC transporter.
+At position 35 to 118, the domain is characterized as ACT 1.
+At position 123 to 200, the domain is characterized as ACT 2.
+At position 259 to 335, the domain is characterized as ACT 3.
+At position 337 to 416, the domain is characterized as ACT 4.
+At position 28 to 105, the domain is characterized as Inhibitor I9.
+At position 110 to 613, the domain is characterized as Peptidase S8.
+At position 390 to 462, the domain is characterized as PA.
+At position 781 to 1052, the domain is characterized as ABC transmembrane type-1 2.
+At position 1119 to 1358, the domain is characterized as ABC transporter 2.
+At position 410 to 602, the domain is characterized as 3'-5' exonuclease.
+At position 725 to 805, the domain is characterized as ERCC4.
+At position 18 to 97, the domain is characterized as RRM 1.
+At position 177 to 250, the domain is characterized as RRM 2.
+At position 26 to 331, the domain is characterized as Protein kinase.
+At position 193 to 384, the domain is characterized as Peptidase S1.
+At position 81 to 684, the domain is characterized as Protein kinase.
+At position 110 to 482, the domain is characterized as Peptidase S8.
+At position 808 to 1082, the domain is characterized as Autotransporter.
+At position 562 to 730, the domain is characterized as Helicase ATP-binding.
+At position 928 to 1079, the domain is characterized as Helicase C-terminal.
+At position 520 to 643, the domain is characterized as STAS.
+At position 244 to 422, the domain is characterized as FAD-binding PCMH-type.
+At position 233 to 359, the domain is characterized as OmpA-like.
+At position 280 to 371, the domain is characterized as RRM.
+At position 841 to 885, the domain is characterized as UBA.
+At position 247 to 492, the domain is characterized as PABS.
+At position 846 to 912, the domain is characterized as BRCT 2.
+At position 164 to 381, the domain is characterized as Radical SAM core.
+At position 1290 to 1547, the domain is characterized as Protein kinase.
+At position 18 to 103, the domain is characterized as MtN3/slv 1.
+At position 138 to 221, the domain is characterized as MtN3/slv 2.
+At position 594 to 804, the domain is characterized as PPM-type phosphatase.
+At position 278 to 324, the domain is characterized as F-box.
+At position 223 to 255, the domain is characterized as LisH.
+At position 426 to 551, the domain is characterized as N-terminal Ras-GEF.
+At position 585 to 816, the domain is characterized as Ras-GEF.
+At position 94 to 287, the domain is characterized as Lon N-terminal.
+At position 679 to 861, the domain is characterized as Lon proteolytic.
+At position 63 to 371, the domain is characterized as AB hydrolase-1.
+At position 116 to 192, the domain is characterized as RRM.
+At position 68 to 233, the domain is characterized as Bms1-type G.
+At position 225 to 396, the domain is characterized as PCI.
+At position 489 to 748, the domain is characterized as Protein kinase.
+At position 370 to 436, the domain is characterized as J.
+At position 1 to 166, the domain is characterized as Thioredoxin.
+At position 568 to 640, the domain is characterized as CBS 1.
+At position 687 to 748, the domain is characterized as CBS 2.
+At position 108 to 340, the domain is characterized as Radical SAM core.
+At position 100 to 304, the domain is characterized as Tyr recombinase.
+At position 221 to 272, the domain is characterized as LRRCT.
+At position 269 to 353, the domain is characterized as Ig-like C2-type.
+At position 295 to 433, the domain is characterized as N-acetyltransferase.
+At position 551 to 612, the domain is characterized as CBS 1.
+At position 628 to 686, the domain is characterized as CBS 2.
+At position 875 to 910, the domain is characterized as UVR.
+At position 130 to 245, the domain is characterized as PilZ.
+At position 973 to 1013, the domain is characterized as UBA.
+At position 160 to 298, the domain is characterized as Plastocyanin-like 2.
+At position 365 to 444, the domain is characterized as Plastocyanin-like 3.
+At position 28 to 298, the domain is characterized as Protein kinase.
+At position 1 to 87, the domain is characterized as HTH arsR-type.
+At position 153 to 272, the domain is characterized as C2 1.
+At position 286 to 419, the domain is characterized as C2 2.
+At position 34 to 178, the domain is characterized as FZ.
+At position 54 to 400, the domain is characterized as Kinesin motor.
+At position 384 to 670, the domain is characterized as Clu.
+At position 51 to 104, the domain is characterized as bHLH.
+At position 147 to 217, the domain is characterized as PAS 1.
+At position 319 to 389, the domain is characterized as PAS 2.
+At position 363 to 406, the domain is characterized as PAC.
+At position 487 to 637, the domain is characterized as HNH Cas9-type.
+At position 244 to 321, the domain is characterized as WWE.
+At position 1 to 124, the domain is characterized as Pyruvate carboxyltransferase.
+At position 38 to 219, the domain is characterized as Rab-GAP TBC.
+At position 327 to 439, the domain is characterized as Rhodanese.
+At position 302 to 514, the domain is characterized as PCI.
+At position 26 to 126, the domain is characterized as CBM39.
+At position 162 to 490, the domain is characterized as GH16.
+At position 24 to 99, the domain is characterized as UPAR/Ly6.
+At position 1 to 140, the domain is characterized as DAGKc.
+At position 1200 to 1364, the domain is characterized as PNPLA.
+At position 1229 to 1464, the domain is characterized as Fibrillar collagen NC1.
+At position 22 to 151, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 187 to 298, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 502 to 678, the domain is characterized as tr-type G.
+At position 108 to 278, the domain is characterized as PA14.
+At position 26 to 155, the domain is characterized as Ephrin RBD.
+At position 14 to 130, the domain is characterized as MSP.
+At position 8 to 120, the domain is characterized as BPL/LPL catalytic.
+At position 369 to 579, the domain is characterized as NR LBD.
+At position 301 to 353, the domain is characterized as AGC-kinase C-terminal.
+At position 98 to 307, the domain is characterized as tr-type G.
+At position 366 to 798, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1276 to 1585, the domain is characterized as PKS/mFAS DH.
+At position 1637 to 1714, the domain is characterized as Carrier.
+At position 376 to 433, the domain is characterized as VWFC 1.
+At position 433 to 494, the domain is characterized as VWFC 2.
+At position 491 to 552, the domain is characterized as VWFC 3.
+At position 558 to 618, the domain is characterized as VWFC 4.
+At position 619 to 677, the domain is characterized as VWFC 5.
+At position 677 to 762, the domain is characterized as VWFC 6.
+At position 57 to 322, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 24 to 214, the domain is characterized as RNase H type-2.
+At position 22 to 76, the domain is characterized as Kazal-like.
+At position 6 to 435, the domain is characterized as PTS EIIC type-2.
+At position 4 to 153, the domain is characterized as NAC.
+At position 508 to 849, the domain is characterized as Protein kinase.
+At position 509 to 737, the domain is characterized as Helicase ATP-binding.
+At position 1021 to 1180, the domain is characterized as Helicase C-terminal.
+At position 1 to 342, the domain is characterized as SMP-LTD.
+At position 55 to 276, the domain is characterized as Saposin B-type.
+At position 128 to 227, the domain is characterized as C-type lectin.
+At position 42 to 71, the domain is characterized as IQ.
+At position 12 to 94, the domain is characterized as GS beta-grasp.
+At position 100 to 435, the domain is characterized as GS catalytic.
+At position 24 to 84, the domain is characterized as Chromo.
+At position 40 to 154, the domain is characterized as Ig-like V-type.
+At position 161 to 256, the domain is characterized as Link 1.
+At position 261 to 353, the domain is characterized as Link 2.
+At position 225 to 285, the domain is characterized as EamA.
+At position 379 to 622, the domain is characterized as Clu.
+At position 125 to 237, the domain is characterized as CENP-V/GFA.
+At position 101 to 412, the domain is characterized as IF rod.
+At position 118 to 373, the domain is characterized as Protein kinase.
+At position 453 to 487, the domain is characterized as EF-hand 2.
+At position 488 to 523, the domain is characterized as EF-hand 3.
+At position 529 to 562, the domain is characterized as EF-hand 4.
+At position 379 to 457, the domain is characterized as RRM.
+At position 96 to 167, the domain is characterized as RRM 2.
+At position 27 to 101, the domain is characterized as IGFBP N-terminal.
+At position 104 to 170, the domain is characterized as VWFC.
+At position 201 to 246, the domain is characterized as TSP type-1.
+At position 191 to 241, the domain is characterized as bHLH.
+At position 18 to 121, the domain is characterized as Ig-like V-type.
+At position 146 to 231, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 339, the domain is characterized as Ig-like C2-type 2.
+At position 344 to 441, the domain is characterized as Ig-like C2-type 3.
+At position 15 to 127, the domain is characterized as HotDog ACOT-type.
+At position 1 to 299, the domain is characterized as Helicase ATP-binding.
+At position 4 to 110, the domain is characterized as STAS.
+At position 246 to 365, the domain is characterized as SET.
+At position 51 to 223, the domain is characterized as Helicase ATP-binding.
+At position 394 to 562, the domain is characterized as Helicase C-terminal.
+At position 836 to 960, the domain is characterized as PAZ.
+At position 985 to 1157, the domain is characterized as RNase III 1.
+At position 1198 to 1340, the domain is characterized as RNase III 2.
+At position 34 to 107, the domain is characterized as Chitin-binding type R&R.
+At position 141 to 260, the domain is characterized as PX.
+At position 260 to 343, the domain is characterized as IPT/TIG.
+At position 220 to 457, the domain is characterized as Peptidase M12B.
+At position 1 to 324, the domain is characterized as PUM-HD.
+At position 189 to 293, the domain is characterized as Fe2OG dioxygenase.
+At position 203 to 290, the domain is characterized as RCK C-terminal 1.
+At position 291 to 374, the domain is characterized as RCK C-terminal 2.
+At position 373 to 432, the domain is characterized as CBS.
+At position 22 to 168, the domain is characterized as Clp R.
+At position 254 to 399, the domain is characterized as JmjC.
+At position 99 to 177, the domain is characterized as RRM 1.
+At position 257 to 335, the domain is characterized as RRM 2.
+At position 36 to 588, the domain is characterized as PLA2c.
+At position 25 to 198, the domain is characterized as EngB-type G.
+At position 1063 to 1314, the domain is characterized as Glutamine amidotransferase type-1.
+At position 35 to 140, the domain is characterized as Glutaredoxin.
+At position 402 to 490, the domain is characterized as ABM.
+At position 64 to 207, the domain is characterized as SCP.
+At position 77 to 335, the domain is characterized as Protein kinase.
+At position 378 to 413, the domain is characterized as EF-hand 1.
+At position 414 to 449, the domain is characterized as EF-hand 2.
+At position 450 to 485, the domain is characterized as EF-hand 3.
+At position 290 to 344, the domain is characterized as HAMP.
+At position 349 to 419, the domain is characterized as PAS.
+At position 421 to 473, the domain is characterized as PAC.
+At position 674 to 886, the domain is characterized as Histidine kinase.
+At position 47 to 141, the domain is characterized as Ig-like C2-type.
+At position 541 to 608, the domain is characterized as BTB.
+At position 26 to 126, the domain is characterized as Phytocyanin.
+At position 17 to 111, the domain is characterized as HTH arsR-type.
+At position 669 to 752, the domain is characterized as BRCT.
+At position 2007 to 2081, the domain is characterized as Carrier 2.
+At position 32 to 206, the domain is characterized as Helicase ATP-binding.
+At position 228 to 378, the domain is characterized as Helicase C-terminal.
+At position 208 to 421, the domain is characterized as SMP-LTD.
+At position 41 to 174, the domain is characterized as MPN.
+At position 698 to 811, the domain is characterized as Fibronectin type-III.
+At position 419 to 654, the domain is characterized as NR LBD.
+At position 606 to 644, the domain is characterized as LRRCT.
+At position 498 to 661, the domain is characterized as Integrase catalytic.
+At position 965 to 1208, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1 to 56, the domain is characterized as TRAM.
+At position 21 to 199, the domain is characterized as VWFA.
+At position 174 to 247, the domain is characterized as Ubiquitin-like.
+At position 508 to 689, the domain is characterized as PBS-linker 2.
+At position 704 to 881, the domain is characterized as PBS-linker 3.
+At position 16 to 144, the domain is characterized as RNase III.
+At position 171 to 240, the domain is characterized as DRBM.
+At position 22 to 102, the domain is characterized as Importin N-terminal.
+At position 135 to 498, the domain is characterized as MACPF.
+At position 539 to 583, the domain is characterized as TSP type-1 2.
+At position 7 to 131, the domain is characterized as RNase III.
+At position 533 to 575, the domain is characterized as CCT.
+At position 454 to 758, the domain is characterized as Protein kinase.
+At position 115 to 312, the domain is characterized as ATP-grasp.
+At position 39 to 117, the domain is characterized as GIY-YIG.
+At position 14 to 436, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 966 to 1273, the domain is characterized as PKS/mFAS DH.
+At position 2497 to 2574, the domain is characterized as Carrier.
+At position 319 to 475, the domain is characterized as Helicase ATP-binding.
+At position 585 to 755, the domain is characterized as Helicase C-terminal.
+At position 11 to 166, the domain is characterized as UBC core.
+At position 33 to 302, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 317 to 566, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 119 to 216, the domain is characterized as HTH araC/xylS-type.
+At position 80 to 325, the domain is characterized as PE-PPE.
+At position 50 to 361, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 5 to 271, the domain is characterized as F-BAR.
+At position 493 to 555, the domain is characterized as SH3 1.
+At position 577 to 633, the domain is characterized as SH3 2.
+At position 416 to 494, the domain is characterized as RRM 3.
+At position 363 to 641, the domain is characterized as Protein kinase.
+At position 45 to 105, the domain is characterized as MADS-box.
+At position 66 to 236, the domain is characterized as Helicase ATP-binding.
+At position 125 to 195, the domain is characterized as RRM 1.
+At position 200 to 275, the domain is characterized as RRM 2.
+At position 70 to 208, the domain is characterized as Flavodoxin-like.
+At position 22 to 375, the domain is characterized as GH18.
+At position 27 to 128, the domain is characterized as Phytocyanin.
+At position 32 to 162, the domain is characterized as Nudix hydrolase.
+At position 167 to 394, the domain is characterized as Sigma-54 factor interaction.
+At position 21 to 114, the domain is characterized as Ig-like.
+At position 365 to 452, the domain is characterized as Ig-like V-type 4.
+At position 175 to 258, the domain is characterized as PPIase FKBP-type.
+At position 21 to 170, the domain is characterized as MRH.
+At position 851 to 870, the domain is characterized as UIM 1.
+At position 877 to 896, the domain is characterized as UIM 2.
+At position 5 to 99, the domain is characterized as Ig-like.
+At position 416 to 488, the domain is characterized as ACT-like 1.
+At position 509 to 580, the domain is characterized as ACT-like 2.
+At position 129 to 152, the domain is characterized as EF-hand 3.
+At position 153 to 187, the domain is characterized as EF-hand 4.
+At position 16 to 152, the domain is characterized as GAF.
+At position 182 to 432, the domain is characterized as Histidine kinase.
+At position 158 to 233, the domain is characterized as PPIase FKBP-type.
+At position 114 to 190, the domain is characterized as Death.
+At position 188 to 237, the domain is characterized as bHLH.
+At position 322 to 371, the domain is characterized as Myb-like 1.
+At position 377 to 459, the domain is characterized as Myb-like 2.
+At position 9 to 52, the domain is characterized as CHCH.
+At position 23 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 198 to 389, the domain is characterized as GMPS ATP-PPase.
+At position 27 to 406, the domain is characterized as USP.
+At position 88 to 141, the domain is characterized as Kazal-like 2.
+At position 26 to 316, the domain is characterized as GH10.
+At position 21 to 101, the domain is characterized as SCP2.
+At position 351 to 414, the domain is characterized as bZIP.
+At position 186 to 232, the domain is characterized as F-box.
+At position 209 to 299, the domain is characterized as HTH La-type RNA-binding.
+At position 556 to 604, the domain is characterized as GYF.
+At position 82 to 151, the domain is characterized as S1-like.
+At position 81 to 225, the domain is characterized as Flavodoxin-like.
+At position 280 to 522, the domain is characterized as FAD-binding FR-type.
+At position 227 to 289, the domain is characterized as t-SNARE coiled-coil homology.
+At position 169 to 262, the domain is characterized as PPIase FKBP-type.
+At position 9 to 337, the domain is characterized as Kinesin motor.
+At position 290 to 569, the domain is characterized as Protein kinase.
+At position 113 to 257, the domain is characterized as Nudix hydrolase.
+At position 19 to 263, the domain is characterized as ABC transporter.
+At position 309 to 591, the domain is characterized as ABC transporter 1.
+At position 611 to 938, the domain is characterized as ABC transporter 2.
+At position 869 to 904, the domain is characterized as EF-hand.
+At position 1701 to 1818, the domain is characterized as BEACH-type PH.
+At position 1828 to 2118, the domain is characterized as BEACH.
+At position 178 to 255, the domain is characterized as Cytochrome c.
+At position 1 to 192, the domain is characterized as HD-GYP.
+At position 231 to 364, the domain is characterized as GGDEF.
+At position 74 to 126, the domain is characterized as bHLH.
+At position 98 to 331, the domain is characterized as Radical SAM core.
+At position 451 to 593, the domain is characterized as Thioredoxin.
+At position 25 to 95, the domain is characterized as UPAR/Ly6.
+At position 229 to 459, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 54, the domain is characterized as HTH lacI-type.
+At position 365 to 428, the domain is characterized as bZIP.
+At position 284 to 415, the domain is characterized as MATH.
+At position 2 to 212, the domain is characterized as ABC transporter.
+At position 12 to 340, the domain is characterized as PTS EIIC type-2.
+At position 380 to 472, the domain is characterized as PTS EIIB type-2.
+At position 503 to 645, the domain is characterized as PTS EIIA type-2.
+At position 1 to 158, the domain is characterized as PTS EIIB type-4.
+At position 12 to 115, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 133 to 362, the domain is characterized as Radical SAM core.
+At position 636 to 700, the domain is characterized as R3H.
+At position 769 to 812, the domain is characterized as G-patch.
+At position 140 to 391, the domain is characterized as SMP-LTD.
+At position 103 to 347, the domain is characterized as Peptidase S1.
+At position 8 to 150, the domain is characterized as PPPDE.
+At position 105 to 206, the domain is characterized as FAD-binding FR-type.
+At position 268 to 482, the domain is characterized as Histidine kinase.
+At position 29 to 120, the domain is characterized as Fibronectin type-III 1.
+At position 238 to 331, the domain is characterized as Fibronectin type-III 2.
+At position 187 to 378, the domain is characterized as CheB-type methylesterase.
+At position 135 to 394, the domain is characterized as Olfactomedin-like.
+At position 784 to 836, the domain is characterized as GPS.
+At position 8 to 153, the domain is characterized as N-acetyltransferase 1.
+At position 156 to 297, the domain is characterized as N-acetyltransferase 2.
+At position 89 to 356, the domain is characterized as PPM-type phosphatase.
+At position 55 to 261, the domain is characterized as ABC transmembrane type-1.
+At position 572 to 676, the domain is characterized as Cadherin 6.
+At position 3 to 189, the domain is characterized as GMPS ATP-PPase.
+At position 398 to 473, the domain is characterized as B5.
+At position 687 to 780, the domain is characterized as FDX-ACB.
+At position 157 to 410, the domain is characterized as Radical SAM core.
+At position 570 to 647, the domain is characterized as Carrier.
+At position 19 to 206, the domain is characterized as Helicase ATP-binding.
+At position 340 to 517, the domain is characterized as Helicase C-terminal.
+At position 537 to 628, the domain is characterized as Dicer dsRNA-binding fold.
+At position 916 to 1038, the domain is characterized as RNase III 1.
+At position 1083 to 1233, the domain is characterized as RNase III 2.
+At position 20 to 234, the domain is characterized as Radical SAM core.
+At position 43 to 154, the domain is characterized as Rieske.
+At position 232 to 463, the domain is characterized as NR LBD.
+At position 285 to 304, the domain is characterized as UIM.
+At position 4 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 206 to 268, the domain is characterized as t-SNARE coiled-coil homology.
+At position 635 to 652, the domain is characterized as WH2.
+At position 1 to 87, the domain is characterized as Core-binding (CB).
+At position 108 to 291, the domain is characterized as Tyr recombinase.
+At position 311 to 592, the domain is characterized as ABC transporter 1.
+At position 612 to 940, the domain is characterized as ABC transporter 2.
+At position 40 to 157, the domain is characterized as tRNA-binding.
+At position 394 to 457, the domain is characterized as bZIP.
+At position 935 to 1193, the domain is characterized as Protein kinase.
+At position 26 to 103, the domain is characterized as UPAR/Ly6.
+At position 39 to 319, the domain is characterized as IF rod.
+At position 208 to 260, the domain is characterized as HAMP.
+At position 41 to 137, the domain is characterized as Plastocyanin-like 1.
+At position 168 to 350, the domain is characterized as Plastocyanin-like 2.
+At position 397 to 577, the domain is characterized as Plastocyanin-like 3.
+At position 548 to 633, the domain is characterized as BRCT 4.
+At position 641 to 738, the domain is characterized as BRCT 5.
+At position 900 to 991, the domain is characterized as BRCT 6.
+At position 1259 to 1351, the domain is characterized as BRCT 7.
+At position 1389 to 1486, the domain is characterized as BRCT 8.
+At position 364 to 541, the domain is characterized as Helicase ATP-binding.
+At position 701 to 866, the domain is characterized as Helicase C-terminal.
+At position 90 to 269, the domain is characterized as ABC transmembrane type-1.
+At position 28 to 83, the domain is characterized as Chitin-binding type-2 1.
+At position 96 to 141, the domain is characterized as Chitin-binding type-2 2.
+At position 190 to 236, the domain is characterized as Chitin-binding type-2 3.
+At position 304 to 357, the domain is characterized as Chitin-binding type-2 4.
+At position 566 to 614, the domain is characterized as Chitin-binding type-2 5.
+At position 689 to 745, the domain is characterized as Chitin-binding type-2 6.
+At position 782 to 838, the domain is characterized as Chitin-binding type-2 7.
+At position 883 to 942, the domain is characterized as Chitin-binding type-2 8.
+At position 1029 to 1081, the domain is characterized as Chitin-binding type-2 9.
+At position 1105 to 1163, the domain is characterized as Chitin-binding type-2 10.
+At position 1179 to 1237, the domain is characterized as Chitin-binding type-2 11.
+At position 1242 to 1298, the domain is characterized as Chitin-binding type-2 12.
+At position 65 to 179, the domain is characterized as Thioredoxin.
+At position 123 to 477, the domain is characterized as PTS EIIC type-1.
+At position 5 to 100, the domain is characterized as Stress-response A/B barrel 1.
+At position 116 to 204, the domain is characterized as Stress-response A/B barrel 2.
+At position 89 to 262, the domain is characterized as Helicase ATP-binding.
+At position 289 to 438, the domain is characterized as Helicase C-terminal.
+At position 273 to 509, the domain is characterized as NR LBD.
+At position 42 to 197, the domain is characterized as MRH.
+At position 505 to 609, the domain is characterized as PTS EIIA type-1.
+At position 684 to 771, the domain is characterized as WWE.
+At position 805 to 946, the domain is characterized as PARP catalytic.
+At position 366 to 434, the domain is characterized as TRAM.
+At position 159 to 338, the domain is characterized as OBG-type G.
+At position 376 to 452, the domain is characterized as OCT.
+At position 5 to 207, the domain is characterized as DPCK.
+At position 1 to 62, the domain is characterized as 4Fe-4S.
+At position 275 to 373, the domain is characterized as SWIRM.
+At position 144 to 263, the domain is characterized as C2 1.
+At position 275 to 408, the domain is characterized as C2 2.
+At position 42 to 102, the domain is characterized as HTH myb-type.
+At position 72 to 156, the domain is characterized as SAND.
+At position 77 to 295, the domain is characterized as Radical SAM core.
+At position 24 to 329, the domain is characterized as Protein kinase.
+At position 1660 to 1818, the domain is characterized as RNase III 2.
+At position 1843 to 1908, the domain is characterized as DRBM.
+At position 11 to 34, the domain is characterized as RIIa.
+At position 349 to 587, the domain is characterized as ABC transporter.
+At position 830 to 895, the domain is characterized as HTH luxR-type.
+At position 83 to 198, the domain is characterized as Laminin N-terminal.
+At position 163 to 349, the domain is characterized as Glutamine amidotransferase type-1.
+At position 23 to 139, the domain is characterized as MTTase N-terminal.
+At position 401 to 469, the domain is characterized as TRAM.
+At position 78 to 154, the domain is characterized as PUA.
+At position 238 to 326, the domain is characterized as Ig-like C2-type 2.
+At position 330 to 417, the domain is characterized as Ig-like C2-type 3.
+At position 422 to 516, the domain is characterized as Ig-like C2-type 4.
+At position 521 to 607, the domain is characterized as Ig-like C2-type 5.
+At position 612 to 698, the domain is characterized as Ig-like C2-type 6.
+At position 707 to 802, the domain is characterized as Ig-like C2-type 7.
+At position 805 to 902, the domain is characterized as Ig-like C2-type 8.
+At position 907 to 1003, the domain is characterized as Fibronectin type-III 1.
+At position 1008 to 1108, the domain is characterized as Fibronectin type-III 2.
+At position 1113 to 1211, the domain is characterized as Fibronectin type-III 3.
+At position 1215 to 1311, the domain is characterized as Fibronectin type-III 4.
+At position 1312 to 1400, the domain is characterized as Ig-like C2-type 9.
+At position 1402 to 1495, the domain is characterized as Fibronectin type-III 5.
+At position 1496 to 1595, the domain is characterized as Fibronectin type-III 6.
+At position 175 to 226, the domain is characterized as bHLH.
+At position 41 to 200, the domain is characterized as Thioredoxin.
+At position 88 to 230, the domain is characterized as Clp R.
+At position 505 to 540, the domain is characterized as UVR.
+At position 7 to 107, the domain is characterized as FAD-binding FR-type.
+At position 237 to 322, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 89 to 217, the domain is characterized as GST C-terminal.
+At position 409 to 487, the domain is characterized as Cytochrome b5 heme-binding.
+At position 12 to 74, the domain is characterized as HTH iclR-type.
+At position 213 to 376, the domain is characterized as TrmE-type G.
+At position 121 to 365, the domain is characterized as Radical SAM core.
+At position 276 to 415, the domain is characterized as Flavodoxin-like.
+At position 80 to 256, the domain is characterized as Helicase ATP-binding.
+At position 269 to 441, the domain is characterized as Helicase C-terminal.
+At position 40 to 260, the domain is characterized as Radical SAM core.
+At position 162 to 332, the domain is characterized as OBG-type G.
+At position 351 to 432, the domain is characterized as OCT.
+At position 82 to 348, the domain is characterized as AB hydrolase-1.
+At position 44 to 213, the domain is characterized as VWFA.
+At position 6 to 125, the domain is characterized as PH.
+At position 58 to 134, the domain is characterized as Biotinyl-binding.
+At position 121 to 382, the domain is characterized as ABC transporter.
+At position 505 to 693, the domain is characterized as Flavodoxin-like.
+At position 745 to 990, the domain is characterized as FAD-binding FR-type.
+At position 224 to 359, the domain is characterized as PAS 1.
+At position 377 to 483, the domain is characterized as PAS 2.
+At position 59 to 184, the domain is characterized as Thioredoxin.
+At position 45 to 132, the domain is characterized as Death.
+At position 131 to 207, the domain is characterized as Ig-like C2-type 1.
+At position 218 to 314, the domain is characterized as Ig-like C2-type 2.
+At position 21 to 133, the domain is characterized as BTB.
+At position 254 to 530, the domain is characterized as NPH3.
+At position 29 to 106, the domain is characterized as KRAB.
+At position 231 to 689, the domain is characterized as TROVE.
+At position 1175 to 1582, the domain is characterized as NACHT.
+At position 27 to 206, the domain is characterized as RNase H type-2.
+At position 34 to 87, the domain is characterized as WAP.
+At position 121 to 172, the domain is characterized as Kazal-like.
+At position 205 to 298, the domain is characterized as Ig-like C2-type.
+At position 323 to 373, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 381 to 431, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 440 to 561, the domain is characterized as NTR.
+At position 1 to 42, the domain is characterized as C-type lysozyme.
+At position 39 to 121, the domain is characterized as Ig-like C2-type 1.
+At position 181 to 279, the domain is characterized as HTH araC/xylS-type.
+At position 86 to 223, the domain is characterized as OmpA-like.
+At position 81 to 262, the domain is characterized as tr-type G.
+At position 41 to 382, the domain is characterized as GH10.
+At position 291 to 410, the domain is characterized as RanBD1.
+At position 583 to 735, the domain is characterized as SEFIR.
+At position 98 to 415, the domain is characterized as Kinesin motor.
+At position 354 to 433, the domain is characterized as Ubiquitin-like.
+At position 523 to 582, the domain is characterized as HTH myb-type.
+At position 252 to 406, the domain is characterized as Helicase C-terminal.
+At position 347 to 619, the domain is characterized as Protein kinase.
+At position 22 to 277, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 527 to 781, the domain is characterized as EAL.
+At position 91 to 259, the domain is characterized as Helicase ATP-binding.
+At position 447 to 631, the domain is characterized as Helicase C-terminal.
+At position 236 to 418, the domain is characterized as FAD-binding PCMH-type.
+At position 80 to 213, the domain is characterized as C1q.
+At position 363 to 426, the domain is characterized as TRAM.
+At position 65 to 196, the domain is characterized as N-terminal Ras-GEF.
+At position 232 to 501, the domain is characterized as Ras-GEF.
+At position 32 to 209, the domain is characterized as GH16.
+At position 16 to 106, the domain is characterized as RRM 1.
+At position 342 to 435, the domain is characterized as RRM 2.
+At position 111 to 305, the domain is characterized as Pentraxin (PTX).
+At position 536 to 585, the domain is characterized as GPS.
+At position 61 to 256, the domain is characterized as HD.
+At position 729 to 815, the domain is characterized as SUEL-type lectin.
+At position 265 to 318, the domain is characterized as SOCS box.
+At position 23 to 95, the domain is characterized as S4 RNA-binding.
+At position 361 to 406, the domain is characterized as FBD.
+At position 76 to 365, the domain is characterized as FAE.
+At position 805 to 912, the domain is characterized as Calponin-homology (CH).
+At position 114 to 374, the domain is characterized as GS catalytic.
+At position 497 to 621, the domain is characterized as STAS.
+At position 422 to 802, the domain is characterized as USP.
+At position 9 to 96, the domain is characterized as Core-binding (CB).
+At position 118 to 284, the domain is characterized as Tyr recombinase.
+At position 38 to 140, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 266 to 467, the domain is characterized as Helicase C-terminal.
+At position 541 to 852, the domain is characterized as SEC63.
+At position 2 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 262 to 549, the domain is characterized as ABC transmembrane type-1 1.
+At position 579 to 807, the domain is characterized as ABC transporter 1.
+At position 862 to 1142, the domain is characterized as ABC transmembrane type-1 2.
+At position 1180 to 1422, the domain is characterized as ABC transporter 2.
+At position 1089 to 1271, the domain is characterized as Ferric oxidoreductase.
+At position 1272 to 1378, the domain is characterized as FAD-binding FR-type.
+At position 21 to 201, the domain is characterized as N-acetyltransferase.
+At position 73 to 325, the domain is characterized as ABC transporter.
+At position 419 to 629, the domain is characterized as ABC transmembrane type-2.
+At position 20 to 50, the domain is characterized as F-box.
+At position 32 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 28 to 190, the domain is characterized as FAD-binding PCMH-type.
+At position 76 to 150, the domain is characterized as Lipoyl-binding.
+At position 24 to 98, the domain is characterized as KRAB.
+At position 409 to 623, the domain is characterized as BURP.
+At position 6 to 206, the domain is characterized as DhaL.
+At position 37 to 185, the domain is characterized as VOC 1.
+At position 128 to 327, the domain is characterized as MAGE.
+At position 110 to 283, the domain is characterized as EngB-type G.
+At position 76 to 246, the domain is characterized as Helicase ATP-binding.
+At position 361 to 674, the domain is characterized as ABC transmembrane type-1 1.
+At position 706 to 947, the domain is characterized as ABC transporter 1.
+At position 1032 to 1333, the domain is characterized as ABC transmembrane type-1 2.
+At position 1372 to 1622, the domain is characterized as ABC transporter 2.
+At position 99 to 272, the domain is characterized as CRAL-TRIO.
+At position 204 to 253, the domain is characterized as Laminin EGF-like 1.
+At position 254 to 300, the domain is characterized as Laminin EGF-like 2.
+At position 301 to 348, the domain is characterized as Laminin EGF-like 3.
+At position 349 to 399, the domain is characterized as Laminin EGF-like 4.
+At position 400 to 451, the domain is characterized as Laminin EGF-like 5.
+At position 460 to 648, the domain is characterized as PID.
+At position 661 to 746, the domain is characterized as PDZ 1.
+At position 752 to 828, the domain is characterized as PDZ 2.
+At position 171 to 229, the domain is characterized as CTLH.
+At position 24 to 123, the domain is characterized as CBM39.
+At position 144 to 488, the domain is characterized as GH16.
+At position 220 to 418, the domain is characterized as B30.2/SPRY.
+At position 16 to 153, the domain is characterized as N-acetyltransferase 1.
+At position 156 to 316, the domain is characterized as N-acetyltransferase 2.
+At position 44 to 186, the domain is characterized as FAS1.
+At position 307 to 411, the domain is characterized as CobW C-terminal.
+At position 5 to 56, the domain is characterized as SpoVT-AbrB 1.
+At position 7 to 119, the domain is characterized as Glutamine amidotransferase type-1; first part.
+At position 141 to 300, the domain is characterized as N-acetyltransferase 1.
+At position 318 to 484, the domain is characterized as N-acetyltransferase 2.
+At position 501 to 580, the domain is characterized as Glutamine amidotransferase type-1; second part.
+At position 612 to 765, the domain is characterized as N-acetyltransferase 3.
+At position 1055 to 1250, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 114, the domain is characterized as Tyrosine-protein phosphatase.
+At position 118 to 192, the domain is characterized as MBD.
+At position 94 to 310, the domain is characterized as RNase H type-2.
+At position 653 to 934, the domain is characterized as Protein kinase.
+At position 237 to 356, the domain is characterized as sHSP.
+At position 443 to 521, the domain is characterized as UBX.
+At position 35 to 100, the domain is characterized as VWFC 1.
+At position 113 to 179, the domain is characterized as VWFC 2.
+At position 258 to 323, the domain is characterized as VWFC 3.
+At position 92 to 404, the domain is characterized as IF rod.
+At position 26 to 235, the domain is characterized as Velvet.
+At position 71 to 270, the domain is characterized as Peptidase M12A.
+At position 92 to 167, the domain is characterized as PUA.
+At position 171 to 277, the domain is characterized as PRD 2.
+At position 219 to 500, the domain is characterized as CN hydrolase.
+At position 138 to 345, the domain is characterized as TLDc.
+At position 112 to 229, the domain is characterized as EamA.
+At position 148 to 461, the domain is characterized as NB-ARC.
+At position 32 to 133, the domain is characterized as SRCR 1.
+At position 159 to 287, the domain is characterized as SRCR 2.
+At position 311 to 411, the domain is characterized as SRCR 3.
+At position 421 to 529, the domain is characterized as SRCR 4.
+At position 87 to 342, the domain is characterized as Protein kinase.
+At position 372 to 401, the domain is characterized as NAF.
+At position 142 to 442, the domain is characterized as Peptidase S8.
+At position 230 to 419, the domain is characterized as Reticulon.
+At position 1 to 138, the domain is characterized as RNase H type-1.
+At position 42 to 111, the domain is characterized as EamA.
+At position 332 to 406, the domain is characterized as ACT-like.
+At position 24 to 102, the domain is characterized as RRM.
+At position 208 to 328, the domain is characterized as Fe2OG dioxygenase.
+At position 1438 to 1510, the domain is characterized as MIB/HERC2.
+At position 2240 to 2648, the domain is characterized as HECT.
+At position 30 to 335, the domain is characterized as Protein kinase.
+At position 14 to 166, the domain is characterized as C2 PI3K-type.
+At position 257 to 439, the domain is characterized as PIK helical.
+At position 515 to 785, the domain is characterized as PI3K/PI4K catalytic.
+At position 724 to 801, the domain is characterized as RRM.
+At position 348 to 400, the domain is characterized as bHLH.
+At position 44 to 148, the domain is characterized as Calponin-homology (CH) 1.
+At position 157 to 263, the domain is characterized as Calponin-homology (CH) 2.
+At position 759 to 794, the domain is characterized as EF-hand 1.
+At position 795 to 830, the domain is characterized as EF-hand 2.
+At position 147 to 205, the domain is characterized as Chromo 2.
+At position 16 to 69, the domain is characterized as HTH cro/C1-type.
+At position 72 to 384, the domain is characterized as IF rod.
+At position 738 to 793, the domain is characterized as Sushi.
+At position 794 to 837, the domain is characterized as EGF-like; calcium-binding.
+At position 348 to 398, the domain is characterized as FBD.
+At position 7 to 231, the domain is characterized as ABC transporter.
+At position 43 to 324, the domain is characterized as PPM-type phosphatase.
+At position 1 to 88, the domain is characterized as Reverse transcriptase.
+At position 91 to 308, the domain is characterized as Radical SAM core.
+At position 10 to 413, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 17 to 102, the domain is characterized as Core-binding (CB).
+At position 123 to 307, the domain is characterized as Tyr recombinase.
+At position 301 to 325, the domain is characterized as NAF.
+At position 52 to 101, the domain is characterized as Tudor-knot.
+At position 162 to 327, the domain is characterized as MRG.
+At position 1 to 273, the domain is characterized as SMP-LTD.
+At position 41 to 177, the domain is characterized as SCP 1.
+At position 242 to 387, the domain is characterized as SCP 2.
+At position 1 to 143, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 109 to 331, the domain is characterized as Radical SAM core.
+At position 147 to 245, the domain is characterized as PH.
+At position 782 to 1030, the domain is characterized as PPM-type phosphatase.
+At position 122 to 294, the domain is characterized as Phosphatase tensin-type.
+At position 299 to 425, the domain is characterized as C2 tensin-type.
+At position 1140 to 1247, the domain is characterized as SH2.
+At position 1275 to 1408, the domain is characterized as PTB.
+At position 14 to 166, the domain is characterized as Flavodoxin-like.
+At position 200 to 384, the domain is characterized as Helicase ATP-binding.
+At position 411 to 562, the domain is characterized as Helicase C-terminal.
+At position 112 to 167, the domain is characterized as FHA.
+At position 525 to 600, the domain is characterized as Bromo.
+At position 34 to 200, the domain is characterized as FAD-binding PCMH-type.
+At position 69 to 113, the domain is characterized as LEM.
+At position 40 to 145, the domain is characterized as Core-binding (CB).
+At position 167 to 346, the domain is characterized as Tyr recombinase.
+At position 29 to 455, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1000 to 1314, the domain is characterized as PKS/mFAS DH.
+At position 2516 to 2593, the domain is characterized as Carrier.
+At position 43 to 170, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 64 to 115, the domain is characterized as FHA.
+At position 24 to 303, the domain is characterized as Protein kinase.
+At position 49 to 267, the domain is characterized as Radical SAM core.
+At position 29 to 139, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 215 to 328, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 369 to 556, the domain is characterized as PID.
+At position 569 to 655, the domain is characterized as PDZ 1.
+At position 660 to 735, the domain is characterized as PDZ 2.
+At position 1484 to 1707, the domain is characterized as Collagen IV NC1.
+At position 397 to 453, the domain is characterized as SH3.
+At position 21 to 285, the domain is characterized as Protein kinase.
+At position 26 to 222, the domain is characterized as Lon N-terminal.
+At position 617 to 798, the domain is characterized as Lon proteolytic.
+At position 130 to 387, the domain is characterized as SMP-LTD.
+At position 23 to 292, the domain is characterized as PPM-type phosphatase.
+At position 1020 to 1198, the domain is characterized as Laminin G-like 4.
+At position 1131 to 1364, the domain is characterized as Fibrillar collagen NC1.
+At position 2 to 74, the domain is characterized as Lipoyl-binding 1.
+At position 117 to 191, the domain is characterized as Lipoyl-binding 2.
+At position 222 to 296, the domain is characterized as Lipoyl-binding 3.
+At position 338 to 375, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 381 to 410, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 418 to 450, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 187 to 455, the domain is characterized as Protein kinase.
+At position 469 to 599, the domain is characterized as Ricin B-type lectin.
+At position 24 to 266, the domain is characterized as Radical SAM core.
+At position 9 to 211, the domain is characterized as YjeF N-terminal.
+At position 125 to 285, the domain is characterized as Integrase catalytic.
+At position 2 to 125, the domain is characterized as Peptidase C39.
+At position 333 to 360, the domain is characterized as KOW 1.
+At position 536 to 563, the domain is characterized as KOW 2.
+At position 750 to 777, the domain is characterized as KOW 3.
+At position 17 to 229, the domain is characterized as HD Cas3-type.
+At position 297 to 504, the domain is characterized as Helicase ATP-binding.
+At position 551 to 745, the domain is characterized as Helicase C-terminal.
+At position 131 to 357, the domain is characterized as ATP-grasp.
+At position 124 to 221, the domain is characterized as PpiC.
+At position 24 to 412, the domain is characterized as Helicase ATP-binding.
+At position 117 to 231, the domain is characterized as SET.
+At position 644 to 714, the domain is characterized as Bromo.
+At position 1083 to 1166, the domain is characterized as PWWP.
+At position 89 to 272, the domain is characterized as tr-type G.
+At position 613 to 794, the domain is characterized as B30.2/SPRY.
+At position 17 to 91, the domain is characterized as ZAD.
+At position 39 to 105, the domain is characterized as Inhibitor I9.
+At position 112 to 381, the domain is characterized as Peptidase S8.
+At position 35 to 92, the domain is characterized as HTH lysR-type.
+At position 392 to 548, the domain is characterized as N-acetyltransferase.
+At position 131 to 197, the domain is characterized as S5 DRBM.
+At position 56 to 150, the domain is characterized as PDZ.
+At position 1229 to 1292, the domain is characterized as SAM.
+At position 4 to 250, the domain is characterized as Deacetylase sirtuin-type.
+At position 416 to 534, the domain is characterized as Toprim.
+At position 944 to 1000, the domain is characterized as CBS.
+At position 6 to 133, the domain is characterized as Longin.
+At position 149 to 209, the domain is characterized as v-SNARE coiled-coil homology.
+At position 5 to 120, the domain is characterized as PCI.
+At position 226 to 440, the domain is characterized as Helicase C-terminal.
+At position 500 to 640, the domain is characterized as DOD-type homing endonuclease.
+At position 451 to 630, the domain is characterized as Rab-GAP TBC.
+At position 27 to 157, the domain is characterized as ENTH.
+At position 56 to 372, the domain is characterized as Protein kinase.
+At position 60 to 99, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 100 to 144, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 150 to 191, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 192 to 234, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 150 to 211, the domain is characterized as SEP 1.
+At position 268 to 343, the domain is characterized as SEP 2.
+At position 357 to 434, the domain is characterized as UBX.
+At position 12 to 155, the domain is characterized as Galectin.
+At position 119 to 193, the domain is characterized as Lipoyl-binding 2.
+At position 444 to 505, the domain is characterized as FH1.
+At position 506 to 935, the domain is characterized as FH2.
+At position 59 to 102, the domain is characterized as CHCH.
+At position 26 to 56, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 64 to 93, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 92 to 121, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 133 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 162 to 191, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 201 to 230, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 231 to 260, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 292 to 326, the domain is characterized as 4Fe-4S ferredoxin-type 9.
+At position 334 to 363, the domain is characterized as 4Fe-4S ferredoxin-type 10.
+At position 113 to 253, the domain is characterized as PPC.
+At position 32 to 282, the domain is characterized as PPM-type phosphatase.
+At position 9 to 93, the domain is characterized as Sm.
+At position 356 to 444, the domain is characterized as CBM3.
+At position 47 to 286, the domain is characterized as Laminin N-terminal.
+At position 287 to 346, the domain is characterized as Laminin EGF-like 1.
+At position 347 to 402, the domain is characterized as Laminin EGF-like 2.
+At position 403 to 449, the domain is characterized as Laminin EGF-like 3.
+At position 450 to 502, the domain is characterized as Laminin EGF-like 4.
+At position 503 to 512, the domain is characterized as Laminin EGF-like 5; first part.
+At position 529 to 701, the domain is characterized as Laminin IV type A.
+At position 702 to 747, the domain is characterized as Laminin EGF-like 5; second part.
+At position 752 to 784, the domain is characterized as Laminin EGF-like 6; truncated.
+At position 785 to 834, the domain is characterized as Laminin EGF-like 7.
+At position 835 to 889, the domain is characterized as Laminin EGF-like 8.
+At position 890 to 945, the domain is characterized as Laminin EGF-like 9.
+At position 946 to 993, the domain is characterized as Laminin EGF-like 10.
+At position 994 to 1040, the domain is characterized as Laminin EGF-like 11.
+At position 300 to 644, the domain is characterized as TTL.
+At position 29 to 88, the domain is characterized as SH3.
+At position 101 to 405, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 10 to 168, the domain is characterized as PPIase cyclophilin-type.
+At position 3 to 219, the domain is characterized as ABC transporter.
+At position 93 to 182, the domain is characterized as EH 1.
+At position 126 to 161, the domain is characterized as EF-hand 1.
+At position 426 to 449, the domain is characterized as EF-hand 2.
+At position 427 to 516, the domain is characterized as EH 2.
+At position 460 to 495, the domain is characterized as EF-hand 3.
+At position 1 to 157, the domain is characterized as RPW8.
+At position 589 to 673, the domain is characterized as BRCT.
+At position 47 to 361, the domain is characterized as GT23.
+At position 206 to 644, the domain is characterized as Myotubularin phosphatase.
+At position 153 to 255, the domain is characterized as BACK.
+At position 31 to 481, the domain is characterized as Biotin carboxylation.
+At position 151 to 348, the domain is characterized as ATP-grasp.
+At position 559 to 828, the domain is characterized as Pyruvate carboxyltransferase.
+At position 20 to 123, the domain is characterized as FAD-binding FR-type.
+At position 205 to 603, the domain is characterized as SEC63.
+At position 556 to 612, the domain is characterized as FHA.
+At position 1701 to 1799, the domain is characterized as PH.
+At position 130 to 279, the domain is characterized as MPN.
+At position 11 to 135, the domain is characterized as ADF-H 1.
+At position 184 to 312, the domain is characterized as ADF-H 2.
+At position 128 to 401, the domain is characterized as Dynamin-type G.
+At position 632 to 721, the domain is characterized as GED.
+At position 222 to 292, the domain is characterized as LIM zinc-binding.
+At position 22 to 130, the domain is characterized as Ig-like V-type.
+At position 31 to 108, the domain is characterized as Inhibitor I9.
+At position 113 to 579, the domain is characterized as Peptidase S8.
+At position 352 to 436, the domain is characterized as PA.
+At position 66 to 297, the domain is characterized as GB1/RHD3-type G.
+At position 59 to 246, the domain is characterized as hSac2.
+At position 135 to 175, the domain is characterized as EGF-like.
+At position 94 to 367, the domain is characterized as Peptidase A1.
+At position 29 to 326, the domain is characterized as GH10.
+At position 49 to 121, the domain is characterized as PDZ.
+At position 34 to 394, the domain is characterized as GBD/FH3.
+At position 589 to 615, the domain is characterized as FH1.
+At position 623 to 1016, the domain is characterized as FH2.
+At position 1013 to 1051, the domain is characterized as DAD.
+At position 23 to 96, the domain is characterized as S1-like.
+At position 419 to 693, the domain is characterized as Protein kinase.
+At position 68 to 279, the domain is characterized as YjeF N-terminal.
+At position 492 to 662, the domain is characterized as tr-type G.
+At position 183 to 498, the domain is characterized as IF rod.
+At position 153 to 215, the domain is characterized as t-SNARE coiled-coil homology.
+At position 163 to 225, the domain is characterized as SH3 1.
+At position 237 to 296, the domain is characterized as SH3 2.
+At position 95 to 270, the domain is characterized as Helicase ATP-binding.
+At position 295 to 443, the domain is characterized as Helicase C-terminal.
+At position 295 to 639, the domain is characterized as TTL.
+At position 35 to 200, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 62, the domain is characterized as PWWP.
+At position 4 to 58, the domain is characterized as ClpX-type ZB.
+At position 354 to 453, the domain is characterized as PH.
+At position 6 to 150, the domain is characterized as SprT-like.
+At position 26 to 222, the domain is characterized as ABC transmembrane type-1.
+At position 335 to 463, the domain is characterized as Ricin B-type lectin 1.
+At position 466 to 598, the domain is characterized as Ricin B-type lectin 2.
+At position 103 to 228, the domain is characterized as OTU.
+At position 36 to 339, the domain is characterized as Protein kinase.
+At position 70 to 229, the domain is characterized as CP-type G.
+At position 22 to 439, the domain is characterized as GH18.
+At position 225 to 528, the domain is characterized as Helicase ATP-binding.
+At position 576 to 723, the domain is characterized as Helicase C-terminal.
+At position 32 to 97, the domain is characterized as NAC-A/B.
+At position 7 to 107, the domain is characterized as Rieske.
+At position 760 to 846, the domain is characterized as SUEL-type lectin.
+At position 21 to 215, the domain is characterized as Lon N-terminal.
+At position 603 to 784, the domain is characterized as Lon proteolytic.
+At position 61 to 217, the domain is characterized as N-acetyltransferase.
+At position 49 to 131, the domain is characterized as PDZ.
+At position 67 to 102, the domain is characterized as ShKT 1.
+At position 113 to 150, the domain is characterized as ShKT 2.
+At position 510 to 602, the domain is characterized as PB1.
+At position 9 to 340, the domain is characterized as Kinesin motor.
+At position 11 to 344, the domain is characterized as PTS EIIC type-2.
+At position 437 to 673, the domain is characterized as NR LBD.
+At position 4 to 126, the domain is characterized as PINc.
+At position 311 to 363, the domain is characterized as GAF.
+At position 379 to 461, the domain is characterized as Histidine kinase.
+At position 617 to 674, the domain is characterized as RAP.
+At position 33 to 315, the domain is characterized as ABC transmembrane type-1.
+At position 136 to 372, the domain is characterized as VWFA.
+At position 65 to 278, the domain is characterized as START.
+At position 333 to 407, the domain is characterized as ACT-like.
+At position 221 to 454, the domain is characterized as NR LBD.
+At position 1316 to 1480, the domain is characterized as PNPLA.
+At position 207 to 535, the domain is characterized as Protein kinase.
+At position 3 to 328, the domain is characterized as SAM-dependent MTase C5-type.
+At position 4 to 268, the domain is characterized as Pyruvate carboxyltransferase.
+At position 520 to 640, the domain is characterized as SMC hinge.
+At position 34 to 125, the domain is characterized as GOLD.
+At position 375 to 455, the domain is characterized as B5.
+At position 673 to 763, the domain is characterized as FDX-ACB.
+At position 15 to 86, the domain is characterized as S1 motif.
+At position 314 to 542, the domain is characterized as Lon N-terminal.
+At position 541 to 650, the domain is characterized as CULT.
+At position 32 to 158, the domain is characterized as GAF.
+At position 2 to 111, the domain is characterized as Thioredoxin.
+At position 449 to 756, the domain is characterized as Protein kinase.
+At position 36 to 263, the domain is characterized as Peptidase S1.
+At position 472 to 600, the domain is characterized as Ricin B-type lectin.
+At position 47 to 250, the domain is characterized as Tyr recombinase.
+At position 2 to 44, the domain is characterized as UBA.
+At position 177 to 353, the domain is characterized as Helicase ATP-binding.
+At position 491 to 627, the domain is characterized as Helicase C-terminal.
+At position 372 to 421, the domain is characterized as SOCS box.
+At position 36 to 86, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 68 to 120, the domain is characterized as bHLH.
+At position 7 to 248, the domain is characterized as ABC transporter 1.
+At position 303 to 536, the domain is characterized as ABC transporter 2.
+At position 48 to 160, the domain is characterized as Plastocyanin-like 1.
+At position 474 to 603, the domain is characterized as Plastocyanin-like 3.
+At position 217 to 295, the domain is characterized as Kringle.
+At position 373 to 614, the domain is characterized as Peptidase S1.
+At position 177 to 361, the domain is characterized as Helicase ATP-binding.
+At position 51 to 158, the domain is characterized as sHSP.
+At position 233 to 385, the domain is characterized as GAF 1.
+At position 417 to 601, the domain is characterized as GAF 2.
+At position 631 to 954, the domain is characterized as PDEase.
+At position 106 to 136, the domain is characterized as EGF-like 1.
+At position 276 to 386, the domain is characterized as PX.
+At position 421 to 628, the domain is characterized as BAR.
+At position 217 to 491, the domain is characterized as Protein kinase.
+At position 71 to 340, the domain is characterized as Protein kinase.
+At position 133 to 263, the domain is characterized as Thioredoxin.
+At position 69 to 250, the domain is characterized as FBA.
+At position 62 to 143, the domain is characterized as RRM 1.
+At position 155 to 234, the domain is characterized as RRM 2.
+At position 261 to 333, the domain is characterized as RRM 3.
+At position 26 to 163, the domain is characterized as CBM-cenC 1.
+At position 197 to 344, the domain is characterized as CBM-cenC 2.
+At position 397 to 692, the domain is characterized as GH10.
+At position 261 to 568, the domain is characterized as Protein kinase.
+At position 125 to 185, the domain is characterized as Myb-like.
+At position 144 to 345, the domain is characterized as ATP-grasp.
+At position 173 to 225, the domain is characterized as bHLH.
+At position 35 to 838, the domain is characterized as Protein kinase.
+At position 839 to 882, the domain is characterized as AGC-kinase C-terminal.
+At position 243 to 401, the domain is characterized as PID.
+At position 797 to 991, the domain is characterized as Rab-GAP TBC.
+At position 29 to 220, the domain is characterized as Tyr recombinase.
+At position 46 to 300, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 191 to 303, the domain is characterized as RRM 1.
+At position 311 to 421, the domain is characterized as RRM 2.
+At position 7 to 186, the domain is characterized as KARI N-terminal Rossmann.
+At position 187 to 329, the domain is characterized as KARI C-terminal knotted.
+At position 98 to 174, the domain is characterized as RRM 2.
+At position 190 to 267, the domain is characterized as RRM 3.
+At position 293 to 369, the domain is characterized as RRM 4.
+At position 372 to 556, the domain is characterized as Helicase ATP-binding.
+At position 592 to 739, the domain is characterized as Helicase C-terminal.
+At position 66 to 141, the domain is characterized as ACT.
+At position 30 to 268, the domain is characterized as Peptidase S1.
+At position 494 to 605, the domain is characterized as F5/8 type C.
+At position 595 to 684, the domain is characterized as BRCT.
+At position 22 to 246, the domain is characterized as ABC transporter.
+At position 42 to 159, the domain is characterized as MTTase N-terminal.
+At position 184 to 417, the domain is characterized as Radical SAM core.
+At position 420 to 483, the domain is characterized as TRAM.
+At position 28 to 141, the domain is characterized as SET.
+At position 38 to 364, the domain is characterized as G-alpha.
+At position 468 to 582, the domain is characterized as LTD.
+At position 35 to 102, the domain is characterized as BTB.
+At position 227 to 497, the domain is characterized as Protein kinase.
+At position 1 to 294, the domain is characterized as FERM.
+At position 592 to 650, the domain is characterized as CBS 1.
+At position 800 to 860, the domain is characterized as CBS 2.
+At position 313 to 375, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 467 to 529, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 465 to 568, the domain is characterized as PTS EIIB type-3.
+At position 2 to 44, the domain is characterized as Thioredoxin.
+At position 60 to 277, the domain is characterized as Radical SAM core.
+At position 1 to 196, the domain is characterized as ABC transporter.
+At position 8 to 63, the domain is characterized as HTH myb-type 1.
+At position 65 to 114, the domain is characterized as HTH myb-type 2.
+At position 21 to 85, the domain is characterized as ABC transporter.
+At position 9 to 207, the domain is characterized as YjeF N-terminal.
+At position 185 to 298, the domain is characterized as C-type lectin.
+At position 49 to 290, the domain is characterized as Peptidase S1.
+At position 145 to 324, the domain is characterized as Phosphatase tensin-type.
+At position 331 to 458, the domain is characterized as C2 tensin-type.
+At position 3 to 73, the domain is characterized as Sm.
+At position 342 to 392, the domain is characterized as FBD.
+At position 25 to 114, the domain is characterized as Ig-like C2-type 1.
+At position 113 to 199, the domain is characterized as Ig-like C2-type 2.
+At position 106 to 438, the domain is characterized as GS catalytic.
+At position 158 to 239, the domain is characterized as PRC barrel.
+At position 76 to 302, the domain is characterized as Radical SAM core.
+At position 160 to 195, the domain is characterized as EF-hand 3.
+At position 6 to 244, the domain is characterized as tr-type G.
+At position 46 to 149, the domain is characterized as Cadherin 1.
+At position 372 to 476, the domain is characterized as Cadherin 4.
+At position 477 to 593, the domain is characterized as Cadherin 5.
+At position 17 to 324, the domain is characterized as IF rod.
+At position 42 to 215, the domain is characterized as PI-PLC X-box.
+At position 10 to 85, the domain is characterized as GST N-terminal.
+At position 2 to 208, the domain is characterized as Glutamine amidotransferase type-1.
+At position 256 to 341, the domain is characterized as PDZ.
+At position 126 to 386, the domain is characterized as Histidine kinase.
+At position 12 to 100, the domain is characterized as Acylphosphatase-like.
+At position 62 to 163, the domain is characterized as C-type lectin.
+At position 12 to 477, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 478 to 786, the domain is characterized as UvrD-like helicase C-terminal.
+At position 357 to 436, the domain is characterized as OCT.
+At position 23 to 147, the domain is characterized as Cyclin N-terminal.
+At position 164 to 232, the domain is characterized as SoHo.
+At position 444 to 503, the domain is characterized as SH3 1.
+At position 518 to 579, the domain is characterized as SH3 2.
+At position 674 to 733, the domain is characterized as SH3 3.
+At position 34 to 53, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 36 to 152, the domain is characterized as GOLD.
+At position 299 to 445, the domain is characterized as N-acetyltransferase.
+At position 38 to 265, the domain is characterized as Radical SAM core.
+At position 25 to 157, the domain is characterized as 6-Cys 1.
+At position 168 to 309, the domain is characterized as 6-Cys 2.
+At position 88 to 266, the domain is characterized as Helicase ATP-binding.
+At position 277 to 514, the domain is characterized as Helicase C-terminal.
+At position 259 to 322, the domain is characterized as bZIP.
+At position 114 to 302, the domain is characterized as uDENN FNIP1/2-type.
+At position 310 to 712, the domain is characterized as cDENN FNIP1/2-type.
+At position 718 to 825, the domain is characterized as dDENN FNIP1/2-type.
+At position 21 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 140 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 344, the domain is characterized as Ig-like C2-type 3.
+At position 457 to 746, the domain is characterized as Protein kinase.
+At position 112 to 218, the domain is characterized as Expansin-like EG45.
+At position 231 to 322, the domain is characterized as Expansin-like CBD.
+At position 1075 to 1205, the domain is characterized as N-terminal Ras-GEF.
+At position 1282 to 1517, the domain is characterized as Ras-GEF.
+At position 18 to 79, the domain is characterized as Chitin-binding type-2 1.
+At position 92 to 153, the domain is characterized as Chitin-binding type-2 2.
+At position 125 to 364, the domain is characterized as VWFA.
+At position 194 to 373, the domain is characterized as ABC transmembrane type-1.
+At position 72 to 101, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 102 to 130, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 67 to 260, the domain is characterized as Peptidase M12A.
+At position 275 to 445, the domain is characterized as PCI.
+At position 64 to 173, the domain is characterized as CBM-cenC 1.
+At position 212 to 318, the domain is characterized as CBM-cenC 2.
+At position 918 to 1006, the domain is characterized as Ig-like 1.
+At position 1008 to 1097, the domain is characterized as Ig-like 2.
+At position 373 to 498, the domain is characterized as CRC.
+At position 38 to 319, the domain is characterized as ABC transmembrane type-1.
+At position 351 to 585, the domain is characterized as ABC transporter.
+At position 52 to 227, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 125, the domain is characterized as PTS EIIA type-4.
+At position 468 to 503, the domain is characterized as EF-hand 4.
+At position 739 to 788, the domain is characterized as KA1.
+At position 43 to 134, the domain is characterized as SUEL-type lectin.
+At position 494 to 541, the domain is characterized as GPS.
+At position 23 to 222, the domain is characterized as VWFA 1.
+At position 223 to 263, the domain is characterized as EGF-like.
+At position 264 to 453, the domain is characterized as VWFA 2.
+At position 904 to 1001, the domain is characterized as S1 motif.
+At position 101 to 179, the domain is characterized as PRC barrel.
+At position 90 to 218, the domain is characterized as PLAT.
+At position 221 to 918, the domain is characterized as Lipoxygenase.
+At position 159 to 342, the domain is characterized as MIF4G.
+At position 444 to 560, the domain is characterized as MI.
+At position 223 to 355, the domain is characterized as DCD.
+At position 449 to 619, the domain is characterized as tr-type G.
+At position 253 to 288, the domain is characterized as EF-hand 1.
+At position 297 to 332, the domain is characterized as EF-hand 2.
+At position 415 to 572, the domain is characterized as Ferric oxidoreductase.
+At position 611 to 732, the domain is characterized as FAD-binding FR-type.
+At position 14 to 130, the domain is characterized as MTTase N-terminal.
+At position 153 to 400, the domain is characterized as Radical SAM core.
+At position 403 to 482, the domain is characterized as TRAM.
+At position 3 to 137, the domain is characterized as PINc.
+At position 114 to 142, the domain is characterized as IQ.
+At position 44 to 88, the domain is characterized as Fibronectin type-II 1.
+At position 89 to 134, the domain is characterized as Fibronectin type-II 2.
+At position 261 to 343, the domain is characterized as Toprim.
+At position 105 to 165, the domain is characterized as CBS 1.
+At position 189 to 248, the domain is characterized as CBS 2.
+At position 274 to 333, the domain is characterized as CBS 3.
+At position 396 to 469, the domain is characterized as CBS 4.
+At position 96 to 653, the domain is characterized as FERM.
+At position 377 to 473, the domain is characterized as PH.
+At position 223 to 327, the domain is characterized as EamA 2.
+At position 1 to 194, the domain is characterized as RNase H type-2.
+At position 5 to 109, the domain is characterized as PH.
+At position 156 to 413, the domain is characterized as Protein kinase.
+At position 414 to 485, the domain is characterized as AGC-kinase C-terminal.
+At position 78 to 189, the domain is characterized as DUF1279.
+At position 93 to 249, the domain is characterized as Helicase ATP-binding.
+At position 618 to 783, the domain is characterized as Toprim.
+At position 170 to 207, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 29 to 171, the domain is characterized as Thioredoxin.
+At position 141 to 239, the domain is characterized as CRM 1.
+At position 261 to 357, the domain is characterized as CRM 2.
+At position 40 to 297, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 66 to 402, the domain is characterized as Dynamin-type G.
+At position 506 to 597, the domain is characterized as Fibronectin type-III 3.
+At position 598 to 687, the domain is characterized as Fibronectin type-III 4.
+At position 1043 to 1131, the domain is characterized as Fibronectin type-III 9.
+At position 814 to 834, the domain is characterized as IQ.
+At position 170 to 362, the domain is characterized as CheB-type methylesterase.
+At position 325 to 606, the domain is characterized as ABC transmembrane type-1 1.
+At position 640 to 863, the domain is characterized as ABC transporter 1.
+At position 950 to 1232, the domain is characterized as ABC transmembrane type-1 2.
+At position 1271 to 1503, the domain is characterized as ABC transporter 2.
+At position 1198 to 1273, the domain is characterized as DEP.
+At position 37 to 136, the domain is characterized as Cadherin 1.
+At position 137 to 252, the domain is characterized as Cadherin 2.
+At position 253 to 364, the domain is characterized as Cadherin 3.
+At position 368 to 485, the domain is characterized as Cadherin 4.
+At position 486 to 590, the domain is characterized as Cadherin 5.
+At position 590 to 709, the domain is characterized as Cadherin 6.
+At position 708 to 812, the domain is characterized as Cadherin 7.
+At position 973 to 1010, the domain is characterized as EGF-like 1.
+At position 1011 to 1217, the domain is characterized as Laminin G-like 1.
+At position 1220 to 1260, the domain is characterized as EGF-like 2.
+At position 1263 to 1454, the domain is characterized as Laminin G-like 2.
+At position 1497 to 1535, the domain is characterized as EGF-like 3; calcium-binding.
+At position 130 to 169, the domain is characterized as UBA.
+At position 655 to 822, the domain is characterized as MOSC.
+At position 83 to 147, the domain is characterized as J.
+At position 67 to 284, the domain is characterized as Radical SAM core.
+At position 7 to 77, the domain is characterized as RRM 1.
+At position 86 to 156, the domain is characterized as RRM 2.
+At position 589 to 652, the domain is characterized as R3H.
+At position 716 to 763, the domain is characterized as G-patch.
+At position 2151 to 2214, the domain is characterized as HP.
+At position 6 to 153, the domain is characterized as MGS-like.
+At position 36 to 212, the domain is characterized as BPL/LPL catalytic.
+At position 17 to 193, the domain is characterized as Thioredoxin.
+At position 32 to 286, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 133 to 225, the domain is characterized as Ig-like C2-type.
+At position 333 to 454, the domain is characterized as Thioredoxin.
+At position 337 to 597, the domain is characterized as Protein kinase.
+At position 36 to 235, the domain is characterized as Cupin type-1 1.
+At position 334 to 483, the domain is characterized as Cupin type-1 2.
+At position 113 to 243, the domain is characterized as Galectin.
+At position 107 to 390, the domain is characterized as ABC transmembrane type-1 1.
+At position 473 to 693, the domain is characterized as ABC transporter 1.
+At position 774 to 1061, the domain is characterized as ABC transmembrane type-1 2.
+At position 1103 to 1337, the domain is characterized as ABC transporter 2.
+At position 3 to 151, the domain is characterized as Thioredoxin.
+At position 48 to 262, the domain is characterized as Radical SAM core.
+At position 191 to 909, the domain is characterized as GH81.
+At position 81 to 295, the domain is characterized as OTU.
+At position 4 to 139, the domain is characterized as HTH marR-type.
+At position 78 to 205, the domain is characterized as TBDR plug.
+At position 213 to 1013, the domain is characterized as TBDR beta-barrel.
+At position 223 to 456, the domain is characterized as Rab-GAP TBC.
+At position 24 to 571, the domain is characterized as PLA2c.
+At position 138 to 645, the domain is characterized as Biotin carboxylation.
+At position 291 to 485, the domain is characterized as ATP-grasp.
+At position 772 to 846, the domain is characterized as Biotinyl-binding.
+At position 1593 to 1932, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1936 to 2251, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 21 to 117, the domain is characterized as EthD.
+At position 51 to 187, the domain is characterized as Peptidase S59.
+At position 673 to 752, the domain is characterized as BRCT.
+At position 470 to 520, the domain is characterized as DHHC.
+At position 586 to 653, the domain is characterized as Chromo 1.
+At position 668 to 734, the domain is characterized as Chromo 2.
+At position 767 to 941, the domain is characterized as Helicase ATP-binding.
+At position 1081 to 1252, the domain is characterized as Helicase C-terminal.
+At position 646 to 682, the domain is characterized as EGF-like.
+At position 695 to 809, the domain is characterized as C-type lectin.
+At position 813 to 873, the domain is characterized as Sushi.
+At position 703 to 846, the domain is characterized as VPS9.
+At position 877 to 963, the domain is characterized as Ras-associating.
+At position 52 to 160, the domain is characterized as PH.
+At position 199 to 425, the domain is characterized as Radical SAM core.
+At position 169 to 274, the domain is characterized as Calponin-homology (CH) 2.
+At position 2147 to 2259, the domain is characterized as PH.
+At position 26 to 288, the domain is characterized as Pyruvate carboxyltransferase.
+At position 563 to 643, the domain is characterized as Biotinyl-binding.
+At position 38 to 704, the domain is characterized as GH81.
+At position 454 to 576, the domain is characterized as HD.
+At position 696 to 778, the domain is characterized as ACT 1.
+At position 805 to 877, the domain is characterized as ACT 2.
+At position 150 to 185, the domain is characterized as Tify.
+At position 28 to 56, the domain is characterized as LRRNT.
+At position 186 to 241, the domain is characterized as LRRCT.
+At position 434 to 487, the domain is characterized as FHA.
+At position 619 to 665, the domain is characterized as G-patch.
+At position 139 to 378, the domain is characterized as Radical SAM core.
+At position 687 to 959, the domain is characterized as Protein kinase.
+At position 467 to 781, the domain is characterized as Protein kinase.
+At position 148 to 303, the domain is characterized as N-acetyltransferase.
+At position 50 to 192, the domain is characterized as BAH.
+At position 176 to 773, the domain is characterized as Lipoxygenase.
+At position 182 to 232, the domain is characterized as DHHC.
+At position 137 to 311, the domain is characterized as CRAL-TRIO.
+At position 107 to 361, the domain is characterized as Protein kinase.
+At position 6 to 57, the domain is characterized as HTH psq-type.
+At position 70 to 149, the domain is characterized as HTH CENPB-type.
+At position 178 to 403, the domain is characterized as DDE-1.
+At position 119 to 412, the domain is characterized as Protein kinase.
+At position 8 to 491, the domain is characterized as SAM-dependent MTase C5-type.
+At position 229 to 289, the domain is characterized as KH.
+At position 355 to 449, the domain is characterized as HD.
+At position 62 to 282, the domain is characterized as Radical SAM core.
+At position 128 to 203, the domain is characterized as RRM 1.
+At position 225 to 301, the domain is characterized as RRM 2.
+At position 1 to 244, the domain is characterized as PABS.
+At position 729 to 804, the domain is characterized as Smr.
+At position 187 to 224, the domain is characterized as STI1 1.
+At position 225 to 256, the domain is characterized as STI1 2.
+At position 388 to 435, the domain is characterized as STI1 3.
+At position 439 to 471, the domain is characterized as STI1 4.
+At position 548 to 593, the domain is characterized as UBA.
+At position 72 to 132, the domain is characterized as SH3 1.
+At position 155 to 217, the domain is characterized as SH3 2.
+At position 278 to 404, the domain is characterized as PX.
+At position 478 to 551, the domain is characterized as PB1.
+At position 282 to 340, the domain is characterized as GYF.
+At position 572 to 801, the domain is characterized as AIG1-type G.
+At position 25 to 407, the domain is characterized as Peptidase S8.
+At position 669 to 932, the domain is characterized as Autotransporter.
+At position 101 to 186, the domain is characterized as CTCK.
+At position 1468 to 1522, the domain is characterized as AWS.
+At position 1524 to 1641, the domain is characterized as SET.
+At position 1648 to 1664, the domain is characterized as Post-SET.
+At position 2362 to 2395, the domain is characterized as WW.
+At position 82 to 171, the domain is characterized as PB1.
+At position 281 to 361, the domain is characterized as TFIIS N-terminal.
+At position 133 to 212, the domain is characterized as UPAR/Ly6.
+At position 200 to 449, the domain is characterized as NR LBD.
+At position 30 to 275, the domain is characterized as AB hydrolase-1.
+At position 524 to 681, the domain is characterized as GOLD.
+At position 308 to 368, the domain is characterized as PAP-associated.
+At position 175 to 218, the domain is characterized as LRRCT.
+At position 226 to 419, the domain is characterized as B30.2/SPRY.
+At position 1036 to 1292, the domain is characterized as Protein kinase.
+At position 65 to 112, the domain is characterized as Collagen-like.
+At position 149 to 265, the domain is characterized as C-type lectin.
+At position 46 to 186, the domain is characterized as GAF.
+At position 219 to 448, the domain is characterized as Sigma-54 factor interaction.
+At position 20 to 147, the domain is characterized as SCP.
+At position 183 to 215, the domain is characterized as ShKT.
+At position 122 to 217, the domain is characterized as PB1.
+At position 27 to 499, the domain is characterized as Sema.
+At position 501 to 552, the domain is characterized as PSI.
+At position 555 to 640, the domain is characterized as Ig-like C2-type.
+At position 95 to 273, the domain is characterized as FBA.
+At position 537 to 615, the domain is characterized as IPT/TIG.
+At position 1049 to 1078, the domain is characterized as IQ 1.
+At position 1102 to 1131, the domain is characterized as IQ 2.
+At position 317 to 363, the domain is characterized as G-patch.
+At position 67 to 179, the domain is characterized as Thioredoxin.
+At position 9 to 438, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 948 to 1254, the domain is characterized as PKS/mFAS DH.
+At position 2462 to 2539, the domain is characterized as Carrier.
+At position 174 to 261, the domain is characterized as Olduvai.
+At position 4 to 66, the domain is characterized as CSD.
+At position 28 to 259, the domain is characterized as Peptidase S1.
+At position 22 to 143, the domain is characterized as Plastocyanin-like 1.
+At position 196 to 296, the domain is characterized as Plastocyanin-like 2.
+At position 411 to 521, the domain is characterized as Plastocyanin-like 3.
+At position 4 to 150, the domain is characterized as MPN.
+At position 195 to 388, the domain is characterized as Velvet.
+At position 111 to 261, the domain is characterized as Fido.
+At position 39 to 183, the domain is characterized as RNase III.
+At position 209 to 273, the domain is characterized as DRBM.
+At position 17 to 165, the domain is characterized as TNase-like 1.
+At position 192 to 327, the domain is characterized as TNase-like 2.
+At position 340 to 495, the domain is characterized as TNase-like 3.
+At position 524 to 659, the domain is characterized as TNase-like 4.
+At position 728 to 786, the domain is characterized as Tudor.
+At position 52 to 180, the domain is characterized as Thioredoxin.
+At position 149 to 288, the domain is characterized as MRH.
+At position 154 to 402, the domain is characterized as NR LBD.
+At position 35 to 121, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 266 to 450, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 139, the domain is characterized as SPX.
+At position 315 to 357, the domain is characterized as CCT.
+At position 23 to 328, the domain is characterized as Dynamin-type G.
+At position 694 to 781, the domain is characterized as GED.
+At position 38 to 318, the domain is characterized as Alpha-carbonic anhydrase.
+At position 126 to 273, the domain is characterized as C2 Aida-type.
+At position 115 to 204, the domain is characterized as Ig-like C2-type 2.
+At position 213 to 298, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 388, the domain is characterized as Ig-like C2-type 4.
+At position 393 to 472, the domain is characterized as Ig-like C2-type 5.
+At position 487 to 566, the domain is characterized as Ig-like C2-type 6.
+At position 573 to 661, the domain is characterized as Ig-like C2-type 7.
+At position 777 to 1048, the domain is characterized as Protein kinase; inactive.
+At position 123 to 501, the domain is characterized as AB hydrolase-1.
+At position 52 to 137, the domain is characterized as BTB.
+At position 157 to 452, the domain is characterized as IF rod.
+At position 1 to 174, the domain is characterized as UmuC.
+At position 68 to 261, the domain is characterized as Lon N-terminal.
+At position 647 to 828, the domain is characterized as Lon proteolytic.
+At position 55 to 162, the domain is characterized as THUMP.
+At position 54 to 88, the domain is characterized as WW.
+At position 46 to 215, the domain is characterized as PCI.
+At position 84 to 394, the domain is characterized as IF rod.
+At position 679 to 728, the domain is characterized as GRIP.
+At position 84 to 165, the domain is characterized as SH2.
+At position 200 to 248, the domain is characterized as SOCS box.
+At position 234 to 283, the domain is characterized as GRAM 1.
+At position 285 to 382, the domain is characterized as PH.
+At position 704 to 770, the domain is characterized as GRAM 2.
+At position 200 to 609, the domain is characterized as Protein kinase.
+At position 727 to 744, the domain is characterized as WH2.
+At position 1 to 485, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 500 to 772, the domain is characterized as UvrD-like helicase C-terminal.
+At position 185 to 228, the domain is characterized as UBA 1.
+At position 288 to 331, the domain is characterized as STI1.
+At position 372 to 413, the domain is characterized as UBA 2.
+At position 109 to 181, the domain is characterized as KRAB.
+At position 108 to 507, the domain is characterized as Glutamine amidotransferase type-2.
+At position 51 to 146, the domain is characterized as PH.
+At position 88 to 278, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 27 to 250, the domain is characterized as ThyX.
+At position 19 to 147, the domain is characterized as ALOG.
+At position 23 to 91, the domain is characterized as LCN-type CS-alpha/beta.
+At position 179 to 238, the domain is characterized as FYR N-terminal.
+At position 239 to 318, the domain is characterized as FYR C-terminal.
+At position 1695 to 1759, the domain is characterized as KH.
+At position 525 to 810, the domain is characterized as Protein kinase.
+At position 141 to 216, the domain is characterized as RRM 1.
+At position 238 to 314, the domain is characterized as RRM 2.
+At position 262 to 425, the domain is characterized as AMOP.
+At position 37 to 158, the domain is characterized as MPN.
+At position 40 to 69, the domain is characterized as EF-hand 2.
+At position 106 to 140, the domain is characterized as EF-hand 4.
+At position 541 to 684, the domain is characterized as ZU5.
+At position 863 to 940, the domain is characterized as Death.
+At position 199 to 288, the domain is characterized as EH 1.
+At position 494 to 583, the domain is characterized as EH 2.
+At position 527 to 562, the domain is characterized as EF-hand 2.
+At position 80 to 160, the domain is characterized as RRM 1.
+At position 173 to 252, the domain is characterized as RRM 2.
+At position 278 to 350, the domain is characterized as RRM 3.
+At position 676 to 851, the domain is characterized as Helicase ATP-binding.
+At position 877 to 1024, the domain is characterized as Helicase C-terminal.
+At position 1212 to 1292, the domain is characterized as HRDC.
+At position 52 to 175, the domain is characterized as C2.
+At position 529 to 562, the domain is characterized as WW 2.
+At position 580 to 613, the domain is characterized as WW 3.
+At position 672 to 1006, the domain is characterized as HECT.
+At position 500 to 533, the domain is characterized as WW.
+At position 355 to 567, the domain is characterized as ABC transmembrane type-2.
+At position 429 to 550, the domain is characterized as C2 1.
+At position 590 to 717, the domain is characterized as C2 2.
+At position 58 to 131, the domain is characterized as Rho RNA-BD.
+At position 317 to 545, the domain is characterized as ABC transporter 2.
+At position 329 to 446, the domain is characterized as FZ.
+At position 456 to 644, the domain is characterized as Laminin G-like.
+At position 413 to 470, the domain is characterized as SH3.
+At position 6 to 203, the domain is characterized as YjeF N-terminal.
+At position 226 to 310, the domain is characterized as Ig-like C2-type 3.
+At position 314 to 396, the domain is characterized as Ig-like C2-type 4.
+At position 69 to 390, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 214 to 299, the domain is characterized as Disintegrin.
+At position 89 to 397, the domain is characterized as IF rod.
+At position 253 to 496, the domain is characterized as ABC transporter 2.
+At position 324 to 511, the domain is characterized as B30.2/SPRY.
+At position 132 to 342, the domain is characterized as ATP-grasp.
+At position 32 to 240, the domain is characterized as BPL/LPL catalytic.
+At position 69 to 216, the domain is characterized as Thioredoxin.
+At position 37 to 148, the domain is characterized as RWD.
+At position 425 to 731, the domain is characterized as Protein kinase.
+At position 1339 to 1387, the domain is characterized as AWS.
+At position 1390 to 1506, the domain is characterized as SET.
+At position 1514 to 1530, the domain is characterized as Post-SET.
+At position 1952 to 2072, the domain is characterized as BAH.
+At position 266 to 376, the domain is characterized as Calponin-homology (CH) 2.
+At position 395 to 504, the domain is characterized as Calponin-homology (CH) 3.
+At position 516 to 625, the domain is characterized as Calponin-homology (CH) 4.
+At position 84 to 145, the domain is characterized as PA.
+At position 55 to 256, the domain is characterized as ABC transmembrane type-1.
+At position 4 to 168, the domain is characterized as MIF4G.
+At position 352 to 420, the domain is characterized as U-box.
+At position 54 to 125, the domain is characterized as Inhibitor I9.
+At position 134 to 409, the domain is characterized as Peptidase S8.
+At position 540 to 626, the domain is characterized as RWP-RK.
+At position 744 to 827, the domain is characterized as PB1.
+At position 323 to 425, the domain is characterized as UBX.
+At position 192 to 279, the domain is characterized as RRM.
+At position 438 to 679, the domain is characterized as Peptidase S1.
+At position 51 to 204, the domain is characterized as MATH.
+At position 230 to 545, the domain is characterized as USP.
+At position 668 to 720, the domain is characterized as SANT.
+At position 884 to 938, the domain is characterized as HTH myb-type.
+At position 54 to 131, the domain is characterized as PDZ.
+At position 180 to 494, the domain is characterized as FERM.
+At position 26 to 185, the domain is characterized as Helicase ATP-binding.
+At position 23 to 74, the domain is characterized as HTH cro/C1-type 1.
+At position 247 to 301, the domain is characterized as HTH cro/C1-type 2.
+At position 40 to 109, the domain is characterized as KH type-2.
+At position 9 to 47, the domain is characterized as F-box.
+At position 324 to 386, the domain is characterized as Sushi 6.
+At position 446 to 507, the domain is characterized as Sushi 8.
+At position 508 to 566, the domain is characterized as Sushi 9.
+At position 567 to 624, the domain is characterized as Sushi 10.
+At position 806 to 863, the domain is characterized as Sushi 14.
+At position 865 to 933, the domain is characterized as Sushi 15.
+At position 934 to 991, the domain is characterized as Sushi 16.
+At position 992 to 1050, the domain is characterized as Sushi 17.
+At position 1051 to 1109, the domain is characterized as Sushi 18.
+At position 1112 to 1170, the domain is characterized as Sushi 19.
+At position 1171 to 1234, the domain is characterized as Sushi 20.
+At position 1062 to 1306, the domain is characterized as Glutamine amidotransferase type-1.
+At position 4 to 160, the domain is characterized as Flavodoxin-like.
+At position 24 to 165, the domain is characterized as Jacalin-type lectin 1.
+At position 168 to 313, the domain is characterized as Jacalin-type lectin 2.
+At position 57 to 140, the domain is characterized as MANSC.
+At position 250 to 300, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 334 to 370, the domain is characterized as LDL-receptor class A.
+At position 391 to 441, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 221 to 438, the domain is characterized as Letm1 RBD.
+At position 142 to 378, the domain is characterized as Radical SAM core.
+At position 39 to 327, the domain is characterized as Protein kinase.
+At position 151 to 330, the domain is characterized as Exonuclease.
+At position 12 to 210, the domain is characterized as Lon N-terminal.
+At position 17 to 93, the domain is characterized as RRM 1.
+At position 14 to 218, the domain is characterized as Cytochrome b561.
+At position 6 to 401, the domain is characterized as ABC transporter.
+At position 39 to 100, the domain is characterized as FHA.
+At position 50 to 166, the domain is characterized as DOMON.
+At position 28 to 312, the domain is characterized as Deacetylase sirtuin-type.
+At position 5 to 272, the domain is characterized as YjeF C-terminal.
+At position 240 to 430, the domain is characterized as GATase cobBQ-type.
+At position 218 to 299, the domain is characterized as BCNT-C.
+At position 28 to 95, the domain is characterized as BTB.
+At position 208 to 493, the domain is characterized as NPH3.
+At position 57 to 135, the domain is characterized as PDZ.
+At position 181 to 496, the domain is characterized as FERM.
+At position 38 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 497 to 564, the domain is characterized as Dockerin.
+At position 196 to 371, the domain is characterized as CRAL-TRIO.
+At position 7 to 84, the domain is characterized as KRAB.
+At position 27 to 188, the domain is characterized as FAD-binding PCMH-type.
+At position 335 to 616, the domain is characterized as Protein kinase.
+At position 336 to 361, the domain is characterized as NAF.
+At position 15 to 237, the domain is characterized as Sigma-54 factor interaction.
+At position 385 to 609, the domain is characterized as Histidine kinase.
+At position 631 to 745, the domain is characterized as Response regulatory.
+At position 201 to 281, the domain is characterized as KH.
+At position 85 to 273, the domain is characterized as RNase H type-2.
+At position 154 to 355, the domain is characterized as Pentraxin (PTX).
+At position 787 to 839, the domain is characterized as GPS.
+At position 105 to 304, the domain is characterized as MAGE.
+At position 1 to 392, the domain is characterized as Kinesin motor.
+At position 239 to 477, the domain is characterized as Grh/CP2 DB.
+At position 149 to 269, the domain is characterized as OmpA-like.
+At position 368 to 805, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1285 to 1591, the domain is characterized as PKS/mFAS DH.
+At position 1637 to 1712, the domain is characterized as Carrier 1.
+At position 1748 to 1823, the domain is characterized as Carrier 2.
+At position 27 to 100, the domain is characterized as H15.
+At position 141 to 369, the domain is characterized as Sigma-54 factor interaction.
+At position 219 to 366, the domain is characterized as TrmE-type G.
+At position 950 to 1235, the domain is characterized as Protein kinase.
+At position 1238 to 1400, the domain is characterized as KEN.
+At position 75 to 268, the domain is characterized as Brix.
+At position 1 to 307, the domain is characterized as Hcy-binding.
+At position 689 to 773, the domain is characterized as ACT 1.
+At position 800 to 869, the domain is characterized as ACT 2.
+At position 292 to 311, the domain is characterized as UIM 1.
+At position 349 to 368, the domain is characterized as UIM 2.
+At position 1 to 452, the domain is characterized as ADPK.
+At position 152 to 338, the domain is characterized as CheB-type methylesterase.
+At position 27 to 279, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 11 to 84, the domain is characterized as S1-like.
+At position 35 to 508, the domain is characterized as Sema.
+At position 858 to 951, the domain is characterized as IPT/TIG 1.
+At position 1041 to 1139, the domain is characterized as IPT/TIG 3.
+At position 1143 to 1228, the domain is characterized as IPT/TIG 4.
+At position 26 to 143, the domain is characterized as Response regulatory.
+At position 110 to 370, the domain is characterized as GS catalytic.
+At position 25 to 180, the domain is characterized as Helicase ATP-binding.
+At position 3 to 53, the domain is characterized as F-box.
+At position 230 to 401, the domain is characterized as TrmE-type G.
+At position 21 to 131, the domain is characterized as Ig-like 1.
+At position 143 to 226, the domain is characterized as Ig-like 2.
+At position 30 to 135, the domain is characterized as Cadherin 1.
+At position 136 to 245, the domain is characterized as Cadherin 2.
+At position 393 to 497, the domain is characterized as Cadherin 4.
+At position 498 to 609, the domain is characterized as Cadherin 5.
+At position 615 to 721, the domain is characterized as Cadherin 6.
+At position 132 to 568, the domain is characterized as Urease.
+At position 10 to 97, the domain is characterized as Acylphosphatase-like.
+At position 225 to 275, the domain is characterized as DHHC.
+At position 335 to 523, the domain is characterized as Protein kinase.
+At position 160 to 434, the domain is characterized as ABC transporter 1.
+At position 512 to 725, the domain is characterized as ABC transmembrane type-2 1.
+At position 826 to 1078, the domain is characterized as ABC transporter 2.
+At position 1151 to 1365, the domain is characterized as ABC transmembrane type-2 2.
+At position 221 to 488, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 55 to 315, the domain is characterized as Protein kinase.
+At position 15 to 269, the domain is characterized as Protein kinase.
+At position 313 to 340, the domain is characterized as NAF.
+At position 892 to 1005, the domain is characterized as PH.
+At position 219 to 320, the domain is characterized as PpiC 1.
+At position 351 to 450, the domain is characterized as PpiC 2.
+At position 9 to 289, the domain is characterized as YjeF C-terminal.
+At position 206 to 312, the domain is characterized as HTH APSES-type.
+At position 113 to 289, the domain is characterized as NodB homology.
+At position 294 to 336, the domain is characterized as EGF-like 1.
+At position 600 to 640, the domain is characterized as EGF-like 2.
+At position 901 to 941, the domain is characterized as EGF-like 3.
+At position 1212 to 1253, the domain is characterized as EGF-like 4.
+At position 1257 to 1295, the domain is characterized as LDL-receptor class A 1.
+At position 1296 to 1332, the domain is characterized as LDL-receptor class A 2.
+At position 1334 to 1370, the domain is characterized as LDL-receptor class A 3.
+At position 21 to 309, the domain is characterized as Protein kinase.
+At position 57 to 172, the domain is characterized as Expansin-like EG45.
+At position 182 to 262, the domain is characterized as Expansin-like CBD.
+At position 11 to 78, the domain is characterized as Histone-fold.
+At position 1 to 25, the domain is characterized as SAND.
+At position 21 to 213, the domain is characterized as Ch-type lysozyme.
+At position 177 to 244, the domain is characterized as Myb-like 1.
+At position 245 to 301, the domain is characterized as HTH myb-type 1.
+At position 304 to 350, the domain is characterized as Myb-like 2.
+At position 351 to 406, the domain is characterized as HTH myb-type 2.
+At position 407 to 459, the domain is characterized as HTH myb-type 3.
+At position 24 to 50, the domain is characterized as Antistasin-like.
+At position 122 to 206, the domain is characterized as Ig-like C2-type 2.
+At position 389 to 497, the domain is characterized as Cadherin 4.
+At position 137 to 192, the domain is characterized as BRX 1.
+At position 276 to 331, the domain is characterized as BRX 2.
+At position 698 to 773, the domain is characterized as Smr.
+At position 167 to 343, the domain is characterized as CP-type G.
+At position 49 to 147, the domain is characterized as Ig-like C2-type 1.
+At position 152 to 248, the domain is characterized as Ig-like C2-type 2.
+At position 255 to 335, the domain is characterized as Ig-like C2-type 3.
+At position 340 to 419, the domain is characterized as Ig-like C2-type 4.
+At position 424 to 520, the domain is characterized as Ig-like C2-type 5.
+At position 780 to 816, the domain is characterized as PAP-associated.
+At position 165 to 293, the domain is characterized as GGDEF.
+At position 66 to 147, the domain is characterized as S1 motif.
+At position 136 to 311, the domain is characterized as CRAL-TRIO.
+At position 212 to 359, the domain is characterized as N-acetyltransferase.
+At position 46 to 308, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 12 to 349, the domain is characterized as Deacetylase sirtuin-type.
+At position 194 to 272, the domain is characterized as RRM.
+At position 571 to 1333, the domain is characterized as Myosin motor.
+At position 1336 to 1365, the domain is characterized as IQ.
+At position 456 to 498, the domain is characterized as CUE.
+At position 320 to 801, the domain is characterized as GH18.
+At position 136 to 179, the domain is characterized as DHHC.
+At position 60 to 171, the domain is characterized as FAD-binding FR-type.
+At position 110 to 303, the domain is characterized as Peptidase M12A.
+At position 368 to 404, the domain is characterized as ShKT 1.
+At position 414 to 450, the domain is characterized as ShKT 2.
+At position 9 to 145, the domain is characterized as B12-binding.
+At position 188 to 420, the domain is characterized as Radical SAM core.
+At position 1 to 675, the domain is characterized as SMP-LTD.
+At position 499 to 614, the domain is characterized as C2.
+At position 95 to 151, the domain is characterized as WHEP-TRS.
+At position 346 to 407, the domain is characterized as LIM zinc-binding 1.
+At position 411 to 470, the domain is characterized as LIM zinc-binding 2.
+At position 471 to 540, the domain is characterized as LIM zinc-binding 3.
+At position 9 to 107, the domain is characterized as PTS EIIA type-3.
+At position 343 to 547, the domain is characterized as Fibrillar collagen NC1.
+At position 88 to 327, the domain is characterized as ABC transporter 1.
+At position 398 to 615, the domain is characterized as ABC transporter 2.
+At position 60 to 203, the domain is characterized as SIS.
+At position 229 to 288, the domain is characterized as CBS 1.
+At position 297 to 350, the domain is characterized as CBS 2.
+At position 341 to 404, the domain is characterized as S4 RNA-binding.
+At position 77 to 142, the domain is characterized as SAM.
+At position 196 to 348, the domain is characterized as HD.
+At position 256 to 326, the domain is characterized as RRM.
+At position 331 to 517, the domain is characterized as PCI.
+At position 20 to 71, the domain is characterized as bHLH.
+At position 145 to 308, the domain is characterized as PPIase cyclophilin-type.
+At position 189 to 462, the domain is characterized as SF4 helicase.
+At position 132 to 491, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 483 to 685, the domain is characterized as Helicase ATP-binding.
+At position 951 to 1134, the domain is characterized as Helicase C-terminal.
+At position 114 to 204, the domain is characterized as Ig-like C1-type.
+At position 4 to 78, the domain is characterized as S1-like.
+At position 25 to 293, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 362 to 636, the domain is characterized as Protein kinase.
+At position 160 to 235, the domain is characterized as Carrier.
+At position 1030 to 1575, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 114 to 314, the domain is characterized as ATP-grasp.
+At position 195 to 299, the domain is characterized as Fe2OG dioxygenase.
+At position 128 to 194, the domain is characterized as PQ-loop 1.
+At position 268 to 333, the domain is characterized as PQ-loop 2.
+At position 271 to 516, the domain is characterized as FAD-binding FR-type.
+At position 40 to 93, the domain is characterized as Tudor.
+At position 36 to 224, the domain is characterized as RNase H type-2.
+At position 185 to 362, the domain is characterized as VWFA.
+At position 298 to 541, the domain is characterized as Glutamine amidotransferase type-1.
+At position 18 to 144, the domain is characterized as Nudix hydrolase.
+At position 273 to 340, the domain is characterized as KH 1.
+At position 366 to 432, the domain is characterized as KH 2.
+At position 691 to 758, the domain is characterized as KH 3.
+At position 427 to 541, the domain is characterized as Toprim.
+At position 229 to 317, the domain is characterized as GAT.
+At position 37 to 170, the domain is characterized as MPN.
+At position 305 to 397, the domain is characterized as PH.
+At position 421 to 543, the domain is characterized as Arf-GAP.
+At position 944 to 1006, the domain is characterized as SH3.
+At position 472 to 506, the domain is characterized as ShKT 1.
+At position 516 to 550, the domain is characterized as ShKT 2.
+At position 591 to 625, the domain is characterized as ShKT 3.
+At position 634 to 667, the domain is characterized as ShKT 4.
+At position 34 to 103, the domain is characterized as POTRA.
+At position 1 to 109, the domain is characterized as Tyrosine-protein phosphatase.
+At position 370 to 405, the domain is characterized as EGF-like 1.
+At position 864 to 896, the domain is characterized as EGF-like 2.
+At position 1188 to 1313, the domain is characterized as C-type lectin.
+At position 1499 to 1533, the domain is characterized as EGF-like 3.
+At position 2016 to 2202, the domain is characterized as VWFA.
+At position 328 to 432, the domain is characterized as Fibronectin type-III 1.
+At position 613 to 875, the domain is characterized as Protein kinase.
+At position 904 to 968, the domain is characterized as SAM.
+At position 37 to 172, the domain is characterized as TBDR plug.
+At position 178 to 790, the domain is characterized as TBDR beta-barrel.
+At position 197 to 295, the domain is characterized as Ig-like.
+At position 222 to 421, the domain is characterized as MAGE.
+At position 45 to 152, the domain is characterized as EamA.
+At position 105 to 140, the domain is characterized as EF-hand 1.
+At position 146 to 174, the domain is characterized as EF-hand 2.
+At position 172 to 207, the domain is characterized as EF-hand 3.
+At position 208 to 244, the domain is characterized as EF-hand 4.
+At position 245 to 274, the domain is characterized as EF-hand 5.
+At position 2 to 172, the domain is characterized as N-acetyltransferase.
+At position 35 to 488, the domain is characterized as Hexokinase.
+At position 5 to 237, the domain is characterized as PABS.
+At position 305 to 383, the domain is characterized as PDZ 1.
+At position 879 to 960, the domain is characterized as PDZ 2.
+At position 88 to 173, the domain is characterized as PNT.
+At position 89 to 254, the domain is characterized as HDAg.
+At position 25 to 131, the domain is characterized as Thioredoxin 1.
+At position 341 to 483, the domain is characterized as Thioredoxin 2.
+At position 2 to 124, the domain is characterized as RCK N-terminal.
+At position 136 to 216, the domain is characterized as RCK C-terminal.
+At position 6 to 252, the domain is characterized as PABS.
+At position 41 to 464, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 935 to 1207, the domain is characterized as PKS/mFAS DH.
+At position 2004 to 2079, the domain is characterized as Carrier.
+At position 469 to 639, the domain is characterized as tr-type G.
+At position 21 to 110, the domain is characterized as SUEL-type lectin.
+At position 82 to 754, the domain is characterized as Peptidase M13.
+At position 293 to 391, the domain is characterized as PpiC 2.
+At position 72 to 235, the domain is characterized as PCI.
+At position 10 to 178, the domain is characterized as TIR.
+At position 192 to 446, the domain is characterized as NB-ARC.
+At position 29 to 116, the domain is characterized as GRAM.
+At position 244 to 432, the domain is characterized as Rab-GAP TBC.
+At position 602 to 637, the domain is characterized as EF-hand 1.
+At position 638 to 673, the domain is characterized as EF-hand 2.
+At position 7 to 87, the domain is characterized as Sm.
+At position 1747 to 1776, the domain is characterized as IQ.
+At position 11 to 67, the domain is characterized as HTH myb-type 1.
+At position 68 to 118, the domain is characterized as HTH myb-type 2.
+At position 70 to 192, the domain is characterized as PX.
+At position 27 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 242 to 342, the domain is characterized as Ig-like C2-type 3.
+At position 462 to 751, the domain is characterized as Protein kinase.
+At position 65 to 111, the domain is characterized as F-box.
+At position 573 to 648, the domain is characterized as RRM 4.
+At position 9 to 626, the domain is characterized as PFL.
+At position 642 to 762, the domain is characterized as Glycine radical.
+At position 471 to 531, the domain is characterized as Kazal-like.
+At position 229 to 313, the domain is characterized as PAZ.
+At position 555 to 879, the domain is characterized as Piwi.
+At position 939 to 1252, the domain is characterized as PKS/mFAS DH.
+At position 2481 to 2558, the domain is characterized as Carrier.
+At position 383 to 550, the domain is characterized as tr-type G.
+At position 30 to 158, the domain is characterized as EamA 1.
+At position 216 to 317, the domain is characterized as EamA 2.
+At position 217 to 389, the domain is characterized as TrmE-type G.
+At position 31 to 108, the domain is characterized as RRM.
+At position 176 to 220, the domain is characterized as bZIP.
+At position 242 to 450, the domain is characterized as DOG1.
+At position 23 to 110, the domain is characterized as CFEM.
+At position 359 to 438, the domain is characterized as PB1.
+At position 149 to 274, the domain is characterized as OTU.
+At position 211 to 268, the domain is characterized as CVC.
+At position 5 to 223, the domain is characterized as ABC transporter.
+At position 77 to 236, the domain is characterized as NAC.
+At position 41 to 155, the domain is characterized as Expansin-like EG45.
+At position 165 to 244, the domain is characterized as Expansin-like CBD.
+At position 21 to 125, the domain is characterized as Phytocyanin.
+At position 941 to 1252, the domain is characterized as PKS/mFAS DH.
+At position 2459 to 2541, the domain is characterized as Carrier.
+At position 81 to 294, the domain is characterized as Ch-type lysozyme.
+At position 69 to 217, the domain is characterized as N-acetyltransferase.
+At position 6 to 76, the domain is characterized as BTB.
+At position 187 to 435, the domain is characterized as NPH3.
+At position 16 to 109, the domain is characterized as GST N-terminal.
+At position 184 to 289, the domain is characterized as PRD 1.
+At position 296 to 403, the domain is characterized as PRD 2.
+At position 407 to 498, the domain is characterized as PTS EIIB type-2.
+At position 499 to 638, the domain is characterized as PTS EIIA type-2.
+At position 33 to 196, the domain is characterized as PPIase cyclophilin-type.
+At position 108 to 159, the domain is characterized as bHLH.
+At position 601 to 770, the domain is characterized as MOSC.
+At position 73 to 108, the domain is characterized as EF-hand 3.
+At position 109 to 144, the domain is characterized as EF-hand 4.
+At position 4 to 147, the domain is characterized as Clp R.
+At position 426 to 461, the domain is characterized as UVR.
+At position 300 to 338, the domain is characterized as LDL-receptor class A.
+At position 339 to 542, the domain is characterized as MAM.
+At position 976 to 1261, the domain is characterized as Protein kinase.
+At position 1 to 80, the domain is characterized as Thioredoxin.
+At position 99 to 214, the domain is characterized as SET.
+At position 332 to 386, the domain is characterized as MIR 1.
+At position 399 to 455, the domain is characterized as MIR 2.
+At position 463 to 521, the domain is characterized as MIR 3.
+At position 372 to 543, the domain is characterized as tr-type G.
+At position 156 to 317, the domain is characterized as Integrase catalytic.
+At position 1366 to 1654, the domain is characterized as Autotransporter.
+At position 670 to 904, the domain is characterized as PH.
+At position 925 to 1045, the domain is characterized as Arf-GAP.
+At position 5 to 304, the domain is characterized as Lon N-terminal.
+At position 756 to 942, the domain is characterized as Lon proteolytic.
+At position 1 to 112, the domain is characterized as MTTase N-terminal.
+At position 130 to 360, the domain is characterized as Radical SAM core.
+At position 99 to 221, the domain is characterized as MSP.
+At position 279 to 395, the domain is characterized as PX.
+At position 2 to 330, the domain is characterized as GH10.
+At position 3 to 253, the domain is characterized as Pyruvate carboxyltransferase.
+At position 89 to 164, the domain is characterized as POTRA.
+At position 371 to 624, the domain is characterized as Protein kinase.
+At position 22 to 318, the domain is characterized as Protein kinase.
+At position 215 to 343, the domain is characterized as OmpA-like.
+At position 149 to 186, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 189 to 412, the domain is characterized as RMT2.
+At position 8 to 197, the domain is characterized as RNase H type-2.
+At position 5 to 237, the domain is characterized as ABC transporter.
+At position 99 to 319, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 10 to 379, the domain is characterized as GBD/FH3.
+At position 457 to 544, the domain is characterized as FH1.
+At position 562 to 1037, the domain is characterized as FH2.
+At position 1065 to 1095, the domain is characterized as DAD.
+At position 9 to 433, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 923 to 1242, the domain is characterized as PKS/mFAS DH.
+At position 2269 to 2346, the domain is characterized as Carrier.
+At position 43 to 107, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 9 to 159, the domain is characterized as NAC.
+At position 228 to 426, the domain is characterized as Helicase ATP-binding.
+At position 478 to 635, the domain is characterized as Helicase C-terminal.
+At position 84 to 186, the domain is characterized as AD.
+At position 7 to 72, the domain is characterized as SAM.
+At position 80 to 174, the domain is characterized as CRIC.
+At position 211 to 293, the domain is characterized as PDZ.
+At position 325 to 546, the domain is characterized as DUF1170.
+At position 377 to 705, the domain is characterized as Kinesin motor.
+At position 259 to 411, the domain is characterized as GAF 1.
+At position 443 to 624, the domain is characterized as GAF 2.
+At position 654 to 1052, the domain is characterized as PDEase.
+At position 6 to 166, the domain is characterized as Thioredoxin.
+At position 1 to 96, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 139 to 168, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 193 to 224, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 46 to 301, the domain is characterized as AB hydrolase-1.
+At position 98 to 169, the domain is characterized as POTRA.
+At position 339 to 485, the domain is characterized as ELMO.
+At position 544 to 679, the domain is characterized as PH.
+At position 119 to 438, the domain is characterized as SAC.
+At position 83 to 301, the domain is characterized as Radical SAM core.
+At position 169 to 327, the domain is characterized as Cupin type-1 1.
+At position 390 to 566, the domain is characterized as Cupin type-1 2.
+At position 15 to 119, the domain is characterized as AB hydrolase-1.
+At position 42 to 165, the domain is characterized as Nudix hydrolase.
+At position 94 to 160, the domain is characterized as bZIP.
+At position 4 to 263, the domain is characterized as Protein kinase.
+At position 142 to 228, the domain is characterized as Ig-like C1-type.
+At position 54 to 200, the domain is characterized as Ricin B-type lectin.
+At position 11 to 53, the domain is characterized as CHCH.
+At position 105 to 145, the domain is characterized as RPE2 insert.
+At position 304 to 638, the domain is characterized as Protein kinase.
+At position 150 to 371, the domain is characterized as Radical SAM core.
+At position 25 to 139, the domain is characterized as Cystatin fetuin-B-type 1.
+At position 150 to 258, the domain is characterized as Cystatin fetuin-B-type 2.
+At position 591 to 696, the domain is characterized as tRNA-binding.
+At position 90 to 421, the domain is characterized as Asparaginase/glutaminase.
+At position 213 to 428, the domain is characterized as BURP.
+At position 406 to 493, the domain is characterized as ARID.
+At position 8 to 152, the domain is characterized as Nudix hydrolase.
+At position 174 to 696, the domain is characterized as GBD/FH3.
+At position 1053 to 1337, the domain is characterized as FH1.
+At position 1348 to 1766, the domain is characterized as FH2.
+At position 1792 to 1826, the domain is characterized as DAD.
+At position 195 to 292, the domain is characterized as ELM2.
+At position 297 to 349, the domain is characterized as SANT.
+At position 375 to 429, the domain is characterized as FBD.
+At position 558 to 622, the domain is characterized as KH.
+At position 709 to 768, the domain is characterized as Tudor.
+At position 2104 to 2139, the domain is characterized as EF-hand 1.
+At position 2141 to 2176, the domain is characterized as EF-hand 2.
+At position 38 to 218, the domain is characterized as BPL/LPL catalytic.
+At position 1211 to 1274, the domain is characterized as LRRCT.
+At position 213 to 271, the domain is characterized as TCP.
+At position 1721 to 1750, the domain is characterized as IQ.
+At position 654 to 938, the domain is characterized as Protein kinase.
+At position 941 to 1072, the domain is characterized as KEN.
+At position 28 to 64, the domain is characterized as EGF-like.
+At position 71 to 152, the domain is characterized as Kringle.
+At position 180 to 426, the domain is characterized as Peptidase S1.
+At position 156 to 297, the domain is characterized as Jacalin-type lectin 2.
+At position 306 to 448, the domain is characterized as Jacalin-type lectin 3.
+At position 9 to 273, the domain is characterized as Kinesin motor.
+At position 202 to 390, the domain is characterized as Glutamine amidotransferase type-1.
+At position 276 to 515, the domain is characterized as MHD.
+At position 257 to 306, the domain is characterized as bHLH.
+At position 377 to 768, the domain is characterized as PIPK.
+At position 10 to 73, the domain is characterized as GST C-terminal.
+At position 5 to 74, the domain is characterized as POTRA.
+At position 97 to 355, the domain is characterized as Protein kinase.
+At position 398 to 433, the domain is characterized as EF-hand 1.
+At position 434 to 469, the domain is characterized as EF-hand 2.
+At position 509 to 539, the domain is characterized as EF-hand 4.
+At position 18 to 216, the domain is characterized as Radical SAM core.
+At position 4 to 62, the domain is characterized as TRAM.
+At position 19 to 324, the domain is characterized as Protein kinase.
+At position 24 to 125, the domain is characterized as Ig-like 1.
+At position 440 to 531, the domain is characterized as Ig-like 5.
+At position 537 to 625, the domain is characterized as Ig-like 6.
+At position 637 to 737, the domain is characterized as Fibronectin type-III.
+At position 745 to 912, the domain is characterized as MAM.
+At position 1 to 164, the domain is characterized as Brix.
+At position 112 to 241, the domain is characterized as C-CAP/cofactor C-like.
+At position 433 to 505, the domain is characterized as Bromo.
+At position 597 to 678, the domain is characterized as NET.
+At position 817 to 830, the domain is characterized as CRIB.
+At position 911 to 1164, the domain is characterized as Protein kinase.
+At position 206 to 371, the domain is characterized as Helicase ATP-binding.
+At position 499 to 650, the domain is characterized as Helicase C-terminal.
+At position 845 to 897, the domain is characterized as SANT 1.
+At position 946 to 1007, the domain is characterized as SANT 2.
+At position 683 to 900, the domain is characterized as Histidine kinase.
+At position 112 to 293, the domain is characterized as Rho-GAP.
+At position 30 to 121, the domain is characterized as Chorein N-terminal.
+At position 232 to 343, the domain is characterized as HIT.
+At position 49 to 141, the domain is characterized as ATP-cone.
+At position 713 to 801, the domain is characterized as Smr.
+At position 266 to 342, the domain is characterized as B5.
+At position 591 to 761, the domain is characterized as tr-type G.
+At position 398 to 448, the domain is characterized as DHHC.
+At position 25 to 159, the domain is characterized as Plastocyanin-like 1.
+At position 170 to 312, the domain is characterized as Plastocyanin-like 2.
+At position 380 to 499, the domain is characterized as Plastocyanin-like 3.
+At position 215 to 309, the domain is characterized as Fe2OG dioxygenase.
+At position 22 to 75, the domain is characterized as Clip.
+At position 110 to 361, the domain is characterized as Peptidase S1.
+At position 61 to 266, the domain is characterized as SEC7.
+At position 37 to 252, the domain is characterized as GB1/RHD3-type G.
+At position 59 to 125, the domain is characterized as Sm.
+At position 112 to 314, the domain is characterized as ATP-grasp.
+At position 16 to 276, the domain is characterized as Deacetylase sirtuin-type.
+At position 142 to 363, the domain is characterized as Radical SAM core.
+At position 114 to 163, the domain is characterized as bHLH.
+At position 17 to 126, the domain is characterized as CFEM.
+At position 162 to 297, the domain is characterized as Fatty acid hydroxylase.
+At position 229 to 302, the domain is characterized as Carrier.
+At position 379 to 508, the domain is characterized as CBM6 1.
+At position 517 to 634, the domain is characterized as CBM6 2.
+At position 498 to 763, the domain is characterized as Protein kinase.
+At position 764 to 854, the domain is characterized as AGC-kinase C-terminal.
+At position 209 to 327, the domain is characterized as Response regulatory.
+At position 216 to 235, the domain is characterized as UIM 1.
+At position 273 to 292, the domain is characterized as UIM 2.
+At position 1853 to 1882, the domain is characterized as IQ.
+At position 8 to 327, the domain is characterized as Kinesin motor.
+At position 22 to 270, the domain is characterized as AB hydrolase-1.
+At position 120 to 201, the domain is characterized as RRM 1.
+At position 591 to 624, the domain is characterized as WW.
+At position 81 to 319, the domain is characterized as Lon N-terminal.
+At position 318 to 426, the domain is characterized as CULT.
+At position 119 to 301, the domain is characterized as ATP-grasp.
+At position 25 to 144, the domain is characterized as NTR.
+At position 219 to 416, the domain is characterized as HIN-200.
+At position 508 to 692, the domain is characterized as Helicase ATP-binding 1.
+At position 718 to 921, the domain is characterized as Helicase C-terminal.
+At position 998 to 1308, the domain is characterized as SEC63 1.
+At position 1357 to 1533, the domain is characterized as Helicase ATP-binding 2.
+At position 1846 to 2160, the domain is characterized as SEC63 2.
+At position 47 to 336, the domain is characterized as ABC transmembrane type-1 1.
+At position 372 to 607, the domain is characterized as ABC transporter 1.
+At position 681 to 969, the domain is characterized as ABC transmembrane type-1 2.
+At position 1004 to 1240, the domain is characterized as ABC transporter 2.
+At position 3 to 138, the domain is characterized as ADF-H.
+At position 275 to 576, the domain is characterized as PI3K/PI4K catalytic.
+At position 22 to 235, the domain is characterized as Radical SAM core.
+At position 127 to 233, the domain is characterized as PH.
+At position 224 to 343, the domain is characterized as C2.
+At position 381 to 567, the domain is characterized as Rho-GAP.
+At position 868 to 1022, the domain is characterized as Helicase C-terminal.
+At position 44 to 117, the domain is characterized as IGFBP N-terminal.
+At position 208 to 253, the domain is characterized as TSP type-1.
+At position 268 to 342, the domain is characterized as CTCK.
+At position 304 to 576, the domain is characterized as Protein kinase.
+At position 241 to 669, the domain is characterized as Peptidase S53.
+At position 86 to 234, the domain is characterized as Ig-like V-type.
+At position 169 to 296, the domain is characterized as sHSP.
+At position 35 to 82, the domain is characterized as KH.
+At position 22 to 137, the domain is characterized as Rhodanese 1.
+At position 167 to 280, the domain is characterized as Rhodanese 2.
+At position 76 to 292, the domain is characterized as RNase H type-2.
+At position 368 to 449, the domain is characterized as PDZ.
+At position 33 to 161, the domain is characterized as PLAT.
+At position 164 to 866, the domain is characterized as Lipoxygenase.
+At position 46 to 399, the domain is characterized as G-alpha.
+At position 233 to 399, the domain is characterized as Helicase ATP-binding.
+At position 424 to 598, the domain is characterized as Helicase C-terminal.
+At position 210 to 501, the domain is characterized as ABC transmembrane type-1.
+At position 608 to 866, the domain is characterized as ABC transporter.
+At position 35 to 77, the domain is characterized as CHCH.
+At position 19 to 97, the domain is characterized as DED 1.
+At position 114 to 187, the domain is characterized as DED 2.
+At position 131 to 196, the domain is characterized as BTB.
+At position 277 to 595, the domain is characterized as Peptidase S8.
+At position 604 to 737, the domain is characterized as P/Homo B.
+At position 9 to 108, the domain is characterized as Ig-like C2-type.
+At position 115 to 327, the domain is characterized as SMP-LTD.
+At position 320 to 448, the domain is characterized as MATH.
+At position 49 to 134, the domain is characterized as PNT.
+At position 72 to 351, the domain is characterized as CN hydrolase.
+At position 437 to 776, the domain is characterized as HECT.
+At position 331 to 613, the domain is characterized as ABC transmembrane type-1.
+At position 654 to 887, the domain is characterized as ABC transporter.
+At position 38 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 209 to 465, the domain is characterized as Fibrinogen C-terminal.
+At position 2 to 129, the domain is characterized as EamA 1.
+At position 141 to 273, the domain is characterized as EamA 2.
+At position 2 to 80, the domain is characterized as ZAD.
+At position 383 to 819, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1324 to 1633, the domain is characterized as PKS/mFAS DH.
+At position 1684 to 1758, the domain is characterized as Carrier 1.
+At position 1796 to 1874, the domain is characterized as Carrier 2.
+At position 1 to 91, the domain is characterized as ATP-cone.
+At position 311 to 384, the domain is characterized as RRM.
+At position 448 to 545, the domain is characterized as SWIRM.
+At position 617 to 668, the domain is characterized as SANT.
+At position 322 to 382, the domain is characterized as PAP-associated.
+At position 76 to 320, the domain is characterized as Radical SAM core 1.
+At position 296 to 436, the domain is characterized as SIS 1.
+At position 317 to 508, the domain is characterized as E2.
+At position 33 to 145, the domain is characterized as AB hydrolase-1.
+At position 603 to 681, the domain is characterized as BRCT.
+At position 577 to 912, the domain is characterized as HECT.
+At position 151 to 266, the domain is characterized as FAD-binding FR-type.
+At position 141 to 303, the domain is characterized as ELMO.
+At position 9 to 90, the domain is characterized as Carrier.
+At position 258 to 327, the domain is characterized as MBD.
+At position 403 to 456, the domain is characterized as FYR N-terminal.
+At position 550 to 698, the domain is characterized as FYR C-terminal.
+At position 1157 to 1228, the domain is characterized as Bromo.
+At position 70 to 244, the domain is characterized as Reticulon.
+At position 55 to 83, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 7 to 363, the domain is characterized as Kinesin motor.
+At position 155 to 361, the domain is characterized as ATP-grasp.
+At position 292 to 366, the domain is characterized as U-box.
+At position 92 to 178, the domain is characterized as PPIase FKBP-type.
+At position 451 to 541, the domain is characterized as Big-1.
+At position 1270 to 1305, the domain is characterized as EF-hand.
+At position 220 to 372, the domain is characterized as TrmE-type G.
+At position 200 to 339, the domain is characterized as CBM21.
+At position 53 to 345, the domain is characterized as Velvet.
+At position 195 to 300, the domain is characterized as PRD 1.
+At position 305 to 410, the domain is characterized as PRD 2.
+At position 413 to 502, the domain is characterized as PTS EIIB type-2.
+At position 536 to 683, the domain is characterized as PTS EIIA type-2.
+At position 235 to 622, the domain is characterized as GRAS.
+At position 179 to 355, the domain is characterized as EngA-type G 2.
+At position 356 to 441, the domain is characterized as KH-like.
+At position 133 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 314 to 409, the domain is characterized as Ig-like C2-type 4.
+At position 418 to 504, the domain is characterized as Ig-like C2-type 5.
+At position 524 to 618, the domain is characterized as Fibronectin type-III 1.
+At position 637 to 735, the domain is characterized as Fibronectin type-III 2.
+At position 739 to 836, the domain is characterized as Fibronectin type-III 3.
+At position 49 to 183, the domain is characterized as Nudix hydrolase.
+At position 807 to 1038, the domain is characterized as ABC transporter 1.
+At position 1793 to 2025, the domain is characterized as ABC transporter 2.
+At position 212 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 59, the domain is characterized as N-terminal Ras-GEF.
+At position 197 to 434, the domain is characterized as Ras-GEF.
+At position 26 to 132, the domain is characterized as WAC.
+At position 578 to 642, the domain is characterized as DDT.
+At position 1321 to 1391, the domain is characterized as Bromo.
+At position 55 to 192, the domain is characterized as EamA 1.
+At position 216 to 340, the domain is characterized as EamA 2.
+At position 28 to 339, the domain is characterized as YjeF C-terminal.
+At position 67 to 375, the domain is characterized as IF rod.
+At position 30 to 74, the domain is characterized as LysM.
+At position 85 to 209, the domain is characterized as Peptidase C51.
+At position 625 to 703, the domain is characterized as BRCT.
+At position 76 to 344, the domain is characterized as Protein kinase.
+At position 394 to 492, the domain is characterized as Zinc-hook.
+At position 67 to 372, the domain is characterized as PPM-type phosphatase.
+At position 21 to 122, the domain is characterized as EH 1.
+At position 268 to 359, the domain is characterized as EH 2.
+At position 301 to 336, the domain is characterized as EF-hand.
+At position 37 to 150, the domain is characterized as sHSP.
+At position 38 to 207, the domain is characterized as Phosphatase tensin-type.
+At position 212 to 337, the domain is characterized as C2 tensin-type.
+At position 1083 to 1187, the domain is characterized as SH2.
+At position 1209 to 1353, the domain is characterized as PTB.
+At position 87 to 160, the domain is characterized as Ubiquitin-like 2.
+At position 508 to 684, the domain is characterized as VWFA.
+At position 22 to 160, the domain is characterized as SIS.
+At position 41 to 87, the domain is characterized as G-patch.
+At position 370 to 636, the domain is characterized as ZP.
+At position 1 to 155, the domain is characterized as SPX.
+At position 172 to 296, the domain is characterized as GST C-terminal.
+At position 297 to 533, the domain is characterized as Glutamine amidotransferase type-1.
+At position 503 to 630, the domain is characterized as Ricin B-type lectin.
+At position 35 to 505, the domain is characterized as Sema.
+At position 507 to 558, the domain is characterized as PSI.
+At position 567 to 649, the domain is characterized as Ig-like C2-type.
+At position 223 to 460, the domain is characterized as NR LBD.
+At position 38 to 67, the domain is characterized as LRRNT.
+At position 33 to 110, the domain is characterized as Inhibitor I9.
+At position 115 to 559, the domain is characterized as Peptidase S8.
+At position 354 to 414, the domain is characterized as PA.
+At position 182 to 328, the domain is characterized as KARI C-terminal knotted.
+At position 51 to 79, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 114 to 365, the domain is characterized as AB hydrolase-1.
+At position 44 to 332, the domain is characterized as AB hydrolase-1.
+At position 1 to 275, the domain is characterized as IF rod.
+At position 61 to 178, the domain is characterized as HD.
+At position 471 to 669, the domain is characterized as MAGE.
+At position 116 to 476, the domain is characterized as PTS EIIC type-1.
+At position 3 to 97, the domain is characterized as FAD-binding FR-type.
+At position 18 to 240, the domain is characterized as Peptidase S1.
+At position 12 to 47, the domain is characterized as EF-hand 3.
+At position 48 to 80, the domain is characterized as EF-hand 4.
+At position 387 to 666, the domain is characterized as Protein kinase.
+At position 45 to 522, the domain is characterized as Sema.
+At position 552 to 663, the domain is characterized as Ig-like C2-type.
+At position 126 to 229, the domain is characterized as Rieske.
+At position 94 to 173, the domain is characterized as PRC barrel.
+At position 492 to 672, the domain is characterized as Helicase C-terminal.
+At position 175 to 292, the domain is characterized as OmpA-like.
+At position 37 to 256, the domain is characterized as ABC transporter.
+At position 16 to 138, the domain is characterized as Rhodanese.
+At position 40 to 72, the domain is characterized as LisH.
+At position 73 to 129, the domain is characterized as CTLH.
+At position 293 to 437, the domain is characterized as Helicase C-terminal.
+At position 48 to 145, the domain is characterized as RRM.
+At position 54 to 338, the domain is characterized as Protein kinase.
+At position 37 to 214, the domain is characterized as Helicase ATP-binding.
+At position 400 to 567, the domain is characterized as Helicase C-terminal.
+At position 585 to 675, the domain is characterized as Dicer dsRNA-binding fold.
+At position 856 to 978, the domain is characterized as PAZ.
+At position 1010 to 1173, the domain is characterized as RNase III 1.
+At position 1214 to 1358, the domain is characterized as RNase III 2.
+At position 1384 to 1451, the domain is characterized as DRBM 1.
+At position 1569 to 1645, the domain is characterized as DRBM 2.
+At position 768 to 855, the domain is characterized as KHA.
+At position 148 to 210, the domain is characterized as TGS.
+At position 3 to 30, the domain is characterized as DPCK.
+At position 175 to 448, the domain is characterized as ABC transporter 1.
+At position 526 to 739, the domain is characterized as ABC transmembrane type-2 1.
+At position 853 to 1106, the domain is characterized as ABC transporter 2.
+At position 1 to 139, the domain is characterized as Nudix hydrolase.
+At position 35 to 156, the domain is characterized as Bulb-type lectin.
+At position 283 to 322, the domain is characterized as EGF-like; atypical.
+At position 338 to 423, the domain is characterized as PAN.
+At position 515 to 814, the domain is characterized as Protein kinase.
+At position 425 to 523, the domain is characterized as Tudor; atypical.
+At position 272 to 358, the domain is characterized as RRM.
+At position 3 to 16, the domain is characterized as CRIB.
+At position 48 to 225, the domain is characterized as Rho-GAP.
+At position 58 to 184, the domain is characterized as Thioredoxin 1.
+At position 380 to 526, the domain is characterized as Thioredoxin 2.
+At position 13 to 83, the domain is characterized as MBD.
+At position 95 to 411, the domain is characterized as IF rod.
+At position 144 to 425, the domain is characterized as Protein kinase.
+At position 59 to 319, the domain is characterized as Protein kinase.
+At position 399 to 434, the domain is characterized as EF-hand 2.
+At position 481 to 508, the domain is characterized as EF-hand 4.
+At position 919 to 983, the domain is characterized as SAM.
+At position 22 to 280, the domain is characterized as OBG-type G.
+At position 301 to 384, the domain is characterized as TGS.
+At position 44 to 267, the domain is characterized as Fibrinogen C-terminal.
+At position 8 to 421, the domain is characterized as Helicase ATP-binding.
+At position 1739 to 1774, the domain is characterized as EF-hand.
+At position 11 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 201 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 209 to 650, the domain is characterized as Myotubularin phosphatase.
+At position 28 to 65, the domain is characterized as LDL-receptor class A 1.
+At position 70 to 107, the domain is characterized as LDL-receptor class A 2.
+At position 112 to 148, the domain is characterized as LDL-receptor class A 3.
+At position 739 to 1071, the domain is characterized as USP.
+At position 144 to 458, the domain is characterized as Protein kinase.
+At position 3 to 142, the domain is characterized as Flavodoxin-like.
+At position 94 to 176, the domain is characterized as PRC barrel.
+At position 809 to 875, the domain is characterized as SAM 1.
+At position 883 to 948, the domain is characterized as SAM 2.
+At position 1055 to 1212, the domain is characterized as PID.
+At position 377 to 552, the domain is characterized as CRAL-TRIO.
+At position 556 to 662, the domain is characterized as GOLD.
+At position 342 to 478, the domain is characterized as GAF 1.
+At position 509 to 650, the domain is characterized as GAF 2.
+At position 671 to 722, the domain is characterized as HAMP.
+At position 727 to 963, the domain is characterized as Methyl-accepting transducer.
+At position 30 to 162, the domain is characterized as HTH marR-type.
+At position 186 to 302, the domain is characterized as TFIIS central.
+At position 3 to 417, the domain is characterized as SAM-dependent MTase C5-type.
+At position 485 to 648, the domain is characterized as Helicase C-terminal.
+At position 825 to 920, the domain is characterized as Dicer dsRNA-binding fold.
+At position 1100 to 1246, the domain is characterized as PAZ.
+At position 1698 to 1919, the domain is characterized as RNase III 1.
+At position 1993 to 2150, the domain is characterized as RNase III 2.
+At position 2175 to 2241, the domain is characterized as DRBM.
+At position 16 to 65, the domain is characterized as F-box.
+At position 353 to 403, the domain is characterized as FBD.
+At position 354 to 419, the domain is characterized as S4 RNA-binding.
+At position 207 to 256, the domain is characterized as bHLH.
+At position 1 to 133, the domain is characterized as HTH marR-type.
+At position 65 to 270, the domain is characterized as Protein kinase.
+At position 41 to 329, the domain is characterized as Protein kinase.
+At position 267 to 503, the domain is characterized as NR LBD.
+At position 39 to 128, the domain is characterized as KH type-2.
+At position 78 to 101, the domain is characterized as BRCT.
+At position 128 to 188, the domain is characterized as Myb-like.
+At position 26 to 98, the domain is characterized as S4 RNA-binding.
+At position 21 to 221, the domain is characterized as YjeF N-terminal.
+At position 119 to 279, the domain is characterized as NodB homology.
+At position 186 to 408, the domain is characterized as Fibrinogen C-terminal.
+At position 98 to 248, the domain is characterized as Flavodoxin-like.
+At position 248 to 276, the domain is characterized as KOW.
+At position 53 to 179, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 25 to 186, the domain is characterized as PPIase cyclophilin-type.
+At position 210 to 272, the domain is characterized as t-SNARE coiled-coil homology.
+At position 22 to 140, the domain is characterized as Ig-like V-type 1.
+At position 145 to 256, the domain is characterized as Ig-like V-type 2.
+At position 107 to 184, the domain is characterized as RRM.
+At position 786 to 850, the domain is characterized as SAM.
+At position 283 to 312, the domain is characterized as IQ 1.
+At position 1117 to 1157, the domain is characterized as LRRCT.
+At position 1335 to 1364, the domain is characterized as IQ 2.
+At position 1395 to 1424, the domain is characterized as IQ 3.
+At position 130 to 301, the domain is characterized as Helicase ATP-binding.
+At position 34 to 304, the domain is characterized as GH18.
+At position 814 to 993, the domain is characterized as DOC.
+At position 97 to 201, the domain is characterized as Cytochrome c.
+At position 98 to 334, the domain is characterized as Radical SAM core.
+At position 421 to 694, the domain is characterized as Protein kinase.
+At position 69 to 145, the domain is characterized as Cytochrome b5 heme-binding.
+At position 8 to 156, the domain is characterized as NAC.
+At position 230 to 340, the domain is characterized as PX.
+At position 371 to 574, the domain is characterized as BAR.
+At position 55 to 283, the domain is characterized as Radical SAM core.
+At position 46 to 727, the domain is characterized as Peptidase M13.
+At position 63 to 172, the domain is characterized as Ig-like V-type 2.
+At position 183 to 266, the domain is characterized as Ig-like C2-type 1.
+At position 271 to 347, the domain is characterized as Ig-like C2-type 2.
+At position 354 to 439, the domain is characterized as Ig-like C2-type 3.
+At position 1 to 181, the domain is characterized as N-acetyltransferase.
+At position 3 to 176, the domain is characterized as Tyr recombinase.
+At position 122 to 194, the domain is characterized as Bromo.
+At position 263 to 344, the domain is characterized as NET.
+At position 50 to 199, the domain is characterized as FPL.
+At position 215 to 325, the domain is characterized as Glutaredoxin.
+At position 177 to 285, the domain is characterized as FAD-binding FR-type.
+At position 162 to 331, the domain is characterized as PCI.
+At position 414 to 500, the domain is characterized as B5.
+At position 159 to 260, the domain is characterized as SWIRM.
+At position 89 to 421, the domain is characterized as Peptidase A1.
+At position 524 to 790, the domain is characterized as Protein kinase.
+At position 10 to 265, the domain is characterized as Chorismate mutase.
+At position 343 to 396, the domain is characterized as bHLH.
+At position 601 to 654, the domain is characterized as bHLH.
+At position 143 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 456, the domain is characterized as TRAM.
+At position 1 to 70, the domain is characterized as J.
+At position 12 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 399, the domain is characterized as GMPS ATP-PPase.
+At position 136 to 366, the domain is characterized as Radical SAM core.
+At position 369 to 437, the domain is characterized as TRAM.
+At position 55 to 137, the domain is characterized as SCAN box.
+At position 234 to 304, the domain is characterized as KRAB.
+At position 5 to 107, the domain is characterized as HIT.
+At position 30 to 376, the domain is characterized as FERM.
+At position 313 to 477, the domain is characterized as Helicase ATP-binding.
+At position 507 to 673, the domain is characterized as Helicase C-terminal.
+At position 262 to 376, the domain is characterized as Sox C-terminal.
+At position 162 to 283, the domain is characterized as CMP/dCMP-type deaminase.
+At position 52 to 114, the domain is characterized as PWWP.
+At position 9 to 260, the domain is characterized as Protein kinase.
+At position 209 to 272, the domain is characterized as bZIP.
+At position 268 to 465, the domain is characterized as B30.2/SPRY.
+At position 476 to 548, the domain is characterized as PAS.
+At position 144 to 458, the domain is characterized as IF rod.
+At position 10 to 84, the domain is characterized as NAB.
+At position 248 to 366, the domain is characterized as SET.
+At position 1 to 371, the domain is characterized as PTS EIIC type-1.
+At position 390 to 472, the domain is characterized as PTS EIIB type-1.
+At position 519 to 623, the domain is characterized as PTS EIIA type-1.
+At position 574 to 725, the domain is characterized as STAS.
+At position 21 to 100, the domain is characterized as G protein gamma.
+At position 447 to 563, the domain is characterized as HD.
+At position 686 to 765, the domain is characterized as ACT 1.
+At position 794 to 862, the domain is characterized as ACT 2.
+At position 258 to 407, the domain is characterized as YDG.
+At position 40 to 387, the domain is characterized as Protein kinase.
+At position 388 to 419, the domain is characterized as AGC-kinase C-terminal.
+At position 46 to 99, the domain is characterized as Inhibitor I9.
+At position 103 to 606, the domain is characterized as Peptidase S8.
+At position 377 to 457, the domain is characterized as PA.
+At position 270 to 517, the domain is characterized as Histidine kinase.
+At position 519 to 653, the domain is characterized as CheW-like.
+At position 678 to 796, the domain is characterized as Response regulatory.
+At position 17 to 82, the domain is characterized as LCN-type CS-alpha/beta.
+At position 15 to 72, the domain is characterized as bHLH.
+At position 93 to 126, the domain is characterized as Orange.
+At position 57 to 90, the domain is characterized as Collagen-like.
+At position 186 to 372, the domain is characterized as Helicase ATP-binding.
+At position 399 to 550, the domain is characterized as Helicase C-terminal.
+At position 140 to 358, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 1361 to 1436, the domain is characterized as DEP.
+At position 253 to 343, the domain is characterized as Ig-like C2-type.
+At position 610 to 943, the domain is characterized as Protein kinase.
+At position 333 to 405, the domain is characterized as PAS.
+At position 175 to 473, the domain is characterized as Protein kinase.
+At position 901 to 1183, the domain is characterized as PKS/mFAS DH.
+At position 2029 to 2104, the domain is characterized as Carrier.
+At position 2 to 201, the domain is characterized as DPCK.
+At position 113 to 622, the domain is characterized as Peptidase S8.
+At position 384 to 476, the domain is characterized as PA.
+At position 43 to 410, the domain is characterized as Peptidase A1.
+At position 108 to 206, the domain is characterized as Ig-like C1-type.
+At position 236 to 434, the domain is characterized as MH2.
+At position 1 to 99, the domain is characterized as Glutaredoxin.
+At position 50 to 79, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 97 to 128, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 129 to 158, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 405 to 1175, the domain is characterized as Myosin motor.
+At position 1178 to 1207, the domain is characterized as IQ.
+At position 255 to 290, the domain is characterized as EF-hand.
+At position 7 to 293, the domain is characterized as Protein kinase.
+At position 25 to 173, the domain is characterized as N-acetyltransferase 1.
+At position 195 to 361, the domain is characterized as N-acetyltransferase 2.
+At position 86 to 314, the domain is characterized as Radical SAM core.
+At position 3 to 459, the domain is characterized as Biotin carboxylation.
+At position 1159 to 1239, the domain is characterized as Biotinyl-binding.
+At position 41 to 78, the domain is characterized as Myb-like.
+At position 356 to 491, the domain is characterized as GGDEF.
+At position 58 to 331, the domain is characterized as Dynamin-type G.
+At position 564 to 652, the domain is characterized as GED.
+At position 75 to 178, the domain is characterized as EamA.
+At position 1 to 51, the domain is characterized as Disintegrin.
+At position 8 to 64, the domain is characterized as DPH-type MB.
+At position 277 to 368, the domain is characterized as Ig-like C2-type 1.
+At position 396 to 498, the domain is characterized as Ig-like C2-type 2.
+At position 512 to 607, the domain is characterized as Fibronectin type-III 1.
+At position 640 to 734, the domain is characterized as Fibronectin type-III 2.
+At position 741 to 834, the domain is characterized as Fibronectin type-III 3.
+At position 933 to 1034, the domain is characterized as Fibronectin type-III 4.
+At position 1041 to 1140, the domain is characterized as Fibronectin type-III 5.
+At position 1132 to 1230, the domain is characterized as Ig-like C2-type 3.
+At position 1358 to 1444, the domain is characterized as Ig-like C2-type 4.
+At position 1573 to 1662, the domain is characterized as Ig-like C2-type 5.
+At position 1 to 295, the domain is characterized as FH2.
+At position 8 to 63, the domain is characterized as HTH deoR-type.
+At position 115 to 305, the domain is characterized as Helicase ATP-binding.
+At position 328 to 485, the domain is characterized as Helicase C-terminal.
+At position 392 to 822, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1302 to 1611, the domain is characterized as PKS/mFAS DH.
+At position 1716 to 1790, the domain is characterized as Carrier.
+At position 55 to 135, the domain is characterized as YbbR-like 1.
+At position 143 to 228, the domain is characterized as YbbR-like 2.
+At position 237 to 316, the domain is characterized as YbbR-like 3.
+At position 329 to 394, the domain is characterized as YbbR-like 4.
+At position 31 to 121, the domain is characterized as Chorein N-terminal.
+At position 54 to 287, the domain is characterized as Radical SAM core.
+At position 615 to 730, the domain is characterized as Response regulatory.
+At position 198 to 292, the domain is characterized as Ras-associating.
+At position 294 to 341, the domain is characterized as SARAH.
+At position 247 to 361, the domain is characterized as PAZ.
+At position 518 to 811, the domain is characterized as Piwi.
+At position 279 to 355, the domain is characterized as PUA.
+At position 119 to 178, the domain is characterized as CBS 1.
+At position 182 to 238, the domain is characterized as CBS 2.
+At position 15 to 443, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 973 to 1285, the domain is characterized as PKS/mFAS DH.
+At position 2594 to 2671, the domain is characterized as Carrier.
+At position 33 to 128, the domain is characterized as Ig-like V-type.
+At position 150 to 223, the domain is characterized as Ig-like C2-type.
+At position 87 to 225, the domain is characterized as Flavodoxin-like.
+At position 258 to 472, the domain is characterized as FAD-binding FR-type.
+At position 32 to 61, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 75 to 105, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 92 to 414, the domain is characterized as ABC transmembrane type-1.
+At position 108 to 227, the domain is characterized as BAH.
+At position 269 to 813, the domain is characterized as SAM-dependent MTase C5-type.
+At position 382 to 447, the domain is characterized as Chromo.
+At position 202 to 352, the domain is characterized as VLRF1.
+At position 302 to 922, the domain is characterized as USP.
+At position 525 to 648, the domain is characterized as STAS.
+At position 285 to 359, the domain is characterized as PUA.
+At position 185 to 270, the domain is characterized as PPIase FKBP-type.
+At position 32 to 114, the domain is characterized as Lipoyl-binding.
+At position 32 to 129, the domain is characterized as Yippee.
+At position 264 to 508, the domain is characterized as ABC transporter 2.
+At position 533 to 706, the domain is characterized as tr-type G.
+At position 125 to 438, the domain is characterized as IF rod.
+At position 207 to 368, the domain is characterized as CP-type G.
+At position 399 to 489, the domain is characterized as BRCT.
+At position 995 to 1100, the domain is characterized as N-terminal Ras-GEF.
+At position 46 to 94, the domain is characterized as F-box.
+At position 105 to 297, the domain is characterized as B30.2/SPRY.
+At position 49 to 291, the domain is characterized as GB1/RHD3-type G.
+At position 1355 to 1643, the domain is characterized as Autotransporter.
+At position 30 to 377, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 380 to 704, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 262 to 422, the domain is characterized as EF-1-gamma C-terminal.
+At position 562 to 737, the domain is characterized as PH 1.
+At position 800 to 961, the domain is characterized as PH 2.
+At position 26 to 88, the domain is characterized as t-SNARE coiled-coil homology.
+At position 34 to 161, the domain is characterized as Response regulatory.
+At position 144 to 238, the domain is characterized as Glutaredoxin 1.
+At position 239 to 337, the domain is characterized as Glutaredoxin 2.
+At position 99 to 189, the domain is characterized as Ig-like C2-type 2.
+At position 360 to 583, the domain is characterized as B30.2/SPRY.
+At position 66 to 138, the domain is characterized as HSA.
+At position 674 to 839, the domain is characterized as Helicase ATP-binding.
+At position 1772 to 1922, the domain is characterized as Helicase C-terminal.
+At position 8 to 167, the domain is characterized as N-acetyltransferase.
+At position 139 to 244, the domain is characterized as Fibronectin type-III 1.
+At position 343 to 438, the domain is characterized as Fibronectin type-III 2.
+At position 313 to 359, the domain is characterized as G-patch.
+At position 467 to 603, the domain is characterized as Ricin B-type lectin.
+At position 1 to 212, the domain is characterized as ABC transporter.
+At position 99 to 159, the domain is characterized as S4 RNA-binding.
+At position 135 to 278, the domain is characterized as FCP1 homology.
+At position 39 to 144, the domain is characterized as Cadherin 1.
+At position 145 to 251, the domain is characterized as Cadherin 2.
+At position 252 to 366, the domain is characterized as Cadherin 3.
+At position 367 to 474, the domain is characterized as Cadherin 4.
+At position 474 to 582, the domain is characterized as Cadherin 5.
+At position 218 to 337, the domain is characterized as C2 1.
+At position 371 to 493, the domain is characterized as C2 2.
+At position 522 to 637, the domain is characterized as C2 3.
+At position 52 to 233, the domain is characterized as ABC transmembrane type-1 1.
+At position 310 to 500, the domain is characterized as ABC transmembrane type-1 2.
+At position 1 to 60, the domain is characterized as HTH tetR-type.
+At position 8 to 56, the domain is characterized as Myosin N-terminal SH3-like.
+At position 61 to 731, the domain is characterized as Myosin motor.
+At position 782 to 811, the domain is characterized as IQ 2.
+At position 831 to 850, the domain is characterized as IQ 3.
+At position 853 to 882, the domain is characterized as IQ 4.
+At position 1327 to 1678, the domain is characterized as Dilute.
+At position 158 to 215, the domain is characterized as KH.
+At position 341 to 502, the domain is characterized as Helicase C-terminal.
+At position 238 to 366, the domain is characterized as Nudix hydrolase.
+At position 67 to 331, the domain is characterized as PPM-type phosphatase.
+At position 158 to 348, the domain is characterized as NodB homology.
+At position 89 to 232, the domain is characterized as GST C-terminal.
+At position 265 to 336, the domain is characterized as Myb-like.
+At position 28 to 464, the domain is characterized as Helicase ATP-binding.
+At position 100 to 412, the domain is characterized as IF rod.
+At position 169 to 222, the domain is characterized as bHLH.
+At position 125 to 223, the domain is characterized as Fibronectin type-III.
+At position 159 to 301, the domain is characterized as PPC.
+At position 114 to 149, the domain is characterized as QLQ.
+At position 180 to 224, the domain is characterized as WRC.
+At position 407 to 567, the domain is characterized as Helicase C-terminal.
+At position 235 to 464, the domain is characterized as Sigma-54 factor interaction.
+At position 33 to 208, the domain is characterized as BPL/LPL catalytic.
+At position 473 to 642, the domain is characterized as Integrase catalytic.
+At position 982 to 1043, the domain is characterized as LIM zinc-binding 2.
+At position 1052 to 1117, the domain is characterized as LIM zinc-binding 3.
+At position 1118 to 1179, the domain is characterized as LIM zinc-binding 4.
+At position 125 to 304, the domain is characterized as VWFA.
+At position 144 to 221, the domain is characterized as PRC barrel.
+At position 496 to 629, the domain is characterized as Ricin B-type lectin.
+At position 121 to 409, the domain is characterized as ABC transmembrane type-1.
+At position 442 to 679, the domain is characterized as ABC transporter.
+At position 428 to 482, the domain is characterized as FF 2.
+At position 484 to 549, the domain is characterized as FF 3.
+At position 587 to 762, the domain is characterized as pG1 pseudoGTPase.
+At position 778 to 940, the domain is characterized as pG2 pseudoGTPase.
+At position 1243 to 1430, the domain is characterized as Rho-GAP.
+At position 230 to 364, the domain is characterized as Histidine kinase.
+At position 9 to 338, the domain is characterized as Kinesin motor.
+At position 31 to 246, the domain is characterized as BPL/LPL catalytic.
+At position 490 to 550, the domain is characterized as PWWP.
+At position 3 to 83, the domain is characterized as Carrier.
+At position 111 to 300, the domain is characterized as ATP-grasp.
+At position 7 to 196, the domain is characterized as tr-type G.
+At position 253 to 312, the domain is characterized as LIM zinc-binding.
+At position 533 to 625, the domain is characterized as RRM.
+At position 307 to 375, the domain is characterized as J.
+At position 296 to 551, the domain is characterized as Peptidase M66.
+At position 5 to 92, the domain is characterized as PPIase FKBP-type.
+At position 80 to 254, the domain is characterized as FAD-binding PCMH-type.
+At position 54 to 333, the domain is characterized as AB hydrolase-1.
+At position 43 to 159, the domain is characterized as Thioredoxin.
+At position 218 to 253, the domain is characterized as UVR.
+At position 210 to 285, the domain is characterized as Thyroglobulin type-1.
+At position 28 to 259, the domain is characterized as AB hydrolase-1.
+At position 254 to 313, the domain is characterized as LIM zinc-binding.
+At position 1337 to 1466, the domain is characterized as GOLD.
+At position 268 to 368, the domain is characterized as Ig-like C2-type 3.
+At position 486 to 774, the domain is characterized as Protein kinase.
+At position 363 to 452, the domain is characterized as HTH La-type RNA-binding.
+At position 195 to 247, the domain is characterized as KH.
+At position 32 to 85, the domain is characterized as KH.
+At position 354 to 410, the domain is characterized as HAMP.
+At position 450 to 664, the domain is characterized as Histidine kinase.
+At position 683 to 798, the domain is characterized as Response regulatory.
+At position 821 to 914, the domain is characterized as HPt.
+At position 77 to 274, the domain is characterized as OTU.
+At position 149 to 380, the domain is characterized as Radical SAM core.
+At position 382 to 451, the domain is characterized as TRAM.
+At position 70 to 330, the domain is characterized as Protein kinase.
+At position 18 to 103, the domain is characterized as LBH.
+At position 4 to 76, the domain is characterized as ACT.
+At position 470 to 506, the domain is characterized as CBM1.
+At position 60 to 429, the domain is characterized as Peptidase A1.
+At position 6 to 150, the domain is characterized as Clp R.
+At position 181 to 343, the domain is characterized as PCI.
+At position 705 to 751, the domain is characterized as G-patch.
+At position 800 to 870, the domain is characterized as DRBM.
+At position 6 to 295, the domain is characterized as tr-type G.
+At position 107 to 299, the domain is characterized as ATP-grasp.
+At position 6 to 158, the domain is characterized as NAC.
+At position 94 to 314, the domain is characterized as Radical SAM core.
+At position 29 to 311, the domain is characterized as ABC transmembrane type-1.
+At position 343 to 579, the domain is characterized as ABC transporter.
+At position 91 to 402, the domain is characterized as Peptidase A1.
+At position 81 to 165, the domain is characterized as KH-like.
+At position 516 to 668, the domain is characterized as RNase NYN.
+At position 3 to 205, the domain is characterized as Glutamine amidotransferase type-1.
+At position 52 to 269, the domain is characterized as L-type lectin-like.
+At position 66 to 153, the domain is characterized as SANTA.
+At position 78 to 306, the domain is characterized as ABC transmembrane type-1.
+At position 46 to 74, the domain is characterized as LysM 1; degenerate.
+At position 108 to 140, the domain is characterized as LysM 2; degenerate.
+At position 168 to 211, the domain is characterized as LysM 3.
+At position 322 to 594, the domain is characterized as Protein kinase.
+At position 146 to 226, the domain is characterized as Ig-like C2-type.
+At position 2 to 149, the domain is characterized as Clp R.
+At position 72 to 181, the domain is characterized as Thioredoxin.
+At position 177 to 371, the domain is characterized as Letm1 RBD.
+At position 255 to 346, the domain is characterized as PDZ 1.
+At position 352 to 457, the domain is characterized as PDZ 2.
+At position 218 to 388, the domain is characterized as PCI.
+At position 51 to 151, the domain is characterized as Glutaredoxin.
+At position 105 to 339, the domain is characterized as Radical SAM core.
+At position 143 to 199, the domain is characterized as BTB.
+At position 314 to 392, the domain is characterized as RRM 2.
+At position 501 to 573, the domain is characterized as RRM 3.
+At position 621 to 704, the domain is characterized as RRM 4.
+At position 719 to 796, the domain is characterized as RRM 5.
+At position 7 to 115, the domain is characterized as CBM20 1.
+At position 150 to 264, the domain is characterized as CBM20 2.
+At position 32 to 225, the domain is characterized as Fibrinogen C-terminal.
+At position 2 to 144, the domain is characterized as Jacalin-type lectin 1.
+At position 147 to 294, the domain is characterized as Jacalin-type lectin 2.
+At position 303 to 446, the domain is characterized as Jacalin-type lectin 3.
+At position 139 to 177, the domain is characterized as STI1 1.
+At position 513 to 552, the domain is characterized as STI1 2.
+At position 185 to 263, the domain is characterized as PDZ.
+At position 24 to 77, the domain is characterized as bHLH.
+At position 100 to 172, the domain is characterized as PAS 1.
+At position 266 to 336, the domain is characterized as PAS 2.
+At position 20 to 138, the domain is characterized as Rhodanese 1.
+At position 169 to 280, the domain is characterized as Rhodanese 2.
+At position 307 to 389, the domain is characterized as Helicase ATP-binding; first part.
+At position 438 to 512, the domain is characterized as H15.
+At position 710 to 868, the domain is characterized as Helicase ATP-binding; second part.
+At position 1514 to 1672, the domain is characterized as Helicase C-terminal.
+At position 121 to 288, the domain is characterized as Helicase ATP-binding.
+At position 349 to 521, the domain is characterized as Helicase C-terminal.
+At position 933 to 996, the domain is characterized as Tudor.
+At position 4 to 281, the domain is characterized as tr-type G.
+At position 770 to 849, the domain is characterized as PDZ.
+At position 135 to 335, the domain is characterized as ATP-grasp.
+At position 260 to 415, the domain is characterized as NIDO.
+At position 647 to 798, the domain is characterized as AMOP.
+At position 811 to 1019, the domain is characterized as VWFD.
+At position 1110 to 1170, the domain is characterized as Sushi.
+At position 71 to 260, the domain is characterized as ABC transmembrane type-1.
+At position 698 to 821, the domain is characterized as C2.
+At position 158 to 340, the domain is characterized as CheB-type methylesterase.
+At position 43 to 270, the domain is characterized as Radical SAM core.
+At position 3 to 190, the domain is characterized as Glutamine amidotransferase type-1.
+At position 191 to 382, the domain is characterized as GMPS ATP-PPase.
+At position 39 to 309, the domain is characterized as AB hydrolase-1.
+At position 76 to 325, the domain is characterized as ABC transporter 1.
+At position 388 to 609, the domain is characterized as ABC transporter 2.
+At position 113 to 580, the domain is characterized as Peptidase S8.
+At position 350 to 436, the domain is characterized as PA.
+At position 456 to 557, the domain is characterized as Ricin B-type lectin.
+At position 73 to 136, the domain is characterized as Pre-SET.
+At position 139 to 263, the domain is characterized as SET.
+At position 283 to 299, the domain is characterized as Post-SET.
+At position 396 to 565, the domain is characterized as tr-type G.
+At position 124 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 177 to 228, the domain is characterized as HAMP.
+At position 236 to 438, the domain is characterized as Histidine kinase.
+At position 303 to 353, the domain is characterized as SANT.
+At position 133 to 248, the domain is characterized as GST C-terminal.
+At position 33 to 189, the domain is characterized as SIS.
+At position 154 to 431, the domain is characterized as Protein kinase.
+At position 3 to 89, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 59 to 87, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 95 to 127, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 136 to 172, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 180 to 211, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 1 to 127, the domain is characterized as tr-type G.
+At position 495 to 531, the domain is characterized as EGF-like.
+At position 138 to 299, the domain is characterized as UBC core.
+At position 69 to 356, the domain is characterized as Protein kinase.
+At position 160 to 219, the domain is characterized as SH3 1.
+At position 231 to 290, the domain is characterized as SH3 2.
+At position 414 to 463, the domain is characterized as bHLH.
+At position 397 to 487, the domain is characterized as HTH La-type RNA-binding.
+At position 253 to 332, the domain is characterized as HSA.
+At position 586 to 642, the domain is characterized as Myb-like.
+At position 69 to 151, the domain is characterized as Kringle.
+At position 359 to 543, the domain is characterized as Helicase ATP-binding.
+At position 577 to 726, the domain is characterized as Helicase C-terminal.
+At position 28 to 80, the domain is characterized as Tudor-knot.
+At position 216 to 490, the domain is characterized as MYST-type HAT.
+At position 12 to 213, the domain is characterized as Sigma-54 factor interaction.
+At position 67 to 316, the domain is characterized as Protein kinase.
+At position 168 to 483, the domain is characterized as Peptidase S8.
+At position 491 to 629, the domain is characterized as P/Homo B.
+At position 3 to 65, the domain is characterized as HTH IS21-type.
+At position 124 to 299, the domain is characterized as Integrase catalytic.
+At position 150 to 196, the domain is characterized as G-patch.
+At position 17 to 81, the domain is characterized as TRAM.
+At position 30 to 200, the domain is characterized as Chitin-binding type-4.
+At position 106 to 301, the domain is characterized as ATP-grasp.
+At position 91 to 163, the domain is characterized as J.
+At position 26 to 105, the domain is characterized as IGFBP N-terminal.
+At position 156 to 231, the domain is characterized as Thyroglobulin type-1.
+At position 73 to 255, the domain is characterized as RNase H type-2.
+At position 28 to 159, the domain is characterized as N-acetyltransferase.
+At position 699 to 728, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 755 to 784, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 7 to 242, the domain is characterized as PABS.
+At position 628 to 722, the domain is characterized as Fibronectin type-III 1.
+At position 730 to 824, the domain is characterized as Fibronectin type-III 2.
+At position 830 to 933, the domain is characterized as Fibronectin type-III 3.
+At position 939 to 1033, the domain is characterized as Fibronectin type-III 4.
+At position 1039 to 1131, the domain is characterized as Fibronectin type-III 5.
+At position 544 to 597, the domain is characterized as bHLH.
+At position 97 to 269, the domain is characterized as Helicase ATP-binding.
+At position 300 to 446, the domain is characterized as Helicase C-terminal.
+At position 224 to 390, the domain is characterized as PA14.
+At position 68 to 131, the domain is characterized as S5 DRBM.
+At position 41 to 119, the domain is characterized as BTB.
+At position 9 to 242, the domain is characterized as ATP-grasp.
+At position 151 to 219, the domain is characterized as POTRA.
+At position 20 to 197, the domain is characterized as EngB-type G.
+At position 27 to 107, the domain is characterized as Importin N-terminal.
+At position 5 to 152, the domain is characterized as MGS-like.
+At position 9 to 57, the domain is characterized as F-box.
+At position 76 to 258, the domain is characterized as Helicase ATP-binding.
+At position 408 to 576, the domain is characterized as Helicase C-terminal.
+At position 600 to 700, the domain is characterized as Dicer dsRNA-binding fold.
+At position 859 to 980, the domain is characterized as PAZ.
+At position 995 to 1166, the domain is characterized as RNase III 1.
+At position 1222 to 1373, the domain is characterized as RNase III 2.
+At position 1409 to 1478, the domain is characterized as DRBM.
+At position 17 to 177, the domain is characterized as NAC.
+At position 383 to 540, the domain is characterized as F5/8 type C.
+At position 349 to 526, the domain is characterized as ABC transmembrane type-1.
+At position 84 to 202, the domain is characterized as MTTase N-terminal.
+At position 225 to 455, the domain is characterized as Radical SAM core.
+At position 458 to 521, the domain is characterized as TRAM.
+At position 37 to 286, the domain is characterized as CN hydrolase.
+At position 20 to 196, the domain is characterized as Exonuclease.
+At position 240 to 497, the domain is characterized as ABC transporter 2.
+At position 50 to 234, the domain is characterized as BPL/LPL catalytic.
+At position 338 to 582, the domain is characterized as Clu.
+At position 196 to 639, the domain is characterized as Myotubularin phosphatase.
+At position 13 to 91, the domain is characterized as ACT.
+At position 31 to 71, the domain is characterized as Chaplin 1.
+At position 112 to 152, the domain is characterized as Chaplin 2.
+At position 48 to 229, the domain is characterized as tr-type G.
+At position 206 to 252, the domain is characterized as F-box.
+At position 375 to 578, the domain is characterized as TR mART core.
+At position 94 to 322, the domain is characterized as Radical SAM core.
+At position 1 to 78, the domain is characterized as WGR.
+At position 28 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 147 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 244 to 346, the domain is characterized as Ig-like C2-type 3.
+At position 465 to 754, the domain is characterized as Protein kinase.
+At position 501 to 620, the domain is characterized as PH.
+At position 629 to 689, the domain is characterized as SH3.
+At position 1 to 119, the domain is characterized as VOC.
+At position 71 to 777, the domain is characterized as Myosin motor.
+At position 781 to 801, the domain is characterized as IQ 1.
+At position 804 to 824, the domain is characterized as IQ 2.
+At position 829 to 849, the domain is characterized as IQ 3.
+At position 876 to 898, the domain is characterized as IQ 4.
+At position 899 to 928, the domain is characterized as IQ 5.
+At position 1164 to 1419, the domain is characterized as Dilute.
+At position 35 to 197, the domain is characterized as PPIase cyclophilin-type.
+At position 103 to 131, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 144 to 225, the domain is characterized as Ig-like C2-type.
+At position 383 to 447, the domain is characterized as TRAM.
+At position 99 to 174, the domain is characterized as PRC barrel.
+At position 336 to 451, the domain is characterized as RGS.
+At position 575 to 680, the domain is characterized as Fibronectin type-III.
+At position 382 to 458, the domain is characterized as UBX.
+At position 192 to 242, the domain is characterized as DHHC.
+At position 382 to 427, the domain is characterized as FBD.
+At position 204 to 336, the domain is characterized as TIR.
+At position 30 to 109, the domain is characterized as Core-binding (CB).
+At position 131 to 304, the domain is characterized as Tyr recombinase.
+At position 338 to 429, the domain is characterized as FDX-ACB.
+At position 272 to 578, the domain is characterized as UvrD-like helicase C-terminal.
+At position 382 to 489, the domain is characterized as SH2.
+At position 484 to 533, the domain is characterized as SOCS box.
+At position 262 to 297, the domain is characterized as EF-hand.
+At position 21 to 138, the domain is characterized as Calponin-homology (CH).
+At position 38 to 349, the domain is characterized as GH26.
+At position 42 to 228, the domain is characterized as GH11.
+At position 33 to 108, the domain is characterized as J.
+At position 107 to 161, the domain is characterized as BSD 1.
+At position 186 to 238, the domain is characterized as BSD 2.
+At position 58 to 183, the domain is characterized as C2.
+At position 249 to 282, the domain is characterized as WW 1.
+At position 405 to 438, the domain is characterized as WW 2.
+At position 460 to 493, the domain is characterized as WW 3.
+At position 552 to 887, the domain is characterized as HECT.
+At position 459 to 702, the domain is characterized as ABC transporter 1.
+At position 295 to 332, the domain is characterized as LRRCT.
+At position 116 to 257, the domain is characterized as PA14.
+At position 28 to 148, the domain is characterized as Phytocyanin.
+At position 47 to 158, the domain is characterized as sHSP.
+At position 9 to 306, the domain is characterized as Protein kinase.
+At position 115 to 150, the domain is characterized as EF-hand.
+At position 138 to 339, the domain is characterized as ATP-grasp.
+At position 494 to 552, the domain is characterized as PAP-associated.
+At position 3 to 155, the domain is characterized as N-acetyltransferase.
+At position 33 to 181, the domain is characterized as sHSP.
+At position 728 to 811, the domain is characterized as ACT 1.
+At position 839 to 919, the domain is characterized as ACT 2.
+At position 137 to 367, the domain is characterized as Radical SAM core.
+At position 370 to 437, the domain is characterized as TRAM.
+At position 100 to 166, the domain is characterized as Kazal-like 1.
+At position 6 to 149, the domain is characterized as N-acetyltransferase 1.
+At position 164 to 345, the domain is characterized as N-acetyltransferase 2.
+At position 33 to 73, the domain is characterized as EGF-like 1; calcium-binding.
+At position 74 to 116, the domain is characterized as EGF-like 2; calcium-binding.
+At position 117 to 153, the domain is characterized as EGF-like 3; calcium-binding.
+At position 166 to 202, the domain is characterized as EGF-like 4.
+At position 206 to 241, the domain is characterized as EGF-like 5.
+At position 245 to 280, the domain is characterized as EGF-like 6.
+At position 282 to 322, the domain is characterized as EGF-like 7; calcium-binding.
+At position 323 to 361, the domain is characterized as EGF-like 8; calcium-binding.
+At position 362 to 402, the domain is characterized as EGF-like 9; calcium-binding.
+At position 798 to 910, the domain is characterized as CUB.
+At position 118 to 272, the domain is characterized as HD.
+At position 201 to 289, the domain is characterized as PDZ 1.
+At position 383 to 468, the domain is characterized as PDZ 2.
+At position 498 to 585, the domain is characterized as PDZ 3.
+At position 396 to 496, the domain is characterized as Ras-associating.
+At position 498 to 545, the domain is characterized as SARAH.
+At position 225 to 264, the domain is characterized as bZIP.
+At position 34 to 104, the domain is characterized as F-box; degenerate.
+At position 103 to 138, the domain is characterized as EF-hand 3.
+At position 213 to 256, the domain is characterized as EGF-like 1.
+At position 283 to 473, the domain is characterized as Laminin G-like 2.
+At position 480 to 672, the domain is characterized as Laminin G-like 3.
+At position 676 to 713, the domain is characterized as EGF-like 2.
+At position 718 to 891, the domain is characterized as Laminin G-like 4.
+At position 905 to 1080, the domain is characterized as Laminin G-like 5.
+At position 1083 to 1120, the domain is characterized as EGF-like 3.
+At position 1126 to 1294, the domain is characterized as Laminin G-like 6.
+At position 90 to 175, the domain is characterized as ELM2.
+At position 176 to 227, the domain is characterized as SANT 1.
+At position 302 to 353, the domain is characterized as SANT 2.
+At position 284 to 495, the domain is characterized as B30.2/SPRY.
+At position 41 to 223, the domain is characterized as Rab-GAP TBC.
+At position 141 to 204, the domain is characterized as bZIP.
+At position 42 to 137, the domain is characterized as Glutaredoxin.
+At position 7 to 159, the domain is characterized as EXPERA.
+At position 46 to 191, the domain is characterized as PHTF.
+At position 423 to 472, the domain is characterized as Chitin-binding type-2.
+At position 90 to 115, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 116 to 145, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 189 to 943, the domain is characterized as TBDR beta-barrel.
+At position 650 to 971, the domain is characterized as DH.
+At position 989 to 1109, the domain is characterized as N-terminal Ras-GEF.
+At position 1232 to 1454, the domain is characterized as Ras-GEF.
+At position 110 to 136, the domain is characterized as EF-hand 4.
+At position 126 to 294, the domain is characterized as Helicase ATP-binding.
+At position 355 to 526, the domain is characterized as Helicase C-terminal.
+At position 935 to 998, the domain is characterized as Tudor.
+At position 195 to 335, the domain is characterized as DOD-type homing endonuclease.
+At position 97 to 175, the domain is characterized as RRM.
+At position 206 to 266, the domain is characterized as HTH myb-type.
+At position 65 to 144, the domain is characterized as BTB.
+At position 13 to 227, the domain is characterized as ABC transporter.
+At position 6 to 61, the domain is characterized as ClpX-type ZB.
+At position 40 to 181, the domain is characterized as Ricin B-type lectin.
+At position 425 to 609, the domain is characterized as C2 DOCK-type.
+At position 1207 to 1617, the domain is characterized as DOCKER.
+At position 363 to 449, the domain is characterized as OCT.
+At position 80 to 161, the domain is characterized as PB1.
+At position 101 to 160, the domain is characterized as KID.
+At position 299 to 357, the domain is characterized as bZIP.
+At position 27 to 163, the domain is characterized as C2.
+At position 364 to 399, the domain is characterized as PLD phosphodiesterase 1.
+At position 171 to 238, the domain is characterized as R3H.
+At position 77 to 166, the domain is characterized as PDZ.
+At position 47 to 136, the domain is characterized as PPIase FKBP-type.
+At position 256 to 333, the domain is characterized as VPS37 C-terminal.
+At position 10 to 154, the domain is characterized as F5/8 type C.
+At position 17 to 119, the domain is characterized as AB hydrolase-1.
+At position 5 to 84, the domain is characterized as H15.
+At position 141 to 357, the domain is characterized as TLC.
+At position 13 to 106, the domain is characterized as KRAB.
+At position 65 to 346, the domain is characterized as tr-type G.
+At position 149 to 181, the domain is characterized as EGF-like 1.
+At position 287 to 339, the domain is characterized as TB 1.
+At position 407 to 459, the domain is characterized as TB 2.
+At position 545 to 586, the domain is characterized as EGF-like 3.
+At position 587 to 628, the domain is characterized as EGF-like 4; calcium-binding.
+At position 629 to 670, the domain is characterized as EGF-like 5; calcium-binding.
+At position 671 to 708, the domain is characterized as EGF-like 6; calcium-binding.
+At position 710 to 751, the domain is characterized as EGF-like 7; calcium-binding.
+At position 752 to 793, the domain is characterized as EGF-like 8; calcium-binding.
+At position 834 to 877, the domain is characterized as EGF-like 9; calcium-binding.
+At position 878 to 919, the domain is characterized as EGF-like 10; calcium-binding.
+At position 920 to 960, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1049 to 1090, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1181 to 1235, the domain is characterized as TB 3.
+At position 1253 to 1295, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1296 to 1337, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1349 to 1402, the domain is characterized as TB 4.
+At position 1533 to 1573, the domain is characterized as EGF-like 15.
+At position 1574 to 1618, the domain is characterized as EGF-like 16.
+At position 64 to 153, the domain is characterized as WWE.
+At position 248 to 469, the domain is characterized as PARP catalytic.
+At position 501 to 572, the domain is characterized as RST.
+At position 24 to 110, the domain is characterized as Acylphosphatase-like.
+At position 390 to 457, the domain is characterized as J.
+At position 222 to 602, the domain is characterized as SEC63.
+At position 36 to 73, the domain is characterized as Myb-like.
+At position 567 to 857, the domain is characterized as Protein kinase.
+At position 927 to 1057, the domain is characterized as Guanylate cyclase.
+At position 101 to 350, the domain is characterized as Protein kinase.
+At position 411 to 525, the domain is characterized as PX.
+At position 91 to 305, the domain is characterized as RNase H type-2.
+At position 1 to 198, the domain is characterized as SMP-LTD.
+At position 98 to 410, the domain is characterized as IF rod.
+At position 234 to 316, the domain is characterized as DEP.
+At position 516 to 654, the domain is characterized as N-terminal Ras-GEF.
+At position 795 to 1028, the domain is characterized as Ras-GEF.
+At position 33 to 90, the domain is characterized as 4Fe-4S Wbl-type.
+At position 101 to 339, the domain is characterized as Radical SAM core.
+At position 25 to 156, the domain is characterized as Ig-like V-type 1.
+At position 23 to 63, the domain is characterized as CHCH.
+At position 1 to 314, the domain is characterized as RanBD1.
+At position 284 to 487, the domain is characterized as MCM.
+At position 208 to 508, the domain is characterized as Protein kinase.
+At position 509 to 589, the domain is characterized as AGC-kinase C-terminal.
+At position 118 to 198, the domain is characterized as CTCK.
+At position 1121 to 1181, the domain is characterized as v-SNARE coiled-coil homology.
+At position 3 to 110, the domain is characterized as Thioredoxin.
+At position 146 to 244, the domain is characterized as Glutaredoxin.
+At position 195 to 422, the domain is characterized as ABC transmembrane type-1.
+At position 303 to 332, the domain is characterized as IQ.
+At position 330 to 407, the domain is characterized as BAG.
+At position 579 to 662, the domain is characterized as S1 motif.
+At position 158 to 412, the domain is characterized as Lon N-terminal.
+At position 844 to 1030, the domain is characterized as Lon proteolytic.
+At position 139 to 205, the domain is characterized as RNase III.
+At position 302 to 372, the domain is characterized as DRBM.
+At position 170 to 349, the domain is characterized as Glutamine amidotransferase type-1.
+At position 235 to 282, the domain is characterized as GRAM 1.
+At position 286 to 383, the domain is characterized as PH.
+At position 771 to 837, the domain is characterized as GRAM 2.
+At position 77 to 373, the domain is characterized as PPM-type phosphatase.
+At position 34 to 135, the domain is characterized as Glutaredoxin.
+At position 37 to 301, the domain is characterized as AB hydrolase-1.
+At position 12 to 131, the domain is characterized as MTTase N-terminal.
+At position 387 to 457, the domain is characterized as TRAM.
+At position 8 to 185, the domain is characterized as DHFR.
+At position 27 to 173, the domain is characterized as PPC.
+At position 54 to 110, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 104 to 225, the domain is characterized as PX.
+At position 392 to 453, the domain is characterized as TGS.
+At position 660 to 734, the domain is characterized as ACT.
+At position 45 to 145, the domain is characterized as Expansin-like EG45.
+At position 54 to 223, the domain is characterized as Helicase ATP-binding.
+At position 357 to 492, the domain is characterized as PLAT.
+At position 215 to 242, the domain is characterized as PLD phosphodiesterase 1.
+At position 434 to 460, the domain is characterized as PLD phosphodiesterase 2.
+At position 233 to 570, the domain is characterized as SET.
+At position 307 to 367, the domain is characterized as Tudor 1.
+At position 536 to 595, the domain is characterized as Tudor 2.
+At position 756 to 815, the domain is characterized as Tudor 3.
+At position 982 to 1040, the domain is characterized as Tudor 4.
+At position 455 to 528, the domain is characterized as ACT.
+At position 558 to 768, the domain is characterized as Lon N-terminal.
+At position 26 to 491, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 519 to 809, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 239, the domain is characterized as Deacetylase sirtuin-type.
+At position 420 to 527, the domain is characterized as Fe2OG dioxygenase.
+At position 120 to 313, the domain is characterized as ATP-grasp.
+At position 35 to 122, the domain is characterized as Ig-like.
+At position 133 to 234, the domain is characterized as Fibronectin type-III.
+At position 241 to 416, the domain is characterized as MAM.
+At position 158 to 345, the domain is characterized as CheB-type methylesterase.
+At position 48 to 145, the domain is characterized as SWIRM.
+At position 1 to 85, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 223 to 279, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 179 to 280, the domain is characterized as Fibronectin type-III.
+At position 176 to 226, the domain is characterized as DHHC.
+At position 50 to 158, the domain is characterized as Cytochrome c 1.
+At position 204 to 355, the domain is characterized as Cytochrome c 2.
+At position 304 to 583, the domain is characterized as Protein kinase.
+At position 253 to 477, the domain is characterized as tr-type G.
+At position 64 to 157, the domain is characterized as Ig-like C2-type 1.
+At position 166 to 268, the domain is characterized as Ig-like C2-type 2.
+At position 389 to 678, the domain is characterized as Protein kinase.
+At position 52 to 296, the domain is characterized as ABC transporter.
+At position 350 to 560, the domain is characterized as ABC transmembrane type-2.
+At position 597 to 674, the domain is characterized as KIX.
+At position 429 to 702, the domain is characterized as Protein kinase.
+At position 36 to 254, the domain is characterized as Cache.
+At position 293 to 347, the domain is characterized as HAMP.
+At position 352 to 588, the domain is characterized as Methyl-accepting transducer.
+At position 18 to 137, the domain is characterized as Calponin-homology (CH).
+At position 216 to 396, the domain is characterized as DH.
+At position 432 to 541, the domain is characterized as PH.
+At position 622 to 726, the domain is characterized as SH2.
+At position 726 to 788, the domain is characterized as SH3.
+At position 587 to 613, the domain is characterized as EF-hand 1.
+At position 617 to 652, the domain is characterized as EF-hand 2.
+At position 14 to 123, the domain is characterized as KRAB.
+At position 1 to 69, the domain is characterized as KRAB.
+At position 46 to 291, the domain is characterized as ZP.
+At position 672 to 766, the domain is characterized as Fibronectin type-III 2.
+At position 272 to 348, the domain is characterized as B5.
+At position 193 to 318, the domain is characterized as C2.
+At position 377 to 567, the domain is characterized as VWFA.
+At position 586 to 674, the domain is characterized as BRCT.
+At position 290 to 569, the domain is characterized as UvrD-like helicase C-terminal.
+At position 44 to 271, the domain is characterized as Radical SAM core.
+At position 130 to 465, the domain is characterized as PI3K/PI4K catalytic.
+At position 133 to 369, the domain is characterized as ABC transmembrane type-2.
+At position 45 to 301, the domain is characterized as Protein kinase.
+At position 302 to 354, the domain is characterized as AGC-kinase C-terminal.
+At position 18 to 139, the domain is characterized as Rhodanese.
+At position 203 to 346, the domain is characterized as Tyrosine-protein phosphatase.
+At position 85 to 392, the domain is characterized as Peptidase A1.
+At position 47 to 61, the domain is characterized as UIM.
+At position 22 to 59, the domain is characterized as LRRNT.
+At position 201 to 253, the domain is characterized as LRRCT.
+At position 266 to 335, the domain is characterized as Ig-like C2-type.
+At position 430 to 518, the domain is characterized as Fibronectin type-III.
+At position 14 to 111, the domain is characterized as Yippee.
+At position 547 to 660, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 661 to 774, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 841 to 919, the domain is characterized as POLO box.
+At position 44 to 122, the domain is characterized as GIY-YIG.
+At position 237 to 295, the domain is characterized as bZIP.
+At position 25 to 261, the domain is characterized as ABC transporter 1.
+At position 268 to 515, the domain is characterized as ABC transporter 2.
+At position 423 to 479, the domain is characterized as Rubredoxin-like.
+At position 264 to 355, the domain is characterized as CS.
+At position 7 to 142, the domain is characterized as Peptidase C51.
+At position 93 to 175, the domain is characterized as RRM 1.
+At position 318 to 408, the domain is characterized as RRM 3.
+At position 192 to 234, the domain is characterized as CHCH.
+At position 30 to 193, the domain is characterized as Exonuclease.
+At position 236 to 477, the domain is characterized as Helicase ATP-binding.
+At position 531 to 747, the domain is characterized as Helicase C-terminal.
+At position 30 to 268, the domain is characterized as AB hydrolase-1.
+At position 1 to 94, the domain is characterized as GLUE N-terminal.
+At position 111 to 144, the domain is characterized as GLUE C-terminal.
+At position 134 to 387, the domain is characterized as SMP-LTD.
+At position 216 to 358, the domain is characterized as VLRF1.
+At position 30 to 269, the domain is characterized as Saposin B-type.
+At position 28 to 71, the domain is characterized as LDL-receptor class A.
+At position 44 to 91, the domain is characterized as F-box.
+At position 113 to 296, the domain is characterized as FBA.
+At position 633 to 864, the domain is characterized as NR LBD.
+At position 182 to 259, the domain is characterized as POU-specific.
+At position 27 to 390, the domain is characterized as GH18.
+At position 28 to 57, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 94 to 224, the domain is characterized as N-acetyltransferase.
+At position 89 to 354, the domain is characterized as Era-type G.
+At position 380 to 461, the domain is characterized as KH type-2.
+At position 87 to 293, the domain is characterized as SMP-LTD.
+At position 365 to 448, the domain is characterized as PDZ.
+At position 681 to 755, the domain is characterized as POU-specific.
+At position 91 to 343, the domain is characterized as Radical SAM core 1.
+At position 551 to 792, the domain is characterized as Radical SAM core 2.
+At position 139 to 326, the domain is characterized as Helicase ATP-binding.
+At position 355 to 512, the domain is characterized as Helicase C-terminal.
+At position 640 to 730, the domain is characterized as BRCT 2.
+At position 751 to 833, the domain is characterized as BRCT 3.
+At position 30 to 238, the domain is characterized as MARVEL.
+At position 583 to 767, the domain is characterized as Helicase ATP-binding.
+At position 803 to 950, the domain is characterized as Helicase C-terminal.
+At position 226 to 460, the domain is characterized as Grh/CP2 DB.
+At position 157 to 246, the domain is characterized as CS.
+At position 268 to 358, the domain is characterized as SGS.
+At position 55 to 296, the domain is characterized as Peptidase S1.
+At position 61 to 269, the domain is characterized as Peptidase M12A.
+At position 299 to 336, the domain is characterized as PLAC.
+At position 40 to 92, the domain is characterized as PISA.
+At position 1 to 87, the domain is characterized as Response regulatory.
+At position 105 to 250, the domain is characterized as PA14.
+At position 5 to 73, the domain is characterized as HTH merR-type.
+At position 2 to 135, the domain is characterized as PINc.
+At position 353 to 571, the domain is characterized as TLDc.
+At position 637 to 728, the domain is characterized as Fe2OG dioxygenase.
+At position 573 to 928, the domain is characterized as Histidine kinase.
+At position 1089 to 1210, the domain is characterized as Response regulatory.
+At position 39 to 195, the domain is characterized as MABP.
+At position 187 to 364, the domain is characterized as uDENN.
+At position 523 to 632, the domain is characterized as dDENN.
+At position 200 to 245, the domain is characterized as G-patch.
+At position 121 to 162, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 163 to 205, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 327 to 365, the domain is characterized as PLD phosphodiesterase 1.
+At position 19 to 124, the domain is characterized as XRN2-binding (XTBD).
+At position 118 to 176, the domain is characterized as P-type.
+At position 1 to 136, the domain is characterized as uDENN.
+At position 152 to 299, the domain is characterized as cDENN.
+At position 717 to 801, the domain is characterized as PB1.
+At position 30 to 419, the domain is characterized as Helicase ATP-binding.
+At position 11 to 243, the domain is characterized as ABC transporter.
+At position 31 to 285, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 242 to 426, the domain is characterized as GATase cobBQ-type.
+At position 254 to 568, the domain is characterized as DOT1.
+At position 40 to 97, the domain is characterized as CTLH.
+At position 102 to 282, the domain is characterized as BAH.
+At position 283 to 386, the domain is characterized as ELM2.
+At position 390 to 442, the domain is characterized as SANT.
+At position 4 to 395, the domain is characterized as BRO1.
+At position 177 to 233, the domain is characterized as HAMP.
+At position 241 to 446, the domain is characterized as Histidine kinase.
+At position 80 to 145, the domain is characterized as J.
+At position 268 to 451, the domain is characterized as ATP-grasp.
+At position 375 to 619, the domain is characterized as Clu.
+At position 174 to 296, the domain is characterized as Fe2OG dioxygenase.
+At position 29 to 253, the domain is characterized as AB hydrolase-1.
+At position 25 to 469, the domain is characterized as Hexokinase 1.
+At position 475 to 911, the domain is characterized as Hexokinase 2.
+At position 6 to 77, the domain is characterized as J.
+At position 91 to 164, the domain is characterized as DPH-type MB.
+At position 1 to 225, the domain is characterized as Peptidase S1.
+At position 594 to 715, the domain is characterized as GAE.
+At position 270 to 584, the domain is characterized as UvrD-like helicase C-terminal.
+At position 1 to 190, the domain is characterized as GH11.
+At position 99 to 203, the domain is characterized as C-type lectin.
+At position 26 to 330, the domain is characterized as GH18.
+At position 554 to 607, the domain is characterized as bHLH.
+At position 462 to 530, the domain is characterized as SAM.
+At position 109 to 266, the domain is characterized as DAC.
+At position 392 to 468, the domain is characterized as B5.
+At position 684 to 776, the domain is characterized as FDX-ACB.
+At position 398 to 642, the domain is characterized as Radical SAM core.
+At position 177 to 372, the domain is characterized as ABC transmembrane type-1.
+At position 28 to 146, the domain is characterized as VIT.
+At position 270 to 428, the domain is characterized as VWFA.
+At position 38 to 240, the domain is characterized as BPL/LPL catalytic.
+At position 268 to 360, the domain is characterized as Chromo 1.
+At position 385 to 448, the domain is characterized as Chromo 2.
+At position 489 to 659, the domain is characterized as Helicase ATP-binding.
+At position 788 to 939, the domain is characterized as Helicase C-terminal.
+At position 200 to 375, the domain is characterized as Helicase ATP-binding.
+At position 389 to 559, the domain is characterized as Helicase C-terminal.
+At position 20 to 77, the domain is characterized as TRAM.
+At position 109 to 297, the domain is characterized as ATP-grasp.
+At position 336 to 486, the domain is characterized as CBM3.
+At position 10 to 92, the domain is characterized as Phosphagen kinase N-terminal.
+At position 122 to 359, the domain is characterized as Phosphagen kinase C-terminal.
+At position 111 to 502, the domain is characterized as BRO1.
+At position 129 to 303, the domain is characterized as PXA.
+At position 335 to 467, the domain is characterized as RGS.
+At position 557 to 677, the domain is characterized as PX.
+At position 111 to 223, the domain is characterized as SET.
+At position 6 to 66, the domain is characterized as HTH asnC-type.
+At position 680 to 758, the domain is characterized as BTB 1.
+At position 808 to 889, the domain is characterized as BTB 2.
+At position 30 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 148, the domain is characterized as Protein kinase.
+At position 120 to 227, the domain is characterized as sHSP.
+At position 38 to 84, the domain is characterized as EGF-like; atypical.
+At position 18 to 146, the domain is characterized as Cyclin N-terminal.
+At position 151 to 237, the domain is characterized as Carrier.
+At position 1007 to 1539, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 645 to 916, the domain is characterized as Protein kinase.
+At position 338 to 493, the domain is characterized as Helicase C-terminal.
+At position 7 to 446, the domain is characterized as Protein kinase.
+At position 191 to 252, the domain is characterized as SH3 1.
+At position 271 to 330, the domain is characterized as SH3 2.
+At position 355 to 414, the domain is characterized as SH3 3.
+At position 431 to 493, the domain is characterized as SH3 4.
+At position 145 to 200, the domain is characterized as Collagen-like 1.
+At position 215 to 273, the domain is characterized as Collagen-like 2.
+At position 621 to 704, the domain is characterized as BRCT.
+At position 40 to 199, the domain is characterized as MABP.
+At position 191 to 363, the domain is characterized as uDENN.
+At position 384 to 520, the domain is characterized as cDENN.
+At position 522 to 640, the domain is characterized as dDENN.
+At position 125 to 221, the domain is characterized as Rieske.
+At position 254 to 356, the domain is characterized as BTB 1.
+At position 420 to 487, the domain is characterized as BTB 2.
+At position 135 to 299, the domain is characterized as SprT-like.
+At position 68 to 103, the domain is characterized as EF-hand.
+At position 53 to 294, the domain is characterized as Peptidase S1.
+At position 19 to 146, the domain is characterized as Thioredoxin.
+At position 17 to 248, the domain is characterized as ABC transporter.
+At position 30 to 138, the domain is characterized as Thioredoxin 1.
+At position 139 to 257, the domain is characterized as Thioredoxin 2.
+At position 24 to 149, the domain is characterized as Bulb-type lectin.
+At position 290 to 379, the domain is characterized as PAN.
+At position 496 to 785, the domain is characterized as Protein kinase.
+At position 52 to 276, the domain is characterized as SET.
+At position 1 to 60, the domain is characterized as POU-specific.
+At position 52 to 223, the domain is characterized as Velvet.
+At position 43 to 113, the domain is characterized as KRAB.
+At position 66 to 166, the domain is characterized as CBM20.
+At position 307 to 379, the domain is characterized as PDZ 1.
+At position 845 to 958, the domain is characterized as PDZ 2.
+At position 25 to 126, the domain is characterized as Cadherin 1.
+At position 131 to 235, the domain is characterized as Cadherin 2.
+At position 242 to 336, the domain is characterized as Cadherin 3.
+At position 569 to 665, the domain is characterized as Cadherin 6.
+At position 65 to 255, the domain is characterized as BPL/LPL catalytic.
+At position 114 to 201, the domain is characterized as Cytochrome c 1.
+At position 209 to 290, the domain is characterized as Cytochrome c 2.
+At position 170 to 372, the domain is characterized as Helicase ATP-binding.
+At position 396 to 609, the domain is characterized as Helicase C-terminal.
+At position 147 to 420, the domain is characterized as ABC transporter 1.
+At position 498 to 711, the domain is characterized as ABC transmembrane type-2 1.
+At position 814 to 1067, the domain is characterized as ABC transporter 2.
+At position 1139 to 1353, the domain is characterized as ABC transmembrane type-2 2.
+At position 118 to 309, the domain is characterized as ATP-grasp.
+At position 134 to 299, the domain is characterized as PINIT.
+At position 96 to 406, the domain is characterized as IF rod.
+At position 149 to 202, the domain is characterized as HAMP 2.
+At position 221 to 459, the domain is characterized as Methyl-accepting transducer.
+At position 225 to 314, the domain is characterized as Ig-like C2-type 1.
+At position 323 to 408, the domain is characterized as Ig-like C2-type 2.
+At position 70 to 385, the domain is characterized as IF rod.
+At position 515 to 590, the domain is characterized as Cytochrome b5 heme-binding.
+At position 16 to 149, the domain is characterized as ENTH.
+At position 33 to 110, the domain is characterized as NAC-A/B.
+At position 875 to 1055, the domain is characterized as RNase III 1.
+At position 1106 to 1232, the domain is characterized as RNase III 2.
+At position 1259 to 1333, the domain is characterized as DRBM.
+At position 326 to 451, the domain is characterized as CRC.
+At position 428 to 487, the domain is characterized as SB.
+At position 139 to 460, the domain is characterized as NACHT.
+At position 229 to 405, the domain is characterized as Helicase ATP-binding.
+At position 416 to 588, the domain is characterized as Helicase C-terminal.
+At position 56 to 143, the domain is characterized as RRM.
+At position 699 to 898, the domain is characterized as Helicase ATP-binding.
+At position 1061 to 1222, the domain is characterized as Helicase C-terminal.
+At position 179 to 253, the domain is characterized as POU-specific.
+At position 243 to 561, the domain is characterized as DOT1.
+At position 101 to 187, the domain is characterized as PDZ.
+At position 188 to 426, the domain is characterized as Peptidase S55.
+At position 1 to 181, the domain is characterized as Macro.
+At position 53 to 281, the domain is characterized as Radical SAM core.
+At position 23 to 53, the domain is characterized as CBM1.
+At position 105 to 384, the domain is characterized as GH10.
+At position 17 to 161, the domain is characterized as SprT-like.
+At position 22 to 113, the domain is characterized as Ig-like V-type 1.
+At position 114 to 206, the domain is characterized as Ig-like V-type 2.
+At position 207 to 299, the domain is characterized as Ig-like V-type 3.
+At position 300 to 397, the domain is characterized as Ig-like V-type 4.
+At position 398 to 495, the domain is characterized as Ig-like V-type 5.
+At position 133 to 391, the domain is characterized as PPM-type phosphatase.
+At position 1 to 142, the domain is characterized as MPN.
+At position 95 to 436, the domain is characterized as Peptidase A1.
+At position 18 to 200, the domain is characterized as Guanylate kinase-like.
+At position 111 to 261, the domain is characterized as Flavodoxin-like.
+At position 316 to 564, the domain is characterized as FAD-binding FR-type.
+At position 10 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 245 to 437, the domain is characterized as FAD-binding PCMH-type.
+At position 5 to 196, the domain is characterized as PNPLA.
+At position 30 to 124, the domain is characterized as B12-binding N-terminal.
+At position 123 to 248, the domain is characterized as B12-binding.
+At position 292 to 399, the domain is characterized as Ig-like C1-type.
+At position 35 to 195, the domain is characterized as N-acetyltransferase.
+At position 142 to 179, the domain is characterized as UBA.
+At position 142 to 312, the domain is characterized as JmjC.
+At position 1 to 112, the domain is characterized as Peptidase M12B.
+At position 27 to 124, the domain is characterized as Ig-like V-type.
+At position 131 to 228, the domain is characterized as Ig-like C2-type.
+At position 34 to 133, the domain is characterized as SRCR 1.
+At position 276 to 367, the domain is characterized as SRCR 3.
+At position 5 to 283, the domain is characterized as GH18.
+At position 27 to 110, the domain is characterized as RRM 1.
+At position 118 to 206, the domain is characterized as RRM 2.
+At position 364 to 581, the domain is characterized as Histidine kinase.
+At position 549 to 602, the domain is characterized as bHLH.
+At position 38 to 201, the domain is characterized as PPIase cyclophilin-type.
+At position 6 to 209, the domain is characterized as RNase H type-2.
+At position 264 to 299, the domain is characterized as EF-hand 1.
+At position 426 to 583, the domain is characterized as Ferric oxidoreductase.
+At position 622 to 742, the domain is characterized as FAD-binding FR-type.
+At position 202 to 221, the domain is characterized as UIM.
+At position 21 to 186, the domain is characterized as FAD-binding PCMH-type.
+At position 255 to 454, the domain is characterized as GATase cobBQ-type.
+At position 377 to 652, the domain is characterized as Protein kinase.
+At position 42 to 234, the domain is characterized as Radical SAM core.
+At position 22 to 113, the domain is characterized as Ig-like C2-type 1.
+At position 128 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 1864 to 1929, the domain is characterized as KH.
+At position 156 to 227, the domain is characterized as HTH crp-type.
+At position 2 to 142, the domain is characterized as RNase H type-1.
+At position 137 to 313, the domain is characterized as Helicase ATP-binding.
+At position 324 to 488, the domain is characterized as Helicase C-terminal.
+At position 335 to 540, the domain is characterized as MIF4G.
+At position 644 to 781, the domain is characterized as MI.
+At position 245 to 368, the domain is characterized as Rhodanese.
+At position 38 to 712, the domain is characterized as Myosin motor.
+At position 716 to 736, the domain is characterized as IQ 1.
+At position 737 to 762, the domain is characterized as IQ 2.
+At position 770 to 953, the domain is characterized as TH1.
+At position 1046 to 1104, the domain is characterized as SH3.
+At position 80 to 201, the domain is characterized as PX.
+At position 223 to 428, the domain is characterized as BAR.
+At position 10 to 155, the domain is characterized as Flavodoxin-like.
+At position 209 to 451, the domain is characterized as FAD-binding FR-type.
+At position 2 to 199, the domain is characterized as CN hydrolase.
+At position 38 to 234, the domain is characterized as GH11.
+At position 90 to 175, the domain is characterized as S4 RNA-binding.
+At position 112 to 236, the domain is characterized as OmpA-like.
+At position 119 to 352, the domain is characterized as Radical SAM core.
+At position 28 to 203, the domain is characterized as CP-type G.
+At position 56 to 366, the domain is characterized as AB hydrolase-1.
+At position 11 to 265, the domain is characterized as Deacetylase sirtuin-type.
+At position 258 to 349, the domain is characterized as Ig-like C2-type 1.
+At position 376 to 478, the domain is characterized as Ig-like C2-type 2.
+At position 492 to 587, the domain is characterized as Fibronectin type-III 1.
+At position 620 to 714, the domain is characterized as Fibronectin type-III 2.
+At position 721 to 814, the domain is characterized as Fibronectin type-III 3.
+At position 918 to 1016, the domain is characterized as Fibronectin type-III 4.
+At position 1023 to 1122, the domain is characterized as Fibronectin type-III 5.
+At position 1114 to 1212, the domain is characterized as Ig-like C2-type 3.
+At position 1340 to 1426, the domain is characterized as Ig-like C2-type 4.
+At position 1555 to 1644, the domain is characterized as Ig-like C2-type 5.
+At position 81 to 270, the domain is characterized as BPL/LPL catalytic.
+At position 82 to 128, the domain is characterized as F-box; degenerate.
+At position 28 to 163, the domain is characterized as VOC 1.
+At position 194 to 353, the domain is characterized as VOC 2.
+At position 98 to 184, the domain is characterized as PB1.
+At position 36 to 175, the domain is characterized as WIF.
+At position 176 to 205, the domain is characterized as EGF-like 1.
+At position 208 to 240, the domain is characterized as EGF-like 2.
+At position 243 to 272, the domain is characterized as EGF-like 3.
+At position 272 to 304, the domain is characterized as EGF-like 4.
+At position 305 to 336, the domain is characterized as EGF-like 5.
+At position 278 to 383, the domain is characterized as C-type lectin.
+At position 362 to 430, the domain is characterized as S4 RNA-binding.
+At position 107 to 293, the domain is characterized as Tyr recombinase.
+At position 44 to 166, the domain is characterized as G8.
+At position 24 to 143, the domain is characterized as PX.
+At position 160 to 402, the domain is characterized as BAR.
+At position 313 to 456, the domain is characterized as SET.
+At position 632 to 863, the domain is characterized as JmjC.
+At position 76 to 212, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 1.
+At position 233 to 359, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 2.
+At position 61 to 117, the domain is characterized as WHEP-TRS.
+At position 80 to 185, the domain is characterized as FAD-binding FR-type.
+At position 2129 to 2260, the domain is characterized as MPN.
+At position 19 to 149, the domain is characterized as Galectin 1.
+At position 173 to 301, the domain is characterized as Galectin 2.
+At position 70 to 176, the domain is characterized as Expansin-like EG45.
+At position 188 to 269, the domain is characterized as Expansin-like CBD.
+At position 36 to 107, the domain is characterized as KRAB.
+At position 16 to 40, the domain is characterized as EF-hand 1.
+At position 255 to 393, the domain is characterized as Flavodoxin-like.
+At position 27 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 119 to 224, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 315, the domain is characterized as Ig-like C2-type 3.
+At position 326 to 415, the domain is characterized as Ig-like C2-type 4.
+At position 483 to 599, the domain is characterized as MaoC-like.
+At position 623 to 735, the domain is characterized as SCP2.
+At position 42 to 71, the domain is characterized as LRRNT.
+At position 369 to 423, the domain is characterized as LRRCT.
+At position 411 to 513, the domain is characterized as Ig-like C2-type.
+At position 690 to 765, the domain is characterized as MBD.
+At position 1004 to 1069, the domain is characterized as DDT.
+At position 2032 to 2102, the domain is characterized as Bromo.
+At position 29 to 85, the domain is characterized as SLH 1.
+At position 86 to 149, the domain is characterized as SLH 2.
+At position 150 to 210, the domain is characterized as SLH 3.
+At position 335 to 517, the domain is characterized as MurNAc-LAA.
+At position 29 to 216, the domain is characterized as WLM.
+At position 259 to 361, the domain is characterized as HTH araC/xylS-type.
+At position 841 to 950, the domain is characterized as PH.
+At position 22 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 502 to 672, the domain is characterized as tr-type G.
+At position 20 to 445, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 984 to 1306, the domain is characterized as PKS/mFAS DH.
+At position 2174 to 2251, the domain is characterized as Carrier.
+At position 432 to 742, the domain is characterized as Protein kinase.
+At position 118 to 189, the domain is characterized as PRC barrel.
+At position 76 to 290, the domain is characterized as Protein kinase.
+At position 490 to 548, the domain is characterized as PAP-associated.
+At position 64 to 250, the domain is characterized as TR mART core.
+At position 221 to 473, the domain is characterized as ABC transporter 1.
+At position 917 to 1159, the domain is characterized as ABC transporter 2.
+At position 1 to 92, the domain is characterized as Big-1.
+At position 127 to 173, the domain is characterized as BIG2.
+At position 779 to 1048, the domain is characterized as Rap-GAP.
+At position 952 to 1118, the domain is characterized as PNPLA.
+At position 408 to 472, the domain is characterized as SAM 1.
+At position 478 to 537, the domain is characterized as SAM 2.
+At position 552 to 695, the domain is characterized as TIR.
+At position 2 to 117, the domain is characterized as Thioredoxin.
+At position 144 to 236, the domain is characterized as Glutaredoxin 1.
+At position 237 to 335, the domain is characterized as Glutaredoxin 2.
+At position 34 to 134, the domain is characterized as PINc.
+At position 141 to 196, the domain is characterized as TSP type-1 1.
+At position 198 to 253, the domain is characterized as TSP type-1 2.
+At position 255 to 310, the domain is characterized as TSP type-1 3.
+At position 400 to 566, the domain is characterized as NIDO.
+At position 568 to 706, the domain is characterized as AMOP.
+At position 706 to 901, the domain is characterized as VWFD.
+At position 1063 to 1108, the domain is characterized as EGF-like 1.
+At position 1110 to 1156, the domain is characterized as EGF-like 2.
+At position 1157 to 1191, the domain is characterized as EGF-like 3; calcium-binding.
+At position 1281 to 1321, the domain is characterized as EGF-like 4; calcium-binding.
+At position 1322 to 1364, the domain is characterized as EGF-like 5; calcium-binding.
+At position 202 to 293, the domain is characterized as NID 2.
+At position 506 to 580, the domain is characterized as RH2.
+At position 357 to 415, the domain is characterized as S4 RNA-binding.
+At position 303 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 233 to 441, the domain is characterized as Helicase ATP-binding.
+At position 207 to 408, the domain is characterized as GMPS ATP-PPase.
+At position 96 to 226, the domain is characterized as MPN.
+At position 48 to 93, the domain is characterized as Oxidoreductase-like.
+At position 519 to 711, the domain is characterized as ATP-grasp 1.
+At position 1052 to 1243, the domain is characterized as ATP-grasp 2.
+At position 1308 to 1462, the domain is characterized as MGS-like.
+At position 110 to 301, the domain is characterized as Tyr recombinase.
+At position 167 to 367, the domain is characterized as Rho-GAP.
+At position 267 to 516, the domain is characterized as ZP.
+At position 16 to 93, the domain is characterized as DEP 1.
+At position 264 to 342, the domain is characterized as DEP 2.
+At position 693 to 941, the domain is characterized as Roc.
+At position 1456 to 1864, the domain is characterized as Protein kinase.
+At position 403 to 480, the domain is characterized as REM-1.
+At position 549 to 610, the domain is characterized as SH3.
+At position 61 to 102, the domain is characterized as JmjN.
+At position 126 to 223, the domain is characterized as ARID.
+At position 471 to 637, the domain is characterized as JmjC.
+At position 202 to 292, the domain is characterized as BRCT.
+At position 322 to 371, the domain is characterized as bHLH.
+At position 31 to 117, the domain is characterized as Ig-like.
+At position 111 to 294, the domain is characterized as Tyr recombinase.
+At position 22 to 367, the domain is characterized as Protein kinase.
+At position 134 to 337, the domain is characterized as ATP-grasp.
+At position 6 to 97, the domain is characterized as ATP-cone.
+At position 231 to 352, the domain is characterized as Rhodanese.
+At position 38 to 208, the domain is characterized as Helicase ATP-binding.
+At position 283 to 434, the domain is characterized as Helicase C-terminal.
+At position 388 to 447, the domain is characterized as SH3.
+At position 97 to 191, the domain is characterized as BTB.
+At position 218 to 384, the domain is characterized as PCI.
+At position 81 to 403, the domain is characterized as NACHT.
+At position 38 to 202, the domain is characterized as TIR.
+At position 217 to 478, the domain is characterized as NB-ARC.
+At position 269 to 381, the domain is characterized as Cadherin 2.
+At position 382 to 493, the domain is characterized as Cadherin 3.
+At position 494 to 599, the domain is characterized as Cadherin 4.
+At position 600 to 704, the domain is characterized as Cadherin 5.
+At position 587 to 666, the domain is characterized as KIX.
+At position 1103 to 1175, the domain is characterized as Bromo.
+At position 1323 to 1700, the domain is characterized as CBP/p300-type HAT.
+At position 584 to 642, the domain is characterized as CBS 1.
+At position 790 to 850, the domain is characterized as CBS 2.
+At position 42 to 230, the domain is characterized as RNase H type-2.
+At position 137 to 483, the domain is characterized as Protein kinase.
+At position 18 to 253, the domain is characterized as PABS.
+At position 217 to 489, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 285 to 557, the domain is characterized as Radical SAM core.
+At position 356 to 399, the domain is characterized as LysM.
+At position 345 to 397, the domain is characterized as TSP type-1.
+At position 633 to 1070, the domain is characterized as PDEase.
+At position 595 to 672, the domain is characterized as Carrier.
+At position 295 to 645, the domain is characterized as TTL.
+At position 38 to 116, the domain is characterized as RRM.
+At position 1 to 93, the domain is characterized as YcgL.
+At position 352 to 556, the domain is characterized as MCM.
+At position 71 to 318, the domain is characterized as Radical SAM core.
+At position 154 to 441, the domain is characterized as Peptidase S8.
+At position 1037 to 1130, the domain is characterized as PB1.
+At position 285 to 368, the domain is characterized as Cyclin N-terminal.
+At position 40 to 715, the domain is characterized as Myosin motor.
+At position 2084 to 2308, the domain is characterized as JmjC.
+At position 1 to 156, the domain is characterized as N-acetyltransferase.
+At position 44 to 175, the domain is characterized as MPN.
+At position 10 to 71, the domain is characterized as HTH asnC-type.
+At position 126 to 161, the domain is characterized as EF-hand 3.
+At position 328 to 660, the domain is characterized as PDEase.
+At position 10 to 164, the domain is characterized as PPIase cyclophilin-type.
+At position 24 to 282, the domain is characterized as Protein kinase.
+At position 361 to 396, the domain is characterized as EF-hand 2.
+At position 397 to 432, the domain is characterized as EF-hand 3.
+At position 436 to 466, the domain is characterized as EF-hand 4.
+At position 236 to 286, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 292 to 342, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 27 to 81, the domain is characterized as TSP type-1 1.
+At position 305 to 362, the domain is characterized as TSP type-1 2.
+At position 363 to 422, the domain is characterized as TSP type-1 3.
+At position 424 to 482, the domain is characterized as TSP type-1 4.
+At position 485 to 540, the domain is characterized as TSP type-1 5.
+At position 750 to 800, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 900 to 990, the domain is characterized as Ig-like C2-type 1.
+At position 1039 to 1128, the domain is characterized as Ig-like C2-type 2.
+At position 19 to 92, the domain is characterized as PAS 1.
+At position 93 to 147, the domain is characterized as PAC.
+At position 159 to 230, the domain is characterized as PAS 2.
+At position 203 to 281, the domain is characterized as GW.
+At position 118 to 358, the domain is characterized as Radical SAM core.
+At position 346 to 556, the domain is characterized as Rab-GAP TBC.
+At position 26 to 170, the domain is characterized as UBC core.
+At position 63 to 151, the domain is characterized as PA.
+At position 40 to 331, the domain is characterized as tr-type G.
+At position 31 to 112, the domain is characterized as GST N-terminal.
+At position 117 to 240, the domain is characterized as GST C-terminal.
+At position 446 to 594, the domain is characterized as N-acetyltransferase.
+At position 37 to 358, the domain is characterized as AB hydrolase-1.
+At position 15 to 153, the domain is characterized as SIS 1.
+At position 181 to 311, the domain is characterized as SIS 2.
+At position 291 to 439, the domain is characterized as Helicase C-terminal.
+At position 45 to 228, the domain is characterized as Helicase ATP-binding.
+At position 257 to 419, the domain is characterized as Helicase C-terminal.
+At position 128 to 385, the domain is characterized as PPM-type phosphatase.
+At position 375 to 466, the domain is characterized as RRM 1.
+At position 483 to 565, the domain is characterized as RRM 2.
+At position 12 to 116, the domain is characterized as Longin.
+At position 41 to 72, the domain is characterized as F-box.
+At position 7 to 168, the domain is characterized as Era-type G.
+At position 433 to 629, the domain is characterized as FtsK.
+At position 103 to 358, the domain is characterized as UmuC.
+At position 90 to 220, the domain is characterized as GST C-terminal.
+At position 423 to 697, the domain is characterized as MYST-type HAT.
+At position 118 to 425, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 26 to 132, the domain is characterized as HD.
+At position 252 to 537, the domain is characterized as Letm1 RBD.
+At position 1 to 25, the domain is characterized as H15.
+At position 59 to 107, the domain is characterized as EGF-like 2.
+At position 107 to 150, the domain is characterized as EGF-like 3.
+At position 151 to 176, the domain is characterized as EGF-like 4; truncated.
+At position 121 to 192, the domain is characterized as RRM 2.
+At position 20 to 243, the domain is characterized as Phosphagen kinase C-terminal.
+At position 182 to 370, the domain is characterized as CheB-type methylesterase.
+At position 1118 to 1283, the domain is characterized as Flo11.
+At position 230 to 498, the domain is characterized as Pterin-binding.
+At position 364 to 431, the domain is characterized as S4 RNA-binding.
+At position 564 to 817, the domain is characterized as Protein kinase.
+At position 92 to 389, the domain is characterized as Protein kinase.
+At position 390 to 458, the domain is characterized as AGC-kinase C-terminal.
+At position 7 to 280, the domain is characterized as CN hydrolase.
+At position 244 to 451, the domain is characterized as Histidine kinase.
+At position 18 to 216, the domain is characterized as DPCK.
+At position 8 to 206, the domain is characterized as tr-type G.
+At position 11 to 149, the domain is characterized as SprT-like.
+At position 19 to 247, the domain is characterized as ABC transporter.
+At position 150 to 230, the domain is characterized as PRC barrel.
+At position 135 to 307, the domain is characterized as 3'-5' exonuclease.
+At position 105 to 263, the domain is characterized as FAS1.
+At position 43 to 77, the domain is characterized as WW.
+At position 226 to 348, the domain is characterized as YkuD.
+At position 37 to 249, the domain is characterized as MIF4G.
+At position 353 to 386, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 396 to 427, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 41 to 207, the domain is characterized as NHR 1.
+At position 317 to 484, the domain is characterized as NHR 2.
+At position 520 to 686, the domain is characterized as NHR 3.
+At position 716 to 884, the domain is characterized as NHR 4.
+At position 913 to 1086, the domain is characterized as NHR 5.
+At position 1131 to 1294, the domain is characterized as NHR 6.
+At position 83 to 402, the domain is characterized as Kinesin motor.
+At position 678 to 951, the domain is characterized as Protein kinase.
+At position 7 to 137, the domain is characterized as MPN.
+At position 25 to 50, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 19 to 141, the domain is characterized as SIS.
+At position 71 to 264, the domain is characterized as Thioredoxin.
+At position 1101 to 1168, the domain is characterized as S1 motif.
+At position 1213 to 1314, the domain is characterized as SH2.
+At position 52 to 292, the domain is characterized as NodB homology.
+At position 123 to 221, the domain is characterized as Rhodanese.
+At position 155 to 445, the domain is characterized as Protein kinase.
+At position 446 to 526, the domain is characterized as AGC-kinase C-terminal.
+At position 4 to 80, the domain is characterized as HTH rpiR-type.
+At position 44 to 93, the domain is characterized as Ricin B-type lectin.
+At position 97 to 434, the domain is characterized as Kinesin motor.
+At position 27 to 54, the domain is characterized as LRRNT.
+At position 176 to 263, the domain is characterized as Ras-associating.
+At position 310 to 419, the domain is characterized as PH.
+At position 22 to 88, the domain is characterized as S1 motif 1.
+At position 106 to 172, the domain is characterized as S1 motif 2.
+At position 278 to 348, the domain is characterized as S1 motif 4.
+At position 365 to 435, the domain is characterized as S1 motif 5.
+At position 452 to 521, the domain is characterized as S1 motif 6.
+At position 1 to 65, the domain is characterized as Protein kinase; truncated.
+At position 255 to 336, the domain is characterized as POLO box.
+At position 439 to 456, the domain is characterized as WH2.
+At position 118 to 210, the domain is characterized as Ig-like C1-type.
+At position 159 to 354, the domain is characterized as CheB-type methylesterase.
+At position 108 to 189, the domain is characterized as RRM 2.
+At position 17 to 160, the domain is characterized as FAS1 1.
+At position 162 to 289, the domain is characterized as FAS1 2.
+At position 560 to 622, the domain is characterized as KH.
+At position 196 to 255, the domain is characterized as TRAM.
+At position 574 to 689, the domain is characterized as Cadherin 6.
+At position 76 to 254, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 154, the domain is characterized as MARVEL.
+At position 136 to 243, the domain is characterized as HTH LytTR-type.
+At position 353 to 435, the domain is characterized as OCT.
+At position 198 to 264, the domain is characterized as GRAM.
+At position 409 to 582, the domain is characterized as VASt.
+At position 8 to 116, the domain is characterized as HIT.
+At position 619 to 708, the domain is characterized as Cytochrome c.
+At position 136 to 458, the domain is characterized as PDEase.
+At position 17 to 170, the domain is characterized as MPN.
+At position 235 to 341, the domain is characterized as Fe2OG dioxygenase.
+At position 53 to 168, the domain is characterized as Rieske.
+At position 444 to 510, the domain is characterized as S4 RNA-binding.
+At position 83 to 154, the domain is characterized as CBS 1.
+At position 252 to 309, the domain is characterized as CBS 3.
+At position 366 to 438, the domain is characterized as CBS 4.
+At position 244 to 302, the domain is characterized as LIM zinc-binding 1.
+At position 303 to 362, the domain is characterized as LIM zinc-binding 2.
+At position 363 to 421, the domain is characterized as LIM zinc-binding 3.
+At position 19 to 182, the domain is characterized as Exonuclease.
+At position 30 to 110, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 153 to 183, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 5 to 262, the domain is characterized as Alpha-carbonic anhydrase.
+At position 560 to 607, the domain is characterized as G-patch.
+At position 58 to 133, the domain is characterized as Carrier.
+At position 42 to 266, the domain is characterized as Radical SAM core.
+At position 98 to 284, the domain is characterized as ATP-grasp.
+At position 1938 to 2170, the domain is characterized as ABC transporter 2.
+At position 39 to 208, the domain is characterized as C2.
+At position 252 to 363, the domain is characterized as PH.
+At position 140 to 344, the domain is characterized as ATP-grasp.
+At position 9 to 77, the domain is characterized as DRBM 1.
+At position 100 to 167, the domain is characterized as DRBM 2.
+At position 267 to 538, the domain is characterized as Protein kinase.
+At position 5 to 185, the domain is characterized as N-acetyltransferase.
+At position 43 to 336, the domain is characterized as GH10.
+At position 393 to 429, the domain is characterized as CBM1.
+At position 507 to 547, the domain is characterized as EGF-like 1.
+At position 551 to 781, the domain is characterized as Nidogen G2 beta-barrel.
+At position 782 to 823, the domain is characterized as EGF-like 2.
+At position 824 to 862, the domain is characterized as EGF-like 3; calcium-binding.
+At position 871 to 914, the domain is characterized as EGF-like 4.
+At position 915 to 953, the domain is characterized as EGF-like 5; calcium-binding.
+At position 965 to 1033, the domain is characterized as Thyroglobulin type-1 1.
+At position 1044 to 1112, the domain is characterized as Thyroglobulin type-1 2.
+At position 347 to 440, the domain is characterized as SH2.
+At position 7 to 302, the domain is characterized as Helicase ATP-binding.
+At position 113 to 185, the domain is characterized as RRM 1.
+At position 187 to 268, the domain is characterized as RRM 2.
+At position 46 to 211, the domain is characterized as Helicase ATP-binding.
+At position 265 to 438, the domain is characterized as Helicase C-terminal.
+At position 267 to 379, the domain is characterized as PAZ.
+At position 541 to 834, the domain is characterized as Piwi.
+At position 105 to 195, the domain is characterized as RRM.
+At position 140 to 173, the domain is characterized as EF-hand 4.
+At position 423 to 456, the domain is characterized as WW 1.
+At position 458 to 491, the domain is characterized as WW 2.
+At position 552 to 599, the domain is characterized as SARAH.
+At position 9 to 176, the domain is characterized as Ku.
+At position 15 to 161, the domain is characterized as VHS.
+At position 398 to 507, the domain is characterized as SH2.
+At position 502 to 552, the domain is characterized as SOCS box.
+At position 357 to 613, the domain is characterized as UvrD-like helicase C-terminal.
+At position 408 to 579, the domain is characterized as tr-type G.
+At position 174 to 260, the domain is characterized as Ig-like C2-type 2.
+At position 378 to 459, the domain is characterized as SAND.
+At position 27 to 321, the domain is characterized as GH18.
+At position 63 to 138, the domain is characterized as S1-like.
+At position 156 to 454, the domain is characterized as GT92.
+At position 191 to 527, the domain is characterized as Protein kinase.
+At position 593 to 658, the domain is characterized as SAM.
+At position 81 to 787, the domain is characterized as Myosin motor.
+At position 223 to 438, the domain is characterized as Histidine kinase.
+At position 151 to 402, the domain is characterized as ABC transporter 1.
+At position 507 to 751, the domain is characterized as ABC transmembrane type-2 1.
+At position 838 to 1082, the domain is characterized as ABC transporter 2.
+At position 1182 to 1405, the domain is characterized as ABC transmembrane type-2 2.
+At position 4 to 68, the domain is characterized as Histone-fold.
+At position 24 to 126, the domain is characterized as Gnk2-homologous 1.
+At position 134 to 238, the domain is characterized as Gnk2-homologous 2.
+At position 321 to 606, the domain is characterized as Protein kinase.
+At position 47 to 307, the domain is characterized as PPM-type phosphatase.
+At position 83 to 353, the domain is characterized as Protein kinase.
+At position 63 to 347, the domain is characterized as Protein kinase.
+At position 121 to 360, the domain is characterized as Radical SAM core.
+At position 21 to 84, the domain is characterized as IGFBP N-terminal.
+At position 64 to 128, the domain is characterized as Kazal-like.
+At position 359 to 444, the domain is characterized as PDZ.
+At position 223 to 394, the domain is characterized as TrmE-type G.
+At position 181 to 253, the domain is characterized as U-box.
+At position 17 to 194, the domain is characterized as Velvet.
+At position 27 to 178, the domain is characterized as Cyclin N-terminal.
+At position 652 to 751, the domain is characterized as FH1.
+At position 766 to 1182, the domain is characterized as FH2.
+At position 125 to 373, the domain is characterized as ABC transporter 1.
+At position 478 to 718, the domain is characterized as ABC transmembrane type-2 1.
+At position 808 to 1052, the domain is characterized as ABC transporter 2.
+At position 1144 to 1369, the domain is characterized as ABC transmembrane type-2 2.
+At position 102 to 290, the domain is characterized as DH.
+At position 319 to 418, the domain is characterized as PH 1.
+At position 544 to 641, the domain is characterized as PH 2.
+At position 8 to 150, the domain is characterized as RNase H type-1.
+At position 139 to 255, the domain is characterized as TFIIS central.
+At position 72 to 194, the domain is characterized as PX.
+At position 29 to 451, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 980 to 1274, the domain is characterized as PKS/mFAS DH.
+At position 2486 to 2565, the domain is characterized as Carrier.
+At position 38 to 175, the domain is characterized as C-type lectin.
+At position 42 to 108, the domain is characterized as HMA.
+At position 479 to 545, the domain is characterized as SAM.
+At position 135 to 228, the domain is characterized as RRM.
+At position 15 to 221, the domain is characterized as Cytochrome b561.
+At position 126 to 346, the domain is characterized as Radical SAM core.
+At position 29 to 161, the domain is characterized as Nudix hydrolase.
+At position 6 to 92, the domain is characterized as Acylphosphatase-like.
+At position 166 to 206, the domain is characterized as LRRCT.
+At position 137 to 190, the domain is characterized as SANT.
+At position 600 to 775, the domain is characterized as Helicase C-terminal.
+At position 142 to 508, the domain is characterized as PDEase.
+At position 279 to 437, the domain is characterized as Helicase C-terminal.
+At position 28 to 374, the domain is characterized as FERM.
+At position 11 to 100, the domain is characterized as EH 1.
+At position 46 to 77, the domain is characterized as EF-hand 2.
+At position 115 to 204, the domain is characterized as EH 2.
+At position 223 to 310, the domain is characterized as EH 3.
+At position 254 to 289, the domain is characterized as EF-hand 4.
+At position 484 to 543, the domain is characterized as SH3.
+At position 559 to 722, the domain is characterized as RUN.
+At position 45 to 64, the domain is characterized as EF-hand 1.
+At position 70 to 98, the domain is characterized as EF-hand 2.
+At position 151 to 169, the domain is characterized as EF-hand 4.
+At position 235 to 385, the domain is characterized as Helicase C-terminal.
+At position 45 to 187, the domain is characterized as GAF.
+At position 229 to 457, the domain is characterized as Sigma-54 factor interaction.
+At position 86 to 162, the domain is characterized as RRM.
+At position 216 to 360, the domain is characterized as FCP1 homology.
+At position 371 to 393, the domain is characterized as WH2.
+At position 446 to 833, the domain is characterized as USP.
+At position 881 to 1054, the domain is characterized as Exonuclease.
+At position 184 to 377, the domain is characterized as CheB-type methylesterase.
+At position 3 to 133, the domain is characterized as TsaA-like.
+At position 8 to 125, the domain is characterized as MTTase N-terminal.
+At position 371 to 439, the domain is characterized as TRAM.
+At position 107 to 195, the domain is characterized as CARD.
+At position 135 to 385, the domain is characterized as Radical SAM core.
+At position 107 to 142, the domain is characterized as EF-hand 1.
+At position 143 to 178, the domain is characterized as EF-hand 2.
+At position 179 to 214, the domain is characterized as EF-hand 3.
+At position 222 to 258, the domain is characterized as EF-hand 4.
+At position 139 to 270, the domain is characterized as SCP.
+At position 316 to 349, the domain is characterized as EGF-like.
+At position 394 to 521, the domain is characterized as C-type lectin.
+At position 127 to 283, the domain is characterized as CBM21.
+At position 15 to 153, the domain is characterized as DAC.
+At position 14 to 344, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 359 to 685, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 2 to 378, the domain is characterized as BRO1.
+At position 40 to 84, the domain is characterized as Fibronectin type-II 1.
+At position 85 to 133, the domain is characterized as Fibronectin type-II 2.
+At position 20 to 121, the domain is characterized as Ig-like V-type.
+At position 621 to 701, the domain is characterized as BRCT.
+At position 27 to 85, the domain is characterized as FHA.
+At position 370 to 737, the domain is characterized as A to I editase.
+At position 26 to 113, the domain is characterized as UPAR/Ly6.
+At position 72 to 149, the domain is characterized as ACT.
+At position 487 to 667, the domain is characterized as Lon proteolytic.
+At position 127 to 311, the domain is characterized as ATP-grasp.
+At position 435 to 473, the domain is characterized as Ubiquitin-like.
+At position 17 to 140, the domain is characterized as RNase III.
+At position 167 to 236, the domain is characterized as DRBM.
+At position 240 to 314, the domain is characterized as Ig-like C2-type 2.
+At position 65 to 249, the domain is characterized as Helicase ATP-binding.
+At position 404 to 575, the domain is characterized as Helicase C-terminal.
+At position 597 to 700, the domain is characterized as Dicer dsRNA-binding fold.
+At position 959 to 1107, the domain is characterized as RNase III 1.
+At position 1153 to 1353, the domain is characterized as RNase III 2.
+At position 1383 to 1483, the domain is characterized as DRBM.
+At position 6 to 199, the domain is characterized as Lon N-terminal.
+At position 33 to 166, the domain is characterized as MPN.
+At position 77 to 155, the domain is characterized as RRM.
+At position 37 to 248, the domain is characterized as Cupin type-1 1.
+At position 436 to 453, the domain is characterized as WH2.
+At position 187 to 376, the domain is characterized as Helicase ATP-binding.
+At position 387 to 547, the domain is characterized as Helicase C-terminal.
+At position 166 to 353, the domain is characterized as Glutamine amidotransferase type-1.
+At position 38 to 379, the domain is characterized as G-alpha.
+At position 14 to 133, the domain is characterized as C2.
+At position 281 to 825, the domain is characterized as PLA2c.
+At position 1 to 133, the domain is characterized as Nudix hydrolase.
+At position 33 to 288, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 987 to 1304, the domain is characterized as DOT1.
+At position 57 to 227, the domain is characterized as Laminin G-like.
+At position 632 to 687, the domain is characterized as VWFC 2.
+At position 692 to 750, the domain is characterized as VWFC 3.
+At position 287 to 321, the domain is characterized as EGF-like 1.
+At position 325 to 362, the domain is characterized as EGF-like 2.
+At position 636 to 675, the domain is characterized as EGF-like 3.
+At position 679 to 715, the domain is characterized as EGF-like 4.
+At position 719 to 753, the domain is characterized as EGF-like 5.
+At position 818 to 854, the domain is characterized as EGF-like 6.
+At position 858 to 897, the domain is characterized as EGF-like 7.
+At position 901 to 938, the domain is characterized as EGF-like 8.
+At position 942 to 979, the domain is characterized as EGF-like 9.
+At position 42 to 70, the domain is characterized as EF-hand 2.
+At position 110 to 145, the domain is characterized as EF-hand 4.
+At position 55 to 122, the domain is characterized as DRBM 1.
+At position 142 to 228, the domain is characterized as DRBM 2.
+At position 254 to 321, the domain is characterized as DRBM 3.
+At position 354 to 422, the domain is characterized as DRBM 4.
+At position 540 to 604, the domain is characterized as DRBM 5.
+At position 368 to 453, the domain is characterized as OCT.
+At position 20 to 377, the domain is characterized as Glutamine amidotransferase type-2.
+At position 35 to 494, the domain is characterized as Hexokinase.
+At position 69 to 271, the domain is characterized as ABC transmembrane type-1.
+At position 539 to 717, the domain is characterized as Helicase C-terminal.
+At position 187 to 294, the domain is characterized as HD.
+At position 141 to 482, the domain is characterized as Kinesin motor.
+At position 1 to 242, the domain is characterized as Radical SAM core.
+At position 353 to 419, the domain is characterized as J.
+At position 166 to 224, the domain is characterized as bZIP.
+At position 319 to 499, the domain is characterized as N-acetyltransferase.
+At position 44 to 306, the domain is characterized as ZP.
+At position 280 to 318, the domain is characterized as LRRCT.
+At position 6 to 201, the domain is characterized as DPCK.
+At position 59 to 197, the domain is characterized as C1q.
+At position 15 to 103, the domain is characterized as GS beta-grasp.
+At position 110 to 442, the domain is characterized as GS catalytic.
+At position 14 to 63, the domain is characterized as bHLH.
+At position 16 to 127, the domain is characterized as Rieske 1.
+At position 165 to 240, the domain is characterized as PPIase FKBP-type.
+At position 43 to 118, the domain is characterized as DEP.
+At position 301 to 434, the domain is characterized as N-terminal Ras-GEF.
+At position 578 to 813, the domain is characterized as Ras-GEF.
+At position 1 to 343, the domain is characterized as Trm1 methyltransferase.
+At position 18 to 78, the domain is characterized as MADS-box.
+At position 108 to 279, the domain is characterized as FAD-binding PCMH-type.
+At position 40 to 174, the domain is characterized as Nudix hydrolase.
+At position 1 to 82, the domain is characterized as Helicase ATP-binding.
+At position 93 to 253, the domain is characterized as Helicase C-terminal.
+At position 47 to 321, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 89 to 248, the domain is characterized as HDAg.
+At position 241 to 402, the domain is characterized as W2.
+At position 51 to 124, the domain is characterized as KH type-2.
+At position 85 to 503, the domain is characterized as Peptidase A1.
+At position 315 to 417, the domain is characterized as Saposin B-type.
+At position 16 to 202, the domain is characterized as Ku.
+At position 694 to 968, the domain is characterized as Protein kinase.
+At position 50 to 253, the domain is characterized as AH.
+At position 464 to 576, the domain is characterized as PH.
+At position 1 to 45, the domain is characterized as Kazal-like.
+At position 1 to 466, the domain is characterized as Biotin carboxylation.
+At position 602 to 681, the domain is characterized as Biotinyl-binding.
+At position 72 to 388, the domain is characterized as Peptidase A1.
+At position 59 to 240, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 41, the domain is characterized as Ubiquitin-like 1.
+At position 42 to 117, the domain is characterized as Ubiquitin-like 2.
+At position 118 to 193, the domain is characterized as Ubiquitin-like 3.
+At position 194 to 269, the domain is characterized as Ubiquitin-like 4.
+At position 270 to 345, the domain is characterized as Ubiquitin-like 5.
+At position 346 to 421, the domain is characterized as Ubiquitin-like 6.
+At position 28 to 109, the domain is characterized as Lipoyl-binding.
+At position 269 to 498, the domain is characterized as Methyl-accepting transducer.
+At position 37 to 191, the domain is characterized as Flavodoxin-like.
+At position 336 to 580, the domain is characterized as Radical SAM core.
+At position 2 to 668, the domain is characterized as GH81.
+At position 242 to 403, the domain is characterized as Helicase C-terminal.
+At position 31 to 73, the domain is characterized as WAP 1.
+At position 86 to 300, the domain is characterized as Radical SAM core.
+At position 569 to 644, the domain is characterized as HSA.
+At position 841 to 899, the domain is characterized as Myb-like.
+At position 132 to 362, the domain is characterized as Radical SAM core.
+At position 365 to 430, the domain is characterized as TRAM.
+At position 147 to 453, the domain is characterized as Peptidase S8.
+At position 254 to 465, the domain is characterized as GATase cobBQ-type.
+At position 25 to 105, the domain is characterized as GST N-terminal.
+At position 110 to 238, the domain is characterized as GST C-terminal.
+At position 34 to 161, the domain is characterized as PLAT.
+At position 91 to 311, the domain is characterized as Glutamine amidotransferase type-2.
+At position 279 to 556, the domain is characterized as ABC transmembrane type-1 1.
+At position 593 to 829, the domain is characterized as ABC transporter 1.
+At position 882 to 1162, the domain is characterized as ABC transmembrane type-1 2.
+At position 1199 to 1431, the domain is characterized as ABC transporter 2.
+At position 50 to 134, the domain is characterized as SCAN box.
+At position 224 to 260, the domain is characterized as KRAB.
+At position 35 to 124, the domain is characterized as PPIase FKBP-type.
+At position 148 to 256, the domain is characterized as Cadherin 1.
+At position 257 to 370, the domain is characterized as Cadherin 2.
+At position 371 to 481, the domain is characterized as Cadherin 3.
+At position 482 to 589, the domain is characterized as Cadherin 4.
+At position 605 to 688, the domain is characterized as Cadherin 5.
+At position 6 to 141, the domain is characterized as MARVEL.
+At position 4 to 295, the domain is characterized as Protein kinase.
+At position 11 to 257, the domain is characterized as Lon N-terminal.
+At position 727 to 914, the domain is characterized as Lon proteolytic.
+At position 61 to 152, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 36 to 156, the domain is characterized as Thioredoxin.
+At position 396 to 503, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 89 to 211, the domain is characterized as C2 1.
+At position 251 to 384, the domain is characterized as C2 2.
+At position 90 to 142, the domain is characterized as HAMP.
+At position 150 to 358, the domain is characterized as Histidine kinase.
+At position 27 to 128, the domain is characterized as Gnk2-homologous 1.
+At position 139 to 246, the domain is characterized as Gnk2-homologous 2.
+At position 340 to 612, the domain is characterized as Protein kinase.
+At position 188 to 393, the domain is characterized as ABC transmembrane type-1 1.
+At position 479 to 669, the domain is characterized as ABC transmembrane type-1 2.
+At position 56 to 111, the domain is characterized as TSP type-1 1.
+At position 117 to 159, the domain is characterized as LDL-receptor class A.
+At position 541 to 587, the domain is characterized as TSP type-1 2.
+At position 364 to 510, the domain is characterized as Helicase C-terminal.
+At position 28 to 322, the domain is characterized as Peptidase S6.
+At position 1280 to 1532, the domain is characterized as Autotransporter.
+At position 22 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 162 to 384, the domain is characterized as Histidine kinase.
+At position 75 to 158, the domain is characterized as RRM 1.
+At position 159 to 238, the domain is characterized as RRM 2.
+At position 772 to 1067, the domain is characterized as Protein kinase.
+At position 240 to 427, the domain is characterized as Glutamine amidotransferase type-1.
+At position 62 to 168, the domain is characterized as Plastocyanin-like 1.
+At position 318 to 381, the domain is characterized as Plastocyanin-like 2.
+At position 486 to 613, the domain is characterized as Plastocyanin-like 3.
+At position 42 to 294, the domain is characterized as CN hydrolase.
+At position 75 to 267, the domain is characterized as N-acetyltransferase.
+At position 87 to 193, the domain is characterized as HTH APSES-type.
+At position 557 to 608, the domain is characterized as GRIP.
+At position 104 to 291, the domain is characterized as Tyr recombinase.
+At position 11 to 183, the domain is characterized as Ku.
+At position 74 to 256, the domain is characterized as ABC transmembrane type-1.
+At position 150 to 251, the domain is characterized as PH.
+At position 242 to 363, the domain is characterized as C2.
+At position 443 to 635, the domain is characterized as Ras-GAP.
+At position 669 to 758, the domain is characterized as BRCT.
+At position 50 to 168, the domain is characterized as HotDog ACOT-type 1.
+At position 224 to 338, the domain is characterized as HotDog ACOT-type 2.
+At position 227 to 395, the domain is characterized as TrmE-type G.
+At position 385 to 466, the domain is characterized as SAND.
+At position 204 to 289, the domain is characterized as Ig-like C1-type.
+At position 72 to 126, the domain is characterized as AWS.
+At position 128 to 245, the domain is characterized as SET.
+At position 252 to 268, the domain is characterized as Post-SET.
+At position 512 to 544, the domain is characterized as WW.
+At position 178 to 215, the domain is characterized as UBA.
+At position 1 to 62, the domain is characterized as Peptidase S8.
+At position 16 to 29, the domain is characterized as CRIB.
+At position 231 to 482, the domain is characterized as Protein kinase.
+At position 10 to 433, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 915 to 1206, the domain is characterized as PKS/mFAS DH.
+At position 2431 to 2509, the domain is characterized as Carrier.
+At position 241 to 555, the domain is characterized as CN hydrolase.
+At position 30 to 73, the domain is characterized as CUE.
+At position 1 to 46, the domain is characterized as SH3.
+At position 78 to 262, the domain is characterized as DH.
+At position 293 to 400, the domain is characterized as PH.
+At position 109 to 144, the domain is characterized as EF-hand 1.
+At position 371 to 505, the domain is characterized as DAGKc.
+At position 36 to 224, the domain is characterized as EngB-type G.
+At position 268 to 388, the domain is characterized as Sox C-terminal.
+At position 16 to 106, the domain is characterized as Core-binding (CB).
+At position 127 to 313, the domain is characterized as Tyr recombinase.
+At position 22 to 105, the domain is characterized as GIY-YIG.
+At position 118 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 239 to 297, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 428, the domain is characterized as Ig-like C2-type 4.
+At position 424 to 513, the domain is characterized as Ig-like C2-type 5.
+At position 537 to 618, the domain is characterized as Ig-like C2-type 6.
+At position 539 to 708, the domain is characterized as N-acetyltransferase.
+At position 107 to 179, the domain is characterized as S4 RNA-binding.
+At position 9 to 86, the domain is characterized as PUA.
+At position 88 to 783, the domain is characterized as Myosin motor.
+At position 783 to 815, the domain is characterized as IQ.
+At position 378 to 439, the domain is characterized as TRAM.
+At position 5 to 168, the domain is characterized as EngA-type G 1.
+At position 78 to 546, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 398 to 523, the domain is characterized as DBINO.
+At position 645 to 817, the domain is characterized as Helicase ATP-binding.
+At position 1220 to 1380, the domain is characterized as Helicase C-terminal.
+At position 78 to 150, the domain is characterized as ACT 1.
+At position 309 to 383, the domain is characterized as ACT 2.
+At position 19 to 114, the domain is characterized as HPt.
+At position 133 to 448, the domain is characterized as Protein kinase.
+At position 177 to 278, the domain is characterized as HTH araC/xylS-type.
+At position 453 to 726, the domain is characterized as Protein kinase.
+At position 727 to 795, the domain is characterized as AGC-kinase C-terminal.
+At position 1042 to 1130, the domain is characterized as PDZ.
+At position 26 to 158, the domain is characterized as Ephrin RBD.
+At position 16 to 106, the domain is characterized as Acylphosphatase-like.
+At position 791 to 978, the domain is characterized as Macro 1.
+At position 1003 to 1190, the domain is characterized as Macro 2.
+At position 1216 to 1387, the domain is characterized as Macro 3.
+At position 1523 to 1601, the domain is characterized as WWE.
+At position 1605 to 1801, the domain is characterized as PARP catalytic.
+At position 203 to 276, the domain is characterized as Chromo 1.
+At position 304 to 365, the domain is characterized as Chromo 2.
+At position 402 to 573, the domain is characterized as Helicase ATP-binding.
+At position 708 to 869, the domain is characterized as Helicase C-terminal.
+At position 124 to 292, the domain is characterized as Helicase ATP-binding.
+At position 450 to 621, the domain is characterized as Helicase C-terminal.
+At position 14 to 150, the domain is characterized as VHS.
+At position 177 to 301, the domain is characterized as GAT.
+At position 391 to 510, the domain is characterized as GAE.
+At position 291 to 371, the domain is characterized as PAH.
+At position 666 to 808, the domain is characterized as TIR.
+At position 800 to 1087, the domain is characterized as NB-ARC.
+At position 1626 to 1877, the domain is characterized as Protein kinase.
+At position 159 to 511, the domain is characterized as USP.
+At position 333 to 379, the domain is characterized as G-patch.
+At position 169 to 397, the domain is characterized as START.
+At position 120 to 245, the domain is characterized as Fe2OG dioxygenase.
+At position 258 to 298, the domain is characterized as ShKT.
+At position 317 to 414, the domain is characterized as Fe2OG dioxygenase.
+At position 82 to 342, the domain is characterized as Protein kinase.
+At position 459 to 550, the domain is characterized as PH.
+At position 44 to 238, the domain is characterized as Peptidase M12A.
+At position 84 to 187, the domain is characterized as Calponin-homology (CH).
+At position 1102 to 1249, the domain is characterized as N-terminal Ras-GEF.
+At position 1267 to 1498, the domain is characterized as Ras-GEF.
+At position 73 to 529, the domain is characterized as IF rod.
+At position 695 to 812, the domain is characterized as SMC hinge.
+At position 15 to 325, the domain is characterized as Kinesin motor.
+At position 142 to 298, the domain is characterized as PID.
+At position 566 to 752, the domain is characterized as Rab-GAP TBC.
+At position 60 to 286, the domain is characterized as SET.
+At position 285 to 540, the domain is characterized as Protein kinase.
+At position 273 to 356, the domain is characterized as Death.
+At position 484 to 726, the domain is characterized as ABC transporter.
+At position 832 to 1029, the domain is characterized as ABC transmembrane type-2.
+At position 85 to 282, the domain is characterized as Peptidase M12A.
+At position 500 to 640, the domain is characterized as CBM6.
+At position 59 to 217, the domain is characterized as SIS 1.
+At position 222 to 366, the domain is characterized as SIS 2.
+At position 34 to 116, the domain is characterized as Doublecortin 1.
+At position 156 to 235, the domain is characterized as Doublecortin 2.
+At position 33 to 306, the domain is characterized as Pyruvate carboxyltransferase.
+At position 121 to 169, the domain is characterized as F-box.
+At position 369 to 542, the domain is characterized as tr-type G.
+At position 131 to 572, the domain is characterized as Urease.
+At position 37 to 86, the domain is characterized as Collagen-like 1.
+At position 60 to 114, the domain is characterized as Collagen-like 2.
+At position 117 to 253, the domain is characterized as C1q.
+At position 152 to 221, the domain is characterized as DRBM.
+At position 9 to 84, the domain is characterized as Lipoyl-binding.
+At position 137 to 360, the domain is characterized as AB hydrolase-1.
+At position 162 to 878, the domain is characterized as Peptidase M13.
+At position 143 to 345, the domain is characterized as TRUD.
+At position 239 to 498, the domain is characterized as NR LBD.
+At position 171 to 261, the domain is characterized as 5'-3' exonuclease.
+At position 95 to 355, the domain is characterized as NR LBD.
+At position 244 to 440, the domain is characterized as GATase cobBQ-type.
+At position 228 to 371, the domain is characterized as PAS 1.
+At position 390 to 493, the domain is characterized as PAS 2.
+At position 163 to 256, the domain is characterized as 5'-3' exonuclease.
+At position 269 to 336, the domain is characterized as PAS 2.
+At position 342 to 380, the domain is characterized as PAC.
+At position 230 to 369, the domain is characterized as Cupin type-1 1.
+At position 414 to 584, the domain is characterized as Cupin type-1 2.
+At position 112 to 323, the domain is characterized as Radical SAM core.
+At position 331 to 394, the domain is characterized as S4 RNA-binding.
+At position 61 to 163, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 3 to 455, the domain is characterized as Biotin carboxylation.
+At position 533 to 802, the domain is characterized as Pyruvate carboxyltransferase.
+At position 51 to 98, the domain is characterized as LysM 1.
+At position 284 to 573, the domain is characterized as Protein kinase.
+At position 31 to 278, the domain is characterized as PPM-type phosphatase.
+At position 1 to 222, the domain is characterized as Peptidase S1.
+At position 1 to 164, the domain is characterized as Reticulon.
+At position 28 to 93, the domain is characterized as BTB.
+At position 200 to 509, the domain is characterized as NPH3.
+At position 538 to 853, the domain is characterized as Protein kinase.
+At position 10 to 63, the domain is characterized as CHCH.
+At position 47 to 251, the domain is characterized as Thioredoxin.
+At position 4 to 81, the domain is characterized as TFIIS N-terminal.
+At position 133 to 248, the domain is characterized as TFIIS central.
+At position 3 to 109, the domain is characterized as Calponin-homology (CH).
+At position 35 to 355, the domain is characterized as G-alpha.
+At position 24 to 168, the domain is characterized as UBC core.
+At position 28 to 84, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 90 to 134, the domain is characterized as WR1.
+At position 1397 to 1504, the domain is characterized as Calponin-homology (CH).
+At position 251 to 431, the domain is characterized as GATase cobBQ-type.
+At position 183 to 261, the domain is characterized as Saposin B-type 2.
+At position 291 to 371, the domain is characterized as Saposin B-type 3.
+At position 393 to 474, the domain is characterized as Saposin B-type 4.
+At position 476 to 516, the domain is characterized as Saposin A-type 2.
+At position 9 to 259, the domain is characterized as Protein kinase.
+At position 525 to 732, the domain is characterized as MCM.
+At position 18 to 189, the domain is characterized as Phosphatase tensin-type.
+At position 957 to 997, the domain is characterized as UBA.
+At position 657 to 746, the domain is characterized as BRCT.
+At position 79 to 154, the domain is characterized as ACT.
+At position 35 to 223, the domain is characterized as GH11.
+At position 256 to 294, the domain is characterized as LRRCT.
+At position 58 to 182, the domain is characterized as Rhodanese.
+At position 67 to 326, the domain is characterized as Protein kinase 1.
+At position 327 to 396, the domain is characterized as AGC-kinase C-terminal.
+At position 420 to 677, the domain is characterized as Protein kinase 2.
+At position 786 to 848, the domain is characterized as RhoBD.
+At position 950 to 1144, the domain is characterized as PH.
+At position 177 to 363, the domain is characterized as Helicase ATP-binding.
+At position 446 to 602, the domain is characterized as Helicase C-terminal.
+At position 10 to 220, the domain is characterized as RNase H type-2.
+At position 138 to 232, the domain is characterized as WSC.
+At position 6 to 29, the domain is characterized as Pentraxin (PTX).
+At position 29 to 75, the domain is characterized as PSI.
+At position 134 to 376, the domain is characterized as VWFA.
+At position 435 to 497, the domain is characterized as EGF-like 1.
+At position 498 to 547, the domain is characterized as EGF-like 2.
+At position 548 to 584, the domain is characterized as EGF-like 3.
+At position 585 to 628, the domain is characterized as EGF-like 4.
+At position 259 to 558, the domain is characterized as Calpain catalytic.
+At position 796 to 831, the domain is characterized as EF-hand 1.
+At position 826 to 861, the domain is characterized as EF-hand 2.
+At position 26 to 107, the domain is characterized as GS beta-grasp.
+At position 114 to 362, the domain is characterized as GS catalytic.
+At position 211 to 378, the domain is characterized as PCI.
+At position 48 to 117, the domain is characterized as BON 1.
+At position 126 to 193, the domain is characterized as BON 2.
+At position 59 to 285, the domain is characterized as Peptidase S1.
+At position 143 to 169, the domain is characterized as PLD phosphodiesterase 1.
+At position 410 to 443, the domain is characterized as PLD phosphodiesterase 2.
+At position 6 to 83, the domain is characterized as Carrier.
+At position 65 to 97, the domain is characterized as LisH.
+At position 250 to 436, the domain is characterized as GATase cobBQ-type.
+At position 240 to 314, the domain is characterized as U-box.
+At position 3 to 109, the domain is characterized as HIT.
+At position 764 to 819, the domain is characterized as WAPL.
+At position 142 to 319, the domain is characterized as FAD-binding PCMH-type.
+At position 250 to 296, the domain is characterized as RPE1 insert.
+At position 578 to 858, the domain is characterized as Protein kinase.
+At position 80 to 200, the domain is characterized as GST C-terminal.
+At position 15 to 176, the domain is characterized as Thioredoxin 1.
+At position 180 to 327, the domain is characterized as Thioredoxin 2.
+At position 9 to 92, the domain is characterized as GIY-YIG.
+At position 10 to 150, the domain is characterized as CheW-like.
+At position 48 to 354, the domain is characterized as Protein kinase.
+At position 90 to 306, the domain is characterized as RNase H type-2.
+At position 103 to 553, the domain is characterized as Sema.
+At position 664 to 720, the domain is characterized as TSP type-1 1.
+At position 722 to 771, the domain is characterized as TSP type-1 2.
+At position 853 to 908, the domain is characterized as TSP type-1 3.
+At position 910 to 965, the domain is characterized as TSP type-1 4.
+At position 966 to 1010, the domain is characterized as TSP type-1 5.
+At position 589 to 668, the domain is characterized as BRCT.
+At position 441 to 612, the domain is characterized as tr-type G.
+At position 105 to 403, the domain is characterized as AB hydrolase-1.
+At position 454 to 535, the domain is characterized as SAND.
+At position 581 to 676, the domain is characterized as Bromo.
+At position 1 to 72, the domain is characterized as Peptidase M12B.
+At position 89 to 161, the domain is characterized as Disintegrin.
+At position 3 to 113, the domain is characterized as VPS28 N-terminal.
+At position 152 to 248, the domain is characterized as VPS28 C-terminal.
+At position 481 to 752, the domain is characterized as Reverse transcriptase.
+At position 1 to 193, the domain is characterized as RNase H type-2.
+At position 19 to 167, the domain is characterized as Reelin.
+At position 4 to 160, the domain is characterized as PPIase cyclophilin-type.
+At position 182 to 280, the domain is characterized as ELM2.
+At position 285 to 337, the domain is characterized as SANT.
+At position 19 to 136, the domain is characterized as Cystatin 1.
+At position 137 to 254, the domain is characterized as Cystatin 2.
+At position 7 to 148, the domain is characterized as N-acetyltransferase.
+At position 111 to 422, the domain is characterized as IF rod.
+At position 321 to 471, the domain is characterized as VPS9.
+At position 5 to 99, the domain is characterized as Toprim.
+At position 27 to 461, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 959 to 1267, the domain is characterized as PKS/mFAS DH.
+At position 2524 to 2601, the domain is characterized as Carrier.
+At position 522 to 677, the domain is characterized as SprT-like.
+At position 40 to 162, the domain is characterized as MARVEL.
+At position 140 to 246, the domain is characterized as Rhodanese.
+At position 18 to 259, the domain is characterized as tr-type G.
+At position 21 to 189, the domain is characterized as Era-type G.
+At position 212 to 296, the domain is characterized as KH type-2.
+At position 1152 to 1205, the domain is characterized as BIG2.
+At position 198 to 283, the domain is characterized as KH.
+At position 581 to 754, the domain is characterized as Helicase ATP-binding.
+At position 848 to 1025, the domain is characterized as Helicase C-terminal.
+At position 1 to 167, the domain is characterized as DHFR.
+At position 258 to 317, the domain is characterized as LIM zinc-binding.
+At position 22 to 129, the domain is characterized as Ig-like 1.
+At position 581 to 850, the domain is characterized as Protein kinase.
+At position 97 to 184, the domain is characterized as Rieske.
+At position 150 to 254, the domain is characterized as C-type lectin.
+At position 109 to 179, the domain is characterized as HTH iclR-type.
+At position 99 to 131, the domain is characterized as LisH.
+At position 519 to 721, the domain is characterized as Peptidase M12A.
+At position 723 to 839, the domain is characterized as CUB 1.
+At position 840 to 954, the domain is characterized as CUB 2.
+At position 954 to 994, the domain is characterized as EGF-like 1; calcium-binding.
+At position 997 to 1114, the domain is characterized as CUB 3.
+At position 1114 to 1154, the domain is characterized as EGF-like 2; calcium-binding.
+At position 1158 to 1270, the domain is characterized as CUB 4.
+At position 1271 to 1391, the domain is characterized as CUB 5.
+At position 24 to 110, the domain is characterized as Ig-like C1-type.
+At position 2 to 134, the domain is characterized as DAGKc.
+At position 76 to 147, the domain is characterized as KRAB.
+At position 288 to 349, the domain is characterized as SH3.
+At position 93 to 319, the domain is characterized as Radical SAM core.
+At position 127 to 322, the domain is characterized as Peptidase M12A.
+At position 317 to 358, the domain is characterized as EGF-like.
+At position 368 to 482, the domain is characterized as CUB.
+At position 507 to 556, the domain is characterized as TSP type-1.
+At position 204 to 377, the domain is characterized as EngA-type G 2.
+At position 378 to 462, the domain is characterized as KH-like.
+At position 11 to 181, the domain is characterized as Era-type G.
+At position 212 to 291, the domain is characterized as KH type-2.
+At position 86 to 278, the domain is characterized as B30.2/SPRY.
+At position 1 to 313, the domain is characterized as 5'-3' exonuclease.
+At position 314 to 488, the domain is characterized as 3'-5' exonuclease.
+At position 98 to 357, the domain is characterized as Protein kinase.
+At position 512 to 542, the domain is characterized as EF-hand 4.
+At position 19 to 71, the domain is characterized as F-box.
+At position 56 to 122, the domain is characterized as HMA 1.
+At position 207 to 273, the domain is characterized as HMA 3; degenerate.
+At position 51 to 433, the domain is characterized as Helicase ATP-binding.
+At position 453 to 612, the domain is characterized as Helicase C-terminal.
+At position 119 to 283, the domain is characterized as AB hydrolase-1.
+At position 394 to 496, the domain is characterized as Thioredoxin.
+At position 402 to 838, the domain is characterized as Urease.
+At position 285 to 379, the domain is characterized as SH2.
+At position 3 to 248, the domain is characterized as SAM-dependent MTase C5-type.
+At position 486 to 673, the domain is characterized as Rab-GAP TBC.
+At position 857 to 892, the domain is characterized as EF-hand.
+At position 107 to 306, the domain is characterized as MAGE.
+At position 8 to 333, the domain is characterized as Protein kinase.
+At position 41 to 322, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 335 to 509, the domain is characterized as tr-type G.
+At position 181 to 494, the domain is characterized as IF rod.
+At position 16 to 288, the domain is characterized as CNH.
+At position 261 to 514, the domain is characterized as EAL.
+At position 1 to 107, the domain is characterized as Ricin B-type lectin 1.
+At position 100 to 248, the domain is characterized as Ricin B-type lectin 2.
+At position 556 to 618, the domain is characterized as KH.
+At position 628 to 698, the domain is characterized as S1 motif.
+At position 386 to 445, the domain is characterized as SH3.
+At position 38 to 195, the domain is characterized as B12-binding.
+At position 268 to 496, the domain is characterized as Radical SAM core.
+At position 17 to 125, the domain is characterized as Rieske.
+At position 458 to 643, the domain is characterized as Cytochrome c.
+At position 30 to 118, the domain is characterized as Cystatin.
+At position 407 to 482, the domain is characterized as ACT 1.
+At position 488 to 565, the domain is characterized as ACT 2.
+At position 139 to 490, the domain is characterized as PUM-HD.
+At position 19 to 124, the domain is characterized as Gnk2-homologous 1.
+At position 131 to 243, the domain is characterized as Gnk2-homologous 2.
+At position 336 to 613, the domain is characterized as Protein kinase.
+At position 37 to 108, the domain is characterized as BTB.
+At position 873 to 996, the domain is characterized as PINc.
+At position 16 to 243, the domain is characterized as Radical SAM core.
+At position 1 to 125, the domain is characterized as C-type lysozyme.
+At position 57 to 246, the domain is characterized as KARI N-terminal Rossmann.
+At position 247 to 394, the domain is characterized as KARI C-terminal knotted.
+At position 281 to 339, the domain is characterized as LIM zinc-binding 1.
+At position 341 to 401, the domain is characterized as LIM zinc-binding 2.
+At position 404 to 471, the domain is characterized as LIM zinc-binding 3.
+At position 4 to 230, the domain is characterized as ABC transporter.
+At position 29 to 185, the domain is characterized as DAC.
+At position 33 to 244, the domain is characterized as BPL/LPL catalytic.
+At position 40 to 429, the domain is characterized as G-alpha.
+At position 270 to 424, the domain is characterized as Helicase C-terminal.
+At position 23 to 109, the domain is characterized as CFEM.
+At position 349 to 535, the domain is characterized as Lon proteolytic.
+At position 39 to 78, the domain is characterized as ShKT.
+At position 255 to 437, the domain is characterized as GAF.
+At position 656 to 727, the domain is characterized as PAS 1.
+At position 790 to 861, the domain is characterized as PAS 2.
+At position 938 to 1157, the domain is characterized as Histidine kinase.
+At position 144 to 343, the domain is characterized as Peptidase M12A.
+At position 345 to 457, the domain is characterized as CUB 1.
+At position 458 to 570, the domain is characterized as CUB 2.
+At position 570 to 610, the domain is characterized as EGF-like 1.
+At position 227 to 290, the domain is characterized as KH.
+At position 570 to 695, the domain is characterized as DBINO.
+At position 810 to 982, the domain is characterized as Helicase ATP-binding.
+At position 1325 to 1485, the domain is characterized as Helicase C-terminal.
+At position 51 to 221, the domain is characterized as MAM 1.
+At position 231 to 269, the domain is characterized as LDL-receptor class A.
+At position 275 to 436, the domain is characterized as MAM 2.
+At position 935 to 1211, the domain is characterized as Protein kinase.
+At position 143 to 221, the domain is characterized as GRAM.
+At position 76 to 288, the domain is characterized as RNase H type-2.
+At position 27 to 160, the domain is characterized as SIS.
+At position 112 to 189, the domain is characterized as RRM 2.
+At position 201 to 278, the domain is characterized as RRM 3.
+At position 509 to 586, the domain is characterized as PABC.
+At position 31 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 126 to 210, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 315, the domain is characterized as Ig-like C2-type 3.
+At position 324 to 417, the domain is characterized as Ig-like C2-type 4.
+At position 420 to 514, the domain is characterized as Ig-like C2-type 5.
+At position 592 to 939, the domain is characterized as Protein kinase.
+At position 826 to 1030, the domain is characterized as Laminin G-like 1.
+At position 1042 to 1222, the domain is characterized as Laminin G-like 2.
+At position 1229 to 1397, the domain is characterized as Laminin G-like 3.
+At position 1462 to 1633, the domain is characterized as Laminin G-like 4.
+At position 1640 to 1813, the domain is characterized as Laminin G-like 5.
+At position 24 to 276, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 168 to 272, the domain is characterized as Cadherin.
+At position 724 to 1016, the domain is characterized as Protein kinase.
+At position 285 to 363, the domain is characterized as RRM 1.
+At position 395 to 479, the domain is characterized as RRM 2.
+At position 111 to 401, the domain is characterized as ABC transmembrane type-1.
+At position 436 to 672, the domain is characterized as ABC transporter.
+At position 192 to 392, the domain is characterized as HIN-200.
+At position 226 to 381, the domain is characterized as TrmE-type G.
+At position 129 to 323, the domain is characterized as ATP-grasp 1.
+At position 660 to 849, the domain is characterized as ATP-grasp 2.
+At position 917 to 1024, the domain is characterized as MGS-like.
+At position 409 to 550, the domain is characterized as SEFIR.
+At position 208 to 1063, the domain is characterized as TBDR beta-barrel.
+At position 275 to 572, the domain is characterized as Protein kinase.
+At position 39 to 88, the domain is characterized as Collagen-like.
+At position 143 to 238, the domain is characterized as C-type lectin.
+At position 184 to 346, the domain is characterized as RNase H type-1.
+At position 2 to 370, the domain is characterized as TTL.
+At position 139 to 170, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 182 to 211, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 258 to 314, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 78 to 392, the domain is characterized as Peptidase A1.
+At position 623 to 686, the domain is characterized as bZIP.
+At position 28 to 299, the domain is characterized as Glutamine amidotransferase type-2.
+At position 7 to 168, the domain is characterized as N-acetyltransferase.
+At position 3 to 119, the domain is characterized as Toprim.
+At position 36 to 482, the domain is characterized as Hexokinase.
+At position 13 to 188, the domain is characterized as TLDc.
+At position 196 to 348, the domain is characterized as GAF 1.
+At position 380 to 564, the domain is characterized as GAF 2.
+At position 594 to 917, the domain is characterized as PDEase.
+At position 761 to 941, the domain is characterized as Flavodoxin-like.
+At position 996 to 1243, the domain is characterized as FAD-binding FR-type.
+At position 34 to 119, the domain is characterized as GOLD.
+At position 4 to 203, the domain is characterized as Flavodoxin-like.
+At position 1 to 152, the domain is characterized as Thioredoxin.
+At position 25 to 130, the domain is characterized as BTB.
+At position 94 to 128, the domain is characterized as EF-hand 2.
+At position 141 to 253, the domain is characterized as Ras-associating.
+At position 594 to 895, the domain is characterized as Dilute.
+At position 11 to 135, the domain is characterized as Arf-GAP.
+At position 72 to 140, the domain is characterized as POTRA.
+At position 33 to 128, the domain is characterized as HD.
+At position 394 to 623, the domain is characterized as NR LBD.
+At position 7 to 82, the domain is characterized as Cytochrome b5 heme-binding.
+At position 266 to 348, the domain is characterized as Toprim.
+At position 113 to 291, the domain is characterized as CP-type G.
+At position 22 to 153, the domain is characterized as MARVEL.
+At position 156 to 376, the domain is characterized as TRUD.
+At position 49 to 298, the domain is characterized as Radical SAM core.
+At position 7 to 125, the domain is characterized as MSP.
+At position 1 to 288, the domain is characterized as BRO1.
+At position 190 to 481, the domain is characterized as Protein kinase.
+At position 42 to 330, the domain is characterized as Protein kinase.
+At position 158 to 265, the domain is characterized as Cadherin 1.
+At position 266 to 378, the domain is characterized as Cadherin 2.
+At position 379 to 489, the domain is characterized as Cadherin 3.
+At position 490 to 595, the domain is characterized as Cadherin 4.
+At position 596 to 706, the domain is characterized as Cadherin 5.
+At position 372 to 784, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1255 to 1566, the domain is characterized as PKS/mFAS DH.
+At position 1620 to 1695, the domain is characterized as Carrier 1.
+At position 1722 to 1802, the domain is characterized as Carrier 2.
+At position 1 to 111, the domain is characterized as CMP/dCMP-type deaminase.
+At position 1 to 129, the domain is characterized as MGS-like.
+At position 59 to 329, the domain is characterized as Pyruvate carboxyltransferase.
+At position 497 to 601, the domain is characterized as Cache.
+At position 466 to 839, the domain is characterized as USP.
+At position 337 to 497, the domain is characterized as Helicase C-terminal.
+At position 250 to 478, the domain is characterized as Lon N-terminal.
+At position 477 to 586, the domain is characterized as CULT.
+At position 24 to 54, the domain is characterized as Peptidase M12B.
+At position 316 to 480, the domain is characterized as Helicase ATP-binding.
+At position 377 to 793, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1260 to 1568, the domain is characterized as PKS/mFAS DH.
+At position 1614 to 1688, the domain is characterized as Carrier.
+At position 284 to 568, the domain is characterized as Protein kinase.
+At position 23 to 90, the domain is characterized as POTRA 1.
+At position 91 to 171, the domain is characterized as POTRA 2.
+At position 174 to 262, the domain is characterized as POTRA 3.
+At position 265 to 344, the domain is characterized as POTRA 4.
+At position 200 to 247, the domain is characterized as GRAM 1.
+At position 251 to 351, the domain is characterized as PH.
+At position 827 to 893, the domain is characterized as GRAM 2.
+At position 838 to 1129, the domain is characterized as Protein kinase.
+At position 268 to 298, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 360 to 391, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 70 to 783, the domain is characterized as Myosin motor.
+At position 786 to 808, the domain is characterized as IQ 1.
+At position 809 to 833, the domain is characterized as IQ 2.
+At position 834 to 856, the domain is characterized as IQ 3.
+At position 857 to 881, the domain is characterized as IQ 4.
+At position 882 to 904, the domain is characterized as IQ 5.
+At position 905 to 934, the domain is characterized as IQ 6.
+At position 1223 to 1498, the domain is characterized as Dilute.
+At position 832 to 902, the domain is characterized as Bromo.
+At position 391 to 824, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1312 to 1621, the domain is characterized as PKS/mFAS DH.
+At position 1715 to 1792, the domain is characterized as Carrier.
+At position 29 to 221, the domain is characterized as GH11.
+At position 1 to 47, the domain is characterized as GH18.
+At position 853 to 1095, the domain is characterized as ABC transporter 2.
+At position 44 to 196, the domain is characterized as Tyrosine-protein phosphatase.
+At position 39 to 247, the domain is characterized as TR mART core.
+At position 93 to 765, the domain is characterized as Peptidase M13.
+At position 44 to 156, the domain is characterized as THUMP.
+At position 2 to 51, the domain is characterized as NB-ARC 1.
+At position 119 to 249, the domain is characterized as NB-ARC 2.
+At position 70 to 246, the domain is characterized as Helicase ATP-binding.
+At position 260 to 430, the domain is characterized as Helicase C-terminal.
+At position 30 to 206, the domain is characterized as PI-PLC X-box.
+At position 85 to 302, the domain is characterized as RNase H type-2.
+At position 238 to 375, the domain is characterized as MPN.
+At position 5 to 150, the domain is characterized as N-acetyltransferase 1.
+At position 160 to 322, the domain is characterized as N-acetyltransferase 2.
+At position 74 to 240, the domain is characterized as Helicase ATP-binding.
+At position 263 to 439, the domain is characterized as Helicase C-terminal.
+At position 91 to 161, the domain is characterized as SH3.
+At position 232 to 421, the domain is characterized as Guanylate kinase-like.
+At position 150 to 206, the domain is characterized as BTB.
+At position 4 to 281, the domain is characterized as Protein kinase.
+At position 6 to 141, the domain is characterized as ADF-H.
+At position 49 to 165, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 249 to 368, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 457 to 588, the domain is characterized as AXH.
+At position 52 to 238, the domain is characterized as ABC transmembrane type-1.
+At position 1025 to 1164, the domain is characterized as PINc.
+At position 116 to 155, the domain is characterized as Pentapeptide repeat 1.
+At position 156 to 196, the domain is characterized as Pentapeptide repeat 2.
+At position 63 to 165, the domain is characterized as HD.
+At position 406 to 467, the domain is characterized as TGS.
+At position 685 to 757, the domain is characterized as ACT.
+At position 307 to 434, the domain is characterized as Ricin B-type lectin 1.
+At position 437 to 561, the domain is characterized as Ricin B-type lectin 2.
+At position 201 to 402, the domain is characterized as Histidine kinase.
+At position 75 to 404, the domain is characterized as Asparaginase/glutaminase.
+At position 87 to 149, the domain is characterized as S4 RNA-binding.
+At position 60 to 123, the domain is characterized as S5 DRBM.
+At position 40 to 131, the domain is characterized as ARID.
+At position 4 to 83, the domain is characterized as Cystatin.
+At position 5 to 108, the domain is characterized as CS.
+At position 159 to 246, the domain is characterized as PDZ 1.
+At position 254 to 341, the domain is characterized as PDZ 2.
+At position 403 to 484, the domain is characterized as PDZ 3.
+At position 518 to 588, the domain is characterized as SH3.
+At position 637 to 812, the domain is characterized as Guanylate kinase-like.
+At position 17 to 167, the domain is characterized as NAC.
+At position 94 to 369, the domain is characterized as tr-type G.
+At position 119 to 199, the domain is characterized as RRM 1.
+At position 213 to 292, the domain is characterized as RRM 2.
+At position 327 to 399, the domain is characterized as RRM 3.
+At position 342 to 502, the domain is characterized as Helicase C-terminal.
+At position 2 to 426, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 960 to 1277, the domain is characterized as PKS/mFAS DH.
+At position 2467 to 2544, the domain is characterized as Carrier.
+At position 11 to 200, the domain is characterized as AMMECR1.
+At position 445 to 558, the domain is characterized as Cytochrome c.
+At position 522 to 626, the domain is characterized as PDZ 1.
+At position 696 to 765, the domain is characterized as PDZ 2.
+At position 395 to 476, the domain is characterized as Disintegrin.
+At position 457 to 554, the domain is characterized as Zinc-hook.
+At position 8 to 153, the domain is characterized as EXPERA.
+At position 73 to 109, the domain is characterized as EGF-like.
+At position 116 to 370, the domain is characterized as ZP.
+At position 6 to 65, the domain is characterized as HTH tetR-type.
+At position 90 to 489, the domain is characterized as Protein kinase.
+At position 25 to 56, the domain is characterized as Phytocyanin 1.
+At position 57 to 102, the domain is characterized as Phytocyanin 2.
+At position 116 to 216, the domain is characterized as Phytocyanin 3.
+At position 248 to 444, the domain is characterized as GATase cobBQ-type.
+At position 186 to 356, the domain is characterized as PCI.
+At position 536 to 609, the domain is characterized as HSA.
+At position 921 to 1086, the domain is characterized as Helicase ATP-binding.
+At position 1470 to 1623, the domain is characterized as Helicase C-terminal.
+At position 63 to 118, the domain is characterized as HAMP 1.
+At position 157 to 209, the domain is characterized as HAMP 2.
+At position 249 to 301, the domain is characterized as HAMP 3.
+At position 341 to 393, the domain is characterized as HAMP 4.
+At position 433 to 485, the domain is characterized as HAMP 5.
+At position 507 to 730, the domain is characterized as Histidine kinase.
+At position 875 to 999, the domain is characterized as Response regulatory.
+At position 4 to 370, the domain is characterized as Trm1 methyltransferase.
+At position 28 to 251, the domain is characterized as Radical SAM core.
+At position 699 to 975, the domain is characterized as Autotransporter.
+At position 213 to 337, the domain is characterized as OTU.
+At position 1 to 75, the domain is characterized as UBC core.
+At position 16 to 117, the domain is characterized as MaoC-like.
+At position 113 to 312, the domain is characterized as ATP-grasp.
+At position 222 to 405, the domain is characterized as MIF4G.
+At position 507 to 623, the domain is characterized as MI.
+At position 25 to 54, the domain is characterized as IQ.
+At position 104 to 396, the domain is characterized as ABC transmembrane type-1 1.
+At position 433 to 668, the domain is characterized as ABC transporter 1.
+At position 781 to 1066, the domain is characterized as ABC transmembrane type-1 2.
+At position 1099 to 1331, the domain is characterized as ABC transporter 2.
+At position 98 to 283, the domain is characterized as tr-type G.
+At position 73 to 344, the domain is characterized as Radical SAM core.
+At position 387 to 534, the domain is characterized as N-acetyltransferase.
+At position 660 to 836, the domain is characterized as Integrase catalytic.
+At position 17 to 128, the domain is characterized as C-type lectin.
+At position 175 to 312, the domain is characterized as VLRF1.
+At position 27 to 109, the domain is characterized as GIY-YIG.
+At position 26 to 87, the domain is characterized as Kazal-like.
+At position 36 to 182, the domain is characterized as UBC core.
+At position 1118 to 1175, the domain is characterized as DEK-C.
+At position 78 to 174, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 30, the domain is characterized as Beta/gamma crystallin 'Greek key'.
+At position 241 to 501, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 533 to 791, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 9 to 117, the domain is characterized as RWD.
+At position 22 to 142, the domain is characterized as DSCP-N.
+At position 188 to 210, the domain is characterized as Follistatin-like 1.
+At position 231 to 253, the domain is characterized as Follistatin-like 2.
+At position 275 to 298, the domain is characterized as Follistatin-like 3.
+At position 315 to 338, the domain is characterized as Follistatin-like 4.
+At position 355 to 378, the domain is characterized as Follistatin-like 5.
+At position 418 to 440, the domain is characterized as Follistatin-like 6.
+At position 479 to 501, the domain is characterized as Follistatin-like 7.
+At position 515 to 535, the domain is characterized as Follistatin-like 8.
+At position 571 to 593, the domain is characterized as Follistatin-like 9.
+At position 25 to 231, the domain is characterized as Velvet.
+At position 333 to 535, the domain is characterized as Protein kinase.
+At position 44 to 267, the domain is characterized as L-type lectin-like.
+At position 49 to 82, the domain is characterized as WW 1.
+At position 96 to 129, the domain is characterized as WW 2.
+At position 702 to 822, the domain is characterized as C2.
+At position 174 to 347, the domain is characterized as PCI.
+At position 916 to 992, the domain is characterized as RRM 3.
+At position 196 to 822, the domain is characterized as USP.
+At position 93 to 410, the domain is characterized as SET.
+At position 106 to 471, the domain is characterized as GS catalytic.
+At position 24 to 228, the domain is characterized as tr-type G.
+At position 1 to 52, the domain is characterized as J.
+At position 81 to 127, the domain is characterized as WAP; atypical.
+At position 8 to 44, the domain is characterized as WW.
+At position 107 to 302, the domain is characterized as ATP-grasp.
+At position 350 to 469, the domain is characterized as BRCT.
+At position 32 to 84, the domain is characterized as bHLH.
+At position 343 to 417, the domain is characterized as Ubiquitin-like.
+At position 23 to 164, the domain is characterized as SprT-like.
+At position 3 to 102, the domain is characterized as FAD-binding FR-type.
+At position 341 to 475, the domain is characterized as Thioredoxin.
+At position 390 to 498, the domain is characterized as BEN.
+At position 164 to 234, the domain is characterized as DRBM.
+At position 27 to 444, the domain is characterized as GH18.
+At position 98 to 273, the domain is characterized as Helicase ATP-binding.
+At position 298 to 450, the domain is characterized as Helicase C-terminal.
+At position 591 to 670, the domain is characterized as HRDC.
+At position 612 to 695, the domain is characterized as BRCT.
+At position 436 to 470, the domain is characterized as EF-hand 3.
+At position 471 to 506, the domain is characterized as EF-hand 4.
+At position 54 to 276, the domain is characterized as Radical SAM core.
+At position 40 to 118, the domain is characterized as Inhibitor I9.
+At position 125 to 602, the domain is characterized as Peptidase S8.
+At position 370 to 456, the domain is characterized as PA.
+At position 60 to 345, the domain is characterized as Protein kinase.
+At position 196 to 284, the domain is characterized as RCK C-terminal 1.
+At position 286 to 372, the domain is characterized as RCK C-terminal 2.
+At position 4 to 144, the domain is characterized as Flavodoxin-like.
+At position 251 to 472, the domain is characterized as Rab-GAP TBC.
+At position 205 to 804, the domain is characterized as RINT1/TIP20.
+At position 34 to 109, the domain is characterized as IGFBP N-terminal.
+At position 95 to 153, the domain is characterized as Kazal-like.
+At position 155 to 259, the domain is characterized as Ig-like C2-type.
+At position 25 to 148, the domain is characterized as NTR.
+At position 208 to 446, the domain is characterized as NR LBD.
+At position 277 to 422, the domain is characterized as SIS 1.
+At position 28 to 124, the domain is characterized as Glutaredoxin.
+At position 255 to 452, the domain is characterized as Hflx-type G.
+At position 311 to 360, the domain is characterized as Myb-like.
+At position 160 to 212, the domain is characterized as bHLH.
+At position 690 to 791, the domain is characterized as Guanylate kinase-like.
+At position 1631 to 1765, the domain is characterized as ZU5.
+At position 286 to 523, the domain is characterized as START.
+At position 54 to 149, the domain is characterized as Toprim.
+At position 364 to 792, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1261 to 1567, the domain is characterized as PKS/mFAS DH.
+At position 1622 to 1699, the domain is characterized as Carrier.
+At position 890 to 923, the domain is characterized as EGF-like.
+At position 932 to 1057, the domain is characterized as SEA.
+At position 17 to 447, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 928 to 1210, the domain is characterized as PKS/mFAS DH.
+At position 2430 to 2507, the domain is characterized as Carrier.
+At position 19 to 208, the domain is characterized as RNase H type-2.
+At position 7 to 131, the domain is characterized as VOC 1.
+At position 152 to 269, the domain is characterized as VOC 2.
+At position 32 to 193, the domain is characterized as N-acetyltransferase.
+At position 639 to 902, the domain is characterized as Protein kinase.
+At position 931 to 995, the domain is characterized as SAM.
+At position 445 to 768, the domain is characterized as Kinesin motor.
+At position 2 to 136, the domain is characterized as ADF-H.
+At position 526 to 632, the domain is characterized as PH.
+At position 714 to 837, the domain is characterized as Arf-GAP.
+At position 455 to 583, the domain is characterized as Guanylate cyclase.
+At position 27 to 209, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 121, the domain is characterized as NR LBD.
+At position 129 to 217, the domain is characterized as Ig-like C1-type.
+At position 24 to 98, the domain is characterized as S1-like.
+At position 50 to 109, the domain is characterized as Collagen-like.
+At position 645 to 708, the domain is characterized as bZIP.
+At position 242 to 501, the domain is characterized as Olfactomedin-like.
+At position 78 to 256, the domain is characterized as Rab-GAP TBC.
+At position 75 to 394, the domain is characterized as Protein kinase.
+At position 395 to 438, the domain is characterized as AGC-kinase C-terminal.
+At position 134 to 265, the domain is characterized as Fatty acid hydroxylase.
+At position 12 to 411, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 946 to 1256, the domain is characterized as PKS/mFAS DH.
+At position 2436 to 2513, the domain is characterized as Carrier.
+At position 94 to 309, the domain is characterized as ABC transmembrane type-1.
+At position 277 to 436, the domain is characterized as FCP1 homology.
+At position 122 to 262, the domain is characterized as SIS.
+At position 226 to 402, the domain is characterized as TrmE-type G.
+At position 336 to 367, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 362 to 391, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 398 to 514, the domain is characterized as Response regulatory.
+At position 564 to 618, the domain is characterized as TSP type-1 2.
+At position 622 to 686, the domain is characterized as TSP type-1 3.
+At position 688 to 736, the domain is characterized as TSP type-1 4.
+At position 737 to 795, the domain is characterized as TSP type-1 5.
+At position 797 to 851, the domain is characterized as TSP type-1 6.
+At position 853 to 908, the domain is characterized as TSP type-1 7.
+At position 912 to 950, the domain is characterized as PLAC.
+At position 121 to 188, the domain is characterized as PAS 1.
+At position 262 to 328, the domain is characterized as PAS 2.
+At position 337 to 380, the domain is characterized as PAC.
+At position 851 to 931, the domain is characterized as Carrier.
+At position 24 to 257, the domain is characterized as ABC transporter.
+At position 529 to 602, the domain is characterized as Tudor 1.
+At position 629 to 686, the domain is characterized as Tudor 2.
+At position 818 to 884, the domain is characterized as MBD.
+At position 946 to 1018, the domain is characterized as Pre-SET.
+At position 1021 to 1237, the domain is characterized as SET.
+At position 1246 to 1262, the domain is characterized as Post-SET.
+At position 71 to 117, the domain is characterized as F-box.
+At position 266 to 363, the domain is characterized as SWIRM.
+At position 268 to 461, the domain is characterized as B30.2/SPRY.
+At position 28 to 166, the domain is characterized as Thioredoxin.
+At position 178 to 349, the domain is characterized as Helicase ATP-binding.
+At position 392 to 596, the domain is characterized as Helicase C-terminal.
+At position 587 to 645, the domain is characterized as CBS 1.
+At position 125 to 219, the domain is characterized as RRM 1.
+At position 239 to 317, the domain is characterized as RRM 2.
+At position 521 to 723, the domain is characterized as Flavodoxin-like.
+At position 776 to 1021, the domain is characterized as FAD-binding FR-type.
+At position 482 to 587, the domain is characterized as Fibronectin type-III 3.
+At position 116 to 195, the domain is characterized as RRM 2.
+At position 237 to 309, the domain is characterized as RRM 3.
+At position 10 to 124, the domain is characterized as C2.
+At position 219 to 252, the domain is characterized as WW 1.
+At position 253 to 286, the domain is characterized as WW 2.
+At position 324 to 358, the domain is characterized as WW 3.
+At position 366 to 399, the domain is characterized as WW 4.
+At position 460 to 794, the domain is characterized as HECT.
+At position 32 to 76, the domain is characterized as CAP-Gly.
+At position 190 to 345, the domain is characterized as RNase NYN.
+At position 51 to 88, the domain is characterized as EF-hand 1.
+At position 10 to 193, the domain is characterized as HORMA.
+At position 10 to 288, the domain is characterized as AB hydrolase-1.
+At position 222 to 391, the domain is characterized as Hflx-type G.
+At position 85 to 157, the domain is characterized as Kringle.
+At position 166 to 267, the domain is characterized as SRCR 1.
+At position 273 to 373, the domain is characterized as SRCR 2.
+At position 386 to 487, the domain is characterized as SRCR 3.
+At position 517 to 760, the domain is characterized as Peptidase S1.
+At position 96 to 166, the domain is characterized as S1 motif 1.
+At position 184 to 248, the domain is characterized as S1 motif 2.
+At position 261 to 329, the domain is characterized as S1 motif 3.
+At position 170 to 272, the domain is characterized as AB hydrolase-1.
+At position 170 to 241, the domain is characterized as KRAB.
+At position 1 to 127, the domain is characterized as C-type lysozyme.
+At position 15 to 221, the domain is characterized as MARVEL.
+At position 359 to 413, the domain is characterized as FBD.
+At position 29 to 285, the domain is characterized as UmuC.
+At position 16 to 45, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 40 to 71, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 71 to 100, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 95 to 129, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 118 to 306, the domain is characterized as FAD-binding PCMH-type.
+At position 133 to 349, the domain is characterized as Histidine kinase.
+At position 87 to 194, the domain is characterized as Calponin-homology (CH) 1.
+At position 254 to 361, the domain is characterized as Calponin-homology (CH) 2.
+At position 599 to 687, the domain is characterized as BRCT.
+At position 1 to 31, the domain is characterized as SAND.
+At position 32 to 146, the domain is characterized as Plastocyanin-like 1.
+At position 157 to 301, the domain is characterized as Plastocyanin-like 2.
+At position 362 to 502, the domain is characterized as Plastocyanin-like 3.
+At position 7 to 385, the domain is characterized as ABC transporter.
+At position 41 to 254, the domain is characterized as Cupin type-1 1.
+At position 328 to 477, the domain is characterized as Cupin type-1 2.
+At position 76 to 236, the domain is characterized as TNase-like.
+At position 34 to 123, the domain is characterized as Link.
+At position 55 to 123, the domain is characterized as BON 1.
+At position 134 to 201, the domain is characterized as BON 2.
+At position 11 to 101, the domain is characterized as RH1.
+At position 240 to 316, the domain is characterized as RH2.
+At position 161 to 203, the domain is characterized as CCT.
+At position 154 to 187, the domain is characterized as CHCH.
+At position 28 to 79, the domain is characterized as Clip.
+At position 342 to 397, the domain is characterized as BRX 2.
+At position 1 to 581, the domain is characterized as ABC transporter 1.
+At position 594 to 909, the domain is characterized as ABC transporter 2.
+At position 1503 to 1814, the domain is characterized as ABC transporter 3.
+At position 34 to 257, the domain is characterized as Peptidase S1.
+At position 98 to 176, the domain is characterized as RRM.
+At position 228 to 244, the domain is characterized as UIM.
+At position 521 to 595, the domain is characterized as RH2.
+At position 23 to 59, the domain is characterized as CBM1.
+At position 1 to 60, the domain is characterized as TRAM.
+At position 607 to 648, the domain is characterized as JmjN.
+At position 671 to 779, the domain is characterized as ARID.
+At position 954 to 1118, the domain is characterized as JmjC.
+At position 96 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 78 to 113, the domain is characterized as EF-hand.
+At position 153 to 249, the domain is characterized as PH 1.
+At position 347 to 441, the domain is characterized as PH 2.
+At position 4 to 45, the domain is characterized as SpoVT-AbrB.
+At position 108 to 183, the domain is characterized as TFIIS N-terminal.
+At position 184 to 416, the domain is characterized as Radical SAM core.
+At position 419 to 487, the domain is characterized as TRAM.
+At position 175 to 257, the domain is characterized as RRM 1.
+At position 282 to 359, the domain is characterized as RRM 2.
+At position 389 to 479, the domain is characterized as RRM 3.
+At position 30 to 171, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 2 to 143, the domain is characterized as Tyrosine-protein phosphatase.
+At position 455 to 730, the domain is characterized as ZP.
+At position 97 to 272, the domain is characterized as Protein kinase.
+At position 196 to 231, the domain is characterized as EF-hand 1.
+At position 232 to 267, the domain is characterized as EF-hand 2.
+At position 347 to 462, the domain is characterized as PH.
+At position 585 to 612, the domain is characterized as PLD phosphodiesterase 1.
+At position 1036 to 1063, the domain is characterized as PLD phosphodiesterase 2.
+At position 735 to 836, the domain is characterized as PH.
+At position 101 to 222, the domain is characterized as MATH.
+At position 241 to 548, the domain is characterized as USP.
+At position 793 to 877, the domain is characterized as PB1.
+At position 83 to 774, the domain is characterized as Peptidase M13.
+At position 134 to 334, the domain is characterized as CheB-type methylesterase.
+At position 187 to 387, the domain is characterized as CN hydrolase.
+At position 439 to 642, the domain is characterized as EXS.
+At position 108 to 281, the domain is characterized as Helicase ATP-binding.
+At position 292 to 456, the domain is characterized as Helicase C-terminal.
+At position 353 to 616, the domain is characterized as ZP.
+At position 146 to 211, the domain is characterized as HTH luxR-type.
+At position 610 to 705, the domain is characterized as Fibronectin type-III 1.
+At position 813 to 902, the domain is characterized as Fibronectin type-III 3.
+At position 2384 to 2424, the domain is characterized as Fibronectin type-I 12.
+At position 396 to 588, the domain is characterized as PNPLA.
+At position 49 to 80, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 167 to 314, the domain is characterized as Cupin type-1.
+At position 429 to 545, the domain is characterized as LTD.
+At position 266 to 357, the domain is characterized as PDZ 1.
+At position 363 to 468, the domain is characterized as PDZ 2.
+At position 124 to 159, the domain is characterized as EF-hand 2.
+At position 309 to 537, the domain is characterized as Lon N-terminal.
+At position 536 to 645, the domain is characterized as CULT.
+At position 247 to 407, the domain is characterized as FAS1.
+At position 61 to 183, the domain is characterized as Cyclin N-terminal.
+At position 21 to 98, the domain is characterized as PDZ.
+At position 223 to 390, the domain is characterized as PID.
+At position 266 to 352, the domain is characterized as Toprim.
+At position 595 to 658, the domain is characterized as CBS 1.
+At position 703 to 768, the domain is characterized as CBS 2.
+At position 14 to 66, the domain is characterized as HTH myb-type 1.
+At position 67 to 121, the domain is characterized as HTH myb-type 2.
+At position 95 to 324, the domain is characterized as Radical SAM core.
+At position 129 to 558, the domain is characterized as Urease.
+At position 107 to 283, the domain is characterized as FBA.
+At position 236 to 326, the domain is characterized as BRCT.
+At position 564 to 709, the domain is characterized as JmjC.
+At position 399 to 477, the domain is characterized as RRM 3.
+At position 19 to 110, the domain is characterized as Ig-like.
+At position 192 to 266, the domain is characterized as POU-specific.
+At position 1006 to 1166, the domain is characterized as JmjC.
+At position 53 to 91, the domain is characterized as EGF-like 1.
+At position 93 to 209, the domain is characterized as CUB.
+At position 207 to 245, the domain is characterized as EGF-like 2.
+At position 614 to 657, the domain is characterized as PSI 1.
+At position 666 to 709, the domain is characterized as PSI 2.
+At position 715 to 760, the domain is characterized as PSI 3.
+At position 755 to 873, the domain is characterized as C-type lectin.
+At position 889 to 939, the domain is characterized as PSI 4.
+At position 942 to 1012, the domain is characterized as PSI 5.
+At position 1014 to 1059, the domain is characterized as Laminin EGF-like 1.
+At position 1060 to 1108, the domain is characterized as Laminin EGF-like 2.
+At position 396 to 525, the domain is characterized as Ricin B-type lectin.
+At position 35 to 345, the domain is characterized as Rab-GAP TBC.
+At position 31 to 221, the domain is characterized as BPL/LPL catalytic.
+At position 39 to 173, the domain is characterized as MPN.
+At position 597 to 656, the domain is characterized as KH.
+At position 668 to 737, the domain is characterized as S1 motif.
+At position 35 to 140, the domain is characterized as PH 1.
+At position 165 to 257, the domain is characterized as PH 2.
+At position 950 to 1162, the domain is characterized as Rap-GAP.
+At position 280 to 367, the domain is characterized as NTF2; truncated.
+At position 65 to 130, the domain is characterized as NAC-A/B.
+At position 23 to 190, the domain is characterized as Era-type G.
+At position 48 to 212, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 231 to 278, the domain is characterized as EGF-like 1.
+At position 279 to 321, the domain is characterized as EGF-like 2; calcium-binding.
+At position 408 to 691, the domain is characterized as Protein kinase.
+At position 43 to 171, the domain is characterized as RNase III.
+At position 1 to 109, the domain is characterized as Fibronectin type-III 1.
+At position 110 to 210, the domain is characterized as Fibronectin type-III 2.
+At position 21 to 129, the domain is characterized as Chorein N-terminal.
+At position 102 to 197, the domain is characterized as TAFH.
+At position 148 to 301, the domain is characterized as DDE Tnp4.
+At position 340 to 366, the domain is characterized as Death; truncated.
+At position 39 to 402, the domain is characterized as GH18.
+At position 27 to 280, the domain is characterized as Protein kinase.
+At position 97 to 173, the domain is characterized as Smr.
+At position 34 to 812, the domain is characterized as Vitellogenin.
+At position 1449 to 1638, the domain is characterized as VWFD.
+At position 34 to 110, the domain is characterized as H15.
+At position 54 to 158, the domain is characterized as Cadherin 1.
+At position 159 to 267, the domain is characterized as Cadherin 2.
+At position 268 to 382, the domain is characterized as Cadherin 3.
+At position 383 to 487, the domain is characterized as Cadherin 4.
+At position 487 to 605, the domain is characterized as Cadherin 5.
+At position 179 to 228, the domain is characterized as KH.
+At position 389 to 473, the domain is characterized as RRM 2.
+At position 49 to 101, the domain is characterized as bHLH.
+At position 150 to 268, the domain is characterized as FAD-binding FR-type.
+At position 37 to 156, the domain is characterized as RGS.
+At position 43 to 223, the domain is characterized as Macro.
+At position 333 to 481, the domain is characterized as CRAL-TRIO.
+At position 38 to 107, the domain is characterized as BIG2 1.
+At position 133 to 190, the domain is characterized as BIG2 2.
+At position 8 to 127, the domain is characterized as PH.
+At position 397 to 453, the domain is characterized as SOCS box.
+At position 42 to 385, the domain is characterized as G-alpha.
+At position 31 to 330, the domain is characterized as Protein kinase.
+At position 358 to 410, the domain is characterized as bHLH.
+At position 63 to 287, the domain is characterized as SET.
+At position 163 to 260, the domain is characterized as Fibronectin type-III.
+At position 238 to 407, the domain is characterized as tr-type G.
+At position 1 to 19, the domain is characterized as Gla.
+At position 31 to 209, the domain is characterized as Eph LBD.
+At position 331 to 446, the domain is characterized as Fibronectin type-III 1.
+At position 447 to 540, the domain is characterized as Fibronectin type-III 2.
+At position 628 to 891, the domain is characterized as Protein kinase.
+At position 920 to 984, the domain is characterized as SAM.
+At position 232 to 354, the domain is characterized as SEA 1.
+At position 571 to 684, the domain is characterized as SEA 2.
+At position 95 to 189, the domain is characterized as Ig-like V-type.
+At position 48 to 253, the domain is characterized as BPL/LPL catalytic.
+At position 23 to 110, the domain is characterized as UPAR/Ly6.
+At position 122 to 211, the domain is characterized as Ricin B-type lectin.
+At position 65 to 132, the domain is characterized as BTB.
+At position 167 to 269, the domain is characterized as BACK.
+At position 60 to 197, the domain is characterized as MPN.
+At position 28 to 279, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 232 to 274, the domain is characterized as CAP-Gly 2.
+At position 27 to 90, the domain is characterized as KRAB-related.
+At position 248 to 362, the domain is characterized as SET.
+At position 201 to 456, the domain is characterized as Protein kinase.
+At position 457 to 512, the domain is characterized as AGC-kinase C-terminal.
+At position 87 to 242, the domain is characterized as Helicase ATP-binding.
+At position 300 to 522, the domain is characterized as Helicase C-terminal.
+At position 542 to 699, the domain is characterized as Toprim.
+At position 1338 to 1922, the domain is characterized as FAT.
+At position 2097 to 2421, the domain is characterized as PI3K/PI4K catalytic.
+At position 2442 to 2474, the domain is characterized as FATC.
+At position 30 to 199, the domain is characterized as EngB-type G.
+At position 189 to 375, the domain is characterized as Glutamine amidotransferase type-1.
+At position 79 to 369, the domain is characterized as Radical SAM core.
+At position 393 to 544, the domain is characterized as N-acetyltransferase.
+At position 51 to 279, the domain is characterized as Radical SAM core.
+At position 494 to 753, the domain is characterized as ATP-grasp.
+At position 436 to 605, the domain is characterized as tr-type G.
+At position 569 to 656, the domain is characterized as Carrier.
+At position 160 to 357, the domain is characterized as CheB-type methylesterase.
+At position 200 to 550, the domain is characterized as Protein kinase.
+At position 49 to 229, the domain is characterized as BPL/LPL catalytic.
+At position 108 to 221, the domain is characterized as SET.
+At position 568 to 836, the domain is characterized as Protein kinase.
+At position 1 to 175, the domain is characterized as CYTH.
+At position 67 to 176, the domain is characterized as PX.
+At position 185 to 485, the domain is characterized as Protein kinase.
+At position 1 to 155, the domain is characterized as Brix.
+At position 81 to 462, the domain is characterized as PRONE.
+At position 98 to 413, the domain is characterized as IF rod.
+At position 233 to 407, the domain is characterized as PCI.
+At position 805 to 947, the domain is characterized as JmjC.
+At position 193 to 440, the domain is characterized as Radical SAM core.
+At position 435 to 499, the domain is characterized as TRAM.
+At position 168 to 348, the domain is characterized as Glutamine amidotransferase type-1.
+At position 190 to 252, the domain is characterized as LRRCT.
+At position 35 to 108, the domain is characterized as H15.
+At position 159 to 209, the domain is characterized as bHLH.
+At position 219 to 389, the domain is characterized as Helicase ATP-binding.
+At position 479 to 649, the domain is characterized as Helicase C-terminal.
+At position 17 to 242, the domain is characterized as Radical SAM core.
+At position 20 to 102, the domain is characterized as GST N-terminal.
+At position 107 to 230, the domain is characterized as GST C-terminal.
+At position 69 to 174, the domain is characterized as PRD 1.
+At position 175 to 278, the domain is characterized as PRD 2.
+At position 128 to 279, the domain is characterized as SIS.
+At position 448 to 570, the domain is characterized as HD.
+At position 687 to 772, the domain is characterized as ACT 1.
+At position 796 to 871, the domain is characterized as ACT 2.
+At position 93 to 172, the domain is characterized as RRM 1.
+At position 346 to 420, the domain is characterized as RRM 2.
+At position 49 to 93, the domain is characterized as Fibronectin type-II 1.
+At position 94 to 140, the domain is characterized as Fibronectin type-II 2.
+At position 1 to 150, the domain is characterized as N-acetyltransferase 1.
+At position 309 to 592, the domain is characterized as ABC transmembrane type-1 1.
+At position 627 to 851, the domain is characterized as ABC transporter 1.
+At position 942 to 1223, the domain is characterized as ABC transmembrane type-1 2.
+At position 1260 to 1494, the domain is characterized as ABC transporter 2.
+At position 483 to 618, the domain is characterized as Ricin B-type lectin.
+At position 56 to 167, the domain is characterized as TBDR plug.
+At position 178 to 676, the domain is characterized as TBDR beta-barrel.
+At position 295 to 381, the domain is characterized as IPT/TIG 1.
+At position 560 to 638, the domain is characterized as IPT/TIG 2.
+At position 642 to 725, the domain is characterized as IPT/TIG 3.
+At position 432 to 586, the domain is characterized as Helicase C-terminal.
+At position 430 to 590, the domain is characterized as TIR.
+At position 2 to 169, the domain is characterized as EngA-type G 1.
+At position 31 to 101, the domain is characterized as BTB.
+At position 507 to 749, the domain is characterized as ABC transporter.
+At position 859 to 1059, the domain is characterized as ABC transmembrane type-2.
+At position 414 to 551, the domain is characterized as DAGKc.
+At position 21 to 81, the domain is characterized as v-SNARE coiled-coil homology.
+At position 24 to 130, the domain is characterized as Calponin-homology (CH).
+At position 80 to 239, the domain is characterized as Thioredoxin.
+At position 1411 to 1476, the domain is characterized as NAC-A/B.
+At position 1666 to 1824, the domain is characterized as RNase III 2.
+At position 1849 to 1914, the domain is characterized as DRBM.
+At position 103 to 263, the domain is characterized as F5/8 type C.
+At position 648 to 916, the domain is characterized as Autotransporter.
+At position 31 to 273, the domain is characterized as ABC transporter 1.
+At position 751 to 979, the domain is characterized as ABC transporter 2.
+At position 156 to 464, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 614 to 692, the domain is characterized as BRCT.
+At position 82 to 479, the domain is characterized as TTL.
+At position 778 to 842, the domain is characterized as SAM.
+At position 1 to 46, the domain is characterized as Gla.
+At position 104 to 155, the domain is characterized as bHLH.
+At position 207 to 371, the domain is characterized as UBC core.
+At position 112 to 282, the domain is characterized as Exonuclease.
+At position 22 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 160 to 304, the domain is characterized as Plastocyanin-like 2.
+At position 373 to 496, the domain is characterized as Plastocyanin-like 3.
+At position 58 to 479, the domain is characterized as Kinesin motor.
+At position 193 to 447, the domain is characterized as Radical SAM core.
+At position 35 to 103, the domain is characterized as J.
+At position 354 to 406, the domain is characterized as FBD.
+At position 188 to 596, the domain is characterized as PUM-HD.
+At position 19 to 135, the domain is characterized as NTF2.
+At position 1 to 78, the domain is characterized as VOC.
+At position 488 to 566, the domain is characterized as Chromo 1.
+At position 612 to 673, the domain is characterized as Chromo 2.
+At position 742 to 924, the domain is characterized as Helicase ATP-binding.
+At position 1056 to 1218, the domain is characterized as Helicase C-terminal.
+At position 212 to 414, the domain is characterized as Peptidase M12B.
+At position 422 to 508, the domain is characterized as Disintegrin.
+At position 654 to 686, the domain is characterized as EGF-like.
+At position 374 to 490, the domain is characterized as PLAT.
+At position 491 to 1066, the domain is characterized as Lipoxygenase.
+At position 335 to 467, the domain is characterized as Nudix hydrolase.
+At position 27 to 77, the domain is characterized as PSI.
+At position 139 to 377, the domain is characterized as VWFA.
+At position 584 to 714, the domain is characterized as B12-binding.
+At position 897 to 1046, the domain is characterized as HNH Cas9-type.
+At position 67 to 182, the domain is characterized as THUMP.
+At position 56 to 240, the domain is characterized as tr-type G.
+At position 391 to 682, the domain is characterized as GH16.
+At position 1 to 416, the domain is characterized as KAP NTPase.
+At position 28 to 89, the domain is characterized as TRAM 1.
+At position 104 to 169, the domain is characterized as TRAM 2.
+At position 21 to 64, the domain is characterized as P-type 1.
+At position 72 to 115, the domain is characterized as P-type 2.
+At position 298 to 343, the domain is characterized as P-type 3.
+At position 351 to 394, the domain is characterized as P-type 4.
+At position 523 to 596, the domain is characterized as Histone-fold.
+At position 27 to 77, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 118 to 168, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 2 to 156, the domain is characterized as Toprim.
+At position 6 to 210, the domain is characterized as AIG1-type G.
+At position 390 to 823, the domain is characterized as FH2.
+At position 224 to 554, the domain is characterized as USP.
+At position 217 to 657, the domain is characterized as Myotubularin phosphatase.
+At position 242 to 377, the domain is characterized as PAS 1.
+At position 395 to 501, the domain is characterized as PAS 2.
+At position 73 to 124, the domain is characterized as HTH myb-type 1.
+At position 125 to 180, the domain is characterized as HTH myb-type 2.
+At position 181 to 231, the domain is characterized as HTH myb-type 3.
+At position 23 to 312, the domain is characterized as ABC transmembrane type-1 1.
+At position 347 to 583, the domain is characterized as ABC transporter 1.
+At position 657 to 945, the domain is characterized as ABC transmembrane type-1 2.
+At position 980 to 1218, the domain is characterized as ABC transporter 2.
+At position 493 to 597, the domain is characterized as PTS EIIA type-1.
+At position 218 to 373, the domain is characterized as TrmE-type G.
+At position 444 to 643, the domain is characterized as Helicase ATP-binding.
+At position 654 to 815, the domain is characterized as Helicase C-terminal.
+At position 67 to 219, the domain is characterized as Cupin type-1.
+At position 40 to 267, the domain is characterized as ABC transporter.
+At position 22 to 86, the domain is characterized as FHA.
+At position 137 to 217, the domain is characterized as VPS37 C-terminal.
+At position 585 to 615, the domain is characterized as PLD phosphodiesterase.
+At position 22 to 129, the domain is characterized as Ig-like C2-type 1.
+At position 149 to 268, the domain is characterized as Ig-like C2-type 2.
+At position 426 to 633, the domain is characterized as MCM.
+At position 98 to 221, the domain is characterized as MPN.
+At position 408 to 502, the domain is characterized as Fibronectin type-III.
+At position 652 to 848, the domain is characterized as FtsK 1.
+At position 984 to 1168, the domain is characterized as FtsK 2.
+At position 1267 to 1444, the domain is characterized as FtsK 3.
+At position 867 to 955, the domain is characterized as PDZ 2.
+At position 1005 to 1094, the domain is characterized as PDZ 3.
+At position 1101 to 1193, the domain is characterized as PDZ 4.
+At position 542 to 624, the domain is characterized as PABC.
+At position 15 to 344, the domain is characterized as Protein kinase.
+At position 24 to 101, the domain is characterized as EMI.
+At position 95 to 130, the domain is characterized as EGF-like 1.
+At position 143 to 173, the domain is characterized as EGF-like 2.
+At position 181 to 216, the domain is characterized as EGF-like 3.
+At position 224 to 259, the domain is characterized as EGF-like 4.
+At position 267 to 302, the domain is characterized as EGF-like 5.
+At position 310 to 345, the domain is characterized as EGF-like 6.
+At position 399 to 434, the domain is characterized as EGF-like 7.
+At position 442 to 477, the domain is characterized as EGF-like 8.
+At position 490 to 520, the domain is characterized as EGF-like 9.
+At position 571 to 606, the domain is characterized as EGF-like 10.
+At position 659 to 694, the domain is characterized as EGF-like 11.
+At position 707 to 737, the domain is characterized as EGF-like 12.
+At position 750 to 780, the domain is characterized as EGF-like 13.
+At position 788 to 823, the domain is characterized as EGF-like 14.
+At position 63 to 233, the domain is characterized as PCI.
+At position 145 to 687, the domain is characterized as USP.
+At position 689 to 782, the domain is characterized as DUSP 1.
+At position 791 to 894, the domain is characterized as DUSP 2.
+At position 297 to 552, the domain is characterized as Clu.
+At position 264 to 346, the domain is characterized as Toprim.
+At position 143 to 343, the domain is characterized as Sigma-54 factor interaction.
+At position 170 to 238, the domain is characterized as Histone-fold.
+At position 33 to 191, the domain is characterized as Thioredoxin.
+At position 89 to 257, the domain is characterized as TNase-like.
+At position 14 to 89, the domain is characterized as Carrier.
+At position 27 to 96, the domain is characterized as S1 motif 1.
+At position 114 to 178, the domain is characterized as S1 motif 2.
+At position 289 to 348, the domain is characterized as SH3 1.
+At position 351 to 408, the domain is characterized as SH3 2.
+At position 40 to 268, the domain is characterized as GB1/RHD3-type G.
+At position 232 to 291, the domain is characterized as SH3 1.
+At position 261 to 421, the domain is characterized as Helicase C-terminal.
+At position 70 to 412, the domain is characterized as Kinesin motor.
+At position 182 to 211, the domain is characterized as CBM10.
+At position 101 to 178, the domain is characterized as RRM.
+At position 870 to 1048, the domain is characterized as Exonuclease.
+At position 18 to 244, the domain is characterized as Chitin-binding type-4.
+At position 272 to 378, the domain is characterized as CBM20.
+At position 621 to 700, the domain is characterized as BRCT.
+At position 8 to 328, the domain is characterized as Hcy-binding.
+At position 359 to 607, the domain is characterized as Pterin-binding.
+At position 303 to 513, the domain is characterized as NEL.
+At position 185 to 380, the domain is characterized as CP-type G.
+At position 2 to 47, the domain is characterized as ATP-cone.
+At position 335 to 505, the domain is characterized as tr-type G.
+At position 7 to 318, the domain is characterized as Helicase ATP-binding.
+At position 368 to 578, the domain is characterized as TRUD.
+At position 338 to 508, the domain is characterized as tr-type G.
+At position 59 to 240, the domain is characterized as Macro.
+At position 54 to 129, the domain is characterized as Ubiquitin-like.
+At position 135 to 214, the domain is characterized as UPAR/Ly6.
+At position 28 to 109, the domain is characterized as Inhibitor I9.
+At position 114 to 591, the domain is characterized as Peptidase S8.
+At position 357 to 442, the domain is characterized as PA.
+At position 190 to 471, the domain is characterized as NR LBD.
+At position 139 to 436, the domain is characterized as Deacetylase sirtuin-type.
+At position 53 to 104, the domain is characterized as TSP type-1.
+At position 14 to 176, the domain is characterized as N-acetyltransferase.
+At position 21 to 265, the domain is characterized as ABC transporter.
+At position 27 to 303, the domain is characterized as Protein kinase.
+At position 51 to 334, the domain is characterized as AB hydrolase-1.
+At position 5 to 77, the domain is characterized as BTB.
+At position 130 to 443, the domain is characterized as IF rod.
+At position 42 to 460, the domain is characterized as uDENN FNIP1/2-type.
+At position 468 to 1040, the domain is characterized as cDENN FNIP1/2-type.
+At position 1050 to 1105, the domain is characterized as dDENN FNIP1/2-type.
+At position 31 to 115, the domain is characterized as Ig-like.
+At position 186 to 424, the domain is characterized as Sigma-54 factor interaction.
+At position 584 to 662, the domain is characterized as BRCT.
+At position 21 to 281, the domain is characterized as Alpha-carbonic anhydrase.
+At position 8 to 93, the domain is characterized as Disintegrin.
+At position 144 to 311, the domain is characterized as Helicase ATP-binding.
+At position 486 to 681, the domain is characterized as Helicase C-terminal.
+At position 45 to 629, the domain is characterized as Peptidase M2 1.
+At position 648 to 1227, the domain is characterized as Peptidase M2 2.
+At position 1230 to 1282, the domain is characterized as PAP-associated 2.
+At position 561 to 608, the domain is characterized as G-patch.
+At position 106 to 234, the domain is characterized as Runt.
+At position 202 to 287, the domain is characterized as Ig-like C1-type.
+At position 625 to 837, the domain is characterized as Histidine kinase.
+At position 781 to 863, the domain is characterized as BRCT.
+At position 1 to 53, the domain is characterized as Ubiquitin-like 1.
+At position 185 to 263, the domain is characterized as Ubiquitin-like 2.
+At position 287 to 343, the domain is characterized as AFP-like.
+At position 46 to 132, the domain is characterized as Ig-like V-type.
+At position 133 to 221, the domain is characterized as Ig-like C2-type.
+At position 49 to 100, the domain is characterized as CTLH.
+At position 464 to 651, the domain is characterized as DH.
+At position 842 to 1137, the domain is characterized as CNH.
+At position 23 to 469, the domain is characterized as GBD/FH3.
+At position 616 to 1007, the domain is characterized as FH2.
+At position 1040 to 1079, the domain is characterized as DAD.
+At position 5 to 156, the domain is characterized as UBC core.
+At position 16 to 87, the domain is characterized as S1-like.
+At position 1 to 115, the domain is characterized as CBM20.
+At position 115 to 287, the domain is characterized as JmjC.
+At position 51 to 93, the domain is characterized as SMB 1.
+At position 139 to 372, the domain is characterized as Radical SAM core.
+At position 138 to 201, the domain is characterized as bZIP.
+At position 267 to 357, the domain is characterized as Ig-like 1.
+At position 432 to 528, the domain is characterized as Ig-like 2.
+At position 941 to 1025, the domain is characterized as Ig-like 3.
+At position 1068 to 1157, the domain is characterized as Ig-like 4.
+At position 1167 to 1257, the domain is characterized as Ig-like 5.
+At position 267 to 573, the domain is characterized as MYST-type HAT.
+At position 143 to 452, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 74 to 179, the domain is characterized as FAD-binding FR-type.
+At position 142 to 216, the domain is characterized as RRM 2.
+At position 269 to 289, the domain is characterized as IQ.
+At position 341 to 389, the domain is characterized as Fibronectin type-II 3.
+At position 195 to 390, the domain is characterized as Glutamine amidotransferase type-1.
+At position 161 to 223, the domain is characterized as t-SNARE coiled-coil homology.
+At position 9 to 418, the domain is characterized as Helicase ATP-binding.
+At position 14 to 183, the domain is characterized as FAD-binding PCMH-type.
+At position 285 to 517, the domain is characterized as Protein kinase.
+At position 334 to 467, the domain is characterized as RanBD1.
+At position 84 to 365, the domain is characterized as Protein kinase.
+At position 15 to 349, the domain is characterized as Kinesin motor.
+At position 251 to 331, the domain is characterized as Toprim.
+At position 1349 to 1483, the domain is characterized as CKK.
+At position 542 to 656, the domain is characterized as SMC hinge.
+At position 54 to 369, the domain is characterized as FERM.
+At position 1 to 129, the domain is characterized as Pyrin.
+At position 194 to 510, the domain is characterized as NACHT.
+At position 354 to 517, the domain is characterized as Cupin type-1 2.
+At position 262 to 282, the domain is characterized as ELK.
+At position 106 to 184, the domain is characterized as PRC barrel.
+At position 38 to 231, the domain is characterized as Peptidase M12A.
+At position 225 to 264, the domain is characterized as EGF-like.
+At position 10 to 112, the domain is characterized as LOB.
+At position 16 to 178, the domain is characterized as PPIase cyclophilin-type.
+At position 153 to 543, the domain is characterized as PPM-type phosphatase.
+At position 19 to 149, the domain is characterized as VHS.
+At position 168 to 187, the domain is characterized as UIM.
+At position 220 to 280, the domain is characterized as SH3.
+At position 99 to 207, the domain is characterized as tRNA-binding.
+At position 135 to 153, the domain is characterized as EF-hand 3.
+At position 45 to 159, the domain is characterized as Expansin-like EG45.
+At position 10 to 139, the domain is characterized as ADF-H.
+At position 11 to 53, the domain is characterized as SpoVT-AbrB 1.
+At position 158 to 217, the domain is characterized as OVATE.
+At position 220 to 679, the domain is characterized as Trm1 methyltransferase.
+At position 27 to 129, the domain is characterized as Gnk2-homologous 1.
+At position 292 to 525, the domain is characterized as Glutamine amidotransferase type-1.
+At position 199 to 358, the domain is characterized as C2 tensin-type.
+At position 974 to 1372, the domain is characterized as FH2.
+At position 20 to 137, the domain is characterized as Rhodanese 1.
+At position 177 to 299, the domain is characterized as Rhodanese 2.
+At position 483 to 622, the domain is characterized as Flavodoxin-like.
+At position 660 to 892, the domain is characterized as FAD-binding FR-type.
+At position 28 to 287, the domain is characterized as ABC transporter 1.
+At position 679 to 941, the domain is characterized as ABC transporter 2.
+At position 115 to 294, the domain is characterized as FAD-binding PCMH-type.
+At position 112 to 425, the domain is characterized as AB hydrolase-1.
+At position 232 to 350, the domain is characterized as C2.
+At position 781 to 1040, the domain is characterized as Protein kinase.
+At position 1041 to 1106, the domain is characterized as AGC-kinase C-terminal.
+At position 462 to 722, the domain is characterized as Protein kinase.
+At position 285 to 395, the domain is characterized as OCEL.
+At position 4 to 46, the domain is characterized as CHCH.
+At position 29 to 92, the domain is characterized as SLH.
+At position 25 to 101, the domain is characterized as UPAR/Ly6.
+At position 339 to 422, the domain is characterized as Death.
+At position 59 to 202, the domain is characterized as Cupin type-1.
+At position 259 to 399, the domain is characterized as MPN.
+At position 28 to 69, the domain is characterized as WAP 1.
+At position 72 to 122, the domain is characterized as WAP 2.
+At position 44 to 148, the domain is characterized as Cadherin 1.
+At position 149 to 256, the domain is characterized as Cadherin 2.
+At position 257 to 370, the domain is characterized as Cadherin 3.
+At position 371 to 470, the domain is characterized as Cadherin 4.
+At position 470 to 581, the domain is characterized as Cadherin 5.
+At position 29 to 224, the domain is characterized as BPL/LPL catalytic.
+At position 7 to 352, the domain is characterized as DhaK.
+At position 30 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 283 to 458, the domain is characterized as Helicase ATP-binding.
+At position 487 to 636, the domain is characterized as Helicase C-terminal.
+At position 52 to 333, the domain is characterized as Protein kinase.
+At position 288 to 493, the domain is characterized as Peptidase M12B.
+At position 494 to 583, the domain is characterized as Disintegrin.
+At position 584 to 639, the domain is characterized as TSP type-1 1.
+At position 872 to 920, the domain is characterized as TSP type-1 2.
+At position 925 to 985, the domain is characterized as TSP type-1 3.
+At position 986 to 1046, the domain is characterized as TSP type-1 4.
+At position 1049 to 1113, the domain is characterized as TSP type-1 5.
+At position 1125 to 1179, the domain is characterized as TSP type-1 6.
+At position 1 to 42, the domain is characterized as H15.
+At position 139 to 386, the domain is characterized as Radical SAM core.
+At position 389 to 467, the domain is characterized as TRAM.
+At position 23 to 141, the domain is characterized as EamA 1.
+At position 197 to 395, the domain is characterized as Histidine kinase.
+At position 452 to 537, the domain is characterized as PDZ 3.
+At position 122 to 481, the domain is characterized as PTS EIIC type-1.
+At position 229 to 445, the domain is characterized as Rap-GAP.
+At position 98 to 265, the domain is characterized as TNase-like.
+At position 648 to 879, the domain is characterized as NR LBD.
+At position 199 to 249, the domain is characterized as bHLH.
+At position 30 to 329, the domain is characterized as Calpain catalytic.
+At position 534 to 569, the domain is characterized as EF-hand 1.
+At position 632 to 665, the domain is characterized as EF-hand 2.
+At position 746 to 924, the domain is characterized as Helicase ATP-binding.
+At position 1003 to 1184, the domain is characterized as Helicase C-terminal.
+At position 213 to 393, the domain is characterized as GAF.
+At position 604 to 674, the domain is characterized as PAS 1.
+At position 737 to 808, the domain is characterized as PAS 2.
+At position 889 to 1111, the domain is characterized as Histidine kinase.
+At position 266 to 412, the domain is characterized as MATH.
+At position 48 to 113, the domain is characterized as J.
+At position 215 to 469, the domain is characterized as NR LBD.
+At position 19 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 399 to 693, the domain is characterized as Clu.
+At position 21 to 97, the domain is characterized as Saposin B-type.
+At position 25 to 348, the domain is characterized as Transferrin-like 1.
+At position 360 to 689, the domain is characterized as Transferrin-like 2.
+At position 256 to 459, the domain is characterized as SEC7.
+At position 509 to 622, the domain is characterized as PH.
+At position 88 to 217, the domain is characterized as PLAT.
+At position 220 to 936, the domain is characterized as Lipoxygenase.
+At position 734 to 763, the domain is characterized as IQ.
+At position 115 to 318, the domain is characterized as BPL/LPL catalytic.
+At position 46 to 132, the domain is characterized as PNT.
+At position 361 to 572, the domain is characterized as TLDc.
+At position 220 to 255, the domain is characterized as EF-hand 2.
+At position 430 to 564, the domain is characterized as DAGKc.
+At position 330 to 683, the domain is characterized as Kinesin motor.
+At position 276 to 335, the domain is characterized as PAP-associated.
+At position 118 to 498, the domain is characterized as Protein kinase.
+At position 219 to 289, the domain is characterized as KRAB.
+At position 1 to 56, the domain is characterized as SH3 1.
+At position 58 to 149, the domain is characterized as SH2.
+At position 1 to 90, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 215 to 404, the domain is characterized as FAD-binding PCMH-type.
+At position 31 to 75, the domain is characterized as LysM 1.
+At position 132 to 179, the domain is characterized as LysM 2.
+At position 320 to 465, the domain is characterized as Exonuclease.
+At position 906 to 1059, the domain is characterized as RNase III 1.
+At position 290 to 421, the domain is characterized as PH.
+At position 467 to 604, the domain is characterized as Arf-GAP.
+At position 192 to 459, the domain is characterized as SF4 helicase.
+At position 27 to 68, the domain is characterized as EGF-like 1.
+At position 69 to 119, the domain is characterized as EGF-like 2; calcium-binding.
+At position 165 to 213, the domain is characterized as EGF-like 3; calcium-binding.
+At position 214 to 261, the domain is characterized as EGF-like 4; calcium-binding.
+At position 479 to 524, the domain is characterized as GPS.
+At position 33 to 420, the domain is characterized as Alpha-carbonic anhydrase.
+At position 188 to 277, the domain is characterized as EH 1.
+At position 440 to 529, the domain is characterized as EH 2.
+At position 473 to 508, the domain is characterized as EF-hand 2.
+At position 211 to 409, the domain is characterized as Peptidase M12B.
+At position 56 to 129, the domain is characterized as GST N-terminal.
+At position 130 to 258, the domain is characterized as GST C-terminal.
+At position 203 to 237, the domain is characterized as EF-hand 3.
+At position 538 to 654, the domain is characterized as PI-PLC Y-box.
+At position 654 to 781, the domain is characterized as C2.
+At position 4 to 74, the domain is characterized as HTH merR-type.
+At position 42 to 348, the domain is characterized as GH18.
+At position 50 to 164, the domain is characterized as Ferric oxidoreductase.
+At position 29 to 134, the domain is characterized as Gnk2-homologous.
+At position 1 to 108, the domain is characterized as B30.2/SPRY.
+At position 597 to 808, the domain is characterized as MRH.
+At position 4 to 135, the domain is characterized as ADF-H.
+At position 545 to 564, the domain is characterized as WH2.
+At position 308 to 374, the domain is characterized as PWWP.
+At position 208 to 265, the domain is characterized as CVC.
+At position 173 to 248, the domain is characterized as Toprim.
+At position 416 to 478, the domain is characterized as t-SNARE coiled-coil homology.
+At position 13 to 191, the domain is characterized as Guanylate kinase-like.
+At position 571 to 839, the domain is characterized as Protein kinase.
+At position 914 to 1044, the domain is characterized as Guanylate cyclase.
+At position 309 to 468, the domain is characterized as PPIase cyclophilin-type.
+At position 164 to 260, the domain is characterized as CRM 1.
+At position 376 to 473, the domain is characterized as CRM 2.
+At position 577 to 677, the domain is characterized as CRM 3.
+At position 873 to 972, the domain is characterized as CRM 4.
+At position 28 to 151, the domain is characterized as UPAR/Ly6.
+At position 30 to 148, the domain is characterized as AB hydrolase-1.
+At position 50 to 175, the domain is characterized as PLAT.
+At position 178 to 865, the domain is characterized as Lipoxygenase.
+At position 71 to 132, the domain is characterized as SH3.
+At position 138 to 237, the domain is characterized as SH2.
+At position 262 to 521, the domain is characterized as Protein kinase.
+At position 159 to 234, the domain is characterized as H15 1.
+At position 487 to 761, the domain is characterized as Protein kinase.
+At position 42 to 141, the domain is characterized as Ig-like C2-type.
+At position 118 to 208, the domain is characterized as RRM.
+At position 88 to 253, the domain is characterized as CRAL-TRIO.
+At position 192 to 365, the domain is characterized as EngA-type G 2.
+At position 366 to 450, the domain is characterized as KH-like.
+At position 21 to 183, the domain is characterized as FAD-binding PCMH-type.
+At position 84 to 774, the domain is characterized as Peptidase M13.
+At position 67 to 307, the domain is characterized as DCUN1.
+At position 159 to 345, the domain is characterized as CheB-type methylesterase.
+At position 216 to 379, the domain is characterized as JmjC.
+At position 2 to 78, the domain is characterized as WGR.
+At position 573 to 665, the domain is characterized as HTH La-type RNA-binding.
+At position 101 to 190, the domain is characterized as PDZ.
+At position 45 to 139, the domain is characterized as Fibronectin type-III.
+At position 282 to 536, the domain is characterized as Peptidase M66.
+At position 174 to 364, the domain is characterized as CheB-type methylesterase.
+At position 2 to 79, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 90 to 144, the domain is characterized as HTH cro/C1-type.
+At position 1 to 114, the domain is characterized as Response regulatory.
+At position 1 to 133, the domain is characterized as Calponin-homology (CH).
+At position 184 to 243, the domain is characterized as SH3.
+At position 271 to 451, the domain is characterized as DH.
+At position 473 to 578, the domain is characterized as PH.
+At position 44 to 124, the domain is characterized as POTRA.
+At position 25 to 125, the domain is characterized as Ig-like C2-type 1.
+At position 154 to 247, the domain is characterized as Ig-like C2-type 2.
+At position 481 to 770, the domain is characterized as Protein kinase.
+At position 140 to 455, the domain is characterized as Protein kinase.
+At position 89 to 149, the domain is characterized as Tudor.
+At position 112 to 219, the domain is characterized as HTH APSES-type.
+At position 118 to 354, the domain is characterized as Radical SAM core.
+At position 28 to 123, the domain is characterized as EthD.
+At position 153 to 228, the domain is characterized as Cache.
+At position 20 to 254, the domain is characterized as ABC transporter.
+At position 31 to 145, the domain is characterized as Ig-like V-type.
+At position 1 to 243, the domain is characterized as tr-type G.
+At position 41 to 87, the domain is characterized as F-box.
+At position 529 to 830, the domain is characterized as Piwi.
+At position 174 to 430, the domain is characterized as ABC transporter 1.
+At position 923 to 1166, the domain is characterized as ABC transporter 2.
+At position 42 to 118, the domain is characterized as VWFC 1.
+At position 162 to 277, the domain is characterized as CHRD 1.
+At position 279 to 398, the domain is characterized as CHRD 2.
+At position 404 to 519, the domain is characterized as CHRD 3.
+At position 525 to 652, the domain is characterized as CHRD 4.
+At position 689 to 748, the domain is characterized as VWFC 2.
+At position 767 to 836, the domain is characterized as VWFC 3.
+At position 855 to 919, the domain is characterized as VWFC 4.
+At position 117 to 625, the domain is characterized as Peptidase S8.
+At position 388 to 483, the domain is characterized as PA.
+At position 86 to 164, the domain is characterized as RRM 1.
+At position 183 to 261, the domain is characterized as RRM 2.
+At position 419 to 506, the domain is characterized as RRM 3; atypical.
+At position 373 to 423, the domain is characterized as SOCS box.
+At position 1 to 164, the domain is characterized as Thioredoxin; atypical.
+At position 270 to 475, the domain is characterized as GATase cobBQ-type.
+At position 272 to 461, the domain is characterized as B30.2/SPRY.
+At position 229 to 481, the domain is characterized as Ku.
+At position 107 to 151, the domain is characterized as WRC.
+At position 24 to 191, the domain is characterized as 3'-5' exonuclease.
+At position 230 to 310, the domain is characterized as HRDC.
+At position 348 to 580, the domain is characterized as Glutamine amidotransferase type-1.
+At position 96 to 353, the domain is characterized as Protein kinase.
+At position 129 to 304, the domain is characterized as Exonuclease.
+At position 1 to 97, the domain is characterized as Pyrin.
+At position 177 to 499, the domain is characterized as NACHT.
+At position 174 to 310, the domain is characterized as RanBD1 1.
+At position 772 to 907, the domain is characterized as RanBD1 2.
+At position 928 to 1084, the domain is characterized as PPIase cyclophilin-type.
+At position 305 to 492, the domain is characterized as BPL/LPL catalytic.
+At position 33 to 373, the domain is characterized as Transferrin-like 1.
+At position 450 to 796, the domain is characterized as Transferrin-like 2.
+At position 113 to 147, the domain is characterized as Pentapeptide repeat.
+At position 18 to 107, the domain is characterized as SUEL-type lectin.
+At position 696 to 743, the domain is characterized as GPS.
+At position 1702 to 1799, the domain is characterized as PH.
+At position 399 to 486, the domain is characterized as BTB 2.
+At position 136 to 195, the domain is characterized as CBS 1.
+At position 200 to 256, the domain is characterized as CBS 2.
+At position 130 to 405, the domain is characterized as Peptidase S8.
+At position 51 to 152, the domain is characterized as SWIRM.
+At position 34 to 213, the domain is characterized as VWFA 1.
+At position 215 to 255, the domain is characterized as EGF-like 1; incomplete.
+At position 256 to 292, the domain is characterized as EGF-like 2.
+At position 297 to 337, the domain is characterized as EGF-like 3.
+At position 342 to 377, the domain is characterized as EGF-like 4.
+At position 386 to 561, the domain is characterized as VWFA 2.
+At position 17 to 112, the domain is characterized as Ig-like C2-type 1.
+At position 224 to 311, the domain is characterized as Ig-like C2-type 2.
+At position 33 to 125, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 128 to 269, the domain is characterized as FAD-binding FR-type.
+At position 494 to 590, the domain is characterized as Fibronectin type-III.
+At position 91 to 141, the domain is characterized as DHHC.
+At position 1330 to 1422, the domain is characterized as DEP.
+At position 46 to 103, the domain is characterized as Ubiquitin-like; degenerate.
+At position 166 to 463, the domain is characterized as PI3K/PI4K catalytic.
+At position 27 to 282, the domain is characterized as Protein kinase.
+At position 318 to 343, the domain is characterized as NAF.
+At position 20 to 120, the domain is characterized as CBM39.
+At position 135 to 494, the domain is characterized as GH16.
+At position 167 to 407, the domain is characterized as Reverse transcriptase.
+At position 259 to 323, the domain is characterized as S4 RNA-binding.
+At position 372 to 646, the domain is characterized as Protein kinase.
+At position 8 to 74, the domain is characterized as BTB.
+At position 455 to 522, the domain is characterized as PAP-associated.
+At position 5 to 61, the domain is characterized as SpoVT-AbrB 1.
+At position 12 to 157, the domain is characterized as CP-type G.
+At position 1240 to 1357, the domain is characterized as PH.
+At position 81 to 264, the domain is characterized as ABC transmembrane type-1 1.
+At position 341 to 524, the domain is characterized as ABC transmembrane type-1 2.
+At position 25 to 106, the domain is characterized as GST N-terminal.
+At position 114 to 244, the domain is characterized as GST C-terminal.
+At position 246 to 435, the domain is characterized as GATase cobBQ-type.
+At position 33 to 259, the domain is characterized as Radical SAM core.
+At position 381 to 518, the domain is characterized as VPS9.
+At position 177 to 279, the domain is characterized as Ig-like C2-type 2.
+At position 167 to 350, the domain is characterized as VWFA.
+At position 1 to 14, the domain is characterized as EF-hand 1.
+At position 88 to 387, the domain is characterized as Calpain catalytic.
+At position 579 to 614, the domain is characterized as EF-hand 2.
+At position 699 to 734, the domain is characterized as EF-hand 3.
+At position 729 to 764, the domain is characterized as EF-hand 4.
+At position 764 to 799, the domain is characterized as EF-hand 5.
+At position 7 to 93, the domain is characterized as GST N-terminal.
+At position 102 to 224, the domain is characterized as GST C-terminal.
+At position 39 to 346, the domain is characterized as Protein kinase.
+At position 76 to 180, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 151 to 432, the domain is characterized as ABC transmembrane type-1 1.
+At position 486 to 707, the domain is characterized as ABC transporter 1.
+At position 783 to 1078, the domain is characterized as ABC transmembrane type-1 2.
+At position 1117 to 1351, the domain is characterized as ABC transporter 2.
+At position 8 to 90, the domain is characterized as PTS EIIB type-1.
+At position 116 to 455, the domain is characterized as PTS EIIC type-1.
+At position 192 to 283, the domain is characterized as PpiC.
+At position 1 to 296, the domain is characterized as IF rod.
+At position 325 to 432, the domain is characterized as Rhodanese.
+At position 239 to 291, the domain is characterized as HAMP.
+At position 296 to 532, the domain is characterized as Methyl-accepting transducer.
+At position 215 to 259, the domain is characterized as PCI.
+At position 7 to 84, the domain is characterized as Ubiquitin-like.
+At position 107 to 193, the domain is characterized as BAG.
+At position 8 to 282, the domain is characterized as F-BAR.
+At position 469 to 530, the domain is characterized as SH3 1.
+At position 567 to 629, the domain is characterized as SH3 2.
+At position 67 to 102, the domain is characterized as EF-hand.
+At position 136 to 204, the domain is characterized as SAM.
+At position 109 to 277, the domain is characterized as Helicase ATP-binding.
+At position 466 to 626, the domain is characterized as Helicase C-terminal.
+At position 334 to 494, the domain is characterized as Helicase C-terminal.
+At position 39 to 161, the domain is characterized as NlpC/P60.
+At position 143 to 237, the domain is characterized as Lipoprotein-associated type-17.
+At position 21 to 124, the domain is characterized as Ig-like.
+At position 1 to 126, the domain is characterized as MSP 1.
+At position 176 to 296, the domain is characterized as MSP 2.
+At position 356 to 493, the domain is characterized as TIR.
+At position 164 to 307, the domain is characterized as FCP1 homology.
+At position 2 to 1161, the domain is characterized as Zinc-hook.
+At position 518 to 638, the domain is characterized as SMC hinge.
+At position 122 to 230, the domain is characterized as CBM21.
+At position 99 to 168, the domain is characterized as S4 RNA-binding.
+At position 433 to 552, the domain is characterized as CMP/dCMP-type deaminase.
+At position 213 to 413, the domain is characterized as HIN-200 1.
+At position 417 to 615, the domain is characterized as HIN-200 2.
+At position 1 to 93, the domain is characterized as HTH hxlR-type.
+At position 7 to 112, the domain is characterized as PH.
+At position 31 to 217, the domain is characterized as Eph LBD.
+At position 341 to 445, the domain is characterized as Fibronectin type-III 1.
+At position 451 to 537, the domain is characterized as Fibronectin type-III 2.
+At position 692 to 988, the domain is characterized as Protein kinase.
+At position 470 to 529, the domain is characterized as SH3.
+At position 570 to 664, the domain is characterized as PDZ.
+At position 1667 to 1730, the domain is characterized as SAM.
+At position 61 to 308, the domain is characterized as Radical SAM core.
+At position 292 to 529, the domain is characterized as Glutamine amidotransferase type-1.
+At position 52 to 132, the domain is characterized as Cytochrome c 1.
+At position 162 to 240, the domain is characterized as Cytochrome c 2.
+At position 124 to 192, the domain is characterized as COMM.
+At position 115 to 161, the domain is characterized as G-patch.
+At position 15 to 764, the domain is characterized as Vitellogenin.
+At position 1390 to 1550, the domain is characterized as VWFD.
+At position 20 to 166, the domain is characterized as MRH.
+At position 28 to 103, the domain is characterized as Ig-like 1.
+At position 113 to 181, the domain is characterized as Ig-like 2.
+At position 78 to 189, the domain is characterized as Thioredoxin.
+At position 175 to 447, the domain is characterized as ABC transporter 1.
+At position 525 to 737, the domain is characterized as ABC transmembrane type-2 1.
+At position 850 to 1103, the domain is characterized as ABC transporter 2.
+At position 1175 to 1389, the domain is characterized as ABC transmembrane type-2 2.
+At position 5 to 73, the domain is characterized as HTH gntR-type.
+At position 25 to 153, the domain is characterized as TIR.
+At position 200 to 327, the domain is characterized as DBB.
+At position 203 to 279, the domain is characterized as Biotinyl-binding.
+At position 743 to 1003, the domain is characterized as Tyrosine-protein phosphatase.
+At position 39 to 145, the domain is characterized as Ig-like C2-type 1.
+At position 151 to 242, the domain is characterized as Ig-like C2-type 2.
+At position 251 to 321, the domain is characterized as Ig-like C2-type 3.
+At position 339 to 427, the domain is characterized as Ig-like C2-type 4.
+At position 433 to 526, the domain is characterized as Ig-like C2-type 5.
+At position 530 to 618, the domain is characterized as Ig-like C2-type 6.
+At position 622 to 711, the domain is characterized as Ig-like C2-type 7.
+At position 716 to 809, the domain is characterized as Ig-like C2-type 8.
+At position 813 to 909, the domain is characterized as Ig-like C2-type 9.
+At position 911 to 1008, the domain is characterized as Fibronectin type-III 1.
+At position 1013 to 1112, the domain is characterized as Fibronectin type-III 2.
+At position 1117 to 1213, the domain is characterized as Fibronectin type-III 3.
+At position 1217 to 1311, the domain is characterized as Fibronectin type-III 4.
+At position 1311 to 1403, the domain is characterized as Ig-like C2-type 10.
+At position 1405 to 1499, the domain is characterized as Fibronectin type-III 5.
+At position 1500 to 1601, the domain is characterized as Fibronectin type-III 6.
+At position 335 to 509, the domain is characterized as Helicase ATP-binding.
+At position 536 to 683, the domain is characterized as Helicase C-terminal.
+At position 31 to 143, the domain is characterized as Plastocyanin-like 1.
+At position 173 to 362, the domain is characterized as Plastocyanin-like 2.
+At position 463 to 594, the domain is characterized as Plastocyanin-like 3.
+At position 8 to 127, the domain is characterized as MaoC-like.
+At position 901 to 1001, the domain is characterized as Rhodanese.
+At position 1 to 197, the domain is characterized as SMP-LTD.
+At position 48 to 367, the domain is characterized as Kinesin motor.
+At position 141 to 247, the domain is characterized as Fe2OG dioxygenase.
+At position 8 to 192, the domain is characterized as HORMA.
+At position 95 to 325, the domain is characterized as Radical SAM core.
+At position 243 to 423, the domain is characterized as SSD.
+At position 53 to 490, the domain is characterized as Sema.
+At position 544 to 629, the domain is characterized as Ig-like C2-type.
+At position 139 to 200, the domain is characterized as KH.
+At position 25 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 339 to 574, the domain is characterized as ABC transporter.
+At position 1524 to 1712, the domain is characterized as PIK helical.
+At position 1802 to 2080, the domain is characterized as PI3K/PI4K catalytic.
+At position 16 to 180, the domain is characterized as NAC.
+At position 108 to 439, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 49, the domain is characterized as Disintegrin.
+At position 246 to 309, the domain is characterized as bZIP.
+At position 27 to 244, the domain is characterized as ABC transporter.
+At position 22 to 99, the domain is characterized as RRM.
+At position 87 to 284, the domain is characterized as Helicase ATP-binding.
+At position 575 to 639, the domain is characterized as Tudor.
+At position 10 to 246, the domain is characterized as ABC transporter 1.
+At position 188 to 374, the domain is characterized as Glutamine amidotransferase type-1.
+At position 83 to 198, the domain is characterized as PINc.
+At position 869 to 969, the domain is characterized as S1 motif.
+At position 189 to 421, the domain is characterized as TRUD.
+At position 338 to 429, the domain is characterized as PAN.
+At position 409 to 595, the domain is characterized as Helicase ATP-binding.
+At position 654 to 800, the domain is characterized as Helicase C-terminal.
+At position 177 to 433, the domain is characterized as NR LBD.
+At position 376 to 454, the domain is characterized as RRM 3.
+At position 48 to 120, the domain is characterized as KRAB.
+At position 117 to 348, the domain is characterized as Sigma-54 factor interaction.
+At position 468 to 573, the domain is characterized as PRD 1.
+At position 574 to 711, the domain is characterized as PTS EIIA type-4.
+At position 831 to 935, the domain is characterized as PRD 2.
+At position 810 to 910, the domain is characterized as HECT.
+At position 905 to 951, the domain is characterized as HNH.
+At position 4 to 88, the domain is characterized as Ubiquitin-like.
+At position 174 to 216, the domain is characterized as CAP-Gly.
+At position 46 to 145, the domain is characterized as Cytochrome b5 heme-binding.
+At position 49 to 135, the domain is characterized as SH2.
+At position 268 to 459, the domain is characterized as Rho-GAP.
+At position 396 to 779, the domain is characterized as USP.
+At position 16 to 147, the domain is characterized as SIS.
+At position 28 to 151, the domain is characterized as PX.
+At position 291 to 362, the domain is characterized as Mop.
+At position 335 to 396, the domain is characterized as S4 RNA-binding.
+At position 323 to 515, the domain is characterized as Roc.
+At position 878 to 1172, the domain is characterized as Protein kinase.
+At position 1366 to 1539, the domain is characterized as N-terminal Ras-GEF.
+At position 1620 to 1706, the domain is characterized as DEP.
+At position 1708 to 1971, the domain is characterized as Ras-GEF.
+At position 2354 to 2414, the domain is characterized as GRAM.
+At position 6 to 284, the domain is characterized as tr-type G.
+At position 86 to 148, the domain is characterized as KH.
+At position 120 to 332, the domain is characterized as Radical SAM core.
+At position 214 to 274, the domain is characterized as KH.
+At position 534 to 677, the domain is characterized as PA14.
+At position 701 to 832, the domain is characterized as CBM6.
+At position 298 to 490, the domain is characterized as PNPLA.
+At position 145 to 222, the domain is characterized as PRC barrel.
+At position 149 to 238, the domain is characterized as Ig-like C2-type 1.
+At position 43 to 148, the domain is characterized as FAD-binding FR-type.
+At position 50 to 108, the domain is characterized as TCP.
+At position 144 to 162, the domain is characterized as R.
+At position 28 to 311, the domain is characterized as ABC transmembrane type-1.
+At position 229 to 262, the domain is characterized as WW 1.
+At position 333 to 366, the domain is characterized as WW 2.
+At position 393 to 426, the domain is characterized as WW 3.
+At position 482 to 815, the domain is characterized as HECT.
+At position 2 to 232, the domain is characterized as Radical SAM core.
+At position 170 to 404, the domain is characterized as NR LBD.
+At position 149 to 263, the domain is characterized as C-type lectin.
+At position 605 to 935, the domain is characterized as Reverse transcriptase.
+At position 58 to 237, the domain is characterized as Macro.
+At position 373 to 530, the domain is characterized as CRAL-TRIO.
+At position 72 to 238, the domain is characterized as Helicase ATP-binding.
+At position 791 to 905, the domain is characterized as WWE.
+At position 1949 to 2056, the domain is characterized as HECT.
+At position 48 to 313, the domain is characterized as Protein kinase.
+At position 34 to 195, the domain is characterized as SIS.
+At position 120 to 132, the domain is characterized as EF-hand 2.
+At position 25 to 212, the domain is characterized as Albumin 1.
+At position 213 to 404, the domain is characterized as Albumin 2.
+At position 405 to 603, the domain is characterized as Albumin 3.
+At position 28 to 92, the domain is characterized as HMA 1.
+At position 121 to 188, the domain is characterized as HMA 2.
+At position 55 to 379, the domain is characterized as Protein kinase.
+At position 340 to 514, the domain is characterized as Helicase ATP-binding.
+At position 541 to 685, the domain is characterized as Helicase C-terminal.
+At position 13 to 31, the domain is characterized as DUF1725 1.
+At position 60 to 79, the domain is characterized as DUF1725 2.
+At position 248 to 331, the domain is characterized as Death.
+At position 273 to 335, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 427 to 489, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 31 to 235, the domain is characterized as Radical SAM core.
+At position 124 to 370, the domain is characterized as Radical SAM core.
+At position 522 to 656, the domain is characterized as GGDEF.
+At position 272 to 361, the domain is characterized as HTH La-type RNA-binding.
+At position 9 to 289, the domain is characterized as tr-type G.
+At position 248 to 528, the domain is characterized as Protein kinase.
+At position 82 to 385, the domain is characterized as Peptidase A1.
+At position 14 to 225, the domain is characterized as Radical SAM core.
+At position 210 to 259, the domain is characterized as bHLH.
+At position 495 to 552, the domain is characterized as Chromo 1.
+At position 590 to 651, the domain is characterized as Chromo 2.
+At position 710 to 894, the domain is characterized as Helicase ATP-binding.
+At position 1026 to 1191, the domain is characterized as Helicase C-terminal.
+At position 34 to 280, the domain is characterized as GB1/RHD3-type G.
+At position 652 to 765, the domain is characterized as Calponin-homology (CH).
+At position 40 to 114, the domain is characterized as RRM.
+At position 78 to 164, the domain is characterized as ZAD.
+At position 377 to 627, the domain is characterized as VWFA.
+At position 113 to 275, the domain is characterized as SIS.
+At position 218 to 238, the domain is characterized as ELK.
+At position 828 to 904, the domain is characterized as Carrier.
+At position 228 to 290, the domain is characterized as t-SNARE coiled-coil homology.
+At position 32 to 161, the domain is characterized as EamA 1.
+At position 210 to 339, the domain is characterized as EamA 2.
+At position 18 to 106, the domain is characterized as PDZ 1.
+At position 114 to 288, the domain is characterized as Guanylate kinase-like.
+At position 293 to 326, the domain is characterized as WW 1.
+At position 410 to 492, the domain is characterized as PDZ 2.
+At position 578 to 654, the domain is characterized as PDZ 3.
+At position 726 to 808, the domain is characterized as PDZ 4.
+At position 851 to 938, the domain is characterized as PDZ 5.
+At position 1021 to 1103, the domain is characterized as PDZ 6.
+At position 40 to 104, the domain is characterized as SCP.
+At position 223 to 295, the domain is characterized as RRM.
+At position 280 to 477, the domain is characterized as Helicase ATP-binding.
+At position 488 to 651, the domain is characterized as Helicase C-terminal.
+At position 354 to 430, the domain is characterized as EGF-like.
+At position 8 to 201, the domain is characterized as Lon N-terminal.
+At position 589 to 770, the domain is characterized as Lon proteolytic.
+At position 30 to 460, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 20 to 111, the domain is characterized as HIG1.
+At position 446 to 475, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 433 to 570, the domain is characterized as Thioredoxin.
+At position 446 to 511, the domain is characterized as SAM 1.
+At position 524 to 588, the domain is characterized as SAM 2.
+At position 612 to 679, the domain is characterized as SAM 3.
+At position 162 to 279, the domain is characterized as Fe2OG dioxygenase.
+At position 20 to 124, the domain is characterized as Ig-like V-type.
+At position 155 to 224, the domain is characterized as DRBM.
+At position 59 to 161, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 222 to 421, the domain is characterized as CN hydrolase.
+At position 6 to 211, the domain is characterized as ABC transporter.
+At position 123 to 197, the domain is characterized as PAS 1.
+At position 197 to 251, the domain is characterized as PAC 1.
+At position 400 to 473, the domain is characterized as PAS 2.
+At position 474 to 528, the domain is characterized as PAC 2.
+At position 594 to 881, the domain is characterized as Protein kinase.
+At position 338 to 475, the domain is characterized as Nudix hydrolase.
+At position 259 to 467, the domain is characterized as Peptidase M12B.
+At position 468 to 555, the domain is characterized as Disintegrin.
+At position 556 to 611, the domain is characterized as TSP type-1 1.
+At position 846 to 904, the domain is characterized as TSP type-1 2.
+At position 905 to 961, the domain is characterized as TSP type-1 3.
+At position 966 to 1023, the domain is characterized as TSP type-1 4.
+At position 1024 to 1073, the domain is characterized as TSP type-1 5.
+At position 1076 to 1135, the domain is characterized as TSP type-1 6.
+At position 1152 to 1206, the domain is characterized as TSP type-1 7.
+At position 1207 to 1264, the domain is characterized as TSP type-1 8.
+At position 1304 to 1356, the domain is characterized as TSP type-1 9.
+At position 1358 to 1416, the domain is characterized as TSP type-1 10.
+At position 1417 to 1475, the domain is characterized as TSP type-1 11.
+At position 1476 to 1531, the domain is characterized as TSP type-1 12.
+At position 1535 to 1588, the domain is characterized as TSP type-1 13.
+At position 1589 to 1652, the domain is characterized as TSP type-1 14.
+At position 1654 to 1710, the domain is characterized as TSP type-1 15.
+At position 1711 to 1910, the domain is characterized as GON.
+At position 3 to 135, the domain is characterized as CID.
+At position 20 to 87, the domain is characterized as COMM.
+At position 31 to 162, the domain is characterized as RNase III.
+At position 189 to 258, the domain is characterized as DRBM.
+At position 180 to 356, the domain is characterized as Hflx-type G.
+At position 872 to 967, the domain is characterized as PH.
+At position 107 to 518, the domain is characterized as PPM-type phosphatase.
+At position 270 to 362, the domain is characterized as Chromo 1.
+At position 387 to 450, the domain is characterized as Chromo 2.
+At position 491 to 661, the domain is characterized as Helicase ATP-binding.
+At position 790 to 941, the domain is characterized as Helicase C-terminal.
+At position 816 to 871, the domain is characterized as CBS 2.
+At position 30 to 169, the domain is characterized as Tyrosine-protein phosphatase.
+At position 65 to 261, the domain is characterized as tr-type G.
+At position 24 to 100, the domain is characterized as HSA.
+At position 412 to 471, the domain is characterized as Myb-like.
+At position 27 to 81, the domain is characterized as Kazal-like.
+At position 149 to 383, the domain is characterized as Radical SAM core.
+At position 438 to 723, the domain is characterized as Protein kinase.
+At position 136 to 282, the domain is characterized as RNase H type-1.
+At position 140 to 217, the domain is characterized as RRM 1.
+At position 245 to 328, the domain is characterized as RRM 2.
+At position 612 to 661, the domain is characterized as Myb-like 1.
+At position 661 to 745, the domain is characterized as Myb-like 2.
+At position 192 to 242, the domain is characterized as KBD.
+At position 294 to 405, the domain is characterized as SPR.
+At position 79 to 132, the domain is characterized as bHLH.
+At position 150 to 222, the domain is characterized as PAS 1.
+At position 333 to 403, the domain is characterized as PAS 2.
+At position 408 to 451, the domain is characterized as PAC.
+At position 160 to 397, the domain is characterized as Radical SAM core.
+At position 399 to 469, the domain is characterized as TRAM.
+At position 17 to 284, the domain is characterized as Radical SAM core.
+At position 67 to 96, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 51 to 92, the domain is characterized as Collagen-like.
+At position 96 to 313, the domain is characterized as Fibrinogen C-terminal.
+At position 14 to 237, the domain is characterized as BAR.
+At position 421 to 487, the domain is characterized as SH3.
+At position 35 to 122, the domain is characterized as GOLD.
+At position 6 to 78, the domain is characterized as HTH asnC-type.
+At position 29 to 283, the domain is characterized as Protein kinase.
+At position 284 to 337, the domain is characterized as AGC-kinase C-terminal.
+At position 284 to 402, the domain is characterized as Nop.
+At position 63 to 137, the domain is characterized as S1 motif.
+At position 147 to 203, the domain is characterized as KH.
+At position 130 to 259, the domain is characterized as Fatty acid hydroxylase.
+At position 5 to 92, the domain is characterized as ATP-cone.
+At position 63 to 163, the domain is characterized as AB hydrolase-1.
+At position 29 to 173, the domain is characterized as N-acetyltransferase 1.
+At position 181 to 338, the domain is characterized as N-acetyltransferase 2.
+At position 5 to 86, the domain is characterized as GST N-terminal.
+At position 92 to 224, the domain is characterized as GST C-terminal.
+At position 214 to 362, the domain is characterized as N-acetyltransferase.
+At position 66 to 213, the domain is characterized as Tyrosine-protein phosphatase.
+At position 537 to 706, the domain is characterized as N-acetyltransferase.
+At position 10 to 346, the domain is characterized as Enoyl reductase (ER).
+At position 74 to 318, the domain is characterized as BURP.
+At position 704 to 855, the domain is characterized as MOSC.
+At position 120 to 603, the domain is characterized as Peptidase S8.
+At position 1 to 199, the domain is characterized as RNase H type-2.
+At position 7 to 178, the domain is characterized as Era-type G.
+At position 209 to 286, the domain is characterized as KH type-2.
+At position 11 to 264, the domain is characterized as CN hydrolase.
+At position 138 to 183, the domain is characterized as LRRCT.
+At position 415 to 477, the domain is characterized as SH3 1.
+At position 495 to 554, the domain is characterized as SH3 2.
+At position 571 to 630, the domain is characterized as SH3 3.
+At position 661 to 720, the domain is characterized as SH3 4.
+At position 730 to 789, the domain is characterized as SH3 5.
+At position 48 to 328, the domain is characterized as GH10.
+At position 15 to 68, the domain is characterized as F-box.
+At position 355 to 406, the domain is characterized as FBD.
+At position 29 to 73, the domain is characterized as PSI.
+At position 131 to 340, the domain is characterized as VWFA.
+At position 1514 to 1609, the domain is characterized as Fibronectin type-III 3.
+At position 1627 to 1723, the domain is characterized as Fibronectin type-III 4.
+At position 40 to 133, the domain is characterized as CBM21.
+At position 151 to 234, the domain is characterized as Helicase ATP-binding.
+At position 83 to 521, the domain is characterized as Peptidase S8.
+At position 438 to 674, the domain is characterized as ABC transporter.
+At position 188 to 282, the domain is characterized as PDZ.
+At position 26 to 115, the domain is characterized as PPIase FKBP-type.
+At position 275 to 303, the domain is characterized as IQ.
+At position 71 to 115, the domain is characterized as LEM.
+At position 1 to 176, the domain is characterized as BPL/LPL catalytic.
+At position 622 to 719, the domain is characterized as Zinc-hook.
+At position 488 to 536, the domain is characterized as GYF.
+At position 210 to 295, the domain is characterized as KH.
+At position 19 to 133, the domain is characterized as XRN2-binding (XTBD).
+At position 462 to 537, the domain is characterized as DRBM.
+At position 236 to 448, the domain is characterized as Helicase ATP-binding.
+At position 488 to 656, the domain is characterized as Helicase C-terminal.
+At position 44 to 103, the domain is characterized as TSP type-1 1.
+At position 107 to 181, the domain is characterized as TSP type-1 2.
+At position 385 to 441, the domain is characterized as TSP type-1 4.
+At position 448 to 535, the domain is characterized as TSP type-1 5.
+At position 537 to 596, the domain is characterized as TSP type-1 6.
+At position 656 to 717, the domain is characterized as TSP type-1 7.
+At position 718 to 797, the domain is characterized as TSP type-1 8.
+At position 799 to 859, the domain is characterized as TSP type-1 9.
+At position 860 to 932, the domain is characterized as TSP type-1 10.
+At position 934 to 985, the domain is characterized as TSP type-1 11.
+At position 988 to 1061, the domain is characterized as TSP type-1 12.
+At position 1063 to 1123, the domain is characterized as TSP type-1 13.
+At position 1124 to 1191, the domain is characterized as TSP type-1 14.
+At position 1193 to 1247, the domain is characterized as TSP type-1 15.
+At position 1248 to 1311, the domain is characterized as TSP type-1 16.
+At position 1313 to 1368, the domain is characterized as TSP type-1 17.
+At position 1369 to 1439, the domain is characterized as TSP type-1 18.
+At position 1441 to 1502, the domain is characterized as TSP type-1 19.
+At position 43 to 160, the domain is characterized as OmpA-like.
+At position 24 to 90, the domain is characterized as bHLH.
+At position 577 to 617, the domain is characterized as UBA.
+At position 117 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 352 to 553, the domain is characterized as MIF4G.
+At position 650 to 764, the domain is characterized as MI.
+At position 11 to 172, the domain is characterized as N-acetyltransferase.
+At position 280 to 547, the domain is characterized as B30.2/SPRY.
+At position 1 to 80, the domain is characterized as Saposin B-type.
+At position 221 to 396, the domain is characterized as TrmE-type G.
+At position 237 to 387, the domain is characterized as Helicase C-terminal.
+At position 157 to 349, the domain is characterized as NodB homology.
+At position 19 to 68, the domain is characterized as bHLH.
+At position 195 to 239, the domain is characterized as CHCH.
+At position 1 to 105, the domain is characterized as PTS EIIB type-2.
+At position 128 to 475, the domain is characterized as PTS EIIC type-2.
+At position 91 to 399, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 396 to 428, the domain is characterized as EGF-like 2.
+At position 552 to 604, the domain is characterized as TB 1.
+At position 622 to 662, the domain is characterized as EGF-like 3; calcium-binding.
+At position 672 to 724, the domain is characterized as TB 2.
+At position 844 to 886, the domain is characterized as EGF-like 4.
+At position 887 to 929, the domain is characterized as EGF-like 5; calcium-binding.
+At position 930 to 969, the domain is characterized as EGF-like 6; calcium-binding.
+At position 970 to 1009, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1010 to 1050, the domain is characterized as EGF-like 8; calcium-binding.
+At position 1051 to 1092, the domain is characterized as EGF-like 9; calcium-binding.
+At position 1093 to 1134, the domain is characterized as EGF-like 10; calcium-binding.
+At position 1135 to 1175, the domain is characterized as EGF-like 11; calcium-binding.
+At position 1176 to 1217, the domain is characterized as EGF-like 12; calcium-binding.
+At position 1218 to 1258, the domain is characterized as EGF-like 13; calcium-binding.
+At position 1259 to 1302, the domain is characterized as EGF-like 14; calcium-binding.
+At position 1303 to 1344, the domain is characterized as EGF-like 15; calcium-binding.
+At position 1345 to 1387, the domain is characterized as EGF-like 16; calcium-binding.
+At position 1411 to 1463, the domain is characterized as TB 3.
+At position 1485 to 1527, the domain is characterized as EGF-like 17; calcium-binding.
+At position 1528 to 1567, the domain is characterized as EGF-like 18; calcium-binding.
+At position 1584 to 1636, the domain is characterized as TB 4.
+At position 1733 to 1773, the domain is characterized as EGF-like 19; calcium-binding.
+At position 1774 to 1818, the domain is characterized as EGF-like 20; calcium-binding.
+At position 398 to 552, the domain is characterized as N-acetyltransferase.
+At position 129 to 190, the domain is characterized as EamA.
+At position 10 to 241, the domain is characterized as ABC transporter.
+At position 13 to 217, the domain is characterized as Glutamine amidotransferase type-1.
+At position 139 to 539, the domain is characterized as GBD/FH3.
+At position 652 to 737, the domain is characterized as FH1.
+At position 759 to 1155, the domain is characterized as FH2.
+At position 1174 to 1209, the domain is characterized as DAD.
+At position 293 to 365, the domain is characterized as U-box.
+At position 2 to 146, the domain is characterized as N-acetyltransferase.
+At position 57 to 118, the domain is characterized as SH3.
+At position 240 to 494, the domain is characterized as Protein kinase.
+At position 435 to 496, the domain is characterized as SH3 3.
+At position 802 to 861, the domain is characterized as SH3 4.
+At position 13 to 223, the domain is characterized as Cytochrome b561.
+At position 82 to 192, the domain is characterized as MTTase N-terminal.
+At position 216 to 453, the domain is characterized as Radical SAM core.
+At position 456 to 525, the domain is characterized as TRAM.
+At position 157 to 340, the domain is characterized as Helicase ATP-binding.
+At position 370 to 520, the domain is characterized as Helicase C-terminal.
+At position 282 to 524, the domain is characterized as Glutamine amidotransferase type-1.
+At position 39 to 359, the domain is characterized as Asparaginase/glutaminase.
+At position 126 to 187, the domain is characterized as CBS 1.
+At position 189 to 245, the domain is characterized as CBS 2.
+At position 198 to 386, the domain is characterized as Glutamine amidotransferase type-1.
+At position 187 to 355, the domain is characterized as PCI.
+At position 160 to 258, the domain is characterized as RRM 1.
+At position 266 to 351, the domain is characterized as RRM 2.
+At position 178 to 687, the domain is characterized as TBDR beta-barrel.
+At position 80 to 361, the domain is characterized as tr-type G.
+At position 24 to 292, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 625 to 897, the domain is characterized as Protein kinase.
+At position 113 to 379, the domain is characterized as Protein kinase.
+At position 379 to 444, the domain is characterized as SH3.
+At position 484 to 498, the domain is characterized as CRIB.
+At position 229 to 307, the domain is characterized as RRM.
+At position 498 to 773, the domain is characterized as Reverse transcriptase.
+At position 16 to 282, the domain is characterized as CNH.
+At position 21 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 118 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 207 to 299, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 401, the domain is characterized as Ig-like C2-type 4.
+At position 404 to 499, the domain is characterized as Ig-like C2-type 5.
+At position 577 to 912, the domain is characterized as Protein kinase.
+At position 143 to 437, the domain is characterized as NB-ARC.
+At position 14 to 123, the domain is characterized as AB hydrolase-1.
+At position 1002 to 1316, the domain is characterized as PKS/mFAS DH.
+At position 2518 to 2595, the domain is characterized as Carrier.
+At position 168 to 487, the domain is characterized as Peptidase S8.
+At position 495 to 635, the domain is characterized as P/Homo B.
+At position 931 to 969, the domain is characterized as PLAC.
+At position 338 to 1052, the domain is characterized as Myosin motor.
+At position 1081 to 1110, the domain is characterized as IQ 2.
+At position 17 to 61, the domain is characterized as WAP 1.
+At position 62 to 106, the domain is characterized as WAP 2.
+At position 480 to 647, the domain is characterized as tr-type G.
+At position 188 to 356, the domain is characterized as SSD.
+At position 333 to 524, the domain is characterized as PCI.
+At position 4 to 156, the domain is characterized as NAC.
+At position 18 to 129, the domain is characterized as MTTase N-terminal.
+At position 385 to 456, the domain is characterized as TRAM.
+At position 107 to 286, the domain is characterized as FAD-binding PCMH-type.
+At position 230 to 461, the domain is characterized as NR LBD.
+At position 774 to 862, the domain is characterized as PKD.
+At position 14 to 79, the domain is characterized as LCN-type CS-alpha/beta.
+At position 60 to 168, the domain is characterized as THUMP.
+At position 26 to 292, the domain is characterized as GH18.
+At position 144 to 205, the domain is characterized as Sushi 3.
+At position 208 to 266, the domain is characterized as Sushi 4.
+At position 267 to 330, the domain is characterized as Sushi 5.
+At position 87 to 166, the domain is characterized as C-type lysozyme.
+At position 29 to 313, the domain is characterized as ABC transmembrane type-1.
+At position 345 to 581, the domain is characterized as ABC transporter.
+At position 133 to 214, the domain is characterized as PDZ 2.
+At position 242 to 322, the domain is characterized as PDZ 3.
+At position 377 to 457, the domain is characterized as PDZ 4.
+At position 157 to 329, the domain is characterized as Helicase ATP-binding.
+At position 408 to 552, the domain is characterized as Helicase C-terminal.
+At position 88 to 151, the domain is characterized as bZIP.
+At position 25 to 192, the domain is characterized as Helicase ATP-binding.
+At position 219 to 363, the domain is characterized as Helicase C-terminal.
+At position 17 to 282, the domain is characterized as CheR-type methyltransferase.
+At position 127 to 207, the domain is characterized as RRM 2.
+At position 393 to 626, the domain is characterized as Roc.
+At position 295 to 555, the domain is characterized as Protein kinase.
+At position 38 to 280, the domain is characterized as Peptidase S1.
+At position 7 to 211, the domain is characterized as DPCK.
+At position 238 to 405, the domain is characterized as tr-type G.
+At position 156 to 208, the domain is characterized as Kazal-like 3.
+At position 244 to 440, the domain is characterized as B30.2/SPRY.
+At position 275 to 348, the domain is characterized as PAS.
+At position 5 to 71, the domain is characterized as HMA 1.
+At position 73 to 139, the domain is characterized as HMA 2.
+At position 85 to 239, the domain is characterized as CRAL-TRIO.
+At position 72 to 247, the domain is characterized as FAD-binding PCMH-type.
+At position 317 to 346, the domain is characterized as LRRCT.
+At position 2 to 203, the domain is characterized as ThyX.
+At position 48 to 180, the domain is characterized as Thioredoxin.
+At position 208 to 239, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 241 to 270, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1 to 256, the domain is characterized as Pterin-binding.
+At position 120 to 416, the domain is characterized as Protein kinase.
+At position 36 to 241, the domain is characterized as Cupin type-1 1.
+At position 323 to 472, the domain is characterized as Cupin type-1 2.
+At position 233 to 465, the domain is characterized as Peptidase S1.
+At position 20 to 80, the domain is characterized as MADS-box.
+At position 106 to 198, the domain is characterized as K-box.
+At position 121 to 256, the domain is characterized as BFN.
+At position 287 to 322, the domain is characterized as UVR.
+At position 96 to 220, the domain is characterized as DOD-type homing endonuclease.
+At position 399 to 616, the domain is characterized as tr-type G.
+At position 72 to 201, the domain is characterized as Nudix hydrolase.
+At position 188 to 361, the domain is characterized as EngA-type G 2.
+At position 333 to 493, the domain is characterized as N-acetyltransferase.
+At position 41 to 330, the domain is characterized as ABC transmembrane type-1 1.
+At position 361 to 597, the domain is characterized as ABC transporter 1.
+At position 982 to 1218, the domain is characterized as ABC transporter 2.
+At position 12 to 149, the domain is characterized as C2 1.
+At position 315 to 439, the domain is characterized as C2 2.
+At position 71 to 176, the domain is characterized as FAD-binding FR-type.
+At position 3 to 191, the domain is characterized as Prephenate dehydratase.
+At position 364 to 544, the domain is characterized as Roc.
+At position 1026 to 1292, the domain is characterized as Protein kinase.
+At position 277 to 426, the domain is characterized as Exonuclease.
+At position 48 to 113, the domain is characterized as Sm.
+At position 676 to 752, the domain is characterized as RRM.
+At position 145 to 235, the domain is characterized as Glutaredoxin 1.
+At position 236 to 334, the domain is characterized as Glutaredoxin 2.
+At position 22 to 127, the domain is characterized as Ig-like V-type.
+At position 132 to 218, the domain is characterized as Ig-like C2-type 1.
+At position 222 to 315, the domain is characterized as Ig-like C2-type 2.
+At position 254 to 380, the domain is characterized as G8.
+At position 310 to 362, the domain is characterized as bHLH.
+At position 10 to 89, the domain is characterized as TFIIS N-terminal.
+At position 210 to 333, the domain is characterized as TFIIS central.
+At position 248 to 440, the domain is characterized as GATase cobBQ-type.
+At position 142 to 276, the domain is characterized as OTU.
+At position 21 to 341, the domain is characterized as Kinesin motor.
+At position 91 to 283, the domain is characterized as ABC transmembrane type-1.
+At position 163 to 245, the domain is characterized as RRM 1.
+At position 247 to 324, the domain is characterized as RRM 2.
+At position 283 to 428, the domain is characterized as SIS 1.
+At position 198 to 388, the domain is characterized as DH.
+At position 442 to 546, the domain is characterized as PH.
+At position 595 to 739, the domain is characterized as N-terminal Ras-GEF.
+At position 778 to 1017, the domain is characterized as Ras-GEF.
+At position 53 to 226, the domain is characterized as Laminin G-like.
+At position 270 to 329, the domain is characterized as VWFC 1.
+At position 553 to 599, the domain is characterized as EGF-like 5; calcium-binding.
+At position 170 to 370, the domain is characterized as Peptidase M12B.
+At position 37 to 290, the domain is characterized as Pyruvate carboxyltransferase.
+At position 655 to 730, the domain is characterized as Carrier.
+At position 273 to 350, the domain is characterized as UBX.
+At position 206 to 286, the domain is characterized as G5.
+At position 10 to 126, the domain is characterized as Fatty acid hydroxylase.
+At position 144 to 218, the domain is characterized as PRC barrel.
+At position 59 to 180, the domain is characterized as PH.
+At position 81 to 407, the domain is characterized as Asparaginase/glutaminase.
+At position 14 to 90, the domain is characterized as RRM 1.
+At position 96 to 176, the domain is characterized as RRM 2.
+At position 191 to 275, the domain is characterized as RRM 3.
+At position 299 to 376, the domain is characterized as RRM 4.
+At position 353 to 403, the domain is characterized as LIM zinc-binding 1.
+At position 412 to 462, the domain is characterized as LIM zinc-binding 2.
+At position 471 to 521, the domain is characterized as LIM zinc-binding 3.
+At position 530 to 580, the domain is characterized as LIM zinc-binding 4.
+At position 290 to 449, the domain is characterized as W2.
+At position 7 to 194, the domain is characterized as Flavodoxin-like.
+At position 129 to 209, the domain is characterized as RRM 1.
+At position 300 to 384, the domain is characterized as RRM 2.
+At position 858 to 904, the domain is characterized as G-patch.
+At position 172 to 250, the domain is characterized as Thyroglobulin type-1.
+At position 45 to 187, the domain is characterized as BAH.
+At position 150 to 332, the domain is characterized as VWFA.
+At position 18 to 134, the domain is characterized as NTF2.
+At position 315 to 386, the domain is characterized as RRM.
+At position 130 to 359, the domain is characterized as Radical SAM core.
+At position 362 to 429, the domain is characterized as TRAM.
+At position 59 to 166, the domain is characterized as AB hydrolase-1.
+At position 154 to 340, the domain is characterized as CNNM transmembrane.
+At position 359 to 420, the domain is characterized as CBS 1.
+At position 426 to 484, the domain is characterized as CBS 2.
+At position 280 to 338, the domain is characterized as GYF.
+At position 32 to 331, the domain is characterized as GH26.
+At position 967 to 1188, the domain is characterized as Histidine kinase.
+At position 1840 to 1967, the domain is characterized as Response regulatory.
+At position 9 to 71, the domain is characterized as LCN-type CS-alpha/beta.
+At position 10 to 158, the domain is characterized as SprT-like.
+At position 522 to 666, the domain is characterized as RUN.
+At position 844 to 902, the domain is characterized as SH3.
+At position 144 to 257, the domain is characterized as LRAT.
+At position 182 to 455, the domain is characterized as ABC transporter 1.
+At position 533 to 746, the domain is characterized as ABC transmembrane type-2 1.
+At position 894 to 1151, the domain is characterized as ABC transporter 2.
+At position 1224 to 1438, the domain is characterized as ABC transmembrane type-2 2.
+At position 27 to 284, the domain is characterized as Protein kinase.
+At position 184 to 420, the domain is characterized as Methyl-accepting transducer.
+At position 12 to 65, the domain is characterized as ClpX-type ZB.
+At position 530 to 659, the domain is characterized as B12-binding.
+At position 181 to 242, the domain is characterized as LIM zinc-binding 1.
+At position 243 to 300, the domain is characterized as LIM zinc-binding 2.
+At position 301 to 370, the domain is characterized as LIM zinc-binding 3.
+At position 78 to 157, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 199 to 229, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 8 to 232, the domain is characterized as tr-type G.
+At position 1 to 169, the domain is characterized as tr-type G.
+At position 204 to 223, the domain is characterized as UIM 1.
+At position 259 to 278, the domain is characterized as UIM 2.
+At position 451 to 502, the domain is characterized as Rubredoxin-like.
+At position 171 to 231, the domain is characterized as SH3.
+At position 239 to 338, the domain is characterized as SH2.
+At position 363 to 615, the domain is characterized as Protein kinase.
+At position 108 to 312, the domain is characterized as BPL/LPL catalytic.
+At position 136 to 366, the domain is characterized as Reverse transcriptase.
+At position 30 to 103, the domain is characterized as U-box 1.
+At position 125 to 198, the domain is characterized as U-box 2.
+At position 101 to 233, the domain is characterized as Nudix hydrolase.
+At position 58 to 127, the domain is characterized as Expansin-like EG45.
+At position 249 to 439, the domain is characterized as GATase cobBQ-type.
+At position 122 to 243, the domain is characterized as MI 1.
+At position 286 to 407, the domain is characterized as MI 2.
+At position 420 to 541, the domain is characterized as MI 3.
+At position 583 to 702, the domain is characterized as MI 4.
+At position 29 to 230, the domain is characterized as Albumin 1.
+At position 231 to 426, the domain is characterized as Albumin 2.
+At position 427 to 608, the domain is characterized as Albumin 3.
+At position 609 to 811, the domain is characterized as Albumin 4.
+At position 812 to 1031, the domain is characterized as Albumin 5.
+At position 1032 to 1226, the domain is characterized as Albumin 6.
+At position 1227 to 1422, the domain is characterized as Albumin 7.
+At position 289 to 384, the domain is characterized as LCCL 1.
+At position 390 to 492, the domain is characterized as LCCL 2.
+At position 57 to 175, the domain is characterized as SEA.
+At position 206 to 437, the domain is characterized as Peptidase S1.
+At position 53 to 304, the domain is characterized as ABC transporter.
+At position 384 to 590, the domain is characterized as ABC transmembrane type-2.
+At position 350 to 703, the domain is characterized as TTL.
+At position 272 to 508, the domain is characterized as NR LBD.
+At position 20 to 371, the domain is characterized as IF rod.
+At position 653 to 764, the domain is characterized as LTD.
+At position 11 to 68, the domain is characterized as bHLH.
+At position 98 to 130, the domain is characterized as Orange.
+At position 20 to 260, the domain is characterized as ABC transporter.
+At position 23 to 307, the domain is characterized as ABC transmembrane type-1.
+At position 340 to 552, the domain is characterized as ABC transporter.
+At position 659 to 782, the domain is characterized as C2.
+At position 4 to 229, the domain is characterized as Radical SAM core.
+At position 190 to 236, the domain is characterized as F-box.
+At position 54 to 283, the domain is characterized as Ferric oxidoreductase.
+At position 284 to 391, the domain is characterized as FAD-binding FR-type.
+At position 23 to 185, the domain is characterized as Flo11 1.
+At position 208 to 382, the domain is characterized as Flo11 2.
+At position 422 to 596, the domain is characterized as Flo11 3.
+At position 21 to 168, the domain is characterized as PX.
+At position 160 to 203, the domain is characterized as P-type 1.
+At position 305 to 348, the domain is characterized as P-type 2.
+At position 352 to 395, the domain is characterized as P-type 3.
+At position 524 to 567, the domain is characterized as P-type 4.
+At position 571 to 614, the domain is characterized as P-type 5.
+At position 619 to 662, the domain is characterized as P-type 6.
+At position 417 to 496, the domain is characterized as G5.
+At position 7 to 132, the domain is characterized as Peptidase C39.
+At position 153 to 435, the domain is characterized as ABC transmembrane type-1.
+At position 469 to 703, the domain is characterized as ABC transporter.
+At position 55 to 187, the domain is characterized as MATH.
+At position 213 to 528, the domain is characterized as USP.
+At position 475 to 874, the domain is characterized as Protein kinase.
+At position 47 to 353, the domain is characterized as AB hydrolase-1.
+At position 436 to 490, the domain is characterized as CBS 2.
+At position 26 to 101, the domain is characterized as S1-like.
+At position 28 to 122, the domain is characterized as HTH La-type RNA-binding.
+At position 125 to 203, the domain is characterized as RRM.
+At position 449 to 562, the domain is characterized as xRRM.
+At position 1 to 31, the domain is characterized as EF-hand 1.
+At position 32 to 67, the domain is characterized as EF-hand 2.
+At position 108 to 143, the domain is characterized as EF-hand 4.
+At position 43 to 497, the domain is characterized as Hexokinase.
+At position 968 to 1056, the domain is characterized as PDZ.
+At position 126 to 257, the domain is characterized as RGS.
+At position 29 to 239, the domain is characterized as Brix.
+At position 141 to 221, the domain is characterized as RRM 2.
+At position 392 to 467, the domain is characterized as RRM 3.
+At position 29 to 54, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 35 to 288, the domain is characterized as Pyruvate carboxyltransferase.
+At position 270 to 305, the domain is characterized as Ubiquitin-like 5.
+At position 137 to 247, the domain is characterized as Gnk2-homologous 2.
+At position 632 to 894, the domain is characterized as Protein kinase.
+At position 363 to 584, the domain is characterized as BURP.
+At position 2 to 171, the domain is characterized as EngA-type G 1.
+At position 181 to 364, the domain is characterized as EngA-type G 2.
+At position 365 to 448, the domain is characterized as KH-like.
+At position 142 to 260, the domain is characterized as C2.
+At position 336 to 599, the domain is characterized as Protein kinase.
+At position 343 to 672, the domain is characterized as PDEase.
+At position 253 to 431, the domain is characterized as GAF.
+At position 646 to 717, the domain is characterized as PAS 1.
+At position 776 to 853, the domain is characterized as PAS 2.
+At position 930 to 1150, the domain is characterized as Histidine kinase.
+At position 79 to 175, the domain is characterized as Toprim.
+At position 802 to 838, the domain is characterized as CBM1.
+At position 1 to 67, the domain is characterized as GRAM.
+At position 133 to 508, the domain is characterized as Myotubularin phosphatase.
+At position 36 to 381, the domain is characterized as G-alpha.
+At position 42 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 35 to 255, the domain is characterized as GH16.
+At position 443 to 472, the domain is characterized as Collagen-like 1.
+At position 473 to 529, the domain is characterized as Collagen-like 2.
+At position 530 to 589, the domain is characterized as Collagen-like 3.
+At position 342 to 430, the domain is characterized as OCT.
+At position 1 to 135, the domain is characterized as MGS-like.
+At position 14 to 204, the domain is characterized as RNase H type-2.
+At position 795 to 870, the domain is characterized as Carrier 1.
+At position 1915 to 1993, the domain is characterized as Carrier 2.
+At position 3 to 84, the domain is characterized as Toprim.
+At position 641 to 712, the domain is characterized as PAS 1.
+At position 775 to 846, the domain is characterized as PAS 2.
+At position 923 to 1143, the domain is characterized as Histidine kinase.
+At position 11 to 127, the domain is characterized as Response regulatory.
+At position 166 to 231, the domain is characterized as HTH luxR-type.
+At position 407 to 607, the domain is characterized as FtsK 1.
+At position 747 to 936, the domain is characterized as FtsK 2.
+At position 1018 to 1201, the domain is characterized as FtsK 3.
+At position 21 to 138, the domain is characterized as Rhodanese.
+At position 175 to 316, the domain is characterized as Tyrosine-protein phosphatase.
+At position 35 to 293, the domain is characterized as PPM-type phosphatase.
+At position 710 to 1003, the domain is characterized as Protein kinase.
+At position 31 to 234, the domain is characterized as Brix.
+At position 262 to 336, the domain is characterized as POU-specific.
+At position 32 to 341, the domain is characterized as Velvet.
+At position 245 to 427, the domain is characterized as GATase cobBQ-type.
+At position 173 to 300, the domain is characterized as Fe2OG dioxygenase.
+At position 279 to 407, the domain is characterized as PH.
+At position 426 to 685, the domain is characterized as Protein kinase.
+At position 26 to 321, the domain is characterized as PPM-type phosphatase.
+At position 48 to 273, the domain is characterized as SET.
+At position 1 to 179, the domain is characterized as CNNM transmembrane.
+At position 198 to 259, the domain is characterized as CBS 1.
+At position 263 to 320, the domain is characterized as CBS 2.
+At position 33 to 303, the domain is characterized as CN hydrolase.
+At position 40 to 92, the domain is characterized as bHLH.
+At position 246 to 487, the domain is characterized as CN hydrolase.
+At position 146 to 210, the domain is characterized as MBD.
+At position 269 to 329, the domain is characterized as Pre-SET.
+At position 332 to 537, the domain is characterized as SET.
+At position 138 to 459, the domain is characterized as NACHT.
+At position 1 to 70, the domain is characterized as Disintegrin.
+At position 45 to 197, the domain is characterized as PID.
+At position 275 to 310, the domain is characterized as EGF-like 6.
+At position 312 to 352, the domain is characterized as EGF-like 7; calcium-binding.
+At position 353 to 391, the domain is characterized as EGF-like 8; calcium-binding.
+At position 392 to 428, the domain is characterized as EGF-like 9; calcium-binding.
+At position 828 to 940, the domain is characterized as CUB.
+At position 5 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 47 to 185, the domain is characterized as F5/8 type C.
+At position 220 to 369, the domain is characterized as Laminin G-like 1.
+At position 403 to 540, the domain is characterized as Laminin G-like 2.
+At position 542 to 579, the domain is characterized as EGF-like 1.
+At position 824 to 962, the domain is characterized as Laminin G-like 3.
+At position 962 to 999, the domain is characterized as EGF-like 2.
+At position 1032 to 1183, the domain is characterized as Laminin G-like 4.
+At position 175 to 259, the domain is characterized as CTCK.
+At position 125 to 296, the domain is characterized as Helicase ATP-binding.
+At position 307 to 488, the domain is characterized as Helicase C-terminal.
+At position 333 to 552, the domain is characterized as TLDc.
+At position 530 to 610, the domain is characterized as IPT/TIG.
+At position 169 to 426, the domain is characterized as MHD.
+At position 19 to 109, the domain is characterized as N-acetyltransferase.
+At position 146 to 256, the domain is characterized as C-type lectin.
+At position 118 to 449, the domain is characterized as PI3K/PI4K catalytic.
+At position 1 to 49, the domain is characterized as PPIase FKBP-type.
+At position 1 to 78, the domain is characterized as WWE 1.
+At position 79 to 155, the domain is characterized as WWE 2.
+At position 295 to 363, the domain is characterized as SH3.
+At position 424 to 618, the domain is characterized as Rho-GAP.
+At position 257 to 339, the domain is characterized as Toprim.
+At position 218 to 306, the domain is characterized as Fibronectin type-III.
+At position 722 to 879, the domain is characterized as MyTH4.
+At position 890 to 1078, the domain is characterized as Rho-GAP.
+At position 716 to 773, the domain is characterized as LRRCT.
+At position 1096 to 1233, the domain is characterized as TIR.
+At position 1 to 438, the domain is characterized as SMP-LTD.
+At position 526 to 629, the domain is characterized as Ricin B-type lectin.
+At position 71 to 289, the domain is characterized as Radical SAM core.
+At position 629 to 687, the domain is characterized as FYR N-terminal.
+At position 689 to 775, the domain is characterized as FYR C-terminal.
+At position 13 to 143, the domain is characterized as RNase III.
+At position 170 to 238, the domain is characterized as DRBM.
+At position 25 to 81, the domain is characterized as Chitin-binding type-2.
+At position 128 to 204, the domain is characterized as HTH OST-type 2.
+At position 288 to 364, the domain is characterized as HTH OST-type 3.
+At position 523 to 581, the domain is characterized as Tudor.
+At position 51 to 133, the domain is characterized as RRM 1.
+At position 136 to 215, the domain is characterized as RRM 2.
+At position 302 to 526, the domain is characterized as CHASE.
+At position 594 to 867, the domain is characterized as Histidine kinase.
+At position 891 to 1013, the domain is characterized as Response regulatory 1.
+At position 1036 to 1173, the domain is characterized as Response regulatory 2.
+At position 115 to 212, the domain is characterized as Ig-like 2.
+At position 221 to 317, the domain is characterized as Ig-like 3.
+At position 18 to 274, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 155 to 352, the domain is characterized as CheB-type methylesterase.
+At position 32 to 97, the domain is characterized as Sushi 1.
+At position 98 to 157, the domain is characterized as Sushi 2.
+At position 160 to 217, the domain is characterized as Sushi 3.
+At position 267 to 466, the domain is characterized as VWFA.
+At position 474 to 754, the domain is characterized as Peptidase S1.
+At position 313 to 533, the domain is characterized as Sigma-54 factor interaction.
+At position 37 to 205, the domain is characterized as FAD-binding PCMH-type.
+At position 37 to 163, the domain is characterized as Ig-like V-type.
+At position 164 to 246, the domain is characterized as Ig-like C2-type 1.
+At position 258 to 341, the domain is characterized as Ig-like C2-type 2.
+At position 345 to 412, the domain is characterized as Ig-like C2-type 3.
+At position 6 to 130, the domain is characterized as MATH.
+At position 354 to 491, the domain is characterized as PA14 1.
+At position 502 to 640, the domain is characterized as PA14 2.
+At position 429 to 583, the domain is characterized as Helicase C-terminal.
+At position 133 to 239, the domain is characterized as THUMP.
+At position 137 to 466, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 530 to 846, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 65 to 235, the domain is characterized as Helicase ATP-binding.
+At position 245 to 405, the domain is characterized as Helicase C-terminal.
+At position 114 to 217, the domain is characterized as Ig-like.
+At position 13 to 299, the domain is characterized as Deacetylase sirtuin-type.
+At position 24 to 293, the domain is characterized as Protein kinase.
+At position 186 to 274, the domain is characterized as PDZ.
+At position 1 to 111, the domain is characterized as C2 NT-type.
+At position 232 to 273, the domain is characterized as CHCH.
+At position 217 to 253, the domain is characterized as EF-hand.
+At position 94 to 276, the domain is characterized as tr-type G.
+At position 397 to 509, the domain is characterized as PH.
+At position 551 to 807, the domain is characterized as Protein kinase.
+At position 12 to 130, the domain is characterized as EamA 1.
+At position 149 to 276, the domain is characterized as EamA 2.
+At position 12 to 141, the domain is characterized as VOC 1.
+At position 155 to 305, the domain is characterized as VOC 2.
+At position 1 to 24, the domain is characterized as EGF-like 1.
+At position 25 to 63, the domain is characterized as EGF-like 2.
+At position 66 to 104, the domain is characterized as EGF-like 3.
+At position 105 to 141, the domain is characterized as EGF-like 4.
+At position 143 to 180, the domain is characterized as EGF-like 5; calcium-binding.
+At position 182 to 219, the domain is characterized as EGF-like 6.
+At position 184 to 263, the domain is characterized as RRM.
+At position 108 to 666, the domain is characterized as Ferric oxidoreductase.
+At position 36 to 141, the domain is characterized as FAD-binding FR-type.
+At position 188 to 501, the domain is characterized as Protein kinase.
+At position 578 to 710, the domain is characterized as N-terminal Ras-GEF.
+At position 748 to 995, the domain is characterized as Ras-GEF.
+At position 25 to 512, the domain is characterized as Velvet.
+At position 579 to 640, the domain is characterized as Sushi 7.
+At position 641 to 702, the domain is characterized as Sushi 8.
+At position 812 to 945, the domain is characterized as C2.
+At position 461 to 632, the domain is characterized as Helicase C-terminal.
+At position 665 to 755, the domain is characterized as Dicer dsRNA-binding fold.
+At position 905 to 1040, the domain is characterized as PAZ.
+At position 1063 to 1219, the domain is characterized as RNase III 1.
+At position 1272 to 1447, the domain is characterized as RNase III 2.
+At position 1478 to 1556, the domain is characterized as DRBM.
+At position 841 to 891, the domain is characterized as G-patch.
+At position 159 to 232, the domain is characterized as HTH crp-type.
+At position 17 to 237, the domain is characterized as BAR.
+At position 28 to 88, the domain is characterized as v-SNARE coiled-coil homology.
+At position 99 to 253, the domain is characterized as UBC core.
+At position 845 to 1024, the domain is characterized as DOC.
+At position 20 to 63, the domain is characterized as CUE.
+At position 334 to 482, the domain is characterized as CRAL-TRIO.
+At position 130 to 228, the domain is characterized as PPIase FKBP-type.
+At position 60 to 100, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 22 to 140, the domain is characterized as CBM6.
+At position 164 to 458, the domain is characterized as GH26.
+At position 491 to 527, the domain is characterized as CBM10 1.
+At position 530 to 566, the domain is characterized as CBM10 2.
+At position 569 to 605, the domain is characterized as CBM10 3.
+At position 68 to 173, the domain is characterized as Thioredoxin.
+At position 329 to 592, the domain is characterized as EndoU.
+At position 2 to 146, the domain is characterized as Ferritin-like diiron.
+At position 151 to 184, the domain is characterized as Rubredoxin-like.
+At position 112 to 160, the domain is characterized as G-patch.
+At position 41 to 73, the domain is characterized as EF-hand 2.
+At position 22 to 254, the domain is characterized as Peptidase S1.
+At position 5 to 62, the domain is characterized as Tudor-knot.
+At position 135 to 329, the domain is characterized as MRG.
+At position 1 to 61, the domain is characterized as OBG-type G.
+At position 82 to 162, the domain is characterized as OCT.
+At position 16 to 167, the domain is characterized as MRH.
+At position 238 to 432, the domain is characterized as Peptidase M12B.
+At position 441 to 525, the domain is characterized as Disintegrin.
+At position 666 to 700, the domain is characterized as EGF-like.
+At position 119 to 355, the domain is characterized as Peptidase S1.
+At position 167 to 301, the domain is characterized as C2.
+At position 807 to 840, the domain is characterized as WW 1.
+At position 985 to 1018, the domain is characterized as WW 2.
+At position 1237 to 1572, the domain is characterized as HECT.
+At position 323 to 504, the domain is characterized as PCI.
+At position 1 to 254, the domain is characterized as Protein kinase.
+At position 59 to 111, the domain is characterized as bHLH.
+At position 178 to 414, the domain is characterized as MHD.
+At position 715 to 808, the domain is characterized as BRCT 1.
+At position 887 to 995, the domain is characterized as BRCT 2.
+At position 797 to 867, the domain is characterized as Bromo.
+At position 174 to 300, the domain is characterized as C-type lectin.
+At position 758 to 1268, the domain is characterized as FH1.
+At position 1283 to 1698, the domain is characterized as FH2.
+At position 85 to 124, the domain is characterized as EGF-like 1.
+At position 125 to 177, the domain is characterized as EGF-like 2; calcium-binding.
+At position 178 to 220, the domain is characterized as EGF-like 3; calcium-binding.
+At position 223 to 265, the domain is characterized as EGF-like 4.
+At position 530 to 744, the domain is characterized as TSP C-terminal.
+At position 624 to 694, the domain is characterized as PAS 1.
+At position 757 to 831, the domain is characterized as PAS 2.
+At position 908 to 1127, the domain is characterized as Histidine kinase.
+At position 6 to 81, the domain is characterized as Cytochrome b5 heme-binding.
+At position 684 to 773, the domain is characterized as ASD1.
+At position 1317 to 1611, the domain is characterized as ASD2.
+At position 66 to 171, the domain is characterized as PA.
+At position 14 to 344, the domain is characterized as PTS EIIC type-2.
+At position 380 to 468, the domain is characterized as PTS EIIB type-2.
+At position 1210 to 1621, the domain is characterized as DOCKER.
+At position 347 to 398, the domain is characterized as HAMP.
+At position 403 to 639, the domain is characterized as Methyl-accepting transducer.
+At position 50 to 138, the domain is characterized as ABM.
+At position 128 to 189, the domain is characterized as HTH cro/C1-type.
+At position 190 to 291, the domain is characterized as PpiC 1.
+At position 302 to 400, the domain is characterized as PpiC 2.
+At position 252 to 475, the domain is characterized as NR LBD.
+At position 85 to 396, the domain is characterized as IF rod.
+At position 318 to 365, the domain is characterized as F-box.
+At position 6 to 25, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 4 to 97, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 169 to 287, the domain is characterized as LTD.
+At position 70 to 325, the domain is characterized as PPM-type phosphatase.
+At position 483 to 582, the domain is characterized as BEN 1.
+At position 667 to 765, the domain is characterized as BEN 2.
+At position 48 to 727, the domain is characterized as Myosin motor.
+At position 731 to 751, the domain is characterized as IQ 1.
+At position 752 to 777, the domain is characterized as IQ 2.
+At position 785 to 980, the domain is characterized as TH1.
+At position 133 to 230, the domain is characterized as RRM.
+At position 29 to 147, the domain is characterized as WH1.
+At position 840 to 958, the domain is characterized as PH.
+At position 1121 to 1188, the domain is characterized as RBD.
+At position 1204 to 1293, the domain is characterized as PDZ.
+At position 1436 to 1630, the domain is characterized as DH.
+At position 669 to 728, the domain is characterized as S1 motif.
+At position 304 to 570, the domain is characterized as Glutamine amidotransferase type-1.
+At position 263 to 309, the domain is characterized as G-patch.
+At position 15 to 49, the domain is characterized as WW.
+At position 192 to 366, the domain is characterized as Helicase ATP-binding.
+At position 395 to 539, the domain is characterized as Helicase C-terminal.
+At position 599 to 942, the domain is characterized as TTL.
+At position 46 to 234, the domain is characterized as BPL/LPL catalytic.
+At position 14 to 112, the domain is characterized as HTH hxlR-type.
+At position 188 to 318, the domain is characterized as Nudix hydrolase.
+At position 123 to 240, the domain is characterized as EamA.
+At position 380 to 450, the domain is characterized as TRAM.
+At position 128 to 215, the domain is characterized as Ig-like C2-type.
+At position 750 to 785, the domain is characterized as EF-hand.
+At position 509 to 838, the domain is characterized as Kinesin motor.
+At position 594 to 681, the domain is characterized as WWE.
+At position 716 to 902, the domain is characterized as PARP catalytic.
+At position 20 to 166, the domain is characterized as SprT-like.
+At position 127 to 217, the domain is characterized as Ig-like C2-type 1.
+At position 243 to 274, the domain is characterized as Collagen-like 1.
+At position 301 to 360, the domain is characterized as Collagen-like 2.
+At position 383 to 405, the domain is characterized as Collagen-like 3.
+At position 501 to 544, the domain is characterized as Collagen-like 4.
+At position 545 to 583, the domain is characterized as Collagen-like 5.
+At position 730 to 769, the domain is characterized as Collagen-like 6.
+At position 798 to 980, the domain is characterized as VWFA 2.
+At position 1072 to 1122, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 439 to 630, the domain is characterized as B30.2/SPRY.
+At position 239 to 268, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 618 to 647, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 651 to 680, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 1 to 138, the domain is characterized as CID.
+At position 115 to 327, the domain is characterized as ATP-grasp.
+At position 328 to 548, the domain is characterized as Peptidase M12B.
+At position 549 to 636, the domain is characterized as Disintegrin.
+At position 637 to 689, the domain is characterized as TSP type-1 1.
+At position 918 to 978, the domain is characterized as TSP type-1 2.
+At position 979 to 1040, the domain is characterized as TSP type-1 3.
+At position 1042 to 1086, the domain is characterized as TSP type-1 4.
+At position 1090 to 1147, the domain is characterized as TSP type-1 5.
+At position 1163 to 1202, the domain is characterized as PLAC.
+At position 108 to 339, the domain is characterized as NR LBD.
+At position 370 to 436, the domain is characterized as S4 RNA-binding.
+At position 1 to 31, the domain is characterized as SUZ-C.
+At position 63 to 129, the domain is characterized as Sm.
+At position 1 to 106, the domain is characterized as VPS28 N-terminal.
+At position 110 to 206, the domain is characterized as VPS28 C-terminal.
+At position 299 to 531, the domain is characterized as NR LBD.
+At position 6 to 228, the domain is characterized as Radical SAM core.
+At position 53 to 334, the domain is characterized as Prephenate/arogenate dehydrogenase 1.
+At position 365 to 640, the domain is characterized as Prephenate/arogenate dehydrogenase 2.
+At position 282 to 502, the domain is characterized as Fibrinogen C-terminal.
+At position 134 to 392, the domain is characterized as Protein kinase.
+At position 435 to 470, the domain is characterized as EF-hand 1.
+At position 507 to 542, the domain is characterized as EF-hand 3.
+At position 545 to 576, the domain is characterized as EF-hand 4.
+At position 22 to 224, the domain is characterized as Cytochrome b561.
+At position 67 to 302, the domain is characterized as Radical SAM core.
+At position 204 to 230, the domain is characterized as EGF-like 2.
+At position 235 to 261, the domain is characterized as EGF-like 3.
+At position 293 to 324, the domain is characterized as EGF-like 5.
+At position 328 to 419, the domain is characterized as Fibronectin type-III 1.
+At position 505 to 596, the domain is characterized as Fibronectin type-III 3.
+At position 597 to 686, the domain is characterized as Fibronectin type-III 4.
+At position 777 to 864, the domain is characterized as Fibronectin type-III 6.
+At position 865 to 953, the domain is characterized as Fibronectin type-III 7.
+At position 954 to 1040, the domain is characterized as Fibronectin type-III 8.
+At position 1041 to 1129, the domain is characterized as Fibronectin type-III 9.
+At position 1127 to 1342, the domain is characterized as Fibrinogen C-terminal.
+At position 196 to 286, the domain is characterized as RRM.
+At position 340 to 583, the domain is characterized as START.
+At position 42 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 13 to 101, the domain is characterized as Acylphosphatase-like.
+At position 1 to 79, the domain is characterized as PUA.
+At position 29 to 348, the domain is characterized as Kinesin motor.
+At position 205 to 220, the domain is characterized as ShKT.
+At position 322 to 911, the domain is characterized as USP.
+At position 672 to 691, the domain is characterized as UIM 1.
+At position 766 to 785, the domain is characterized as UIM 2.
+At position 788 to 807, the domain is characterized as UIM 3.
+At position 41 to 218, the domain is characterized as FAD-binding PCMH-type.
+At position 4 to 130, the domain is characterized as HTH rrf2-type.
+At position 3 to 59, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 5 to 81, the domain is characterized as SH3 1.
+At position 82 to 139, the domain is characterized as SH3 2.
+At position 508 to 568, the domain is characterized as SH3 3.
+At position 273 to 470, the domain is characterized as B30.2/SPRY.
+At position 48 to 110, the domain is characterized as SH3.
+At position 122 to 211, the domain is characterized as SH2.
+At position 235 to 482, the domain is characterized as Protein kinase.
+At position 95 to 237, the domain is characterized as Clp R.
+At position 207 to 292, the domain is characterized as KH.
+At position 613 to 715, the domain is characterized as tRNA-binding.
+At position 22 to 311, the domain is characterized as Peptidase S8.
+At position 157 to 386, the domain is characterized as Lon N-terminal.
+At position 385 to 494, the domain is characterized as CULT.
+At position 60 to 180, the domain is characterized as BAH.
+At position 36 to 160, the domain is characterized as Galectin.
+At position 91 to 134, the domain is characterized as SpoVT-AbrB 2.
+At position 693 to 951, the domain is characterized as Protein kinase.
+At position 23 to 118, the domain is characterized as PB1.
+At position 242 to 307, the domain is characterized as KH.
+At position 88 to 381, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 84, the domain is characterized as PTS EIIB type-1.
+At position 102 to 465, the domain is characterized as PTS EIIC type-1.
+At position 495 to 599, the domain is characterized as PTS EIIA type-1.
+At position 212 to 602, the domain is characterized as Peptidase S53.
+At position 40 to 363, the domain is characterized as Protein kinase.
+At position 265 to 517, the domain is characterized as PPM-type phosphatase.
+At position 63 to 279, the domain is characterized as Radical SAM core.
+At position 639 to 955, the domain is characterized as Protein kinase.
+At position 1027 to 1158, the domain is characterized as Guanylate cyclase.
+At position 147 to 205, the domain is characterized as TRAM.
+At position 232 to 275, the domain is characterized as CUE.
+At position 18 to 288, the domain is characterized as Protein kinase.
+At position 15 to 290, the domain is characterized as Septin-type G.
+At position 114 to 377, the domain is characterized as Peptidase S8.
+At position 23 to 200, the domain is characterized as DHFR.
+At position 4 to 226, the domain is characterized as ABC transporter.
+At position 126 to 401, the domain is characterized as Peptidase S8.
+At position 284 to 422, the domain is characterized as SIS 1.
+At position 452 to 592, the domain is characterized as SIS 2.
+At position 1 to 230, the domain is characterized as Peptidase S1.
+At position 262 to 321, the domain is characterized as SH3.
+At position 26 to 169, the domain is characterized as MAM 1.
+At position 170 to 330, the domain is characterized as MAM 2.
+At position 341 to 500, the domain is characterized as MAM 3.
+At position 509 to 669, the domain is characterized as MAM 4.
+At position 34 to 287, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 87 to 505, the domain is characterized as Peptidase A1.
+At position 317 to 419, the domain is characterized as Saposin B-type.
+At position 620 to 795, the domain is characterized as PCI.
+At position 19 to 140, the domain is characterized as C-type lysozyme.
+At position 480 to 567, the domain is characterized as Ig-like C2-type 5.
+At position 122 to 254, the domain is characterized as Nudix hydrolase.
+At position 44 to 232, the domain is characterized as GH11.
+At position 562 to 655, the domain is characterized as BRCT 1.
+At position 654 to 742, the domain is characterized as BRCT 2.
+At position 741 to 823, the domain is characterized as BRCT 3.
+At position 137 to 239, the domain is characterized as Fe2OG dioxygenase.
+At position 192 to 335, the domain is characterized as EamA 2.
+At position 34 to 85, the domain is characterized as SMB.
+At position 12 to 96, the domain is characterized as MtN3/slv 1.
+At position 537 to 805, the domain is characterized as MHD.
+At position 29 to 79, the domain is characterized as LIM zinc-binding 1.
+At position 89 to 145, the domain is characterized as LIM zinc-binding 2.
+At position 272 to 395, the domain is characterized as Glutamine amidotransferase type-1.
+At position 128 to 238, the domain is characterized as SET.
+At position 24 to 75, the domain is characterized as SMB.
+At position 74 to 125, the domain is characterized as TSP type-1.
+At position 51 to 116, the domain is characterized as SAM.
+At position 181 to 452, the domain is characterized as Protein kinase.
+At position 112 to 203, the domain is characterized as CARD.
+At position 13 to 130, the domain is characterized as C-type lectin.
+At position 3 to 329, the domain is characterized as Kinesin motor.
+At position 130 to 220, the domain is characterized as PpiC.
+At position 1029 to 1165, the domain is characterized as RanBD1 1.
+At position 1326 to 1462, the domain is characterized as RanBD1 2.
+At position 1693 to 1743, the domain is characterized as GRIP.
+At position 137 to 241, the domain is characterized as AB hydrolase-1.
+At position 178 to 227, the domain is characterized as bHLH.
+At position 43 to 215, the domain is characterized as VWFA.
+At position 42 to 178, the domain is characterized as 6-Cys 1.
+At position 181 to 326, the domain is characterized as 6-Cys 2.
+At position 35 to 252, the domain is characterized as Protein kinase.
+At position 107 to 151, the domain is characterized as bZIP.
+At position 176 to 389, the domain is characterized as DOG1.
+At position 36 to 169, the domain is characterized as VIT.
+At position 316 to 496, the domain is characterized as VWFA.
+At position 132 to 243, the domain is characterized as Ig-like C2-type 1.
+At position 253 to 340, the domain is characterized as Ig-like C2-type 2.
+At position 344 to 436, the domain is characterized as Ig-like C2-type 3.
+At position 440 to 529, the domain is characterized as Ig-like C2-type 4.
+At position 536 to 624, the domain is characterized as Ig-like C2-type 5.
+At position 632 to 728, the domain is characterized as Fibronectin type-III 1.
+At position 760 to 851, the domain is characterized as Fibronectin type-III 2.
+At position 167 to 202, the domain is characterized as QLQ.
+At position 441 to 513, the domain is characterized as HSA.
+At position 741 to 906, the domain is characterized as Helicase ATP-binding.
+At position 1059 to 1221, the domain is characterized as Helicase C-terminal.
+At position 1406 to 1476, the domain is characterized as Bromo.
+At position 133 to 439, the domain is characterized as NB-ARC.
+At position 1118 to 1180, the domain is characterized as SH3.
+At position 12 to 202, the domain is characterized as Glutamine amidotransferase type-1.
+At position 11 to 96, the domain is characterized as bHLH.
+At position 49 to 250, the domain is characterized as Rho-GAP.
+At position 306 to 578, the domain is characterized as Protein kinase.
+At position 155 to 616, the domain is characterized as TBDR beta-barrel.
+At position 20 to 114, the domain is characterized as PH.
+At position 385 to 614, the domain is characterized as START.
+At position 85 to 213, the domain is characterized as GST C-terminal.
+At position 271 to 430, the domain is characterized as EF-1-gamma C-terminal.
+At position 107 to 158, the domain is characterized as SANT.
+At position 344 to 442, the domain is characterized as SWIRM.
+At position 548 to 680, the domain is characterized as MPN.
+At position 11 to 295, the domain is characterized as Protein kinase.
+At position 359 to 514, the domain is characterized as Helicase C-terminal.
+At position 522 to 576, the domain is characterized as LRRCT.
+At position 632 to 775, the domain is characterized as TIR.
+At position 1 to 200, the domain is characterized as SMP-LTD.
+At position 165 to 246, the domain is characterized as Ig-like C2-type 1.
+At position 57 to 137, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 210 to 268, the domain is characterized as CTLH.
+At position 33 to 120, the domain is characterized as PDZ 1.
+At position 307 to 385, the domain is characterized as PDZ 2.
+At position 509 to 590, the domain is characterized as PDZ 3.
+At position 604 to 669, the domain is characterized as SH3.
+At position 678 to 876, the domain is characterized as Guanylate kinase-like.
+At position 122 to 352, the domain is characterized as Radical SAM core.
+At position 228 to 324, the domain is characterized as CRM 1.
+At position 346 to 442, the domain is characterized as CRM 2.
+At position 47 to 117, the domain is characterized as KH type-2.
+At position 37 to 166, the domain is characterized as VOC.
+At position 170 to 252, the domain is characterized as RRM 1.
+At position 374 to 451, the domain is characterized as RRM 2.
+At position 455 to 529, the domain is characterized as RRM 3.
+At position 777 to 956, the domain is characterized as SPOC.
+At position 324 to 403, the domain is characterized as Ubiquitin-like.
+At position 504 to 563, the domain is characterized as HTH myb-type.
+At position 852 to 1072, the domain is characterized as Histidine kinase.
+At position 1119 to 1234, the domain is characterized as Response regulatory.
+At position 1266 to 1365, the domain is characterized as HTH araC/xylS-type.
+At position 103 to 138, the domain is characterized as UVR.
+At position 452 to 556, the domain is characterized as Zinc-hook.
+At position 377 to 642, the domain is characterized as Radical SAM core.
+At position 175 to 221, the domain is characterized as F-box.
+At position 30 to 291, the domain is characterized as Protein kinase.
+At position 307 to 532, the domain is characterized as NR LBD.
+At position 21 to 449, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 953 to 1245, the domain is characterized as PKS/mFAS DH.
+At position 2336 to 2413, the domain is characterized as Carrier.
+At position 182 to 228, the domain is characterized as F-box.
+At position 75 to 150, the domain is characterized as Rho RNA-BD.
+At position 125 to 371, the domain is characterized as Lon N-terminal.
+At position 760 to 951, the domain is characterized as Lon proteolytic.
+At position 84 to 162, the domain is characterized as RRM 1.
+At position 184 to 260, the domain is characterized as RRM 2.
+At position 1 to 156, the domain is characterized as TCTP.
+At position 51 to 100, the domain is characterized as bHLH.
+At position 44 to 115, the domain is characterized as BIG2.
+At position 291 to 561, the domain is characterized as Radical SAM core.
+At position 30 to 112, the domain is characterized as Lipoyl-binding.
+At position 279 to 299, the domain is characterized as ELK.
+At position 243 to 304, the domain is characterized as bZIP.
+At position 293 to 500, the domain is characterized as Peptidase M12A.
+At position 504 to 540, the domain is characterized as ShKT.
+At position 22 to 77, the domain is characterized as Sushi 1; atypical; lacks a Cys.
+At position 79 to 135, the domain is characterized as Sushi 2.
+At position 136 to 270, the domain is characterized as Fatty acid hydroxylase.
+At position 154 to 682, the domain is characterized as USP.
+At position 684 to 777, the domain is characterized as DUSP 1.
+At position 785 to 888, the domain is characterized as DUSP 2.
+At position 32 to 299, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 596 to 752, the domain is characterized as Exonuclease.
+At position 267 to 404, the domain is characterized as MPN.
+At position 107 to 444, the domain is characterized as PUM-HD.
+At position 17 to 81, the domain is characterized as KH 1.
+At position 139 to 204, the domain is characterized as KH 2.
+At position 248 to 316, the domain is characterized as KH 3.
+At position 16 to 171, the domain is characterized as N-acetyltransferase.
+At position 158 to 276, the domain is characterized as Response regulatory.
+At position 587 to 674, the domain is characterized as BRCT.
+At position 187 to 448, the domain is characterized as NR LBD.
+At position 8 to 173, the domain is characterized as PPIase cyclophilin-type.
+At position 129 to 409, the domain is characterized as Peptidase S8.
+At position 22 to 142, the domain is characterized as MSP.
+At position 38 to 144, the domain is characterized as HD.
+At position 177 to 270, the domain is characterized as Fibronectin type-III.
+At position 30 to 71, the domain is characterized as JmjN.
+At position 232 to 398, the domain is characterized as JmjC.
+At position 58 to 88, the domain is characterized as EF-hand 2.
+At position 173 to 323, the domain is characterized as N-acetyltransferase 2.
+At position 50 to 238, the domain is characterized as BPL/LPL catalytic.
+At position 96 to 332, the domain is characterized as Radical SAM core.
+At position 19 to 78, the domain is characterized as Chromo.
+At position 115 to 172, the domain is characterized as Chromo 2; shadow subtype.
+At position 64 to 282, the domain is characterized as Radical SAM core.
+At position 172 to 206, the domain is characterized as SAP.
+At position 99 to 338, the domain is characterized as Radical SAM core.
+At position 23 to 108, the domain is characterized as Cytochrome c 1.
+At position 118 to 210, the domain is characterized as Cytochrome c 2.
+At position 937 to 1009, the domain is characterized as Bromo.
+At position 1128 to 1239, the domain is characterized as PH.
+At position 3 to 414, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 129 to 302, the domain is characterized as Helicase ATP-binding.
+At position 331 to 478, the domain is characterized as Helicase C-terminal.
+At position 242 to 401, the domain is characterized as JmjC.
+At position 597 to 717, the domain is characterized as C2 2.
+At position 330 to 659, the domain is characterized as PDEase.
+At position 168 to 315, the domain is characterized as Ricin B-type lectin.
+At position 29 to 270, the domain is characterized as ABC transporter 1.
+At position 280 to 524, the domain is characterized as ABC transporter 2.
+At position 251 to 382, the domain is characterized as MPN.
+At position 403 to 489, the domain is characterized as RRM.
+At position 1029 to 1146, the domain is characterized as SET.
+At position 1154 to 1170, the domain is characterized as Post-SET.
+At position 32 to 314, the domain is characterized as FERM.
+At position 428 to 462, the domain is characterized as PLD phosphodiesterase.
+At position 89 to 359, the domain is characterized as Lon N-terminal.
+At position 784 to 971, the domain is characterized as Lon proteolytic.
+At position 36 to 208, the domain is characterized as Helicase ATP-binding.
+At position 235 to 378, the domain is characterized as Helicase C-terminal.
+At position 28 to 70, the domain is characterized as CHCH.
+At position 353 to 490, the domain is characterized as NYN.
+At position 791 to 870, the domain is characterized as RRM.
+At position 875 to 949, the domain is characterized as HTH OST-type 1.
+At position 1003 to 1079, the domain is characterized as HTH OST-type 2.
+At position 1099 to 1173, the domain is characterized as HTH OST-type 3.
+At position 1175 to 1250, the domain is characterized as HTH OST-type 4.
+At position 1259 to 1334, the domain is characterized as HTH OST-type 5.
+At position 1335 to 1410, the domain is characterized as HTH OST-type 6.
+At position 1411 to 1485, the domain is characterized as HTH OST-type 7.
+At position 290 to 369, the domain is characterized as B5.
+At position 452 to 652, the domain is characterized as Helicase ATP-binding.
+At position 891 to 1056, the domain is characterized as Helicase C-terminal.
+At position 384 to 863, the domain is characterized as ABC transporter.
+At position 27 to 226, the domain is characterized as Pentraxin (PTX).
+At position 186 to 383, the domain is characterized as Peptidase M12B.
+At position 391 to 479, the domain is characterized as Disintegrin.
+At position 622 to 654, the domain is characterized as EGF-like.
+At position 401 to 452, the domain is characterized as FBD.
+At position 86 to 396, the domain is characterized as IF rod.
+At position 1640 to 1818, the domain is characterized as VWFD.
+At position 611 to 725, the domain is characterized as SMC hinge.
+At position 102 to 275, the domain is characterized as Helicase ATP-binding.
+At position 303 to 459, the domain is characterized as Helicase C-terminal.
+At position 107 to 142, the domain is characterized as EF-hand 2.
+At position 150 to 231, the domain is characterized as PRC barrel.
+At position 34 to 158, the domain is characterized as PLAT.
+At position 161 to 859, the domain is characterized as Lipoxygenase.
+At position 8 to 178, the domain is characterized as Flavodoxin-like.
+At position 179 to 370, the domain is characterized as Glutamine amidotransferase type-1.
+At position 168 to 431, the domain is characterized as MIF4G 1.
+At position 569 to 758, the domain is characterized as MIF4G 2.
+At position 773 to 986, the domain is characterized as MIF4G 3.
+At position 93 to 268, the domain is characterized as Helicase ATP-binding.
+At position 280 to 441, the domain is characterized as Helicase C-terminal.
+At position 316 to 453, the domain is characterized as ZU5.
+At position 653 to 723, the domain is characterized as SH3 2.
+At position 54 to 239, the domain is characterized as Helicase ATP-binding.
+At position 264 to 419, the domain is characterized as Helicase C-terminal.
+At position 7 to 153, the domain is characterized as PPIase cyclophilin-type.
+At position 36 to 259, the domain is characterized as Cache.
+At position 139 to 243, the domain is characterized as C-type lectin.
+At position 47 to 83, the domain is characterized as EGF-like 1.
+At position 135 to 357, the domain is characterized as Peptidase S1.
+At position 297 to 538, the domain is characterized as Glutamine amidotransferase type-1.
+At position 17 to 284, the domain is characterized as Protein kinase 1.
+At position 285 to 353, the domain is characterized as AGC-kinase C-terminal.
+At position 382 to 653, the domain is characterized as Protein kinase 2.
+At position 57 to 215, the domain is characterized as Thioredoxin.
+At position 210 to 449, the domain is characterized as FAD-binding FR-type.
+At position 94 to 189, the domain is characterized as Rieske.
+At position 124 to 224, the domain is characterized as PB1.
+At position 1 to 128, the domain is characterized as MGS-like.
+At position 555 to 608, the domain is characterized as bHLH.
+At position 59 to 112, the domain is characterized as J.
+At position 1 to 87, the domain is characterized as Reverse transcriptase.
+At position 43 to 359, the domain is characterized as IF rod.
+At position 24 to 309, the domain is characterized as ABC transporter.
+At position 673 to 739, the domain is characterized as Dockerin.
+At position 995 to 1100, the domain is characterized as Calponin-homology (CH).
+At position 371 to 464, the domain is characterized as Fibronectin type-III.
+At position 11 to 199, the domain is characterized as KARI N-terminal Rossmann.
+At position 200 to 347, the domain is characterized as KARI C-terminal knotted.
+At position 205 to 429, the domain is characterized as tr-type G.
+At position 512 to 924, the domain is characterized as USP.
+At position 988 to 1158, the domain is characterized as Exonuclease.
+At position 25 to 128, the domain is characterized as Ig-like V-type.
+At position 129 to 209, the domain is characterized as Ig-like C2-type.
+At position 30 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 133 to 216, the domain is characterized as Ig-like C2-type 2.
+At position 221 to 325, the domain is characterized as Fibronectin type-III 1.
+At position 330 to 422, the domain is characterized as Fibronectin type-III 2.
+At position 530 to 801, the domain is characterized as Protein kinase.
+At position 360 to 446, the domain is characterized as RRM.
+At position 165 to 375, the domain is characterized as ATP-grasp.
+At position 29 to 182, the domain is characterized as SIS.
+At position 587 to 663, the domain is characterized as BRCT.
+At position 257 to 418, the domain is characterized as Helicase C-terminal.
+At position 109 to 311, the domain is characterized as ATP-grasp.
+At position 824 to 887, the domain is characterized as SAM.
+At position 82 to 211, the domain is characterized as SET.
+At position 15 to 106, the domain is characterized as ABM.
+At position 31 to 119, the domain is characterized as WSC.
+At position 5 to 51, the domain is characterized as SpoVT-AbrB.
+At position 284 to 460, the domain is characterized as CRAL-TRIO.
+At position 522 to 641, the domain is characterized as GOLD.
+At position 168 to 279, the domain is characterized as PH.
+At position 336 to 434, the domain is characterized as SH2.
+At position 263 to 301, the domain is characterized as PAS.
+At position 85 to 132, the domain is characterized as Fibronectin type-II 2.
+At position 8 to 349, the domain is characterized as DhaK.
+At position 384 to 580, the domain is characterized as DhaL.
+At position 214 to 283, the domain is characterized as S1 motif.
+At position 525 to 688, the domain is characterized as Helicase ATP-binding.
+At position 706 to 886, the domain is characterized as Helicase C-terminal.
+At position 373 to 556, the domain is characterized as Helicase ATP-binding.
+At position 570 to 740, the domain is characterized as Helicase C-terminal.
+At position 19 to 32, the domain is characterized as Fibronectin type-II.
+At position 26 to 185, the domain is characterized as RabBD.
+At position 668 to 754, the domain is characterized as PDZ.
+At position 805 to 928, the domain is characterized as C2 1.
+At position 1257 to 1375, the domain is characterized as C2 2.
+At position 225 to 387, the domain is characterized as TrmE-type G.
+At position 18 to 72, the domain is characterized as TSP type-1 1.
+At position 77 to 117, the domain is characterized as LDL-receptor class A.
+At position 115 to 480, the domain is characterized as MACPF.
+At position 481 to 511, the domain is characterized as EGF-like.
+At position 531 to 572, the domain is characterized as TSP type-1 2.
+At position 122 to 322, the domain is characterized as VWFA.
+At position 386 to 600, the domain is characterized as Alpha-type protein kinase.
+At position 150 to 341, the domain is characterized as Helicase ATP-binding.
+At position 386 to 533, the domain is characterized as Helicase C-terminal.
+At position 985 to 1140, the domain is characterized as ZU5 1.
+At position 1142 to 1289, the domain is characterized as ZU5 2.
+At position 1478 to 1562, the domain is characterized as Death.
+At position 449 to 752, the domain is characterized as Protein kinase.
+At position 29 to 81, the domain is characterized as HTH myb-type 1.
+At position 82 to 136, the domain is characterized as HTH myb-type 2.
+At position 969 to 1087, the domain is characterized as PLAT 8.
+At position 1100 to 1225, the domain is characterized as PLAT 9.
+At position 1254 to 1372, the domain is characterized as PLAT 10.
+At position 1421 to 1539, the domain is characterized as PLAT 11.
+At position 1552 to 1667, the domain is characterized as PLAT 12.
+At position 1679 to 1797, the domain is characterized as PLAT 13.
+At position 1810 to 1931, the domain is characterized as PLAT 14.
+At position 1948 to 2064, the domain is characterized as PLAT 15.
+At position 99 to 132, the domain is characterized as Orange.
+At position 43 to 267, the domain is characterized as Radical SAM core.
+At position 296 to 577, the domain is characterized as Reverse transcriptase.
+At position 55 to 128, the domain is characterized as S1 motif 1.
+At position 144 to 211, the domain is characterized as S1 motif 2.
+At position 231 to 299, the domain is characterized as S1 motif 3.
+At position 316 to 385, the domain is characterized as S1 motif 4.
+At position 3 to 180, the domain is characterized as DHFR.
+At position 218 to 406, the domain is characterized as Glutamine amidotransferase type-1.
+At position 9 to 221, the domain is characterized as Glutamine amidotransferase type-1.
+At position 37 to 161, the domain is characterized as OTU.
+At position 202 to 250, the domain is characterized as UBA-like.
+At position 213 to 271, the domain is characterized as bZIP.
+At position 507 to 800, the domain is characterized as Protein kinase.
+At position 873 to 1003, the domain is characterized as Guanylate cyclase.
+At position 1575 to 1673, the domain is characterized as PH.
+At position 63 to 207, the domain is characterized as SCP.
+At position 10 to 74, the domain is characterized as J.
+At position 113 to 194, the domain is characterized as PRC barrel.
+At position 7 to 96, the domain is characterized as MtN3/slv 1.
+At position 197 to 246, the domain is characterized as bHLH.
+At position 54 to 119, the domain is characterized as NAC-A/B.
+At position 383 to 737, the domain is characterized as Tyrosine-protein phosphatase.
+At position 74 to 127, the domain is characterized as TSP type-1.
+At position 295 to 345, the domain is characterized as Myb-like.
+At position 3 to 76, the domain is characterized as RRM.
+At position 60 to 347, the domain is characterized as Protein kinase.
+At position 581 to 660, the domain is characterized as BRCT.
+At position 24 to 137, the domain is characterized as Thioredoxin 1.
+At position 344 to 475, the domain is characterized as Thioredoxin 2.
+At position 10 to 108, the domain is characterized as BMC circularly permuted.
+At position 15 to 94, the domain is characterized as GS beta-grasp.
+At position 101 to 364, the domain is characterized as GS catalytic.
+At position 96 to 194, the domain is characterized as FAD-binding FR-type.
+At position 438 to 742, the domain is characterized as Protein kinase.
+At position 105 to 202, the domain is characterized as HD.
+At position 450 to 511, the domain is characterized as TGS.
+At position 714 to 788, the domain is characterized as ACT.
+At position 35 to 69, the domain is characterized as SAP.
+At position 2517 to 2637, the domain is characterized as BAH.
+At position 12 to 192, the domain is characterized as Exonuclease.
+At position 108 to 185, the domain is characterized as RRM.
+At position 15 to 217, the domain is characterized as ABC transmembrane type-1.
+At position 38 to 326, the domain is characterized as Protein kinase.
+At position 259 to 372, the domain is characterized as PAZ.
+At position 541 to 851, the domain is characterized as Piwi.
+At position 96 to 384, the domain is characterized as Peptidase A1.
+At position 25 to 61, the domain is characterized as CBM1.
+At position 161 to 376, the domain is characterized as Histidine kinase.
+At position 291 to 495, the domain is characterized as MCM.
+At position 633 to 668, the domain is characterized as EF-hand.
+At position 193 to 299, the domain is characterized as GTD-binding.
+At position 8 to 304, the domain is characterized as Protein kinase.
+At position 134 to 336, the domain is characterized as ATP-grasp.
+At position 1 to 221, the domain is characterized as ABC transporter 1.
+At position 289 to 516, the domain is characterized as ABC transporter 2.
+At position 7 to 86, the domain is characterized as RRM.
+At position 488 to 546, the domain is characterized as SH3.
+At position 8 to 196, the domain is characterized as PPIase cyclophilin-type.
+At position 11 to 219, the domain is characterized as AIG1-type G.
+At position 29 to 90, the domain is characterized as TRAM.
+At position 662 to 731, the domain is characterized as S1 motif.
+At position 43 to 146, the domain is characterized as Plastocyanin-like 1.
+At position 192 to 301, the domain is characterized as Plastocyanin-like 2.
+At position 392 to 514, the domain is characterized as Plastocyanin-like 3.
+At position 190 to 378, the domain is characterized as PPIase cyclophilin-type.
+At position 77 to 259, the domain is characterized as Helicase ATP-binding.
+At position 293 to 477, the domain is characterized as Helicase C-terminal.
+At position 154 to 397, the domain is characterized as Radical SAM core.
+At position 400 to 467, the domain is characterized as TRAM.
+At position 426 to 534, the domain is characterized as PAZ.
+At position 774 to 1081, the domain is characterized as Piwi.
+At position 22 to 109, the domain is characterized as Acylphosphatase-like.
+At position 296 to 331, the domain is characterized as GRAM 1.
+At position 359 to 520, the domain is characterized as PH.
+At position 816 to 880, the domain is characterized as GRAM 2.
+At position 220 to 316, the domain is characterized as CRM 1.
+At position 663 to 763, the domain is characterized as CRM 3.
+At position 27 to 242, the domain is characterized as YjeF N-terminal.
+At position 30 to 653, the domain is characterized as Vitellogenin.
+At position 1 to 103, the domain is characterized as PTS EIIB type-3.
+At position 177 to 236, the domain is characterized as HTH myb-type.
+At position 141 to 340, the domain is characterized as TRUD.
+At position 16 to 198, the domain is characterized as Guanylate kinase-like.
+At position 93 to 212, the domain is characterized as GST C-terminal.
+At position 34 to 102, the domain is characterized as KH 1.
+At position 120 to 188, the domain is characterized as KH 2.
+At position 233 to 300, the domain is characterized as KH 3.
+At position 1 to 59, the domain is characterized as IBB.
+At position 1 to 186, the domain is characterized as Peptidase M12A.
+At position 199 to 301, the domain is characterized as PB1.
+At position 30 to 309, the domain is characterized as tr-type G.
+At position 2 to 219, the domain is characterized as ABC transporter.
+At position 34 to 225, the domain is characterized as PBC.
+At position 8 to 117, the domain is characterized as Tudor 1.
+At position 502 to 649, the domain is characterized as Helicase ATP-binding.
+At position 929 to 1043, the domain is characterized as Tudor 2.
+At position 1317 to 1401, the domain is characterized as CS.
+At position 8 to 286, the domain is characterized as CN hydrolase.
+At position 38 to 154, the domain is characterized as Cadherin 1.
+At position 155 to 255, the domain is characterized as Cadherin 2.
+At position 39 to 142, the domain is characterized as Gnk2-homologous 1.
+At position 148 to 265, the domain is characterized as Gnk2-homologous 2.
+At position 21 to 214, the domain is characterized as RNase H type-2.
+At position 1724 to 1753, the domain is characterized as IQ.
+At position 127 to 162, the domain is characterized as UVR.
+At position 8 to 240, the domain is characterized as ABC transporter.
+At position 5 to 406, the domain is characterized as BRO1.
+At position 8 to 88, the domain is characterized as Cytochrome b5 heme-binding.
+At position 267 to 382, the domain is characterized as Sox C-terminal.
+At position 13 to 68, the domain is characterized as HTH cro/C1-type.
+At position 143 to 376, the domain is characterized as Radical SAM core.
+At position 65 to 155, the domain is characterized as GS beta-grasp.
+At position 159 to 589, the domain is characterized as GS catalytic.
+At position 1140 to 1268, the domain is characterized as C2 2.
+At position 1552 to 1695, the domain is characterized as MHD1.
+At position 1798 to 1954, the domain is characterized as MHD2.
+At position 1969 to 2097, the domain is characterized as C2 3.
+At position 860 to 1157, the domain is characterized as ABC transmembrane type-1 2.
+At position 56 to 136, the domain is characterized as IGFBP N-terminal.
+At position 127 to 177, the domain is characterized as Kazal-like.
+At position 179 to 276, the domain is characterized as Ig-like C2-type.
+At position 253 to 288, the domain is characterized as GRAM 1.
+At position 323 to 471, the domain is characterized as PH.
+At position 854 to 920, the domain is characterized as GRAM 2.
+At position 188 to 471, the domain is characterized as ABC transmembrane type-1.
+At position 504 to 740, the domain is characterized as ABC transporter.
+At position 105 to 247, the domain is characterized as PI-PLC X-box.
+At position 267 to 385, the domain is characterized as PI-PLC Y-box.
+At position 389 to 513, the domain is characterized as C2.
+At position 11 to 138, the domain is characterized as C-type lectin.
+At position 74 to 142, the domain is characterized as BTB.
+At position 2 to 351, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 229 to 348, the domain is characterized as PAZ.
+At position 517 to 818, the domain is characterized as Piwi.
+At position 205 to 263, the domain is characterized as TRAM.
+At position 11 to 442, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 958 to 1276, the domain is characterized as PKS/mFAS DH.
+At position 2585 to 2662, the domain is characterized as Carrier.
+At position 146 to 399, the domain is characterized as ABC transporter 1.
+At position 124 to 199, the domain is characterized as Ig-like C2-type.
+At position 187 to 279, the domain is characterized as CS.
+At position 591 to 620, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 51 to 170, the domain is characterized as C-type lectin.
+At position 534 to 647, the domain is characterized as SMC hinge.
+At position 149 to 588, the domain is characterized as Urease.
+At position 108 to 255, the domain is characterized as Tyrosine-protein phosphatase.
+At position 148 to 340, the domain is characterized as CheB-type methylesterase.
+At position 9 to 85, the domain is characterized as RRM 1.
+At position 97 to 175, the domain is characterized as RRM 2.
+At position 205 to 277, the domain is characterized as RRM 3.
+At position 1 to 19, the domain is characterized as bZIP.
+At position 215 to 474, the domain is characterized as NR LBD.
+At position 6 to 136, the domain is characterized as RNase III.
+At position 194 to 280, the domain is characterized as KH type-2.
+At position 29 to 165, the domain is characterized as VHS.
+At position 192 to 317, the domain is characterized as GAT.
+At position 440 to 556, the domain is characterized as GAE.
+At position 298 to 496, the domain is characterized as PCI.
+At position 183 to 213, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 111 to 187, the domain is characterized as PRC barrel.
+At position 103 to 222, the domain is characterized as BAH.
+At position 188 to 276, the domain is characterized as RCK C-terminal 1.
+At position 3 to 40, the domain is characterized as Gnk2-homologous.
+At position 203 to 394, the domain is characterized as Peptidase M12A.
+At position 380 to 433, the domain is characterized as EGF-like.
+At position 434 to 554, the domain is characterized as CUB.
+At position 610 to 647, the domain is characterized as ShKT.
+At position 160 to 354, the domain is characterized as Helicase ATP-binding.
+At position 400 to 586, the domain is characterized as Helicase C-terminal.
+At position 164 to 281, the domain is characterized as C2.
+At position 203 to 291, the domain is characterized as Ig-like C1-type.
+At position 85 to 146, the domain is characterized as SH3.
+At position 152 to 249, the domain is characterized as SH2.
+At position 106 to 216, the domain is characterized as TBDR plug.
+At position 221 to 758, the domain is characterized as TBDR beta-barrel.
+At position 47 to 155, the domain is characterized as Ig-like C2-type.
+At position 164 to 266, the domain is characterized as Link 1.
+At position 271 to 363, the domain is characterized as Link 2.
+At position 198 to 264, the domain is characterized as KH.
+At position 193 to 445, the domain is characterized as Protein kinase.
+At position 80 to 240, the domain is characterized as TNase-like.
+At position 479 to 545, the domain is characterized as HMA 6.
+At position 555 to 621, the domain is characterized as HMA 7.
+At position 3 to 184, the domain is characterized as YrdC-like.
+At position 248 to 422, the domain is characterized as TrmE-type G.
+At position 581 to 655, the domain is characterized as RRM 1.
+At position 942 to 1011, the domain is characterized as RRM 2.
+At position 232 to 352, the domain is characterized as C-type lectin.
+At position 8 to 190, the domain is characterized as Clp R.
+At position 646 to 952, the domain is characterized as Autotransporter.
+At position 4 to 239, the domain is characterized as PABS.
+At position 329 to 536, the domain is characterized as Peptidase M12A.
+At position 539 to 575, the domain is characterized as ShKT.
+At position 42 to 112, the domain is characterized as KRAB.
+At position 930 to 1049, the domain is characterized as MGS-like.
+At position 296 to 517, the domain is characterized as Histidine kinase.
+At position 23 to 367, the domain is characterized as USP.
+At position 328 to 501, the domain is characterized as tr-type G.
+At position 7 to 127, the domain is characterized as Arf-GAP.
+At position 990 to 1194, the domain is characterized as Alpha-type protein kinase.
+At position 13 to 90, the domain is characterized as RRM.
+At position 35 to 110, the domain is characterized as Lipoyl-binding.
+At position 168 to 206, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 141 to 375, the domain is characterized as Radical SAM core.
+At position 134 to 219, the domain is characterized as Ig-like C2-type 1.
+At position 224 to 310, the domain is characterized as Ig-like C2-type 2.
+At position 112 to 304, the domain is characterized as 3'-5' exonuclease.
+At position 49 to 117, the domain is characterized as SH3.
+At position 123 to 215, the domain is characterized as SH2.
+At position 241 to 498, the domain is characterized as Protein kinase.
+At position 747 to 776, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 802 to 831, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1248 to 1391, the domain is characterized as Flavodoxin-like.
+At position 1425 to 1650, the domain is characterized as FAD-binding FR-type.
+At position 6 to 196, the domain is characterized as DPCK.
+At position 29 to 216, the domain is characterized as GH11.
+At position 11 to 153, the domain is characterized as VOC 1.
+At position 166 to 301, the domain is characterized as VOC 2.
+At position 23 to 97, the domain is characterized as REM-1.
+At position 108 to 457, the domain is characterized as BRO1.
+At position 513 to 592, the domain is characterized as PDZ.
+At position 631 to 765, the domain is characterized as OTU.
+At position 25 to 134, the domain is characterized as sHSP 1.
+At position 439 to 532, the domain is characterized as sHSP 2.
+At position 46 to 244, the domain is characterized as Velvet.
+At position 14 to 440, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 2279 to 2357, the domain is characterized as Carrier.
+At position 23 to 161, the domain is characterized as Thioredoxin.
+At position 1233 to 1411, the domain is characterized as Rho-GAP.
+At position 546 to 777, the domain is characterized as ABC transporter 1.
+At position 1379 to 1603, the domain is characterized as ABC transporter 2.
+At position 55 to 148, the domain is characterized as BLUF 1.
+At position 204 to 332, the domain is characterized as Guanylate cyclase 1.
+At position 467 to 559, the domain is characterized as BLUF 2.
+At position 615 to 744, the domain is characterized as Guanylate cyclase 2.
+At position 174 to 268, the domain is characterized as 5'-3' exonuclease.
+At position 302 to 470, the domain is characterized as 3'-5' exonuclease.
+At position 75 to 386, the domain is characterized as Peptidase A1.
+At position 165 to 232, the domain is characterized as KH.
+At position 11 to 74, the domain is characterized as HMA 1.
+At position 89 to 152, the domain is characterized as HMA 2.
+At position 23 to 173, the domain is characterized as Ephrin RBD.
+At position 997 to 1119, the domain is characterized as RCK N-terminal.
+At position 53 to 87, the domain is characterized as EGF-like 1.
+At position 95 to 130, the domain is characterized as EGF-like 2.
+At position 155 to 191, the domain is characterized as EGF-like 3.
+At position 215 to 249, the domain is characterized as EGF-like 4.
+At position 302 to 339, the domain is characterized as EGF-like 5.
+At position 351 to 382, the domain is characterized as EGF-like 6.
+At position 87 to 172, the domain is characterized as APO 1.
+At position 228 to 313, the domain is characterized as APO 2.
+At position 87 to 197, the domain is characterized as PH.
+At position 287 to 476, the domain is characterized as Rho-GAP.
+At position 56 to 498, the domain is characterized as Trm1 methyltransferase.
+At position 1 to 10, the domain is characterized as Runt.
+At position 165 to 266, the domain is characterized as BACK.
+At position 31 to 178, the domain is characterized as VWFA 1.
+At position 289 to 474, the domain is characterized as VWFA 2.
+At position 491 to 618, the domain is characterized as C-type lectin.
+At position 547 to 628, the domain is characterized as G5 2.
+At position 139 to 257, the domain is characterized as Ig-like C2-type.
+At position 45 to 162, the domain is characterized as FZ.
+At position 178 to 300, the domain is characterized as NTR.
+At position 50 to 98, the domain is characterized as SMB.
+At position 313 to 366, the domain is characterized as TSP type-1.
+At position 88 to 393, the domain is characterized as Peptidase A1.
+At position 818 to 912, the domain is characterized as Fibronectin type-III 3.
+At position 92 to 399, the domain is characterized as Peptidase A1.
+At position 344 to 437, the domain is characterized as BRCT.
+At position 329 to 392, the domain is characterized as SH3.
+At position 756 to 874, the domain is characterized as CNA-B 1.
+At position 875 to 984, the domain is characterized as CNA-B 2.
+At position 6 to 66, the domain is characterized as HTH iclR-type.
+At position 477 to 576, the domain is characterized as CBM20.
+At position 49 to 110, the domain is characterized as KH; atypical.
+At position 202 to 272, the domain is characterized as Bromo.
+At position 553 to 613, the domain is characterized as CBS 1.
+At position 630 to 689, the domain is characterized as CBS 2.
+At position 7 to 61, the domain is characterized as SpoVT-AbrB 1.
+At position 90 to 133, the domain is characterized as SpoVT-AbrB 2.
+At position 25 to 116, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 219, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 314, the domain is characterized as Ig-like C2-type 3.
+At position 322 to 415, the domain is characterized as Ig-like C2-type 4.
+At position 480 to 559, the domain is characterized as Ig-like C2-type 5.
+At position 46 to 128, the domain is characterized as GOLD.
+At position 57 to 285, the domain is characterized as Radical SAM core.
+At position 48 to 160, the domain is characterized as Expansin-like EG45.
+At position 170 to 250, the domain is characterized as Expansin-like CBD.
+At position 84 to 126, the domain is characterized as CHCH.
+At position 27 to 246, the domain is characterized as ABC transporter.
+At position 33 to 349, the domain is characterized as G-alpha.
+At position 177 to 372, the domain is characterized as Helicase ATP-binding.
+At position 406 to 596, the domain is characterized as Helicase C-terminal.
+At position 559 to 590, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 932 to 1040, the domain is characterized as Rieske.
+At position 309 to 394, the domain is characterized as SCD.
+At position 619 to 640, the domain is characterized as R.
+At position 839 to 904, the domain is characterized as J.
+At position 70 to 137, the domain is characterized as BTB.
+At position 172 to 264, the domain is characterized as BACK.
+At position 23 to 130, the domain is characterized as WAC.
+At position 423 to 483, the domain is characterized as DDT.
+At position 8 to 183, the domain is characterized as Clp R.
+At position 96 to 149, the domain is characterized as MEIS N-terminal.
+At position 29 to 210, the domain is characterized as BPL/LPL catalytic.
+At position 617 to 778, the domain is characterized as Helicase ATP-binding.
+At position 800 to 953, the domain is characterized as Helicase C-terminal.
+At position 166 to 250, the domain is characterized as Ras-associating.
+At position 290 to 399, the domain is characterized as PH.
+At position 493 to 574, the domain is characterized as SH2.
+At position 224 to 301, the domain is characterized as RRM 2.
+At position 514 to 590, the domain is characterized as RRM 3.
+At position 111 to 175, the domain is characterized as S4 RNA-binding.
+At position 548 to 577, the domain is characterized as IQ 1.
+At position 869 to 898, the domain is characterized as IQ 2.
+At position 21 to 143, the domain is characterized as C-type lysozyme.
+At position 527 to 811, the domain is characterized as Protein kinase.
+At position 124 to 192, the domain is characterized as POTRA.
+At position 582 to 634, the domain is characterized as HTH psq-type 1.
+At position 1034 to 1086, the domain is characterized as HTH psq-type 2.
+At position 247 to 343, the domain is characterized as RRM 1.
+At position 348 to 428, the domain is characterized as RRM 2.
+At position 465 to 545, the domain is characterized as RRM 3.
+At position 91 to 403, the domain is characterized as IF rod.
+At position 5 to 93, the domain is characterized as ABM.
+At position 361 to 395, the domain is characterized as EF-hand 1.
+At position 474 to 509, the domain is characterized as EF-hand 4.
+At position 52 to 102, the domain is characterized as Collagen-like.
+At position 106 to 323, the domain is characterized as Fibrinogen C-terminal.
+At position 26 to 213, the domain is characterized as FtsK.
+At position 65 to 158, the domain is characterized as PH.
+At position 328 to 463, the domain is characterized as DAGKc.
+At position 3 to 72, the domain is characterized as NAC-A/B.
+At position 5 to 146, the domain is characterized as C2.
+At position 586 to 648, the domain is characterized as FIP-RBD.
+At position 117 to 248, the domain is characterized as Fatty acid hydroxylase.
+At position 7 to 210, the domain is characterized as DHFR.
+At position 128 to 341, the domain is characterized as BURP.
+At position 670 to 768, the domain is characterized as HTH araC/xylS-type.
+At position 21 to 119, the domain is characterized as Ig-like.
+At position 129 to 539, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 54 to 106, the domain is characterized as F-box.
+At position 3 to 67, the domain is characterized as HTH iclR-type.
+At position 29 to 136, the domain is characterized as Ig-like C2-type 1.
+At position 146 to 233, the domain is characterized as Ig-like C2-type 2.
+At position 41 to 101, the domain is characterized as v-SNARE coiled-coil homology.
+At position 37 to 151, the domain is characterized as TBDR plug.
+At position 154 to 615, the domain is characterized as TBDR beta-barrel.
+At position 2 to 181, the domain is characterized as Glutamine amidotransferase type-1.
+At position 193 to 253, the domain is characterized as HTH myb-type.
+At position 285 to 613, the domain is characterized as NR LBD.
+At position 55 to 229, the domain is characterized as FAD-binding PCMH-type.
+At position 268 to 342, the domain is characterized as B5.
+At position 74 to 181, the domain is characterized as VPS28 N-terminal.
+At position 191 to 287, the domain is characterized as VPS28 C-terminal.
+At position 1537 to 1635, the domain is characterized as PH.
+At position 6 to 118, the domain is characterized as Calponin-homology (CH).
+At position 53 to 164, the domain is characterized as sHSP.
+At position 53 to 157, the domain is characterized as FAD-binding FR-type.
+At position 91 to 184, the domain is characterized as K-box.
+At position 62 to 183, the domain is characterized as SCP.
+At position 835 to 928, the domain is characterized as Fibronectin type-III 3.
+At position 1000 to 1275, the domain is characterized as Protein kinase.
+At position 39 to 327, the domain is characterized as ABC transmembrane type-1.
+At position 361 to 595, the domain is characterized as ABC transporter.
+At position 482 to 816, the domain is characterized as HECT.
+At position 4 to 155, the domain is characterized as uDENN.
+At position 183 to 326, the domain is characterized as cDENN.
+At position 328 to 428, the domain is characterized as dDENN.
+At position 96 to 164, the domain is characterized as DRBM.
+At position 249 to 574, the domain is characterized as A to I editase.
+At position 152 to 388, the domain is characterized as Methyl-accepting transducer.
+At position 609 to 1069, the domain is characterized as USP.
+At position 31 to 88, the domain is characterized as Sushi 1.
+At position 90 to 147, the domain is characterized as Sushi 2.
+At position 162 to 404, the domain is characterized as Peptidase S1.
+At position 51 to 153, the domain is characterized as THUMP.
+At position 33 to 111, the domain is characterized as Inhibitor I9.
+At position 121 to 404, the domain is characterized as Peptidase S8.
+At position 38 to 337, the domain is characterized as Protein kinase.
+At position 25 to 74, the domain is characterized as G-patch.
+At position 497 to 613, the domain is characterized as Toprim.
+At position 174 to 229, the domain is characterized as LysM.
+At position 36 to 423, the domain is characterized as Helicase ATP-binding.
+At position 43 to 270, the domain is characterized as ATP-grasp.
+At position 38 to 127, the domain is characterized as CTCK.
+At position 6 to 135, the domain is characterized as MATH.
+At position 190 to 356, the domain is characterized as PCI.
+At position 109 to 144, the domain is characterized as EF-hand 2.
+At position 238 to 273, the domain is characterized as EF-hand 5.
+At position 274 to 309, the domain is characterized as EF-hand 6.
+At position 1 to 262, the domain is characterized as PABS.
+At position 147 to 283, the domain is characterized as Fatty acid hydroxylase.
+At position 20 to 159, the domain is characterized as Thioredoxin.
+At position 29 to 213, the domain is characterized as MARVEL.
+At position 682 to 773, the domain is characterized as FDX-ACB.
+At position 34 to 196, the domain is characterized as FeoB-type G.
+At position 323 to 574, the domain is characterized as Protein kinase.
+At position 24 to 292, the domain is characterized as Tyrosine-protein phosphatase.
+At position 105 to 154, the domain is characterized as bHLH.
+At position 457 to 615, the domain is characterized as SSD.
+At position 36 to 257, the domain is characterized as ABC transporter.
+At position 56 to 270, the domain is characterized as Radical SAM core.
+At position 151 to 434, the domain is characterized as ABC transmembrane type-1.
+At position 467 to 701, the domain is characterized as ABC transporter.
+At position 50 to 150, the domain is characterized as SRCR 1.
+At position 157 to 258, the domain is characterized as SRCR 2.
+At position 824 to 927, the domain is characterized as SRCR 8.
+At position 930 to 1030, the domain is characterized as SRCR 9.
+At position 556 to 628, the domain is characterized as HSA.
+At position 1002 to 1167, the domain is characterized as Helicase ATP-binding.
+At position 1537 to 1692, the domain is characterized as Helicase C-terminal.
+At position 33 to 147, the domain is characterized as Response regulatory.
+At position 107 to 260, the domain is characterized as NIDO.
+At position 281 to 321, the domain is characterized as EGF-like 1.
+At position 325 to 550, the domain is characterized as Nidogen G2 beta-barrel.
+At position 545 to 583, the domain is characterized as EGF-like 2.
+At position 591 to 631, the domain is characterized as EGF-like 3; calcium-binding.
+At position 788 to 829, the domain is characterized as EGF-like 4.
+At position 832 to 874, the domain is characterized as EGF-like 5.
+At position 912 to 953, the domain is characterized as EGF-like 6.
+At position 955 to 996, the domain is characterized as EGF-like 7.
+At position 997 to 1037, the domain is characterized as EGF-like 8.
+At position 365 to 422, the domain is characterized as S4 RNA-binding.
+At position 288 to 372, the domain is characterized as RCK C-terminal 2.
+At position 40 to 289, the domain is characterized as Radical SAM core.
+At position 34 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 31 to 109, the domain is characterized as GIY-YIG.
+At position 32 to 174, the domain is characterized as C-type lectin.
+At position 260 to 301, the domain is characterized as EGF-like 1.
+At position 302 to 344, the domain is characterized as EGF-like 2.
+At position 345 to 384, the domain is characterized as EGF-like 3; calcium-binding.
+At position 385 to 426, the domain is characterized as EGF-like 4; calcium-binding.
+At position 427 to 468, the domain is characterized as EGF-like 5; calcium-binding.
+At position 70 to 139, the domain is characterized as EamA 1.
+At position 160 to 286, the domain is characterized as EamA 2.
+At position 2 to 263, the domain is characterized as NodB homology.
+At position 51 to 158, the domain is characterized as HIT.
+At position 45 to 343, the domain is characterized as PPM-type phosphatase.
+At position 34 to 167, the domain is characterized as C2 1.
+At position 178 to 305, the domain is characterized as C2 2.
+At position 51 to 246, the domain is characterized as tr-type G.
+At position 197 to 371, the domain is characterized as Helicase ATP-binding.
+At position 623 to 777, the domain is characterized as Helicase C-terminal.
+At position 1 to 40, the domain is characterized as PTS EIIB type-1.
+At position 620 to 678, the domain is characterized as CBS 2.
+At position 566 to 868, the domain is characterized as Protein kinase.
+At position 144 to 377, the domain is characterized as Radical SAM core.
+At position 57 to 103, the domain is characterized as IPT/TIG 1.
+At position 136 to 204, the domain is characterized as IPT/TIG 2.
+At position 232 to 304, the domain is characterized as IPT/TIG 3.
+At position 105 to 225, the domain is characterized as PPIase FKBP-type.
+At position 322 to 346, the domain is characterized as NAF.
+At position 178 to 370, the domain is characterized as Glutamine amidotransferase type-1.
+At position 9 to 92, the domain is characterized as Sm.
+At position 453 to 489, the domain is characterized as DFDF.
+At position 10 to 114, the domain is characterized as Ig-like 1.
+At position 1786 to 1874, the domain is characterized as Ig-like 2.
+At position 1901 to 2133, the domain is characterized as Alpha-type protein kinase.
+At position 14 to 154, the domain is characterized as N-acetyltransferase.
+At position 27 to 134, the domain is characterized as HIT.
+At position 27 to 129, the domain is characterized as Gnk2-homologous.
+At position 69 to 91, the domain is characterized as Follistatin-like.
+At position 87 to 149, the domain is characterized as Kazal-like.
+At position 259 to 294, the domain is characterized as EF-hand.
+At position 129 to 146, the domain is characterized as EF-hand 2.
+At position 189 to 220, the domain is characterized as EF-hand 4.
+At position 149 to 201, the domain is characterized as bHLH.
+At position 198 to 371, the domain is characterized as Helicase ATP-binding.
+At position 538 to 696, the domain is characterized as Helicase C-terminal.
+At position 112 to 186, the domain is characterized as RRM 2.
+At position 107 to 271, the domain is characterized as CP-type G.
+At position 133 to 570, the domain is characterized as Urease.
+At position 8 to 289, the domain is characterized as Protein kinase.
+At position 508 to 630, the domain is characterized as Ricin B-type lectin.
+At position 475 to 590, the domain is characterized as Toprim.
+At position 1213 to 1492, the domain is characterized as ASD2.
+At position 61 to 249, the domain is characterized as VWFA 1.
+At position 630 to 820, the domain is characterized as VWFA 2.
+At position 848 to 1029, the domain is characterized as VWFA 3.
+At position 286 to 385, the domain is characterized as PpiC 2.
+At position 56 to 237, the domain is characterized as ABC transmembrane type-1.
+At position 24 to 143, the domain is characterized as Thioredoxin 1.
+At position 357 to 484, the domain is characterized as Thioredoxin 2.
+At position 137 to 468, the domain is characterized as USP.
+At position 477 to 551, the domain is characterized as RRM.
+At position 470 to 546, the domain is characterized as Carrier 1.
+At position 658 to 1077, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1669 to 1743, the domain is characterized as Carrier 2.
+At position 1792 to 2022, the domain is characterized as AB hydrolase-1.
+At position 28 to 136, the domain is characterized as CUB 1.
+At position 139 to 175, the domain is characterized as LDL-receptor class A 1.
+At position 192 to 305, the domain is characterized as CUB 2.
+At position 307 to 354, the domain is characterized as LDL-receptor class A 2.
+At position 355 to 397, the domain is characterized as LDL-receptor class A 3.
+At position 398 to 434, the domain is characterized as LDL-receptor class A 4.
+At position 34 to 143, the domain is characterized as Ig-like V-type.
+At position 149 to 244, the domain is characterized as Link 1.
+At position 250 to 347, the domain is characterized as Link 2.
+At position 520 to 615, the domain is characterized as Link 3.
+At position 621 to 717, the domain is characterized as Link 4.
+At position 1855 to 1892, the domain is characterized as EGF-like.
+At position 1901 to 2019, the domain is characterized as C-type lectin.
+At position 2022 to 2082, the domain is characterized as Sushi.
+At position 1 to 123, the domain is characterized as RNase III.
+At position 148 to 217, the domain is characterized as DRBM.
+At position 5 to 93, the domain is characterized as Plastocyanin-like.
+At position 132 to 384, the domain is characterized as Radical SAM core.
+At position 35 to 138, the domain is characterized as Ig-like C2-type.
+At position 63 to 116, the domain is characterized as TSP type-1 1.
+At position 120 to 155, the domain is characterized as LDL-receptor class A.
+At position 157 to 503, the domain is characterized as MACPF.
+At position 404 to 534, the domain is characterized as EGF-like.
+At position 544 to 587, the domain is characterized as TSP type-1 2.
+At position 23 to 146, the domain is characterized as Plastocyanin-like 1.
+At position 158 to 315, the domain is characterized as Plastocyanin-like 2.
+At position 384 to 507, the domain is characterized as Plastocyanin-like 3.
+At position 179 to 209, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 459 to 648, the domain is characterized as BPL/LPL catalytic.
+At position 184 to 380, the domain is characterized as ATP-grasp 1.
+At position 748 to 960, the domain is characterized as ATP-grasp 2.
+At position 1032 to 1167, the domain is characterized as MGS-like.
+At position 26 to 223, the domain is characterized as tr-type G.
+At position 57 to 97, the domain is characterized as EGF-like.
+At position 8 to 189, the domain is characterized as Guanylate kinase-like.
+At position 2293 to 2533, the domain is characterized as I/LWEQ.
+At position 378 to 732, the domain is characterized as Protein kinase.
+At position 771 to 831, the domain is characterized as AGC-kinase C-terminal.
+At position 46 to 299, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 43 to 314, the domain is characterized as Protein kinase.
+At position 2 to 204, the domain is characterized as DPCK.
+At position 129 to 232, the domain is characterized as Fibronectin type-III 2.
+At position 233 to 331, the domain is characterized as Fibronectin type-III 3.
+At position 40 to 97, the domain is characterized as bHLH.
+At position 116 to 149, the domain is characterized as Orange.
+At position 76 to 440, the domain is characterized as PRONE.
+At position 287 to 321, the domain is characterized as SAP.
+At position 205 to 293, the domain is characterized as Ig-like C1-type.
+At position 37 to 233, the domain is characterized as Cupin type-1 1.
+At position 348 to 497, the domain is characterized as Cupin type-1 2.
+At position 707 to 841, the domain is characterized as BAH 1.
+At position 909 to 1026, the domain is characterized as BAH 2.
+At position 1071 to 1505, the domain is characterized as SAM-dependent MTase C5-type.
+At position 27 to 276, the domain is characterized as Zn-dependent PLC.
+At position 282 to 398, the domain is characterized as PLAT.
+At position 65 to 393, the domain is characterized as PORR.
+At position 210 to 310, the domain is characterized as HTH araC/xylS-type.
+At position 34 to 109, the domain is characterized as KH 1.
+At position 113 to 187, the domain is characterized as KH 2.
+At position 189 to 259, the domain is characterized as KH 3.
+At position 270 to 342, the domain is characterized as KH 4.
+At position 344 to 419, the domain is characterized as KH 5.
+At position 18 to 76, the domain is characterized as Collagen-like 1.
+At position 75 to 134, the domain is characterized as Collagen-like 2.
+At position 135 to 193, the domain is characterized as Collagen-like 3.
+At position 195 to 252, the domain is characterized as Collagen-like 4.
+At position 522 to 579, the domain is characterized as Collagen-like 5.
+At position 555 to 613, the domain is characterized as Collagen-like 6.
+At position 618 to 676, the domain is characterized as Collagen-like 7.
+At position 678 to 736, the domain is characterized as Collagen-like 8.
+At position 804 to 861, the domain is characterized as Collagen-like 9.
+At position 918 to 976, the domain is characterized as Collagen-like 10.
+At position 972 to 1030, the domain is characterized as Collagen-like 11.
+At position 236 to 425, the domain is characterized as FAD-binding PCMH-type.
+At position 484 to 681, the domain is characterized as VWFA 1.
+At position 923 to 1094, the domain is characterized as VWFA 2.
+At position 252 to 448, the domain is characterized as GATase cobBQ-type.
+At position 137 to 252, the domain is characterized as Ig-like C2-type 1.
+At position 359 to 451, the domain is characterized as Ig-like C2-type 2.
+At position 452 to 542, the domain is characterized as Ig-like C2-type 3.
+At position 543 to 640, the domain is characterized as Ig-like C2-type 4.
+At position 644 to 763, the domain is characterized as Ig-like C2-type 5.
+At position 772 to 868, the domain is characterized as Fibronectin type-III 1.
+At position 870 to 965, the domain is characterized as Fibronectin type-III 2.
+At position 969 to 1057, the domain is characterized as Ig-like C2-type 6.
+At position 1066 to 1161, the domain is characterized as Fibronectin type-III 3.
+At position 1179 to 1263, the domain is characterized as Ig-like C2-type 7.
+At position 56 to 325, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 34 to 122, the domain is characterized as GOLD.
+At position 417 to 516, the domain is characterized as Zinc-hook.
+At position 296 to 529, the domain is characterized as NR LBD.
+At position 157 to 243, the domain is characterized as Doublecortin 1.
+At position 314 to 397, the domain is characterized as Doublecortin 2.
+At position 484 to 742, the domain is characterized as Protein kinase.
+At position 74 to 172, the domain is characterized as Fe2OG dioxygenase.
+At position 10 to 154, the domain is characterized as Toprim.
+At position 36 to 85, the domain is characterized as FHA-like.
+At position 206 to 312, the domain is characterized as HIT.
+At position 2 to 111, the domain is characterized as TRM112.
+At position 74 to 273, the domain is characterized as Glutamine amidotransferase type-1.
+At position 194 to 462, the domain is characterized as SF4 helicase.
+At position 57 to 306, the domain is characterized as GB1/RHD3-type G.
+At position 132 to 212, the domain is characterized as Ig-like 2.
+At position 236 to 334, the domain is characterized as Ig-like 3.
+At position 352 to 442, the domain is characterized as Ig-like 4.
+At position 452 to 553, the domain is characterized as Ig-like 5.
+At position 73 to 144, the domain is characterized as POTRA.
+At position 219 to 357, the domain is characterized as VPS9.
+At position 529 to 571, the domain is characterized as CUE.
+At position 135 to 232, the domain is characterized as Rhodanese.
+At position 68 to 135, the domain is characterized as J.
+At position 160 to 284, the domain is characterized as Fatty acid hydroxylase.
+At position 56 to 270, the domain is characterized as Laminin G-like.
+At position 24 to 209, the domain is characterized as Helicase ATP-binding.
+At position 430 to 594, the domain is characterized as Helicase C-terminal.
+At position 61 to 204, the domain is characterized as EXPERA.
+At position 174 to 251, the domain is characterized as KH.
+At position 256 to 322, the domain is characterized as R3H.
+At position 189 to 265, the domain is characterized as PDZ.
+At position 223 to 258, the domain is characterized as EF-hand 6.
+At position 280 to 479, the domain is characterized as Helicase ATP-binding.
+At position 531 to 675, the domain is characterized as Helicase C-terminal.
+At position 151 to 327, the domain is characterized as Helicase ATP-binding.
+At position 338 to 502, the domain is characterized as Helicase C-terminal.
+At position 82 to 256, the domain is characterized as FAD-binding PCMH-type.
+At position 30 to 114, the domain is characterized as RRM 1.
+At position 153 to 229, the domain is characterized as RRM 2.
+At position 329 to 403, the domain is characterized as RRM 3.
+At position 446 to 521, the domain is characterized as RRM 4.
+At position 240 to 501, the domain is characterized as ABC transporter 2.
+At position 1 to 169, the domain is characterized as SPX.
+At position 871 to 1178, the domain is characterized as GP-PDE.
+At position 219 to 281, the domain is characterized as LRRCT.
+At position 461 to 567, the domain is characterized as Ig-like C2-type 1.
+At position 571 to 661, the domain is characterized as Ig-like C2-type 2.
+At position 1619 to 1710, the domain is characterized as Ig-like C2-type 3.
+At position 1715 to 1807, the domain is characterized as Ig-like C2-type 4.
+At position 1812 to 1901, the domain is characterized as Ig-like C2-type 5.
+At position 1912 to 2005, the domain is characterized as Ig-like C2-type 6.
+At position 2008 to 2106, the domain is characterized as Ig-like C2-type 7.
+At position 2112 to 2200, the domain is characterized as Ig-like C2-type 8.
+At position 2205 to 2302, the domain is characterized as Ig-like C2-type 9.
+At position 2308 to 2398, the domain is characterized as Ig-like C2-type 10.
+At position 2403 to 2493, the domain is characterized as Ig-like C2-type 11.
+At position 2499 to 2592, the domain is characterized as Ig-like C2-type 12.
+At position 28 to 118, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 128 to 229, the domain is characterized as FAD-binding FR-type.
+At position 171 to 378, the domain is characterized as CP-type G.
+At position 14 to 100, the domain is characterized as Disintegrin.
+At position 563 to 848, the domain is characterized as Protein kinase.
+At position 184 to 284, the domain is characterized as Fe2OG dioxygenase.
+At position 222 to 282, the domain is characterized as Tudor 1.
+At position 453 to 512, the domain is characterized as Tudor 2.
+At position 674 to 733, the domain is characterized as Tudor 3.
+At position 925 to 983, the domain is characterized as Tudor 4.
+At position 673 to 769, the domain is characterized as BRCT 1.
+At position 821 to 927, the domain is characterized as BRCT 2.
+At position 27 to 341, the domain is characterized as Transferrin-like 1.
+At position 354 to 686, the domain is characterized as Transferrin-like 2.
+At position 662 to 856, the domain is characterized as Rab-GAP TBC.
+At position 36 to 211, the domain is characterized as FAD-binding PCMH-type.
+At position 79 to 340, the domain is characterized as Chorismate mutase.
+At position 482 to 566, the domain is characterized as RWP-RK.
+At position 673 to 759, the domain is characterized as PB1.
+At position 25 to 111, the domain is characterized as GS beta-grasp.
+At position 118 to 454, the domain is characterized as GS catalytic.
+At position 69 to 397, the domain is characterized as Peptidase A1.
+At position 330 to 350, the domain is characterized as ELK.
+At position 5 to 111, the domain is characterized as HTH APSES-type.
+At position 214 to 354, the domain is characterized as PADR1 zinc-binding.
+At position 380 to 471, the domain is characterized as BRCT.
+At position 525 to 622, the domain is characterized as WGR.
+At position 644 to 761, the domain is characterized as PARP alpha-helical.
+At position 770 to 994, the domain is characterized as PARP catalytic.
+At position 431 to 686, the domain is characterized as Bin3-type SAM.
+At position 167 to 429, the domain is characterized as NB-ARC.
+At position 207 to 226, the domain is characterized as UIM 1.
+At position 110 to 239, the domain is characterized as GST C-terminal.
+At position 5 to 197, the domain is characterized as Lon N-terminal.
+At position 585 to 766, the domain is characterized as Lon proteolytic.
+At position 77 to 410, the domain is characterized as SAM-dependent MTase C5-type.
+At position 191 to 366, the domain is characterized as EngA-type G 2.
+At position 367 to 453, the domain is characterized as KH-like.
+At position 286 to 349, the domain is characterized as bZIP.
+At position 339 to 568, the domain is characterized as TLDc.
+At position 3 to 135, the domain is characterized as PINc.
+At position 66 to 243, the domain is characterized as FAD-binding PCMH-type.
+At position 9 to 142, the domain is characterized as SprT-like.
+At position 149 to 248, the domain is characterized as Ig-like C1-type 1.
+At position 255 to 343, the domain is characterized as Ig-like C1-type 2.
+At position 25 to 64, the domain is characterized as EGF-like 1.
+At position 59 to 193, the domain is characterized as C-type lectin.
+At position 180 to 219, the domain is characterized as EGF-like 2.
+At position 233 to 322, the domain is characterized as SUEL-type lectin.
+At position 838 to 885, the domain is characterized as GPS.
+At position 18 to 253, the domain is characterized as Peptidase S1.
+At position 597 to 673, the domain is characterized as BRCT.
+At position 95 to 386, the domain is characterized as ABC transmembrane type-1 1.
+At position 417 to 667, the domain is characterized as ABC transporter 1.
+At position 781 to 1056, the domain is characterized as ABC transmembrane type-1 2.
+At position 1097 to 1325, the domain is characterized as ABC transporter 2.
+At position 194 to 278, the domain is characterized as Ras-associating.
+At position 318 to 427, the domain is characterized as PH.
+At position 520 to 601, the domain is characterized as SH2.
+At position 369 to 461, the domain is characterized as BRICHOS.
+At position 508 to 623, the domain is characterized as STAS.
+At position 25 to 277, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 527 to 577, the domain is characterized as SANT.
+At position 627 to 731, the domain is characterized as CXC.
+At position 746 to 861, the domain is characterized as SET.
+At position 10 to 239, the domain is characterized as ABC transporter.
+At position 137 to 407, the domain is characterized as Protein kinase.
+At position 10 to 253, the domain is characterized as ABC transporter.
+At position 523 to 593, the domain is characterized as Bromo.
+At position 21 to 136, the domain is characterized as MTTase N-terminal.
+At position 392 to 462, the domain is characterized as TRAM.
+At position 246 to 531, the domain is characterized as Peptidase S1.
+At position 46 to 326, the domain is characterized as GH10.
+At position 192 to 357, the domain is characterized as Helicase ATP-binding.
+At position 487 to 638, the domain is characterized as Helicase C-terminal.
+At position 840 to 892, the domain is characterized as SANT 1.
+At position 943 to 1007, the domain is characterized as SANT 2.
+At position 76 to 204, the domain is characterized as HD.
+At position 82 to 257, the domain is characterized as Helicase ATP-binding.
+At position 269 to 430, the domain is characterized as Helicase C-terminal.
+At position 22 to 171, the domain is characterized as CENP-V/GFA.
+At position 29 to 120, the domain is characterized as ARID.
+At position 399 to 520, the domain is characterized as CHRD 3.
+At position 526 to 646, the domain is characterized as CHRD 4.
+At position 699 to 759, the domain is characterized as VWFC 2.
+At position 779 to 845, the domain is characterized as VWFC 3.
+At position 867 to 927, the domain is characterized as VWFC 4.
+At position 9 to 286, the domain is characterized as CN hydrolase.
+At position 35 to 249, the domain is characterized as ABC transporter.
+At position 154 to 685, the domain is characterized as USP.
+At position 788 to 891, the domain is characterized as DUSP 2.
+At position 7 to 277, the domain is characterized as CN hydrolase.
+At position 8 to 153, the domain is characterized as UBC core.
+At position 1 to 123, the domain is characterized as HotDog ACOT-type.
+At position 78 to 393, the domain is characterized as RHD.
+At position 366 to 697, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 267 to 380, the domain is characterized as PAZ.
+At position 550 to 857, the domain is characterized as Piwi.
+At position 337 to 433, the domain is characterized as PH.
+At position 93 to 248, the domain is characterized as Protein kinase.
+At position 981 to 1147, the domain is characterized as PNPLA.
+At position 615 to 733, the domain is characterized as MHD1.
+At position 834 to 966, the domain is characterized as C2.
+At position 1044 to 1184, the domain is characterized as MHD2.
+At position 46 to 83, the domain is characterized as LDL-receptor class A 1.
+At position 123 to 160, the domain is characterized as LDL-receptor class A 2.
+At position 121 to 259, the domain is characterized as N-acetyltransferase.
+At position 174 to 270, the domain is characterized as CRM 1.
+At position 378 to 475, the domain is characterized as CRM 2.
+At position 590 to 690, the domain is characterized as CRM 3.
+At position 157 to 407, the domain is characterized as NR LBD.
+At position 40 to 280, the domain is characterized as Radical SAM core.
+At position 35 to 118, the domain is characterized as WWE 1.
+At position 119 to 201, the domain is characterized as WWE 2.
+At position 348 to 394, the domain is characterized as F-box.
+At position 464 to 571, the domain is characterized as PH.
+At position 701 to 885, the domain is characterized as Rho-GAP.
+At position 21 to 339, the domain is characterized as CNH.
+At position 230 to 321, the domain is characterized as GIY-YIG.
+At position 205 to 348, the domain is characterized as FCP1 homology.
+At position 42 to 113, the domain is characterized as H15.
+At position 203 to 272, the domain is characterized as Rieske.
+At position 80 to 109, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 110 to 141, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 10 to 160, the domain is characterized as Tyrosine-protein phosphatase.
+At position 22 to 229, the domain is characterized as AIG1-type G.
+At position 101 to 358, the domain is characterized as Protein kinase.
+At position 359 to 434, the domain is characterized as AGC-kinase C-terminal.
+At position 99 to 250, the domain is characterized as FBA.
+At position 38 to 396, the domain is characterized as GH64.
+At position 422 to 548, the domain is characterized as Ricin B-type lectin.
+At position 693 to 774, the domain is characterized as BRCT.
+At position 161 to 265, the domain is characterized as PB1.
+At position 32 to 159, the domain is characterized as ALOG.
+At position 1393 to 1461, the domain is characterized as Sushi 1.
+At position 1462 to 1521, the domain is characterized as Sushi 2.
+At position 1523 to 1592, the domain is characterized as Sushi 3.
+At position 1593 to 1648, the domain is characterized as Sushi 4.
+At position 1651 to 1731, the domain is characterized as Sushi 5.
+At position 1 to 66, the domain is characterized as PAS 1.
+At position 67 to 114, the domain is characterized as PAC 1.
+At position 115 to 188, the domain is characterized as PAS 2.
+At position 191 to 241, the domain is characterized as PAC 2.
+At position 242 to 417, the domain is characterized as Methyl-accepting transducer.
+At position 204 to 293, the domain is characterized as Ig-like C1-type.
+At position 143 to 510, the domain is characterized as PUM-HD.
+At position 133 to 195, the domain is characterized as t-SNARE coiled-coil homology.
+At position 609 to 682, the domain is characterized as SH3.
+At position 267 to 428, the domain is characterized as SUN.
+At position 103 to 166, the domain is characterized as bZIP.
+At position 48 to 97, the domain is characterized as bZIP.
+At position 58 to 95, the domain is characterized as EF-hand 1.
+At position 172 to 204, the domain is characterized as EF-hand 3.
+At position 37 to 135, the domain is characterized as Cadherin 1.
+At position 249 to 349, the domain is characterized as Cadherin 3.
+At position 354 to 453, the domain is characterized as Cadherin 4.
+At position 458 to 563, the domain is characterized as Cadherin 5.
+At position 570 to 673, the domain is characterized as Cadherin 6.
+At position 115 to 222, the domain is characterized as AB hydrolase-1.
+At position 285 to 481, the domain is characterized as B30.2/SPRY.
+At position 582 to 641, the domain is characterized as KH.
+At position 653 to 722, the domain is characterized as S1 motif.
+At position 124 to 190, the domain is characterized as PQ-loop 1.
+At position 266 to 326, the domain is characterized as PQ-loop 2.
+At position 244 to 348, the domain is characterized as PH 2.
+At position 945 to 1109, the domain is characterized as SUN.
+At position 353 to 595, the domain is characterized as NR LBD.
+At position 320 to 513, the domain is characterized as Sigma-54 factor interaction.
+At position 26 to 69, the domain is characterized as P-type.
+At position 134 to 375, the domain is characterized as Radical SAM core.
+At position 3 to 77, the domain is characterized as Carrier.
+At position 45 to 129, the domain is characterized as SCAN box.
+At position 184 to 291, the domain is characterized as Calponin-homology (CH).
+At position 467 to 478, the domain is characterized as IQ 1.
+At position 528 to 539, the domain is characterized as IQ 2.
+At position 556 to 567, the domain is characterized as IQ 3.
+At position 586 to 597, the domain is characterized as IQ 4.
+At position 616 to 627, the domain is characterized as IQ 5.
+At position 642 to 653, the domain is characterized as IQ 6.
+At position 672 to 683, the domain is characterized as IQ 7.
+At position 734 to 745, the domain is characterized as IQ 8.
+At position 764 to 775, the domain is characterized as IQ 9.
+At position 958 to 1193, the domain is characterized as Ras-GAP.
+At position 146 to 322, the domain is characterized as Helicase ATP-binding.
+At position 351 to 500, the domain is characterized as Helicase C-terminal.
+At position 267 to 427, the domain is characterized as SUN.
+At position 293 to 359, the domain is characterized as Mop.
+At position 48 to 82, the domain is characterized as WW.
+At position 184 to 356, the domain is characterized as PCI.
+At position 197 to 270, the domain is characterized as PAS.
+At position 324 to 554, the domain is characterized as Sigma-54 factor interaction.
+At position 58 to 333, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 47 to 276, the domain is characterized as Chitin-binding type-4.
+At position 1158 to 1281, the domain is characterized as Rab-GAP TBC.
+At position 1 to 188, the domain is characterized as VWFA.
+At position 212 to 231, the domain is characterized as UIM 1.
+At position 276 to 295, the domain is characterized as UIM 2.
+At position 303 to 322, the domain is characterized as UIM 3.
+At position 16 to 127, the domain is characterized as WH1.
+At position 547 to 567, the domain is characterized as WH2.
+At position 933 to 988, the domain is characterized as Bromo.
+At position 31 to 255, the domain is characterized as ABC transporter.
+At position 362 to 538, the domain is characterized as N-acetyltransferase.
+At position 54 to 191, the domain is characterized as Fido.
+At position 498 to 614, the domain is characterized as Toprim.
+At position 35 to 68, the domain is characterized as Chitin-binding type-1.
+At position 147 to 367, the domain is characterized as Rab-GAP TBC.
+At position 51 to 231, the domain is characterized as EngB-type G.
+At position 281 to 510, the domain is characterized as Methyl-accepting transducer.
+At position 135 to 153, the domain is characterized as IQ 2.
+At position 157 to 183, the domain is characterized as IQ 3.
+At position 10 to 189, the domain is characterized as Guanylate kinase-like.
+At position 370 to 496, the domain is characterized as DOD-type homing endonuclease.
+At position 773 to 952, the domain is characterized as Lon proteolytic.
+At position 17 to 64, the domain is characterized as F-box.
+At position 370 to 423, the domain is characterized as FBD.
+At position 230 to 263, the domain is characterized as WW 1.
+At position 334 to 367, the domain is characterized as WW 2.
+At position 394 to 427, the domain is characterized as WW 3.
+At position 483 to 816, the domain is characterized as HECT.
+At position 207 to 445, the domain is characterized as NR LBD.
+At position 78 to 253, the domain is characterized as FAD-binding PCMH-type.
+At position 1375 to 1510, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1644 to 1790, the domain is characterized as RNase H Ty1/copia-type.
+At position 494 to 757, the domain is characterized as ATP-grasp.
+At position 351 to 467, the domain is characterized as BRCT.
+At position 773 to 847, the domain is characterized as HSA.
+At position 1043 to 1097, the domain is characterized as Myb-like.
+At position 203 to 299, the domain is characterized as Ig-like C1-type.
+At position 220 to 261, the domain is characterized as CHCH.
+At position 13 to 229, the domain is characterized as tr-type G.
+At position 153 to 191, the domain is characterized as Rubredoxin-like.
+At position 194 to 389, the domain is characterized as Helicase ATP-binding.
+At position 443 to 670, the domain is characterized as Helicase C-terminal.
+At position 3 to 132, the domain is characterized as Velvet.
+At position 95 to 173, the domain is characterized as PA.
+At position 90 to 197, the domain is characterized as Cytochrome c.
+At position 1 to 46, the domain is characterized as HTH asnC-type.
+At position 98 to 479, the domain is characterized as PRONE.
+At position 24 to 264, the domain is characterized as ABC transporter.
+At position 5 to 371, the domain is characterized as SAM-dependent MTase C5-type.
+At position 26 to 55, the domain is characterized as LRRNT.
+At position 489 to 525, the domain is characterized as LRRNT 3.
+At position 656 to 706, the domain is characterized as LRRCT 3.
+At position 710 to 746, the domain is characterized as LRRNT 4.
+At position 851 to 901, the domain is characterized as LRRCT 4.
+At position 912 to 947, the domain is characterized as EGF-like 1.
+At position 949 to 988, the domain is characterized as EGF-like 2.
+At position 990 to 1026, the domain is characterized as EGF-like 3.
+At position 1028 to 1066, the domain is characterized as EGF-like 4.
+At position 1068 to 1104, the domain is characterized as EGF-like 5.
+At position 1113 to 1149, the domain is characterized as EGF-like 6.
+At position 1152 to 1325, the domain is characterized as Laminin G-like.
+At position 1329 to 1360, the domain is characterized as EGF-like 7.
+At position 1363 to 1399, the domain is characterized as EGF-like 8.
+At position 1404 to 1440, the domain is characterized as EGF-like 9.
+At position 1445 to 1520, the domain is characterized as CTCK.
+At position 1 to 111, the domain is characterized as C2 1.
+At position 116 to 246, the domain is characterized as C2 2.
+At position 286 to 503, the domain is characterized as VWFA.
+At position 165 to 235, the domain is characterized as DRBM.
+At position 491 to 658, the domain is characterized as tr-type G.
+At position 10 to 234, the domain is characterized as Radical SAM core.
+At position 88 to 144, the domain is characterized as HTH myb-type.
+At position 6 to 26, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 361 to 401, the domain is characterized as UBA.
+At position 82 to 155, the domain is characterized as S4 RNA-binding.
+At position 4 to 364, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 866 to 1159, the domain is characterized as PKS/mFAS DH.
+At position 2318 to 2396, the domain is characterized as Carrier.
+At position 65 to 134, the domain is characterized as HTH iclR-type.
+At position 580 to 631, the domain is characterized as LRRCT.
+At position 674 to 817, the domain is characterized as TIR.
+At position 83 to 156, the domain is characterized as PUB.
+At position 25 to 254, the domain is characterized as Peptidase S1.
+At position 77 to 214, the domain is characterized as PPC.
+At position 307 to 332, the domain is characterized as NAF.
+At position 95 to 288, the domain is characterized as ABC transmembrane type-1.
+At position 163 to 234, the domain is characterized as RRM.
+At position 531 to 713, the domain is characterized as N-acetyltransferase.
+At position 24 to 142, the domain is characterized as Calponin-homology (CH).
+At position 332 to 651, the domain is characterized as Kinesin motor.
+At position 513 to 601, the domain is characterized as Ig-like.
+At position 24 to 58, the domain is characterized as Chitin-binding type-1.
+At position 172 to 270, the domain is characterized as 5'-3' exonuclease.
+At position 7 to 100, the domain is characterized as PH.
+At position 103 to 241, the domain is characterized as DAGKc.
+At position 9 to 126, the domain is characterized as C-type lectin.
+At position 83 to 192, the domain is characterized as Thioredoxin.
+At position 58 to 169, the domain is characterized as THUMP.
+At position 185 to 259, the domain is characterized as POU-specific.
+At position 77 to 385, the domain is characterized as AB hydrolase-1.
+At position 28 to 114, the domain is characterized as UPAR/Ly6.
+At position 34 to 261, the domain is characterized as Radical SAM core.
+At position 474 to 855, the domain is characterized as USP.
+At position 907 to 1079, the domain is characterized as Exonuclease.
+At position 23 to 435, the domain is characterized as PUM-HD.
+At position 345 to 406, the domain is characterized as LIM zinc-binding 1.
+At position 410 to 470, the domain is characterized as LIM zinc-binding 2.
+At position 471 to 539, the domain is characterized as LIM zinc-binding 3.
+At position 766 to 839, the domain is characterized as Carrier 1.
+At position 1843 to 1926, the domain is characterized as Carrier 2.
+At position 115 to 589, the domain is characterized as Peptidase S8.
+At position 362 to 442, the domain is characterized as PA.
+At position 325 to 388, the domain is characterized as bZIP.
+At position 23 to 307, the domain is characterized as Peptidase S8.
+At position 43 to 117, the domain is characterized as H15 1.
+At position 176 to 251, the domain is characterized as H15 2.
+At position 90 to 221, the domain is characterized as GST C-terminal.
+At position 6 to 208, the domain is characterized as ABC transporter.
+At position 48 to 348, the domain is characterized as ABC transmembrane type-1 1.
+At position 372 to 663, the domain is characterized as ABC transporter 1.
+At position 738 to 1025, the domain is characterized as ABC transmembrane type-1 2.
+At position 1062 to 1300, the domain is characterized as ABC transporter 2.
+At position 23 to 109, the domain is characterized as Ig-like V-type.
+At position 123 to 219, the domain is characterized as Ig-like C2-type 1.
+At position 242 to 300, the domain is characterized as LIM zinc-binding 1.
+At position 301 to 360, the domain is characterized as LIM zinc-binding 2.
+At position 361 to 419, the domain is characterized as LIM zinc-binding 3.
+At position 1228 to 1784, the domain is characterized as FAT.
+At position 1958 to 2285, the domain is characterized as PI3K/PI4K catalytic.
+At position 2305 to 2337, the domain is characterized as FATC.
+At position 78 to 323, the domain is characterized as AB hydrolase-1.
+At position 144 to 208, the domain is characterized as S5 DRBM.
+At position 575 to 754, the domain is characterized as Helicase ATP-binding.
+At position 780 to 933, the domain is characterized as Helicase C-terminal.
+At position 362 to 512, the domain is characterized as ZP.
+At position 411 to 866, the domain is characterized as FH2.
+At position 51 to 110, the domain is characterized as Collagen-like.
+At position 153 to 269, the domain is characterized as C-type lectin.
+At position 44 to 311, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 185 to 354, the domain is characterized as tr-type G.
+At position 221 to 486, the domain is characterized as Deacetylase sirtuin-type.
+At position 317 to 353, the domain is characterized as CBM1.
+At position 199 to 376, the domain is characterized as tr-type G.
+At position 89 to 191, the domain is characterized as Glutaredoxin.
+At position 98 to 176, the domain is characterized as RRM 2.
+At position 14 to 217, the domain is characterized as DarT.
+At position 11 to 96, the domain is characterized as MtN3/slv 1.
+At position 39 to 116, the domain is characterized as RRM.
+At position 72 to 122, the domain is characterized as Sushi 1.
+At position 123 to 181, the domain is characterized as Sushi 2.
+At position 180 to 264, the domain is characterized as HYR.
+At position 265 to 324, the domain is characterized as Sushi 3.
+At position 39 to 95, the domain is characterized as HTH myb-type 1.
+At position 96 to 154, the domain is characterized as HTH myb-type 2.
+At position 155 to 205, the domain is characterized as HTH myb-type 3.
+At position 32 to 142, the domain is characterized as Ig-like V-type 1.
+At position 147 to 257, the domain is characterized as Ig-like V-type 2.
+At position 274 to 355, the domain is characterized as Ig-like C2-type 1.
+At position 363 to 441, the domain is characterized as Ig-like C2-type 2.
+At position 448 to 541, the domain is characterized as Ig-like C2-type 3.
+At position 644 to 769, the domain is characterized as C2 1.
+At position 784 to 913, the domain is characterized as C2 2.
+At position 42 to 246, the domain is characterized as ABC transmembrane type-1.
+At position 86 to 219, the domain is characterized as Cupin type-1.
+At position 6 to 154, the domain is characterized as RNase H type-1.
+At position 116 to 169, the domain is characterized as BSD 1.
+At position 190 to 241, the domain is characterized as BSD 2.
+At position 120 to 243, the domain is characterized as Nudix hydrolase.
+At position 237 to 332, the domain is characterized as Ig-like C2-type.
+At position 341 to 382, the domain is characterized as EGF-like.
+At position 1 to 192, the domain is characterized as Rho-GAP.
+At position 312 to 411, the domain is characterized as Fibronectin type-III.
+At position 170 to 352, the domain is characterized as Rho-GAP.
+At position 595 to 656, the domain is characterized as SAM.
+At position 249 to 457, the domain is characterized as Rab-GAP TBC.
+At position 14 to 264, the domain is characterized as F-BAR.
+At position 422 to 611, the domain is characterized as Rho-GAP.
+At position 312 to 368, the domain is characterized as HAMP.
+At position 365 to 574, the domain is characterized as Histidine kinase.
+At position 221 to 383, the domain is characterized as TrmE-type G.
+At position 33 to 204, the domain is characterized as Helicase ATP-binding.
+At position 236 to 436, the domain is characterized as Helicase C-terminal.
+At position 101 to 143, the domain is characterized as CHCH.
+At position 796 to 948, the domain is characterized as DIPSY.
+At position 59 to 431, the domain is characterized as GBD/FH3.
+At position 512 to 596, the domain is characterized as FH1.
+At position 601 to 1001, the domain is characterized as FH2.
+At position 1022 to 1054, the domain is characterized as DAD.
+At position 106 to 263, the domain is characterized as SSD.
+At position 32 to 98, the domain is characterized as Importin N-terminal.
+At position 479 to 582, the domain is characterized as STAS.
+At position 149 to 199, the domain is characterized as SANT.
+At position 109 to 173, the domain is characterized as SEP.
+At position 225 to 302, the domain is characterized as UBX.
+At position 98 to 255, the domain is characterized as PPIase cyclophilin-type.
+At position 6 to 75, the domain is characterized as TGS.
+At position 18 to 168, the domain is characterized as Nudix hydrolase.
+At position 197 to 247, the domain is characterized as bHLH.
+At position 18 to 87, the domain is characterized as BTB.
+At position 34 to 155, the domain is characterized as FZ.
+At position 687 to 762, the domain is characterized as MBD.
+At position 1010 to 1075, the domain is characterized as DDT.
+At position 2039 to 2109, the domain is characterized as Bromo.
+At position 438 to 510, the domain is characterized as RRM.
+At position 67 to 255, the domain is characterized as RNase H type-2.
+At position 1477 to 1637, the domain is characterized as Exonuclease.
+At position 68 to 363, the domain is characterized as Protein kinase.
+At position 46 to 165, the domain is characterized as FZ.
+At position 386 to 446, the domain is characterized as LIM zinc-binding.
+At position 6 to 85, the domain is characterized as Carrier 1.
+At position 1350 to 1425, the domain is characterized as Carrier 2.
+At position 10 to 162, the domain is characterized as MARVEL.
+At position 5 to 140, the domain is characterized as N-acetyltransferase.
+At position 213 to 373, the domain is characterized as Tyrosine-protein phosphatase.
+At position 191 to 331, the domain is characterized as DOD-type homing endonuclease.
+At position 25 to 77, the domain is characterized as Myosin N-terminal SH3-like.
+At position 81 to 821, the domain is characterized as Myosin motor.
+At position 824 to 851, the domain is characterized as IQ 1.
+At position 872 to 901, the domain is characterized as IQ 2.
+At position 943 to 972, the domain is characterized as IQ 3.
+At position 1969 to 2188, the domain is characterized as Dilute.
+At position 96 to 179, the domain is characterized as PRC barrel.
+At position 250 to 605, the domain is characterized as NPH3.
+At position 340 to 547, the domain is characterized as Protein kinase.
+At position 5 to 220, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 174, the domain is characterized as PfpI endopeptidase 1.
+At position 212 to 378, the domain is characterized as PfpI endopeptidase 2.
+At position 78 to 255, the domain is characterized as FAD-binding PCMH-type.
+At position 314 to 668, the domain is characterized as Protein kinase.
+At position 1 to 417, the domain is characterized as PTS EIIC type-1.
+At position 447 to 526, the domain is characterized as PTS EIIB type-1.
+At position 12 to 194, the domain is characterized as Glutamine amidotransferase type-2.
+At position 163 to 259, the domain is characterized as PPIase FKBP-type.
+At position 114 to 304, the domain is characterized as ATP-grasp.
+At position 30 to 126, the domain is characterized as Phytocyanin.
+At position 660 to 754, the domain is characterized as Big-1 2.
+At position 924 to 935, the domain is characterized as BIG2.
+At position 411 to 483, the domain is characterized as PAS.
+At position 171 to 335, the domain is characterized as UBC core.
+At position 366 to 576, the domain is characterized as NR LBD.
+At position 39 to 152, the domain is characterized as PH.
+At position 61 to 340, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 696 to 799, the domain is characterized as PH.
+At position 17 to 101, the domain is characterized as Rhodanese.
+At position 13 to 108, the domain is characterized as PH.
+At position 112 to 125, the domain is characterized as CRIB.
+At position 204 to 458, the domain is characterized as Protein kinase.
+At position 8 to 278, the domain is characterized as Pyruvate carboxyltransferase.
+At position 6 to 69, the domain is characterized as RRM 1.
+At position 100 to 166, the domain is characterized as RRM 2.
+At position 53 to 497, the domain is characterized as USP.
+At position 31 to 98, the domain is characterized as DRBM 1.
+At position 123 to 191, the domain is characterized as DRBM 2.
+At position 236 to 304, the domain is characterized as DRBM 3.
+At position 115 to 187, the domain is characterized as SoHo.
+At position 380 to 439, the domain is characterized as SH3 1.
+At position 454 to 515, the domain is characterized as SH3 2.
+At position 612 to 671, the domain is characterized as SH3 3.
+At position 171 to 271, the domain is characterized as Ig-like C2-type 2.
+At position 71 to 217, the domain is characterized as SCP.
+At position 604 to 788, the domain is characterized as PID.
+At position 801 to 886, the domain is characterized as PDZ 1.
+At position 892 to 968, the domain is characterized as PDZ 2.
+At position 126 to 167, the domain is characterized as EGF-like; calcium-binding.
+At position 234 to 276, the domain is characterized as Collagen-like 1.
+At position 286 to 319, the domain is characterized as Collagen-like 2.
+At position 3 to 222, the domain is characterized as ABC transporter.
+At position 175 to 382, the domain is characterized as Helicase ATP-binding.
+At position 408 to 631, the domain is characterized as Helicase C-terminal.
+At position 63 to 108, the domain is characterized as CHCH.
+At position 27 to 346, the domain is characterized as Protein kinase.
+At position 88 to 425, the domain is characterized as Peptidase A1.
+At position 13 to 205, the domain is characterized as RNase H type-2.
+At position 653 to 725, the domain is characterized as S1 motif.
+At position 438 to 806, the domain is characterized as GRAS.
+At position 227 to 518, the domain is characterized as Protein kinase.
+At position 279 to 330, the domain is characterized as LRRCT.
+At position 33 to 61, the domain is characterized as EF-hand 1.
+At position 67 to 95, the domain is characterized as EF-hand 2.
+At position 160 to 259, the domain is characterized as PB1.
+At position 595 to 643, the domain is characterized as LRRCT.
+At position 52 to 155, the domain is characterized as FAD-binding FR-type.
+At position 4 to 149, the domain is characterized as N-acetyltransferase.
+At position 312 to 593, the domain is characterized as Protein kinase.
+At position 417 to 586, the domain is characterized as tr-type G.
+At position 17 to 98, the domain is characterized as REM-1.
+At position 309 to 416, the domain is characterized as PH.
+At position 146 to 187, the domain is characterized as EGF-like.
+At position 280 to 502, the domain is characterized as TLDc.
+At position 66 to 168, the domain is characterized as Glutaredoxin.
+At position 30 to 105, the domain is characterized as Lipoyl-binding.
+At position 146 to 183, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 85 to 293, the domain is characterized as Helicase ATP-binding.
+At position 334 to 551, the domain is characterized as Helicase C-terminal.
+At position 26 to 154, the domain is characterized as Response regulatory.
+At position 124 to 407, the domain is characterized as Peptidase S1.
+At position 74 to 127, the domain is characterized as HTH cro/C1-type.
+At position 51 to 140, the domain is characterized as Ig-like C2-type 1.
+At position 150 to 241, the domain is characterized as Ig-like C2-type 2.
+At position 256 to 344, the domain is characterized as Ig-like C2-type 3.
+At position 349 to 437, the domain is characterized as Ig-like C2-type 4.
+At position 443 to 528, the domain is characterized as Ig-like C2-type 5.
+At position 532 to 623, the domain is characterized as Ig-like C2-type 6.
+At position 829 to 931, the domain is characterized as Fibronectin type-III 3.
+At position 935 to 1030, the domain is characterized as Fibronectin type-III 4.
+At position 1032 to 1129, the domain is characterized as Fibronectin type-III 5.
+At position 37 to 114, the domain is characterized as Inhibitor I9.
+At position 15 to 292, the domain is characterized as Deacetylase sirtuin-type.
+At position 26 to 133, the domain is characterized as Thioredoxin.
+At position 302 to 428, the domain is characterized as SSD.
+At position 122 to 174, the domain is characterized as bHLH.
+At position 214 to 312, the domain is characterized as HTH araC/xylS-type.
+At position 65 to 323, the domain is characterized as Protein kinase.
+At position 366 to 401, the domain is characterized as EF-hand 1.
+At position 438 to 473, the domain is characterized as EF-hand 3.
+At position 478 to 508, the domain is characterized as EF-hand 4.
+At position 39 to 397, the domain is characterized as G-alpha.
+At position 4 to 477, the domain is characterized as Hexokinase.
+At position 16 to 88, the domain is characterized as KRAB.
+At position 197 to 281, the domain is characterized as KH type-2.
+At position 181 to 349, the domain is characterized as tr-type G.
+At position 187 to 521, the domain is characterized as Kinesin motor.
+At position 29 to 314, the domain is characterized as GH18.
+At position 68 to 134, the domain is characterized as HMA 1.
+At position 267 to 333, the domain is characterized as HMA 3.
+At position 361 to 427, the domain is characterized as HMA 4.
+At position 490 to 556, the domain is characterized as HMA 5.
+At position 566 to 632, the domain is characterized as HMA 6.
+At position 480 to 627, the domain is characterized as uDENN.
+At position 649 to 782, the domain is characterized as cDENN.
+At position 784 to 874, the domain is characterized as dDENN.
+At position 47 to 127, the domain is characterized as KH type-2.
+At position 85 to 256, the domain is characterized as Fe2OG dioxygenase.
+At position 32 to 456, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 978 to 1296, the domain is characterized as PKS/mFAS DH.
+At position 2509 to 2586, the domain is characterized as Carrier.
+At position 195 to 387, the domain is characterized as CheB-type methylesterase.
+At position 11 to 71, the domain is characterized as TRAM.
+At position 131 to 248, the domain is characterized as PilZ.
+At position 9 to 265, the domain is characterized as ABC transporter 1.
+At position 347 to 547, the domain is characterized as ABC transporter 2.
+At position 223 to 358, the domain is characterized as PAS 1.
+At position 376 to 482, the domain is characterized as PAS 2.
+At position 7 to 83, the domain is characterized as RRM.
+At position 29 to 85, the domain is characterized as DPH-type MB.
+At position 585 to 763, the domain is characterized as Helicase ATP-binding.
+At position 794 to 940, the domain is characterized as Helicase C-terminal.
+At position 1 to 423, the domain is characterized as Protein kinase 1.
+At position 1487 to 1557, the domain is characterized as Bromo 1.
+At position 1515 to 2065, the domain is characterized as Protein kinase 2.
+At position 1609 to 1679, the domain is characterized as Bromo 2.
+At position 1 to 91, the domain is characterized as CS.
+At position 242 to 379, the domain is characterized as MPN.
+At position 16 to 113, the domain is characterized as HTH hxlR-type.
+At position 71 to 331, the domain is characterized as Protein kinase.
+At position 491 to 518, the domain is characterized as EF-hand 4.
+At position 18 to 90, the domain is characterized as S4 RNA-binding.
+At position 34 to 110, the domain is characterized as Myb-like.
+At position 111 to 165, the domain is characterized as HTH myb-type 1.
+At position 166 to 218, the domain is characterized as HTH myb-type 2.
+At position 140 to 247, the domain is characterized as AB hydrolase-1.
+At position 171 to 393, the domain is characterized as START.
+At position 1774 to 1823, the domain is characterized as GRIP.
+At position 58 to 308, the domain is characterized as Radical SAM core.
+At position 43 to 174, the domain is characterized as Cyclin N-terminal.
+At position 46 to 265, the domain is characterized as Radical SAM core.
+At position 293 to 531, the domain is characterized as Glutamine amidotransferase type-1.
+At position 11 to 1200, the domain is characterized as Zinc-hook.
+At position 518 to 632, the domain is characterized as SMC hinge.
+At position 36 to 256, the domain is characterized as Radical SAM core.
+At position 243 to 430, the domain is characterized as GATase cobBQ-type.
+At position 3 to 150, the domain is characterized as Ferritin-like diiron.
+At position 157 to 191, the domain is characterized as Rubredoxin-like.
+At position 85 to 384, the domain is characterized as Peptidase A1.
+At position 146 to 174, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 523 to 567, the domain is characterized as LysM.
+At position 249 to 263, the domain is characterized as SAP 2.
+At position 9 to 96, the domain is characterized as GIY-YIG.
+At position 166 to 289, the domain is characterized as OTU.
+At position 154 to 220, the domain is characterized as KH.
+At position 338 to 582, the domain is characterized as TRUD.
+At position 551 to 626, the domain is characterized as Cytochrome b5 heme-binding.
+At position 670 to 782, the domain is characterized as FAD-binding FR-type.
+At position 133 to 330, the domain is characterized as ATP-grasp 1.
+At position 716 to 907, the domain is characterized as ATP-grasp 2.
+At position 973 to 1112, the domain is characterized as MGS-like.
+At position 1 to 198, the domain is characterized as PPIase cyclophilin-type.
+At position 204 to 402, the domain is characterized as GMPS ATP-PPase.
+At position 10 to 195, the domain is characterized as Guanylate kinase-like.
+At position 145 to 366, the domain is characterized as Radical SAM core.
+At position 32 to 145, the domain is characterized as Ig-like V-type.
+At position 52 to 189, the domain is characterized as MPN.
+At position 28 to 335, the domain is characterized as uDENN.
+At position 365 to 492, the domain is characterized as cDENN.
+At position 494 to 640, the domain is characterized as dDENN.
+At position 12 to 74, the domain is characterized as HTH tetR-type.
+At position 38 to 323, the domain is characterized as Protein kinase.
+At position 47 to 346, the domain is characterized as AB hydrolase-1.
+At position 367 to 423, the domain is characterized as CBS 1.
+At position 428 to 483, the domain is characterized as CBS 2.
+At position 26 to 89, the domain is characterized as SLH 1.
+At position 90 to 153, the domain is characterized as SLH 2.
+At position 154 to 203, the domain is characterized as SLH 3.
+At position 64 to 165, the domain is characterized as CBM-cenC 1.
+At position 207 to 319, the domain is characterized as CBM-cenC 2.
+At position 360 to 490, the domain is characterized as CBM-cenC 3.
+At position 514 to 851, the domain is characterized as GH10.
+At position 1279 to 1342, the domain is characterized as SLH 1.
+At position 1345 to 1404, the domain is characterized as SLH 2.
+At position 1407 to 1462, the domain is characterized as SLH 3.
+At position 517 to 811, the domain is characterized as UvrD-like helicase C-terminal.
+At position 314 to 580, the domain is characterized as ABC transporter 1.
+At position 590 to 913, the domain is characterized as ABC transporter 2.
+At position 63 to 394, the domain is characterized as Peptidase A1.
+At position 48 to 314, the domain is characterized as ABC transporter.
+At position 72 to 266, the domain is characterized as Peptidase M12A.
+At position 300 to 334, the domain is characterized as ShKT.
+At position 34 to 320, the domain is characterized as ABC transmembrane type-1.
+At position 353 to 593, the domain is characterized as ABC transporter.
+At position 436 to 530, the domain is characterized as Olduvai 2.
+At position 707 to 799, the domain is characterized as Olduvai 3.
+At position 800 to 888, the domain is characterized as Olduvai 4.
+At position 891 to 946, the domain is characterized as Olduvai 5.
+At position 947 to 1038, the domain is characterized as Olduvai 6.
+At position 1041 to 1114, the domain is characterized as Olduvai 7.
+At position 1116 to 1214, the domain is characterized as Olduvai 8.
+At position 40 to 168, the domain is characterized as MsrB.
+At position 1 to 310, the domain is characterized as Hcy-binding.
+At position 106 to 185, the domain is characterized as GRAM.
+At position 99 to 301, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 88, the domain is characterized as PTS EIIB type-1.
+At position 108 to 470, the domain is characterized as PTS EIIC type-1.
+At position 22 to 217, the domain is characterized as Lon N-terminal.
+At position 188 to 275, the domain is characterized as PDZ.
+At position 311 to 364, the domain is characterized as bHLH.
+At position 203 to 463, the domain is characterized as NR LBD.
+At position 148 to 275, the domain is characterized as MH1.
+At position 331 to 496, the domain is characterized as MH2.
+At position 626 to 684, the domain is characterized as CBS 2.
+At position 47 to 259, the domain is characterized as Ras-GAP.
+At position 512 to 673, the domain is characterized as CRAL-TRIO.
+At position 514 to 575, the domain is characterized as LIM zinc-binding 1.
+At position 579 to 639, the domain is characterized as LIM zinc-binding 2.
+At position 640 to 708, the domain is characterized as LIM zinc-binding 3.
+At position 24 to 89, the domain is characterized as NAC-A/B.
+At position 153 to 191, the domain is characterized as UBA.
+At position 186 to 215, the domain is characterized as IQ.
+At position 359 to 445, the domain is characterized as PA.
+At position 5 to 204, the domain is characterized as uDENN.
+At position 248 to 386, the domain is characterized as cDENN.
+At position 388 to 476, the domain is characterized as dDENN.
+At position 30 to 105, the domain is characterized as RRM.
+At position 13 to 73, the domain is characterized as HTH tetR-type 1.
+At position 217 to 277, the domain is characterized as HTH tetR-type 2.
+At position 428 to 477, the domain is characterized as bHLH.
+At position 277 to 365, the domain is characterized as IPT/TIG 1.
+At position 710 to 767, the domain is characterized as IPT/TIG 2.
+At position 29 to 76, the domain is characterized as MADS-box.
+At position 504 to 534, the domain is characterized as EGF-like.
+At position 7 to 44, the domain is characterized as EF-hand 1.
+At position 255 to 453, the domain is characterized as VWFA.
+At position 465 to 742, the domain is characterized as Peptidase S1.
+At position 19 to 221, the domain is characterized as RNase H type-2.
+At position 165 to 257, the domain is characterized as Olduvai 1.
+At position 258 to 329, the domain is characterized as Olduvai 2.
+At position 330 to 421, the domain is characterized as Olduvai 3.
+At position 424 to 479, the domain is characterized as Olduvai 4.
+At position 480 to 572, the domain is characterized as Olduvai 5.
+At position 573 to 670, the domain is characterized as Olduvai 6.
+At position 17 to 170, the domain is characterized as NAC.
+At position 142 to 200, the domain is characterized as HTH cro/C1-type.
+At position 45 to 149, the domain is characterized as Expansin-like EG45.
+At position 163 to 245, the domain is characterized as Expansin-like CBD.
+At position 63 to 121, the domain is characterized as TCP.
+At position 51 to 119, the domain is characterized as SAM.
+At position 283 to 421, the domain is characterized as Flavodoxin-like.
+At position 1 to 69, the domain is characterized as Lipoyl-binding.
+At position 6 to 164, the domain is characterized as PPIase cyclophilin-type.
+At position 58 to 115, the domain is characterized as SMP 1.
+At position 123 to 181, the domain is characterized as SMP 2.
+At position 32 to 149, the domain is characterized as MTTase N-terminal.
+At position 172 to 405, the domain is characterized as Radical SAM core.
+At position 60 to 293, the domain is characterized as Peptidase S1.
+At position 10 to 115, the domain is characterized as Longin.
+At position 131 to 191, the domain is characterized as v-SNARE coiled-coil homology.
+At position 784 to 860, the domain is characterized as Carrier 1.
+At position 1842 to 1924, the domain is characterized as Carrier 2.
+At position 26 to 68, the domain is characterized as MADS-box.
+At position 20 to 52, the domain is characterized as bZIP.
+At position 113 to 356, the domain is characterized as RGS 1.
+At position 366 to 493, the domain is characterized as RGS 2.
+At position 38 to 98, the domain is characterized as LIM zinc-binding.
+At position 5 to 356, the domain is characterized as Kinesin motor.
+At position 438 to 497, the domain is characterized as SH3.
+At position 242 to 480, the domain is characterized as Peptidase M12B.
+At position 511 to 615, the domain is characterized as Disintegrin.
+At position 108 to 276, the domain is characterized as CP-type G.
+At position 174 to 237, the domain is characterized as HTH crp-type.
+At position 13 to 166, the domain is characterized as Nudix hydrolase.
+At position 883 to 955, the domain is characterized as PDZ 2.
+At position 117 to 201, the domain is characterized as GST N-terminal.
+At position 210 to 359, the domain is characterized as GST C-terminal.
+At position 15 to 301, the domain is characterized as Protein kinase.
+At position 516 to 619, the domain is characterized as Calponin-homology (CH).
+At position 1001 to 1063, the domain is characterized as LIM zinc-binding.
+At position 30 to 311, the domain is characterized as GH18.
+At position 15 to 112, the domain is characterized as PDZ.
+At position 56 to 92, the domain is characterized as LRRNT.
+At position 50 to 162, the domain is characterized as THUMP.
+At position 23 to 117, the domain is characterized as Ig-like C2-type 1.
+At position 124 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 240 to 340, the domain is characterized as Ig-like C2-type 3.
+At position 393 to 478, the domain is characterized as Ig-like C2-type 4.
+At position 487 to 585, the domain is characterized as Ig-like C2-type 5.
+At position 712 to 1000, the domain is characterized as Protein kinase.
+At position 484 to 666, the domain is characterized as Laminin G-like 2.
+At position 112 to 144, the domain is characterized as LisH.
+At position 150 to 207, the domain is characterized as CTLH.
+At position 9 to 141, the domain is characterized as HTH marR-type.
+At position 300 to 376, the domain is characterized as SPOR.
+At position 83 to 135, the domain is characterized as Kazal-like 1.
+At position 174 to 227, the domain is characterized as Kazal-like 2.
+At position 24 to 132, the domain is characterized as Bulb-type lectin.
+At position 99 to 275, the domain is characterized as FBA.
+At position 269 to 324, the domain is characterized as DEK-C.
+At position 328 to 469, the domain is characterized as Tyrosine-protein phosphatase.
+At position 41 to 318, the domain is characterized as tr-type G.
+At position 1 to 430, the domain is characterized as SMP-LTD.
+At position 172 to 263, the domain is characterized as SH2 1.
+At position 270 to 332, the domain is characterized as SH3.
+At position 342 to 432, the domain is characterized as SH2 2.
+At position 465 to 568, the domain is characterized as PH.
+At position 568 to 681, the domain is characterized as C2.
+At position 739 to 933, the domain is characterized as Ras-GAP.
+At position 16 to 110, the domain is characterized as ATP-cone.
+At position 195 to 367, the domain is characterized as PCI.
+At position 779 to 870, the domain is characterized as ELM2.
+At position 885 to 936, the domain is characterized as SANT.
+At position 534 to 610, the domain is characterized as Carrier 1.
+At position 1570 to 1646, the domain is characterized as Carrier 2.
+At position 2106 to 2176, the domain is characterized as Carrier 3.
+At position 35 to 225, the domain is characterized as RNase H type-2.
+At position 91 to 349, the domain is characterized as Protein kinase.
+At position 463 to 498, the domain is characterized as EF-hand 3.
+At position 499 to 533, the domain is characterized as EF-hand 4.
+At position 11 to 130, the domain is characterized as Arf-GAP.
+At position 84 to 173, the domain is characterized as PB1.
+At position 60 to 92, the domain is characterized as EGF-like.
+At position 99 to 342, the domain is characterized as ZP.
+At position 50 to 323, the domain is characterized as Septin-type G.
+At position 435 to 564, the domain is characterized as Guanylate cyclase.
+At position 678 to 813, the domain is characterized as Galectin 1.
+At position 925 to 1059, the domain is characterized as Galectin 2.
+At position 60 to 369, the domain is characterized as Peptidase A1.
+At position 71 to 108, the domain is characterized as VM.
+At position 15 to 199, the domain is characterized as YrdC-like.
+At position 64 to 246, the domain is characterized as PPIase cyclophilin-type.
+At position 230 to 416, the domain is characterized as Helicase C-terminal.
+At position 24 to 289, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 37 to 106, the domain is characterized as KH type-2.
+At position 13 to 70, the domain is characterized as ASCH.
+At position 1 to 189, the domain is characterized as KARI N-terminal Rossmann.
+At position 190 to 335, the domain is characterized as KARI C-terminal knotted.
+At position 146 to 196, the domain is characterized as LIM zinc-binding 3.
+At position 205 to 255, the domain is characterized as LIM zinc-binding 4.
+At position 113 to 164, the domain is characterized as SANT.
+At position 363 to 461, the domain is characterized as SWIRM.
+At position 568 to 700, the domain is characterized as MPN.
+At position 52 to 245, the domain is characterized as Rho-GAP.
+At position 22 to 264, the domain is characterized as Radical SAM core.
+At position 54 to 214, the domain is characterized as TNase-like.
+At position 62 to 156, the domain is characterized as FAR1.
+At position 277 to 373, the domain is characterized as MULE.
+At position 11 to 113, the domain is characterized as LOB.
+At position 133 to 477, the domain is characterized as Protein kinase.
+At position 81 to 262, the domain is characterized as BAR.
+At position 63 to 198, the domain is characterized as C1q.
+At position 11 to 86, the domain is characterized as S1-like.
+At position 161 to 224, the domain is characterized as SANT.
+At position 41 to 130, the domain is characterized as Ig-like 1.
+At position 148 to 235, the domain is characterized as Ig-like 2.
+At position 244 to 331, the domain is characterized as Ig-like 3.
+At position 336 to 421, the domain is characterized as Ig-like 4.
+At position 442 to 532, the domain is characterized as Fibronectin type-III 1.
+At position 538 to 630, the domain is characterized as Fibronectin type-III 2.
+At position 635 to 730, the domain is characterized as Fibronectin type-III 3.
+At position 739 to 830, the domain is characterized as Fibronectin type-III 4.
+At position 851 to 944, the domain is characterized as Fibronectin type-III 5.
+At position 947 to 1046, the domain is characterized as Fibronectin type-III 6.
+At position 15 to 113, the domain is characterized as Ras-associating.
+At position 147 to 1007, the domain is characterized as Myosin motor.
+At position 1012 to 1039, the domain is characterized as IQ 1.
+At position 1063 to 1092, the domain is characterized as IQ 2.
+At position 1102 to 1131, the domain is characterized as IQ 3.
+At position 1125 to 1154, the domain is characterized as IQ 4.
+At position 2054 to 2242, the domain is characterized as Rho-GAP.
+At position 6 to 176, the domain is characterized as PNPLA.
+At position 203 to 388, the domain is characterized as Glutamine amidotransferase type-1.
+At position 87 to 161, the domain is characterized as PUA.
+At position 76 to 98, the domain is characterized as EF-hand 1.
+At position 160 to 194, the domain is characterized as EF-hand 3.
+At position 186 to 369, the domain is characterized as Histidine kinase.
+At position 28 to 128, the domain is characterized as SRCR 1.
+At position 135 to 227, the domain is characterized as SRCR 2.
+At position 232 to 326, the domain is characterized as SRCR 3.
+At position 328 to 428, the domain is characterized as SRCR 4.
+At position 434 to 534, the domain is characterized as SRCR 5.
+At position 555 to 656, the domain is characterized as SRCR 6.
+At position 661 to 761, the domain is characterized as SRCR 7.
+At position 786 to 886, the domain is characterized as SRCR 8.
+At position 39 to 255, the domain is characterized as Radical SAM core.
+At position 8 to 188, the domain is characterized as YrdC-like.
+At position 7 to 92, the domain is characterized as PB1.
+At position 657 to 701, the domain is characterized as UBA.
+At position 29 to 515, the domain is characterized as Sema.
+At position 99 to 174, the domain is characterized as MIT.
+At position 18 to 257, the domain is characterized as YjeF N-terminal.
+At position 334 to 592, the domain is characterized as Autotransporter.
+At position 57 to 147, the domain is characterized as WGR.
+At position 181 to 299, the domain is characterized as PARP alpha-helical.
+At position 341 to 515, the domain is characterized as Helicase ATP-binding.
+At position 542 to 689, the domain is characterized as Helicase C-terminal.
+At position 19 to 98, the domain is characterized as GS beta-grasp.
+At position 23 to 76, the domain is characterized as Clip 1.
+At position 77 to 127, the domain is characterized as Clip 2.
+At position 174 to 440, the domain is characterized as Peptidase S1.
+At position 202 to 237, the domain is characterized as EF-hand 1.
+At position 234 to 269, the domain is characterized as EF-hand 2.
+At position 694 to 756, the domain is characterized as FIP-RBD.
+At position 142 to 230, the domain is characterized as Ig-like C1-type.
+At position 150 to 213, the domain is characterized as bZIP.
+At position 136 to 368, the domain is characterized as Radical SAM core.
+At position 369 to 430, the domain is characterized as TRAM.
+At position 26 to 210, the domain is characterized as Ku.
+At position 12 to 204, the domain is characterized as DPCK.
+At position 404 to 479, the domain is characterized as Rhodanese.
+At position 219 to 257, the domain is characterized as Myb-like 1.
+At position 262 to 327, the domain is characterized as HTH myb-type.
+At position 333 to 382, the domain is characterized as Myb-like 2.
+At position 490 to 702, the domain is characterized as ABC transmembrane type-2 1.
+At position 813 to 1065, the domain is characterized as ABC transporter 2.
+At position 1138 to 1352, the domain is characterized as ABC transmembrane type-2 2.
+At position 37 to 95, the domain is characterized as PQ-loop 1.
+At position 152 to 202, the domain is characterized as PQ-loop 2.
+At position 18 to 120, the domain is characterized as PH.
+At position 1 to 114, the domain is characterized as Reverse transcriptase.
+At position 5 to 242, the domain is characterized as AB hydrolase-1.
+At position 1851 to 1914, the domain is characterized as SAM.
+At position 4 to 218, the domain is characterized as Glutamine amidotransferase type-1.
+At position 158 to 394, the domain is characterized as Radical SAM core.
+At position 397 to 467, the domain is characterized as TRAM.
+At position 34 to 260, the domain is characterized as ABC transporter.
+At position 1 to 64, the domain is characterized as Carrier.
+At position 338 to 413, the domain is characterized as Histone-fold.
+At position 165 to 509, the domain is characterized as USP.
+At position 40 to 141, the domain is characterized as Fibronectin type-III.
+At position 100 to 135, the domain is characterized as STI1 1.
+At position 139 to 178, the domain is characterized as STI1 2.
+At position 339 to 380, the domain is characterized as STI1 3.
+At position 383 to 415, the domain is characterized as STI1 4.
+At position 480 to 523, the domain is characterized as UBA.
+At position 1 to 135, the domain is characterized as PCI.
+At position 143 to 418, the domain is characterized as CNH.
+At position 1 to 169, the domain is characterized as VWFD 1.
+At position 257 to 312, the domain is characterized as TIL 1.
+At position 350 to 534, the domain is characterized as VWFD 2.
+At position 619 to 676, the domain is characterized as TIL 2.
+At position 737 to 782, the domain is characterized as TIL 3.
+At position 821 to 993, the domain is characterized as VWFD 3.
+At position 87 to 292, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 17 to 159, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 183, the domain is characterized as Tyr recombinase.
+At position 141 to 324, the domain is characterized as VWFD.
+At position 472 to 543, the domain is characterized as VWFC 1.
+At position 581 to 648, the domain is characterized as VWFC 2.
+At position 732 to 817, the domain is characterized as CTCK.
+At position 79 to 254, the domain is characterized as FAD-binding PCMH-type.
+At position 41 to 404, the domain is characterized as Peptidase A1.
+At position 119 to 497, the domain is characterized as AB hydrolase-1.
+At position 50 to 212, the domain is characterized as E1.
+At position 293 to 484, the domain is characterized as E2.
+At position 99 to 182, the domain is characterized as MEIS N-terminal.
+At position 590 to 759, the domain is characterized as N-acetyltransferase.
+At position 371 to 426, the domain is characterized as HTH myb-type.
+At position 129 to 237, the domain is characterized as CBM21.
+At position 271 to 330, the domain is characterized as LIM zinc-binding 1.
+At position 331 to 388, the domain is characterized as LIM zinc-binding 2.
+At position 389 to 448, the domain is characterized as LIM zinc-binding 3.
+At position 449 to 506, the domain is characterized as LIM zinc-binding 4.
+At position 24 to 287, the domain is characterized as Protein kinase.
+At position 1 to 95, the domain is characterized as Glutaredoxin.
+At position 139 to 330, the domain is characterized as Rho-GAP.
+At position 1 to 64, the domain is characterized as Cytochrome b5 heme-binding.
+At position 109 to 321, the domain is characterized as Adrift-type SAM-dependent 2'-O-MTase.
+At position 82 to 164, the domain is characterized as S1 motif.
+At position 7 to 242, the domain is characterized as ABC transporter.
+At position 112 to 140, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 143 to 368, the domain is characterized as Sigma-54 factor interaction.
+At position 624 to 678, the domain is characterized as KH.
+At position 689 to 757, the domain is characterized as S1 motif 1.
+At position 920 to 982, the domain is characterized as S1 motif 2.
+At position 52 to 160, the domain is characterized as Expansin-like EG45.
+At position 173 to 254, the domain is characterized as Expansin-like CBD.
+At position 19 to 130, the domain is characterized as WH1.
+At position 499 to 518, the domain is characterized as WH2.
+At position 261 to 352, the domain is characterized as PDZ 1.
+At position 358 to 458, the domain is characterized as PDZ 2.
+At position 2 to 130, the domain is characterized as FAS1.
+At position 207 to 272, the domain is characterized as Laminin EGF-like 1.
+At position 296 to 334, the domain is characterized as EGF-like 1.
+At position 335 to 376, the domain is characterized as EGF-like 2.
+At position 377 to 418, the domain is characterized as EGF-like 3.
+At position 419 to 460, the domain is characterized as EGF-like 4.
+At position 460 to 588, the domain is characterized as FAS1 2.
+At position 604 to 745, the domain is characterized as FAS1 3.
+At position 822 to 887, the domain is characterized as Laminin EGF-like 2.
+At position 947 to 987, the domain is characterized as EGF-like 5.
+At position 988 to 1030, the domain is characterized as EGF-like 6.
+At position 1063 to 1156, the domain is characterized as Link.
+At position 1176 to 1310, the domain is characterized as FAS1 4.
+At position 205 to 374, the domain is characterized as PCI.
+At position 293 to 379, the domain is characterized as Histone-fold.
+At position 38 to 175, the domain is characterized as SCP.
+At position 373 to 419, the domain is characterized as LysM.
+At position 124 to 481, the domain is characterized as GH16.
+At position 9 to 133, the domain is characterized as MsrB.
+At position 212 to 600, the domain is characterized as Peptidase S53.
+At position 31 to 247, the domain is characterized as Peptidase S1.
+At position 17 to 98, the domain is characterized as J.
+At position 5 to 89, the domain is characterized as IPT/TIG.
+At position 98 to 178, the domain is characterized as ACT 1.
+At position 213 to 283, the domain is characterized as ACT 2.
+At position 6 to 105, the domain is characterized as HTH hxlR-type.
+At position 354 to 450, the domain is characterized as Rhodanese.
+At position 255 to 304, the domain is characterized as bHLH.
+At position 27 to 90, the domain is characterized as bZIP.
+At position 161 to 237, the domain is characterized as RRM 1.
+At position 261 to 338, the domain is characterized as RRM 2.
+At position 376 to 453, the domain is characterized as RRM 3.
+At position 62 to 127, the domain is characterized as SCAN box.
+At position 3 to 172, the domain is characterized as PPIase cyclophilin-type.
+At position 22 to 298, the domain is characterized as Protein kinase.
+At position 94 to 327, the domain is characterized as PPM-type phosphatase.
+At position 28 to 324, the domain is characterized as Deacetylase sirtuin-type.
+At position 225 to 260, the domain is characterized as EF-hand 2.
+At position 310 to 461, the domain is characterized as Fe2OG dioxygenase.
+At position 140 to 305, the domain is characterized as Helicase ATP-binding.
+At position 435 to 586, the domain is characterized as Helicase C-terminal.
+At position 795 to 847, the domain is characterized as SANT 1.
+At position 898 to 962, the domain is characterized as SANT 2.
+At position 77 to 125, the domain is characterized as RPE1 insert.
+At position 252 to 383, the domain is characterized as Plus3.
+At position 1 to 148, the domain is characterized as SPX.
+At position 117 to 184, the domain is characterized as SUI1.
+At position 282 to 352, the domain is characterized as PAH.
+At position 1 to 209, the domain is characterized as EAL.
+At position 203 to 392, the domain is characterized as HDOD.
+At position 322 to 415, the domain is characterized as BRCT.
+At position 46 to 149, the domain is characterized as Ig-like C2-type 1.
+At position 250 to 339, the domain is characterized as Ig-like C2-type 2.
+At position 340 to 432, the domain is characterized as Ig-like C2-type 3.
+At position 433 to 533, the domain is characterized as Ig-like C2-type 4.
+At position 534 to 633, the domain is characterized as Ig-like C2-type 5.
+At position 636 to 732, the domain is characterized as Fibronectin type-III 1.
+At position 734 to 829, the domain is characterized as Fibronectin type-III 2.
+At position 833 to 927, the domain is characterized as Ig-like C2-type 6.
+At position 930 to 1025, the domain is characterized as Fibronectin type-III 3.
+At position 1043 to 1136, the domain is characterized as Ig-like C2-type 7.
+At position 4 to 227, the domain is characterized as Collagen IV NC1.
+At position 24 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 150 to 258, the domain is characterized as CBM21.
+At position 85 to 271, the domain is characterized as Reticulon.
+At position 6 to 76, the domain is characterized as HTH merR-type.
+At position 164 to 285, the domain is characterized as B12-binding.
+At position 12 to 80, the domain is characterized as TRAM.
+At position 1081 to 1245, the domain is characterized as PNPLA.
+At position 70 to 134, the domain is characterized as GRAM.
+At position 272 to 444, the domain is characterized as VASt.
+At position 299 to 439, the domain is characterized as SIS 1.
+At position 472 to 625, the domain is characterized as SIS 2.
+At position 139 to 174, the domain is characterized as UVR.
+At position 1 to 91, the domain is characterized as Integrase catalytic.
+At position 44 to 120, the domain is characterized as Inhibitor I9.
+At position 127 to 603, the domain is characterized as Peptidase S8.
+At position 369 to 457, the domain is characterized as PA.
+At position 11 to 233, the domain is characterized as YjeF N-terminal.
+At position 223 to 391, the domain is characterized as TrmE-type G.
+At position 5 to 119, the domain is characterized as PCI.
+At position 54 to 94, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 166 to 241, the domain is characterized as Toprim.
+At position 504 to 516, the domain is characterized as EF-hand.
+At position 194 to 391, the domain is characterized as Peptidase M12B.
+At position 350 to 624, the domain is characterized as Protein kinase.
+At position 99 to 206, the domain is characterized as Calponin-homology (CH) 1.
+At position 266 to 373, the domain is characterized as Calponin-homology (CH) 2.
+At position 109 to 360, the domain is characterized as Protein kinase.
+At position 14 to 69, the domain is characterized as HTH cro/C1-type.
+At position 406 to 569, the domain is characterized as B5.
+At position 799 to 891, the domain is characterized as FDX-ACB.
+At position 141 to 456, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 440 to 533, the domain is characterized as Fibronectin type-III 1.
+At position 824 to 924, the domain is characterized as Fibronectin type-III 2.
+At position 1202 to 1290, the domain is characterized as Fibronectin type-III 3.
+At position 1294 to 1397, the domain is characterized as Fibronectin type-III 4.
+At position 1801 to 1901, the domain is characterized as Fibronectin type-III 5.
+At position 1902 to 1988, the domain is characterized as Fibronectin type-III 6.
+At position 1995 to 2117, the domain is characterized as Fibronectin type-III 7.
+At position 2209 to 2485, the domain is characterized as Protein kinase.
+At position 8 to 99, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 16 to 100, the domain is characterized as ENT.
+At position 1 to 123, the domain is characterized as Bulb-type lectin.
+At position 810 to 866, the domain is characterized as Kazal-like 9.
+At position 1023 to 1145, the domain is characterized as SEA.
+At position 1220 to 1258, the domain is characterized as EGF-like 1.
+At position 1263 to 1439, the domain is characterized as Laminin G-like 1.
+At position 1440 to 1477, the domain is characterized as EGF-like 2.
+At position 1479 to 1516, the domain is characterized as EGF-like 3.
+At position 1526 to 1708, the domain is characterized as Laminin G-like 2.
+At position 1709 to 1748, the domain is characterized as EGF-like 4.
+At position 1784 to 1956, the domain is characterized as Laminin G-like 3.
+At position 90 to 360, the domain is characterized as CN hydrolase.
+At position 98 to 271, the domain is characterized as tr-type G.
+At position 2178 to 2225, the domain is characterized as GRIP.
+At position 196 to 275, the domain is characterized as RRM.
+At position 2 to 168, the domain is characterized as Flavodoxin-like.
+At position 611 to 640, the domain is characterized as IQ.
+At position 121 to 208, the domain is characterized as BRCT.
+At position 355 to 415, the domain is characterized as HTH myb-type.
+At position 833 to 980, the domain is characterized as bMERB.
+At position 183 to 350, the domain is characterized as Helicase ATP-binding.
+At position 361 to 538, the domain is characterized as Helicase C-terminal.
+At position 66 to 317, the domain is characterized as Protein kinase.
+At position 344 to 384, the domain is characterized as UBA.
+At position 101 to 259, the domain is characterized as FCP1 homology.
+At position 301 to 550, the domain is characterized as Glutamine amidotransferase type-1.
+At position 12 to 74, the domain is characterized as 4Fe-4S Wbl-type.
+At position 161 to 434, the domain is characterized as ABC transporter 1.
+At position 837 to 1089, the domain is characterized as ABC transporter 2.
+At position 1162 to 1376, the domain is characterized as ABC transmembrane type-2 2.
+At position 17 to 214, the domain is characterized as Glutamine amidotransferase type-1.
+At position 124 to 167, the domain is characterized as CUE.
+At position 75 to 186, the domain is characterized as HD.
+At position 39 to 164, the domain is characterized as EamA 1.
+At position 191 to 319, the domain is characterized as EamA 2.
+At position 25 to 68, the domain is characterized as Fibronectin type-II 1.
+At position 15 to 291, the domain is characterized as ABC transmembrane type-1.
+At position 323 to 547, the domain is characterized as ABC transporter.
+At position 57 to 320, the domain is characterized as ZP.
+At position 360 to 465, the domain is characterized as PDZ 2.
+At position 24 to 58, the domain is characterized as LRRNT.
+At position 212 to 267, the domain is characterized as LRRCT.
+At position 268 to 371, the domain is characterized as Ig-like C2-type.
+At position 16 to 175, the domain is characterized as MRH.
+At position 1 to 74, the domain is characterized as RRM.
+At position 129 to 482, the domain is characterized as PUM-HD.
+At position 76 to 198, the domain is characterized as THUMP.
+At position 93 to 172, the domain is characterized as PA.
+At position 214 to 327, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 44 to 173, the domain is characterized as MsrB.
+At position 295 to 539, the domain is characterized as NR LBD.
+At position 7 to 154, the domain is characterized as UBC core.
+At position 20 to 87, the domain is characterized as DRBM 1.
+At position 112 to 180, the domain is characterized as DRBM 2.
+At position 225 to 293, the domain is characterized as DRBM 3.
+At position 66 to 145, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 1 to 133, the domain is characterized as Ras-associating.
+At position 430 to 491, the domain is characterized as Sushi 5.
+At position 492 to 550, the domain is characterized as Sushi 6.
+At position 3 to 153, the domain is characterized as MGS-like.
+At position 83 to 288, the domain is characterized as ABC transmembrane type-1.
+At position 103 to 174, the domain is characterized as KRAB 1.
+At position 232 to 299, the domain is characterized as KRAB 2.
+At position 1 to 273, the domain is characterized as Sema.
+At position 275 to 295, the domain is characterized as PSI.
+At position 521 to 794, the domain is characterized as Protein kinase.
+At position 11 to 152, the domain is characterized as RNase H type-1.
+At position 557 to 575, the domain is characterized as EF-hand 1.
+At position 584 to 609, the domain is characterized as EF-hand 2.
+At position 614 to 649, the domain is characterized as EF-hand 3.
+At position 679 to 713, the domain is characterized as EF-hand 4.
+At position 201 to 277, the domain is characterized as KH type-2.
+At position 14 to 56, the domain is characterized as EGF-like.
+At position 217 to 290, the domain is characterized as RRM 1.
+At position 302 to 375, the domain is characterized as RRM 2.
+At position 26 to 163, the domain is characterized as PPPDE.
+At position 51 to 351, the domain is characterized as SAC.
+At position 66 to 118, the domain is characterized as J.
+At position 527 to 755, the domain is characterized as NB-ARC.
+At position 404 to 515, the domain is characterized as PAZ.
+At position 694 to 1012, the domain is characterized as Piwi.
+At position 37 to 104, the domain is characterized as BTB.
+At position 96 to 431, the domain is characterized as Peptidase A1.
+At position 425 to 488, the domain is characterized as bZIP.
+At position 41 to 493, the domain is characterized as Biotin carboxylation.
+At position 579 to 847, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1116 to 1191, the domain is characterized as Biotinyl-binding.
+At position 79 to 184, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 136 to 390, the domain is characterized as ABC transporter 1.
+At position 828 to 1070, the domain is characterized as ABC transporter 2.
+At position 27 to 117, the domain is characterized as Ig-like V-type.
+At position 73 to 312, the domain is characterized as GP-PDE.
+At position 30 to 289, the domain is characterized as Alpha-carbonic anhydrase.
+At position 262 to 292, the domain is characterized as GS.
+At position 293 to 593, the domain is characterized as Protein kinase.
+At position 300 to 371, the domain is characterized as RBD 1.
+At position 373 to 443, the domain is characterized as RBD 2.
+At position 497 to 519, the domain is characterized as GoLoco.
+At position 40 to 335, the domain is characterized as Protein kinase.
+At position 6 to 110, the domain is characterized as tRNA-binding.
+At position 467 to 633, the domain is characterized as JmjC.
+At position 136 to 364, the domain is characterized as Radical SAM core.
+At position 367 to 435, the domain is characterized as TRAM.
+At position 28 to 161, the domain is characterized as Ephrin RBD.
+At position 64 to 288, the domain is characterized as SET.
+At position 144 to 381, the domain is characterized as Radical SAM core.
+At position 384 to 451, the domain is characterized as TRAM.
+At position 124 to 363, the domain is characterized as SMP-LTD.
+At position 178 to 254, the domain is characterized as Biotinyl-binding.
+At position 151 to 294, the domain is characterized as Jacalin-type lectin 2.
+At position 307 to 448, the domain is characterized as Jacalin-type lectin 3.
+At position 451 to 594, the domain is characterized as Jacalin-type lectin 4.
+At position 601 to 744, the domain is characterized as Jacalin-type lectin 5.
+At position 11 to 172, the domain is characterized as PPIase cyclophilin-type.
+At position 27 to 67, the domain is characterized as Chitin-binding type-1.
+At position 22 to 122, the domain is characterized as AB hydrolase-1.
+At position 214 to 315, the domain is characterized as PpiC 1.
+At position 326 to 425, the domain is characterized as PpiC 2.
+At position 573 to 674, the domain is characterized as tRNA-binding.
+At position 29 to 82, the domain is characterized as WAP.
+At position 112 to 163, the domain is characterized as Kazal-like.
+At position 190 to 283, the domain is characterized as Ig-like C2-type.
+At position 289 to 355, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 363 to 413, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 413 to 544, the domain is characterized as NTR.
+At position 58 to 146, the domain is characterized as PPIase FKBP-type 1.
+At position 170 to 258, the domain is characterized as PPIase FKBP-type 2.
+At position 282 to 369, the domain is characterized as PPIase FKBP-type 3.
+At position 393 to 481, the domain is characterized as PPIase FKBP-type 4.
+At position 492 to 527, the domain is characterized as EF-hand 1.
+At position 537 to 572, the domain is characterized as EF-hand 2.
+At position 133 to 225, the domain is characterized as WSC 1.
+At position 236 to 330, the domain is characterized as WSC 2.
+At position 94 to 490, the domain is characterized as GBD/FH3.
+At position 659 to 851, the domain is characterized as FH1.
+At position 868 to 1290, the domain is characterized as FH2.
+At position 1302 to 1336, the domain is characterized as DAD.
+At position 76 to 147, the domain is characterized as PAS.
+At position 148 to 200, the domain is characterized as PAC.
+At position 221 to 426, the domain is characterized as Histidine kinase.
+At position 721 to 901, the domain is characterized as Rho-GAP.
+At position 775 to 851, the domain is characterized as Carrier.
+At position 37 to 141, the domain is characterized as PTS EIIA type-1.
+At position 8 to 265, the domain is characterized as ABC transporter 1.
+At position 307 to 537, the domain is characterized as ABC transporter 2.
+At position 11 to 189, the domain is characterized as Eph LBD.
+At position 311 to 424, the domain is characterized as Fibronectin type-III 1.
+At position 425 to 522, the domain is characterized as Fibronectin type-III 2.
+At position 623 to 886, the domain is characterized as Protein kinase.
+At position 915 to 979, the domain is characterized as SAM.
+At position 107 to 305, the domain is characterized as ATP-grasp.
+At position 371 to 431, the domain is characterized as PAP-associated.
+At position 939 to 1015, the domain is characterized as BRCT.
+At position 269 to 361, the domain is characterized as Ig-like C2-type 2.
+At position 375 to 469, the domain is characterized as Fibronectin type-III 1.
+At position 503 to 598, the domain is characterized as Fibronectin type-III 2.
+At position 604 to 696, the domain is characterized as Fibronectin type-III 3.
+At position 702 to 797, the domain is characterized as Fibronectin type-III 4.
+At position 804 to 899, the domain is characterized as Fibronectin type-III 5.
+At position 1120 to 1205, the domain is characterized as Ig-like C2-type 3.
+At position 1334 to 1423, the domain is characterized as Ig-like C2-type 4.
+At position 444 to 640, the domain is characterized as FtsK.
+At position 35 to 295, the domain is characterized as ZP.
+At position 580 to 677, the domain is characterized as PilZ.
+At position 7 to 69, the domain is characterized as SH3.
+At position 81 to 170, the domain is characterized as SH2.
+At position 194 to 443, the domain is characterized as Protein kinase.
+At position 75 to 197, the domain is characterized as MsrB.
+At position 147 to 266, the domain is characterized as PX.
+At position 318 to 572, the domain is characterized as BAR.
+At position 7 to 295, the domain is characterized as Helicase ATP-binding.
+At position 50 to 106, the domain is characterized as WHEP-TRS.
+At position 249 to 346, the domain is characterized as Fibronectin type-III 1.
+At position 348 to 443, the domain is characterized as Fibronectin type-III 2.
+At position 2 to 73, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 2 to 119, the domain is characterized as FAD-binding FR-type.
+At position 39 to 176, the domain is characterized as Thioredoxin.
+At position 118 to 193, the domain is characterized as MIT.
+At position 120 to 314, the domain is characterized as ATP-grasp.
+At position 24 to 107, the domain is characterized as G protein gamma.
+At position 484 to 861, the domain is characterized as USP.
+At position 917 to 1091, the domain is characterized as Exonuclease.
+At position 36 to 140, the domain is characterized as PTS EIIA type-1.
+At position 52 to 312, the domain is characterized as Protein kinase.
+At position 6 to 229, the domain is characterized as Peptidase S1.
+At position 83 to 183, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 304 to 348, the domain is characterized as CHCH.
+At position 183 to 446, the domain is characterized as Protein kinase.
+At position 85 to 271, the domain is characterized as NodB homology.
+At position 207 to 285, the domain is characterized as RRM.
+At position 458 to 580, the domain is characterized as HD.
+At position 701 to 782, the domain is characterized as ACT 1.
+At position 809 to 879, the domain is characterized as ACT 2.
+At position 5 to 182, the domain is characterized as Guanylate kinase-like.
+At position 72 to 173, the domain is characterized as Glutaredoxin.
+At position 1 to 76, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 76 to 115, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 133 to 164, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 178 to 206, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 3 to 263, the domain is characterized as ABC transporter.
+At position 539 to 660, the domain is characterized as STAS.
+At position 295 to 520, the domain is characterized as Sigma-54 factor interaction.
+At position 20 to 348, the domain is characterized as Lon N-terminal.
+At position 903 to 1131, the domain is characterized as Lon proteolytic.
+At position 223 to 550, the domain is characterized as ABC transporter.
+At position 32 to 103, the domain is characterized as KRAB.
+At position 12 to 196, the domain is characterized as DOC.
+At position 26 to 218, the domain is characterized as RNase H type-2.
+At position 145 to 213, the domain is characterized as MBD.
+At position 351 to 430, the domain is characterized as Ubiquitin-like.
+At position 529 to 588, the domain is characterized as HTH myb-type.
+At position 534 to 584, the domain is characterized as SANT.
+At position 26 to 295, the domain is characterized as EndoU.
+At position 59 to 146, the domain is characterized as PPIase FKBP-type.
+At position 90 to 187, the domain is characterized as CRM.
+At position 239 to 297, the domain is characterized as LIM zinc-binding 1.
+At position 298 to 357, the domain is characterized as LIM zinc-binding 2.
+At position 358 to 416, the domain is characterized as LIM zinc-binding 3.
+At position 150 to 188, the domain is characterized as KH 1.
+At position 219 to 260, the domain is characterized as KH 2.
+At position 291 to 333, the domain is characterized as KH 3.
+At position 360 to 402, the domain is characterized as KH 4.
+At position 431 to 473, the domain is characterized as KH 5.
+At position 504 to 545, the domain is characterized as KH 6.
+At position 577 to 619, the domain is characterized as KH 7.
+At position 651 to 693, the domain is characterized as KH 8.
+At position 724 to 766, the domain is characterized as KH 9.
+At position 798 to 840, the domain is characterized as KH 10.
+At position 872 to 913, the domain is characterized as KH 11.
+At position 970 to 1012, the domain is characterized as KH 12.
+At position 1051 to 1093, the domain is characterized as KH 13.
+At position 1126 to 1168, the domain is characterized as KH 14.
+At position 23 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 2 to 89, the domain is characterized as GST N-terminal.
+At position 91 to 207, the domain is characterized as GST C-terminal.
+At position 7 to 448, the domain is characterized as ABC transporter.
+At position 170 to 370, the domain is characterized as Histidine kinase.
+At position 24 to 111, the domain is characterized as MtN3/slv 1.
+At position 147 to 230, the domain is characterized as MtN3/slv 2.
+At position 340 to 669, the domain is characterized as Transferrin-like 2.
+At position 250 to 385, the domain is characterized as CMP/dCMP-type deaminase.
+At position 668 to 845, the domain is characterized as Helicase ATP-binding.
+At position 900 to 1051, the domain is characterized as Helicase C-terminal.
+At position 37 to 127, the domain is characterized as DEP.
+At position 155 to 220, the domain is characterized as TGS.
+At position 6 to 132, the domain is characterized as PINc.
+At position 52 to 198, the domain is characterized as Cupin type-1.
+At position 529 to 622, the domain is characterized as FDX-ACB.
+At position 135 to 386, the domain is characterized as ABC transporter 1.
+At position 32 to 90, the domain is characterized as Chromo.
+At position 93 to 441, the domain is characterized as MRG.
+At position 303 to 400, the domain is characterized as Rhodanese.
+At position 286 to 341, the domain is characterized as Laminin EGF-like 1.
+At position 342 to 397, the domain is characterized as Laminin EGF-like 2.
+At position 398 to 444, the domain is characterized as Laminin EGF-like 3.
+At position 445 to 494, the domain is characterized as Laminin EGF-like 4.
+At position 495 to 504, the domain is characterized as Laminin EGF-like 5; first part.
+At position 514 to 689, the domain is characterized as Laminin IV type A.
+At position 690 to 723, the domain is characterized as Laminin EGF-like 5; second part.
+At position 724 to 772, the domain is characterized as Laminin EGF-like 6.
+At position 773 to 827, the domain is characterized as Laminin EGF-like 7.
+At position 828 to 883, the domain is characterized as Laminin EGF-like 8.
+At position 884 to 934, the domain is characterized as Laminin EGF-like 9.
+At position 935 to 982, the domain is characterized as Laminin EGF-like 10.
+At position 983 to 1030, the domain is characterized as Laminin EGF-like 11.
+At position 232 to 317, the domain is characterized as Ig-like C2-type 3.
+At position 322 to 398, the domain is characterized as Ig-like C2-type 4.
+At position 404 to 491, the domain is characterized as Ig-like C2-type 5.
+At position 496 to 592, the domain is characterized as Ig-like C2-type 6.
+At position 597 to 695, the domain is characterized as Fibronectin type-III 1.
+At position 700 to 797, the domain is characterized as Fibronectin type-III 2.
+At position 802 to 897, the domain is characterized as Fibronectin type-III 3.
+At position 899 to 990, the domain is characterized as Fibronectin type-III 4.
+At position 41 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 120 to 220, the domain is characterized as Ig-like C2-type 2.
+At position 244 to 355, the domain is characterized as Ig-like V-type 3.
+At position 1 to 182, the domain is characterized as Guanylate kinase-like.
+At position 8 to 62, the domain is characterized as Myosin N-terminal SH3-like.
+At position 67 to 753, the domain is characterized as Myosin motor.
+At position 756 to 779, the domain is characterized as IQ 1.
+At position 780 to 806, the domain is characterized as IQ 2.
+At position 807 to 829, the domain is characterized as IQ 3.
+At position 830 to 854, the domain is characterized as IQ 4.
+At position 855 to 884, the domain is characterized as IQ 5.
+At position 1421 to 1697, the domain is characterized as Dilute.
+At position 68 to 462, the domain is characterized as FH2.
+At position 157 to 237, the domain is characterized as Ubiquitin-like.
+At position 259 to 339, the domain is characterized as BAG.
+At position 191 to 365, the domain is characterized as tr-type G.
+At position 152 to 194, the domain is characterized as EGF-like.
+At position 1 to 123, the domain is characterized as Ferritin-like diiron.
+At position 143 to 317, the domain is characterized as Helicase ATP-binding.
+At position 331 to 501, the domain is characterized as Helicase C-terminal.
+At position 385 to 642, the domain is characterized as Olfactomedin-like.
+At position 620 to 655, the domain is characterized as EF-hand.
+At position 523 to 641, the domain is characterized as SMC hinge.
+At position 49 to 325, the domain is characterized as Septin-type G.
+At position 49 to 190, the domain is characterized as RUN.
+At position 323 to 388, the domain is characterized as PWWP 1.
+At position 1756 to 1818, the domain is characterized as PWWP 2.
+At position 1890 to 1940, the domain is characterized as AWS.
+At position 1942 to 2059, the domain is characterized as SET.
+At position 2066 to 2082, the domain is characterized as Post-SET.
+At position 104 to 179, the domain is characterized as POTRA.
+At position 76 to 132, the domain is characterized as CBS 2.
+At position 153 to 187, the domain is characterized as ACP-type MB.
+At position 31 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 130 to 230, the domain is characterized as Fibronectin type-III 2.
+At position 1 to 224, the domain is characterized as SMP-LTD.
+At position 26 to 286, the domain is characterized as Protein kinase.
+At position 409 to 493, the domain is characterized as Disintegrin.
+At position 38 to 167, the domain is characterized as TBDR plug.
+At position 175 to 972, the domain is characterized as TBDR beta-barrel.
+At position 12 to 267, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 34 to 254, the domain is characterized as Bin3-type SAM.
+At position 34 to 131, the domain is characterized as Ig-like V-type.
+At position 140 to 249, the domain is characterized as Ig-like C1-type.
+At position 42 to 350, the domain is characterized as YjeF C-terminal.
+At position 71 to 115, the domain is characterized as LysM.
+At position 159 to 350, the domain is characterized as CheB-type methylesterase.
+At position 51 to 147, the domain is characterized as PPIase FKBP-type 1.
+At position 175 to 260, the domain is characterized as PPIase FKBP-type 2.
+At position 291 to 383, the domain is characterized as PPIase FKBP-type 3.
+At position 620 to 694, the domain is characterized as S1 motif.
+At position 27 to 102, the domain is characterized as Ig-like C2-type 1.
+At position 111 to 194, the domain is characterized as Ig-like C2-type 2.
+At position 201 to 294, the domain is characterized as Ig-like C2-type 3.
+At position 303 to 396, the domain is characterized as Ig-like C2-type 4.
+At position 399 to 497, the domain is characterized as Ig-like C2-type 5.
+At position 575 to 913, the domain is characterized as Protein kinase.
+At position 46 to 76, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 496 to 540, the domain is characterized as F-box.
+At position 387 to 420, the domain is characterized as WW 3.
+At position 705 to 809, the domain is characterized as HECT.
+At position 983 to 1107, the domain is characterized as PH.
+At position 670 to 759, the domain is characterized as BRCT.
+At position 175 to 400, the domain is characterized as Peptidase S1.
+At position 154 to 388, the domain is characterized as Radical SAM core.
+At position 394 to 456, the domain is characterized as TRAM.
+At position 1 to 29, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 308 to 395, the domain is characterized as Fibronectin type-III 1.
+At position 425 to 523, the domain is characterized as Fibronectin type-III 2.
+At position 77 to 411, the domain is characterized as Rab-GAP TBC.
+At position 79 to 403, the domain is characterized as HAP1 N-terminal.
+At position 92 to 225, the domain is characterized as GST C-terminal.
+At position 85 to 208, the domain is characterized as Thioredoxin 1.
+At position 429 to 550, the domain is characterized as Thioredoxin 2.
+At position 403 to 558, the domain is characterized as TIR.
+At position 39 to 110, the domain is characterized as KRAB.
+At position 245 to 469, the domain is characterized as NR LBD.
+At position 38 to 163, the domain is characterized as Nudix hydrolase.
+At position 8 to 213, the domain is characterized as YjeF N-terminal.
+At position 217 to 485, the domain is characterized as YjeF C-terminal.
+At position 2 to 47, the domain is characterized as LysM.
+At position 336 to 385, the domain is characterized as FBD.
+At position 521 to 783, the domain is characterized as Protein kinase.
+At position 215 to 409, the domain is characterized as Helicase ATP-binding.
+At position 643 to 677, the domain is characterized as SAP.
+At position 654 to 922, the domain is characterized as Autotransporter.
+At position 24 to 66, the domain is characterized as CUE.
+At position 1 to 238, the domain is characterized as ABC transporter.
+At position 420 to 615, the domain is characterized as Flavodoxin-like.
+At position 669 to 914, the domain is characterized as FAD-binding FR-type.
+At position 216 to 315, the domain is characterized as Fe2OG dioxygenase.
+At position 167 to 235, the domain is characterized as HMA.
+At position 150 to 194, the domain is characterized as DSL.
+At position 195 to 228, the domain is characterized as EGF-like 1.
+At position 229 to 259, the domain is characterized as EGF-like 2; atypical.
+At position 261 to 299, the domain is characterized as EGF-like 3.
+At position 301 to 337, the domain is characterized as EGF-like 4.
+At position 339 to 375, the domain is characterized as EGF-like 5; calcium-binding.
+At position 377 to 413, the domain is characterized as EGF-like 6; calcium-binding.
+At position 415 to 450, the domain is characterized as EGF-like 7; calcium-binding.
+At position 452 to 488, the domain is characterized as EGF-like 8.
+At position 490 to 527, the domain is characterized as EGF-like 9.
+At position 529 to 589, the domain is characterized as EGF-like 10; atypical.
+At position 591 to 627, the domain is characterized as EGF-like 11; calcium-binding.
+At position 629 to 665, the domain is characterized as EGF-like 12; calcium-binding.
+At position 667 to 703, the domain is characterized as EGF-like 13.
+At position 706 to 742, the domain is characterized as EGF-like 14.
+At position 744 to 780, the domain is characterized as EGF-like 15; calcium-binding.
+At position 782 to 818, the domain is characterized as EGF-like 16; calcium-binding.
+At position 845 to 934, the domain is characterized as EH.
+At position 277 to 421, the domain is characterized as SIS 1.
+At position 450 to 588, the domain is characterized as SIS 2.
+At position 250 to 496, the domain is characterized as ABC transporter 2.
+At position 348 to 413, the domain is characterized as LIM zinc-binding.
+At position 78 to 259, the domain is characterized as Brix.
+At position 89 to 399, the domain is characterized as IF rod.
+At position 169 to 540, the domain is characterized as TTL.
+At position 274 to 326, the domain is characterized as bHLH.
+At position 61 to 85, the domain is characterized as EF-hand 2.
+At position 34 to 98, the domain is characterized as J.
+At position 5 to 149, the domain is characterized as Nudix hydrolase.
+At position 249 to 458, the domain is characterized as GATase cobBQ-type.
+At position 520 to 808, the domain is characterized as UvrD-like helicase C-terminal.
+At position 92 to 367, the domain is characterized as Septin-type G.
+At position 9 to 98, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 240 to 427, the domain is characterized as FAD-binding PCMH-type.
+At position 83 to 152, the domain is characterized as FHA.
+At position 30 to 117, the domain is characterized as Cystatin.
+At position 149 to 386, the domain is characterized as AIG1-type G.
+At position 100 to 207, the domain is characterized as Cadherin 1.
+At position 208 to 320, the domain is characterized as Cadherin 2.
+At position 321 to 432, the domain is characterized as Cadherin 3.
+At position 433 to 538, the domain is characterized as Cadherin 4.
+At position 539 to 645, the domain is characterized as Cadherin 5.
+At position 514 to 708, the domain is characterized as SEC7.
+At position 758 to 871, the domain is characterized as PH.
+At position 258 to 319, the domain is characterized as CBS 1.
+At position 334 to 392, the domain is characterized as CBS 2.
+At position 61 to 281, the domain is characterized as GB1/RHD3-type G.
+At position 73 to 136, the domain is characterized as S5 DRBM.
+At position 114 to 205, the domain is characterized as SH2.
+At position 217 to 485, the domain is characterized as Protein kinase.
+At position 16 to 118, the domain is characterized as LOB.
+At position 37 to 141, the domain is characterized as FAD-binding FR-type.
+At position 2 to 46, the domain is characterized as LysM 1.
+At position 51 to 95, the domain is characterized as LysM 2.
+At position 103 to 431, the domain is characterized as GH18.
+At position 275 to 616, the domain is characterized as Peptidase A1.
+At position 8 to 357, the domain is characterized as DhaK.
+At position 392 to 599, the domain is characterized as DhaL.
+At position 14 to 73, the domain is characterized as LIM zinc-binding 1.
+At position 73 to 136, the domain is characterized as LIM zinc-binding 2.
+At position 119 to 138, the domain is characterized as UIM 1.
+At position 181 to 200, the domain is characterized as UIM 2.
+At position 244 to 263, the domain is characterized as UIM 3.
+At position 284 to 355, the domain is characterized as LIM zinc-binding.
+At position 484 to 541, the domain is characterized as HTH myb-type.
+At position 18 to 101, the domain is characterized as LBH.
+At position 137 to 221, the domain is characterized as MtN3/slv 2.
+At position 195 to 426, the domain is characterized as NR LBD.
+At position 202 to 251, the domain is characterized as Laminin EGF-like 1.
+At position 252 to 298, the domain is characterized as Laminin EGF-like 2.
+At position 299 to 346, the domain is characterized as Laminin EGF-like 3.
+At position 347 to 397, the domain is characterized as Laminin EGF-like 4.
+At position 398 to 449, the domain is characterized as Laminin EGF-like 5.
+At position 520 to 765, the domain is characterized as ABC transporter.
+At position 34 to 142, the domain is characterized as C-type lectin.
+At position 1018 to 1067, the domain is characterized as GPS.
+At position 1129 to 1246, the domain is characterized as PLAT.
+At position 2 to 210, the domain is characterized as RNase H type-2.
+At position 1271 to 1343, the domain is characterized as MIB/HERC2.
+At position 2156 to 2618, the domain is characterized as HECT.
+At position 85 to 157, the domain is characterized as S4 RNA-binding.
+At position 26 to 59, the domain is characterized as LRRNT.
+At position 93 to 121, the domain is characterized as EF-hand 1.
+At position 165 to 195, the domain is characterized as EF-hand 3.
+At position 198 to 233, the domain is characterized as EF-hand 4.
+At position 116 to 196, the domain is characterized as Smr.
+At position 83 to 174, the domain is characterized as BRCT.
+At position 375 to 556, the domain is characterized as UmuC.
+At position 2 to 258, the domain is characterized as Alpha-carbonic anhydrase.
+At position 12 to 463, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 967 to 1273, the domain is characterized as PKS/mFAS DH.
+At position 2404 to 2479, the domain is characterized as Carrier.
+At position 25 to 190, the domain is characterized as Helicase ATP-binding.
+At position 27 to 161, the domain is characterized as Galectin 1.
+At position 190 to 314, the domain is characterized as Galectin 2.
+At position 98 to 341, the domain is characterized as Radical SAM core.
+At position 195 to 377, the domain is characterized as Helicase ATP-binding.
+At position 414 to 570, the domain is characterized as Helicase C-terminal.
+At position 80 to 320, the domain is characterized as Calpain catalytic.
+At position 1 to 310, the domain is characterized as SAM-dependent MTase C5-type.
+At position 615 to 700, the domain is characterized as BRCT.
+At position 29 to 177, the domain is characterized as FAS1 1.
+At position 205 to 351, the domain is characterized as FAS1 2.
+At position 412 to 646, the domain is characterized as ABC transporter 1.
+At position 418 to 747, the domain is characterized as Kinesin motor.
+At position 13 to 164, the domain is characterized as NAC.
+At position 71 to 355, the domain is characterized as GH16.
+At position 66 to 129, the domain is characterized as bZIP.
+At position 623 to 882, the domain is characterized as Protein kinase.
+At position 883 to 934, the domain is characterized as AGC-kinase C-terminal.
+At position 676 to 854, the domain is characterized as STAS.
+At position 232 to 262, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 1 to 53, the domain is characterized as Oxytoxin-type inhibitor cystine knot (ICK).
+At position 143 to 206, the domain is characterized as Ig-like C2-type 2.
+At position 326 to 412, the domain is characterized as Ig-like C2-type 4.
+At position 419 to 542, the domain is characterized as Ig-like C2-type 5.
+At position 545 to 636, the domain is characterized as Ig-like C2-type 6.
+At position 643 to 728, the domain is characterized as Ig-like C2-type 7.
+At position 809 to 1139, the domain is characterized as Protein kinase.
+At position 159 to 387, the domain is characterized as SMP-LTD.
+At position 535 to 803, the domain is characterized as MHD.
+At position 655 to 745, the domain is characterized as ARID.
+At position 443 to 624, the domain is characterized as Thioredoxin.
+At position 176 to 271, the domain is characterized as Rieske.
+At position 661 to 849, the domain is characterized as ATP-grasp 2.
+At position 915 to 1043, the domain is characterized as MGS-like.
+At position 217 to 318, the domain is characterized as Fe2OG dioxygenase.
+At position 634 to 701, the domain is characterized as S1 motif.
+At position 523 to 695, the domain is characterized as tr-type G.
+At position 347 to 417, the domain is characterized as PAS.
+At position 100 to 182, the domain is characterized as PRC barrel.
+At position 20 to 153, the domain is characterized as Calponin-homology (CH).
+At position 458 to 654, the domain is characterized as FtsK.
+At position 1 to 118, the domain is characterized as Reverse transcriptase.
+At position 32 to 126, the domain is characterized as Fibronectin type-III 1.
+At position 127 to 227, the domain is characterized as Fibronectin type-III 2.
+At position 331 to 432, the domain is characterized as Fibronectin type-III 4.
+At position 40 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 67 to 139, the domain is characterized as KH 1.
+At position 175 to 245, the domain is characterized as KH 2.
+At position 324 to 391, the domain is characterized as KH 3.
+At position 408 to 476, the domain is characterized as KH 4.
+At position 576 to 640, the domain is characterized as KH 5.
+At position 66 to 389, the domain is characterized as Peptidase S8.
+At position 31 to 182, the domain is characterized as MRH.
+At position 44 to 123, the domain is characterized as PAS.
+At position 209 to 255, the domain is characterized as F-box.
+At position 35 to 119, the domain is characterized as Inhibitor I9.
+At position 129 to 403, the domain is characterized as Peptidase S8.
+At position 6 to 71, the domain is characterized as HTH asnC-type.
+At position 36 to 89, the domain is characterized as Clip.
+At position 128 to 391, the domain is characterized as Peptidase S1.
+At position 572 to 655, the domain is characterized as PDZ.
+At position 803 to 986, the domain is characterized as Guanylate kinase-like.
+At position 143 to 220, the domain is characterized as PRC barrel.
+At position 60 to 225, the domain is characterized as Helicase ATP-binding.
+At position 59 to 167, the domain is characterized as sHSP.
+At position 1289 to 1427, the domain is characterized as RanBD1.
+At position 16 to 97, the domain is characterized as CBS 1.
+At position 113 to 185, the domain is characterized as CBS 2.
+At position 198 to 273, the domain is characterized as CBS 3.
+At position 293 to 351, the domain is characterized as CBS 4.
+At position 33 to 383, the domain is characterized as IF rod.
+At position 70 to 280, the domain is characterized as CHASE.
+At position 660 to 948, the domain is characterized as Protein kinase.
+At position 133 to 168, the domain is characterized as EF-hand.
+At position 274 to 373, the domain is characterized as PpiC 2.
+At position 404 to 439, the domain is characterized as EF-hand 2.
+At position 100 to 151, the domain is characterized as bHLH.
+At position 254 to 289, the domain is characterized as EF-hand.
+At position 413 to 570, the domain is characterized as Ferric oxidoreductase.
+At position 609 to 729, the domain is characterized as FAD-binding FR-type.
+At position 69 to 299, the domain is characterized as PPM-type phosphatase.
+At position 162 to 337, the domain is characterized as OBG-type G.
+At position 22 to 49, the domain is characterized as EF-hand 1.
+At position 18 to 114, the domain is characterized as Fibronectin type-III 1.
+At position 115 to 217, the domain is characterized as Fibronectin type-III 2.
+At position 394 to 470, the domain is characterized as B5.
+At position 681 to 774, the domain is characterized as FDX-ACB.
+At position 14 to 98, the domain is characterized as GIY-YIG.
+At position 159 to 335, the domain is characterized as Helicase ATP-binding.
+At position 349 to 519, the domain is characterized as Helicase C-terminal.
+At position 444 to 687, the domain is characterized as NR LBD.
+At position 449 to 613, the domain is characterized as YDG.
+At position 46 to 280, the domain is characterized as Radical SAM core.
+At position 8 to 77, the domain is characterized as HTH merR-type.
+At position 13 to 65, the domain is characterized as bHLH.
+At position 2 to 316, the domain is characterized as Glutamine amidotransferase type-2.
+At position 389 to 528, the domain is characterized as SIS 1.
+At position 561 to 703, the domain is characterized as SIS 2.
+At position 21 to 261, the domain is characterized as ABC transporter.
+At position 37 to 100, the domain is characterized as NAC-A/B.
+At position 267 to 464, the domain is characterized as B30.2/SPRY.
+At position 24 to 149, the domain is characterized as VOC 1.
+At position 155 to 283, the domain is characterized as VOC 2.
+At position 6 to 160, the domain is characterized as NAC.
+At position 2 to 114, the domain is characterized as Response regulatory.
+At position 148 to 345, the domain is characterized as HD-GYP.
+At position 37 to 113, the domain is characterized as Lipoyl-binding.
+At position 175 to 215, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 1 to 168, the domain is characterized as B30.2/SPRY.
+At position 218 to 393, the domain is characterized as Helicase ATP-binding.
+At position 407 to 577, the domain is characterized as Helicase C-terminal.
+At position 97 to 383, the domain is characterized as tr-type G.
+At position 5 to 193, the domain is characterized as DPCK.
+At position 7 to 210, the domain is characterized as Glutamine amidotransferase type-1.
+At position 109 to 198, the domain is characterized as HTH La-type RNA-binding.
+At position 199 to 277, the domain is characterized as RRM.
+At position 324 to 376, the domain is characterized as TSP type-1.
+At position 254 to 349, the domain is characterized as PH.
+At position 13 to 306, the domain is characterized as Protein kinase.
+At position 93 to 148, the domain is characterized as CBS 1.
+At position 152 to 210, the domain is characterized as CBS 2.
+At position 1158 to 1437, the domain is characterized as Protein kinase.
+At position 1501 to 1887, the domain is characterized as HECT.
+At position 31 to 246, the domain is characterized as GB1/RHD3-type G.
+At position 338 to 451, the domain is characterized as PAZ.
+At position 625 to 946, the domain is characterized as Piwi.
+At position 244 to 387, the domain is characterized as FCP1 homology.
+At position 49 to 126, the domain is characterized as RRM 1.
+At position 332 to 409, the domain is characterized as RRM 4.
+At position 571 to 648, the domain is characterized as PABC.
+At position 121 to 211, the domain is characterized as RRM.
+At position 105 to 337, the domain is characterized as Radical SAM core.
+At position 77 to 400, the domain is characterized as AB hydrolase-1.
+At position 41 to 146, the domain is characterized as MaoC-like.
+At position 175 to 324, the domain is characterized as GAF 1.
+At position 356 to 512, the domain is characterized as GAF 2.
+At position 542 to 866, the domain is characterized as PDEase.
+At position 150 to 194, the domain is characterized as EGF-like.
+At position 702 to 1024, the domain is characterized as HECT.
+At position 266 to 426, the domain is characterized as BTB 1.
+At position 484 to 551, the domain is characterized as BTB 2.
+At position 175 to 262, the domain is characterized as Ras-associating.
+At position 305 to 414, the domain is characterized as PH.
+At position 38 to 544, the domain is characterized as Biotin carboxylation.
+At position 190 to 384, the domain is characterized as ATP-grasp.
+At position 671 to 745, the domain is characterized as Biotinyl-binding.
+At position 1502 to 1843, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1847 to 2163, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 10 to 138, the domain is characterized as Runt.
+At position 106 to 333, the domain is characterized as Radical SAM core.
+At position 196 to 462, the domain is characterized as SF4 helicase; first part.
+At position 341 to 604, the domain is characterized as SF4 helicase; second part.
+At position 146 to 327, the domain is characterized as FAD-binding PCMH-type.
+At position 21 to 219, the domain is characterized as KIND.
+At position 263 to 277, the domain is characterized as WH2 1.
+At position 357 to 374, the domain is characterized as WH2 2.
+At position 40 to 111, the domain is characterized as KRAB.
+At position 87 to 232, the domain is characterized as Fe2OG dioxygenase.
+At position 61 to 271, the domain is characterized as YjeF N-terminal.
+At position 22 to 500, the domain is characterized as Sema.
+At position 554 to 636, the domain is characterized as Ig-like C2-type.
+At position 50 to 192, the domain is characterized as Cupin type-1 1.
+At position 228 to 369, the domain is characterized as Cupin type-1 2.
+At position 216 to 294, the domain is characterized as SPAZ 1.
+At position 354 to 504, the domain is characterized as SPAZ 2.
+At position 33 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 169 to 259, the domain is characterized as Ig-like C2-type 2.
+At position 272 to 372, the domain is characterized as Ig-like C2-type 3.
+At position 490 to 777, the domain is characterized as Protein kinase.
+At position 33 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 214 to 309, the domain is characterized as Ig-like C2-type 3.
+At position 331 to 403, the domain is characterized as Ig-like C2-type 4.
+At position 416 to 524, the domain is characterized as Ig-like C2-type 5.
+At position 600 to 962, the domain is characterized as Protein kinase.
+At position 95 to 159, the domain is characterized as J.
+At position 11 to 342, the domain is characterized as GH10.
+At position 14 to 62, the domain is characterized as F-box.
+At position 353 to 404, the domain is characterized as FBD.
+At position 440 to 511, the domain is characterized as Histone-fold.
+At position 35 to 151, the domain is characterized as Cadherin 1.
+At position 152 to 252, the domain is characterized as Cadherin 2.
+At position 57 to 96, the domain is characterized as CBS.
+At position 11 to 147, the domain is characterized as MPN.
+At position 297 to 382, the domain is characterized as SCD.
+At position 5 to 126, the domain is characterized as Fido.
+At position 1 to 263, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 602 to 956, the domain is characterized as Reverse transcriptase.
+At position 230 to 293, the domain is characterized as KH.
+At position 356 to 449, the domain is characterized as HD.
+At position 27 to 162, the domain is characterized as Nudix hydrolase.
+At position 198 to 283, the domain is characterized as RCK C-terminal 1.
+At position 285 to 369, the domain is characterized as RCK C-terminal 2.
+At position 10 to 117, the domain is characterized as HIT.
+At position 42 to 138, the domain is characterized as Fibronectin type-III 1.
+At position 139 to 245, the domain is characterized as Fibronectin type-III 2.
+At position 27 to 169, the domain is characterized as SIS 1.
+At position 180 to 317, the domain is characterized as SIS 2.
+At position 7 to 269, the domain is characterized as F-BAR.
+At position 551 to 807, the domain is characterized as MHD.
+At position 165 to 339, the domain is characterized as VWFA.
+At position 60 to 276, the domain is characterized as Radical SAM core.
+At position 184 to 439, the domain is characterized as NR LBD.
+At position 156 to 188, the domain is characterized as EF-hand 3.
+At position 20 to 85, the domain is characterized as GRAM.
+At position 216 to 404, the domain is characterized as Rab-GAP TBC.
+At position 166 to 303, the domain is characterized as Helicase ATP-binding.
+At position 104 to 359, the domain is characterized as Tyrosine-protein phosphatase.
+At position 20 to 138, the domain is characterized as Ig-like V-type.
+At position 143 to 235, the domain is characterized as Ig-like C2-type 1.
+At position 331 to 416, the domain is characterized as Ig-like C2-type 3.
+At position 419 to 500, the domain is characterized as Ig-like C2-type 4.
+At position 505 to 582, the domain is characterized as Ig-like C2-type 5.
+At position 593 to 676, the domain is characterized as Ig-like C2-type 6.
+At position 539 to 826, the domain is characterized as NB-ARC.
+At position 133 to 164, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 178 to 299, the domain is characterized as Ferric oxidoreductase.
+At position 328 to 445, the domain is characterized as FAD-binding FR-type.
+At position 305 to 440, the domain is characterized as Fido.
+At position 369 to 386, the domain is characterized as ITAM.
+At position 178 to 229, the domain is characterized as Rubredoxin-like.
+At position 1 to 86, the domain is characterized as MSS4.
+At position 87 to 126, the domain is characterized as EGF-like 1.
+At position 127 to 179, the domain is characterized as EGF-like 2; calcium-binding.
+At position 180 to 222, the domain is characterized as EGF-like 3; calcium-binding.
+At position 225 to 267, the domain is characterized as EGF-like 4.
+At position 532 to 746, the domain is characterized as TSP C-terminal.
+At position 58 to 195, the domain is characterized as Reverse transcriptase.
+At position 800 to 875, the domain is characterized as Peptidase A2.
+At position 890 to 936, the domain is characterized as G-patch.
+At position 65 to 105, the domain is characterized as Disintegrin.
+At position 733 to 855, the domain is characterized as N-terminal Ras-GEF.
+At position 891 to 1118, the domain is characterized as Ras-GEF.
+At position 22 to 122, the domain is characterized as Ig-like V-type.
+At position 204 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 38 to 83, the domain is characterized as SANT.
+At position 946 to 1227, the domain is characterized as ABC transmembrane type-1 2.
+At position 1264 to 1498, the domain is characterized as ABC transporter 2.
+At position 744 to 800, the domain is characterized as WHEP-TRS 1.
+At position 816 to 872, the domain is characterized as WHEP-TRS 2.
+At position 890 to 946, the domain is characterized as WHEP-TRS 3.
+At position 969 to 1025, the domain is characterized as WHEP-TRS 4.
+At position 1044 to 1100, the domain is characterized as WHEP-TRS 5.
+At position 1118 to 1174, the domain is characterized as WHEP-TRS 6.
+At position 81 to 165, the domain is characterized as Saposin B-type.
+At position 9 to 230, the domain is characterized as ABC transporter.
+At position 64 to 291, the domain is characterized as Radical SAM core.
+At position 1 to 72, the domain is characterized as PBS-linker.
+At position 239 to 344, the domain is characterized as BTB 1.
+At position 405 to 472, the domain is characterized as BTB 2.
+At position 43 to 111, the domain is characterized as SH3.
+At position 117 to 209, the domain is characterized as SH2.
+At position 235 to 492, the domain is characterized as Protein kinase.
+At position 139 to 199, the domain is characterized as OVATE.
+At position 61 to 533, the domain is characterized as Sema.
+At position 535 to 587, the domain is characterized as PSI 1.
+At position 683 to 730, the domain is characterized as PSI 2.
+At position 834 to 880, the domain is characterized as PSI 3.
+At position 888 to 975, the domain is characterized as IPT/TIG 1.
+At position 977 to 1064, the domain is characterized as IPT/TIG 2.
+At position 1097 to 1193, the domain is characterized as IPT/TIG 3.
+At position 98 to 278, the domain is characterized as ABC transmembrane type-1.
+At position 134 to 201, the domain is characterized as KH 1.
+At position 286 to 350, the domain is characterized as KH 2.
+At position 875 to 938, the domain is characterized as SAM.
+At position 204 to 422, the domain is characterized as Radical SAM core.
+At position 2 to 53, the domain is characterized as Rubredoxin-like 1.
+At position 22 to 136, the domain is characterized as Ig-like V-type.
+At position 139 to 226, the domain is characterized as Ig-like C2-type.
+At position 10 to 400, the domain is characterized as Trm1 methyltransferase.
+At position 67 to 385, the domain is characterized as YcaO.
+At position 6 to 220, the domain is characterized as Radical SAM core.
+At position 87 to 137, the domain is characterized as HTH cro/C1-type.
+At position 20 to 259, the domain is characterized as ABC transporter.
+At position 109 to 240, the domain is characterized as GST C-terminal.
+At position 2 to 180, the domain is characterized as Glutamine amidotransferase type-2.
+At position 280 to 541, the domain is characterized as Asparagine synthetase.
+At position 220 to 533, the domain is characterized as Protein kinase.
+At position 152 to 330, the domain is characterized as VWFA.
+At position 52 to 144, the domain is characterized as ARID.
+At position 280 to 471, the domain is characterized as PNPLA.
+At position 208 to 554, the domain is characterized as Protein kinase.
+At position 48 to 354, the domain is characterized as AB hydrolase-1.
+At position 438 to 490, the domain is characterized as CBS 2.
+At position 286 to 462, the domain is characterized as CRAL-TRIO.
+At position 512 to 631, the domain is characterized as GOLD.
+At position 39 to 492, the domain is characterized as Hexokinase.
+At position 141 to 312, the domain is characterized as Helicase ATP-binding.
+At position 336 to 486, the domain is characterized as Helicase C-terminal.
+At position 28 to 149, the domain is characterized as Ig-like C2-type 1.
+At position 162 to 286, the domain is characterized as Ig-like C2-type 2.
+At position 303 to 424, the domain is characterized as Ig-like C2-type 3.
+At position 431 to 560, the domain is characterized as Ig-like C2-type 4.
+At position 1141 to 1381, the domain is characterized as Glutamine amidotransferase type-1.
+At position 427 to 476, the domain is characterized as Chitin-binding type-2.
+At position 83 to 207, the domain is characterized as GST C-terminal.
+At position 73 to 276, the domain is characterized as ABC transmembrane type-1.
+At position 828 to 1111, the domain is characterized as Protein kinase.
+At position 1112 to 1216, the domain is characterized as AGC-kinase C-terminal.
+At position 639 to 728, the domain is characterized as BRCT.
+At position 154 to 216, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 401 to 463, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 1 to 35, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 306 to 342, the domain is characterized as CBM1.
+At position 286 to 321, the domain is characterized as EF-hand 1.
+At position 331 to 366, the domain is characterized as EF-hand 2.
+At position 548 to 682, the domain is characterized as DAGKc.
+At position 147 to 266, the domain is characterized as C2 1.
+At position 278 to 411, the domain is characterized as C2 2.
+At position 149 to 238, the domain is characterized as CS.
+At position 260 to 350, the domain is characterized as SGS.
+At position 35 to 270, the domain is characterized as ABC transporter 1.
+At position 281 to 524, the domain is characterized as ABC transporter 2.
+At position 523 to 623, the domain is characterized as PB1.
+At position 148 to 455, the domain is characterized as Protein kinase.
+At position 36 to 207, the domain is characterized as Helicase ATP-binding.
+At position 218 to 379, the domain is characterized as Helicase C-terminal.
+At position 98 to 354, the domain is characterized as Radical SAM core.
+At position 140 to 291, the domain is characterized as Exonuclease.
+At position 94 to 166, the domain is characterized as AB hydrolase-1.
+At position 349 to 427, the domain is characterized as RRM.
+At position 55 to 201, the domain is characterized as UBC core.
+At position 194 to 551, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 179 to 231, the domain is characterized as bHLH.
+At position 39 to 125, the domain is characterized as WSC.
+At position 131 to 246, the domain is characterized as Fibronectin type-III.
+At position 493 to 758, the domain is characterized as Protein kinase.
+At position 27 to 361, the domain is characterized as BPP.
+At position 140 to 345, the domain is characterized as ABC transmembrane type-1 1.
+At position 431 to 632, the domain is characterized as ABC transmembrane type-1 2.
+At position 188 to 273, the domain is characterized as PPIase FKBP-type.
+At position 92 to 143, the domain is characterized as bHLH.
+At position 659 to 782, the domain is characterized as PX.
+At position 54 to 112, the domain is characterized as F-box.
+At position 213 to 274, the domain is characterized as CBS 1.
+At position 289 to 347, the domain is characterized as CBS 2.
+At position 27 to 115, the domain is characterized as Plastocyanin-like.
+At position 548 to 689, the domain is characterized as SIS 2.
+At position 20 to 85, the domain is characterized as Kazal-like.
+At position 218 to 456, the domain is characterized as START.
+At position 163 to 239, the domain is characterized as RRM.
+At position 30 to 216, the domain is characterized as ATLF-like.
+At position 1 to 188, the domain is characterized as RNase H type-2.
+At position 71 to 424, the domain is characterized as IF rod.
+At position 457 to 574, the domain is characterized as LTD.
+At position 34 to 275, the domain is characterized as ABC transporter.
+At position 14 to 319, the domain is characterized as Protein kinase.
+At position 22 to 241, the domain is characterized as tr-type G.
+At position 26 to 104, the domain is characterized as Inhibitor I9.
+At position 134 to 645, the domain is characterized as Peptidase S8.
+At position 400 to 494, the domain is characterized as PA.
+At position 7 to 75, the domain is characterized as KRAB.
+At position 268 to 302, the domain is characterized as SAP.
+At position 3 to 145, the domain is characterized as Jacalin-type lectin.
+At position 571 to 649, the domain is characterized as SH3.
+At position 36 to 101, the domain is characterized as VWFC 1.
+At position 115 to 181, the domain is characterized as VWFC 2.
+At position 262 to 327, the domain is characterized as VWFC 3.
+At position 11 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 418, the domain is characterized as GMPS ATP-PPase.
+At position 4 to 169, the domain is characterized as 3'-5' exonuclease.
+At position 624 to 779, the domain is characterized as MOSC.
+At position 83 to 282, the domain is characterized as Glutamine amidotransferase type-1.
+At position 43 to 87, the domain is characterized as bZIP.
+At position 110 to 326, the domain is characterized as DOG1.
+At position 16 to 134, the domain is characterized as PID.
+At position 422 to 612, the domain is characterized as Rab-GAP TBC.
+At position 76 to 255, the domain is characterized as FAD-binding PCMH-type.
+At position 8 to 71, the domain is characterized as LCN-type CS-alpha/beta.
+At position 46 to 233, the domain is characterized as PCI.
+At position 154 to 183, the domain is characterized as IQ 1.
+At position 199 to 226, the domain is characterized as IQ 2.
+At position 24 to 87, the domain is characterized as SH3b.
+At position 282 to 374, the domain is characterized as PH 1.
+At position 389 to 478, the domain is characterized as PH 2.
+At position 479 to 606, the domain is characterized as Arf-GAP.
+At position 671 to 785, the domain is characterized as PH 3.
+At position 795 to 901, the domain is characterized as PH 4.
+At position 903 to 1084, the domain is characterized as Rho-GAP.
+At position 1113 to 1206, the domain is characterized as Ras-associating.
+At position 1219 to 1321, the domain is characterized as PH 5.
+At position 554 to 613, the domain is characterized as SH3.
+At position 663 to 757, the domain is characterized as PDZ.
+At position 2104 to 2167, the domain is characterized as SAM.
+At position 27 to 125, the domain is characterized as GOLD.
+At position 660 to 779, the domain is characterized as C2.
+At position 816 to 1031, the domain is characterized as Rho-GAP.
+At position 178 to 352, the domain is characterized as EngA-type G 2.
+At position 43 to 143, the domain is characterized as Expansin-like EG45.
+At position 462 to 523, the domain is characterized as LIM zinc-binding 1.
+At position 527 to 587, the domain is characterized as LIM zinc-binding 2.
+At position 587 to 656, the domain is characterized as LIM zinc-binding 3.
+At position 93 to 257, the domain is characterized as Helicase ATP-binding.
+At position 281 to 448, the domain is characterized as Helicase C-terminal.
+At position 46 to 190, the domain is characterized as SCP.
+At position 1 to 382, the domain is characterized as PTS EIIC type-1.
+At position 397 to 478, the domain is characterized as PTS EIIB type-1.
+At position 515 to 619, the domain is characterized as PTS EIIA type-1.
+At position 46 to 126, the domain is characterized as Saposin B-type.
+At position 106 to 289, the domain is characterized as tr-type G.
+At position 18 to 181, the domain is characterized as EngB-type G.
+At position 120 to 214, the domain is characterized as Rhodanese.
+At position 37 to 257, the domain is characterized as Peptidase S1.
+At position 62 to 168, the domain is characterized as TBDR plug.
+At position 173 to 743, the domain is characterized as TBDR beta-barrel.
+At position 61 to 164, the domain is characterized as Ras-associating.
+At position 284 to 342, the domain is characterized as FHA.
+At position 516 to 809, the domain is characterized as Dilute.
+At position 1027 to 1112, the domain is characterized as PDZ.
+At position 32 to 105, the domain is characterized as Ig-like C2-type 1.
+At position 64 to 95, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 97 to 126, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 845 to 914, the domain is characterized as BTB.
+At position 311 to 408, the domain is characterized as RRM 1.
+At position 430 to 511, the domain is characterized as RRM 2.
+At position 33 to 231, the domain is characterized as Lon N-terminal.
+At position 620 to 801, the domain is characterized as Lon proteolytic.
+At position 57 to 133, the domain is characterized as FAR1 1.
+At position 225 to 301, the domain is characterized as FAR1 2.
+At position 399 to 495, the domain is characterized as MULE.
+At position 660 to 729, the domain is characterized as S1 motif.
+At position 42 to 61, the domain is characterized as UIM 1.
+At position 87 to 106, the domain is characterized as UIM 2.
+At position 122 to 141, the domain is characterized as UIM 3; degenerate.
+At position 149 to 168, the domain is characterized as UIM 4.
+At position 188 to 248, the domain is characterized as LIM zinc-binding.
+At position 342 to 490, the domain is characterized as Helicase C-terminal.
+At position 48 to 86, the domain is characterized as LRRNT.
+At position 311 to 363, the domain is characterized as LRRCT.
+At position 364 to 452, the domain is characterized as Ig-like C2-type.
+At position 184 to 342, the domain is characterized as Cupin type-1 1.
+At position 401 to 563, the domain is characterized as Cupin type-1 2.
+At position 54 to 178, the domain is characterized as C-type lectin.
+At position 228 to 312, the domain is characterized as Death.
+At position 611 to 689, the domain is characterized as BRCT.
+At position 251 to 329, the domain is characterized as RRM.
+At position 43 to 97, the domain is characterized as HTH cro/C1-type.
+At position 534 to 553, the domain is characterized as WH2.
+At position 7 to 202, the domain is characterized as tr-type G.
+At position 198 to 390, the domain is characterized as Peptidase M12B.
+At position 625 to 654, the domain is characterized as EGF-like.
+At position 320 to 350, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 368 to 397, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 331 to 1046, the domain is characterized as Myosin motor.
+At position 1048 to 1077, the domain is characterized as IQ 1.
+At position 1075 to 1104, the domain is characterized as IQ 2.
+At position 32 to 322, the domain is characterized as Protein kinase.
+At position 309 to 377, the domain is characterized as S1 motif 1.
+At position 484 to 552, the domain is characterized as S1 motif 2.
+At position 569 to 638, the domain is characterized as S1 motif 3.
+At position 203 to 254, the domain is characterized as VWFC.
+At position 29 to 367, the domain is characterized as Transferrin-like 1.
+At position 374 to 719, the domain is characterized as Transferrin-like 2.
+At position 48 to 161, the domain is characterized as sHSP.
+At position 103 to 187, the domain is characterized as GST N-terminal.
+At position 196 to 345, the domain is characterized as GST C-terminal.
+At position 31 to 61, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 322 to 488, the domain is characterized as SUN.
+At position 149 to 186, the domain is characterized as EF-hand 4.
+At position 229 to 350, the domain is characterized as C2 1.
+At position 361 to 494, the domain is characterized as C2 2.
+At position 925 to 1209, the domain is characterized as PKS/mFAS DH.
+At position 2431 to 2508, the domain is characterized as Carrier.
+At position 77 to 179, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 1.
+At position 200 to 325, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 2.
+At position 31 to 108, the domain is characterized as ACT.
+At position 176 to 211, the domain is characterized as EF-hand 1.
+At position 342 to 502, the domain is characterized as Ferric oxidoreductase.
+At position 541 to 657, the domain is characterized as FAD-binding FR-type.
+At position 296 to 441, the domain is characterized as Jacalin-type lectin 3.
+At position 448 to 588, the domain is characterized as Jacalin-type lectin 4.
+At position 2 to 193, the domain is characterized as N-acetyltransferase.
+At position 57 to 132, the domain is characterized as Carrier.
+At position 677 to 712, the domain is characterized as Anaphylatoxin-like.
+At position 1497 to 1640, the domain is characterized as NTR.
+At position 43 to 238, the domain is characterized as Brix.
+At position 1 to 139, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 139 to 233, the domain is characterized as Rhodanese.
+At position 108 to 227, the domain is characterized as PX.
+At position 10 to 75, the domain is characterized as TRAM.
+At position 69 to 316, the domain is characterized as ABC transporter.
+At position 3 to 460, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 492 to 780, the domain is characterized as UvrD-like helicase C-terminal.
+At position 482 to 576, the domain is characterized as Fibronectin type-III.
+At position 353 to 505, the domain is characterized as N-acetyltransferase.
+At position 1679 to 1714, the domain is characterized as EF-hand.
+At position 246 to 311, the domain is characterized as VWFC 3.
+At position 19 to 336, the domain is characterized as DOT1.
+At position 413 to 493, the domain is characterized as POLO box 1.
+At position 515 to 597, the domain is characterized as POLO box 2.
+At position 131 to 302, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 35 to 134, the domain is characterized as Ig-like C2-type.
+At position 140 to 235, the domain is characterized as Fibronectin type-III 1.
+At position 240 to 344, the domain is characterized as Fibronectin type-III 2.
+At position 34 to 191, the domain is characterized as PPIase cyclophilin-type.
+At position 83 to 341, the domain is characterized as Protein kinase.
+At position 384 to 419, the domain is characterized as EF-hand 1.
+At position 420 to 455, the domain is characterized as EF-hand 2.
+At position 456 to 491, the domain is characterized as EF-hand 3.
+At position 493 to 526, the domain is characterized as EF-hand 4.
+At position 2 to 117, the domain is characterized as Histone H2A.
+At position 184 to 370, the domain is characterized as Macro.
+At position 5 to 81, the domain is characterized as HTH rpiR-type.
+At position 129 to 269, the domain is characterized as SIS.
+At position 128 to 285, the domain is characterized as CRAL-TRIO.
+At position 444 to 719, the domain is characterized as Protein kinase.
+At position 321 to 423, the domain is characterized as STAS.
+At position 21 to 92, the domain is characterized as S1 motif.
+At position 317 to 376, the domain is characterized as SH3.
+At position 7 to 295, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 296 to 554, the domain is characterized as UvrD-like helicase C-terminal.
+At position 622 to 716, the domain is characterized as S1 motif.
+At position 43 to 75, the domain is characterized as LisH.
+At position 16 to 148, the domain is characterized as Cyclin N-terminal.
+At position 846 to 911, the domain is characterized as S1 motif 9.
+At position 1047 to 1120, the domain is characterized as S1 motif 10.
+At position 1160 to 1233, the domain is characterized as S1 motif 11.
+At position 1241 to 1309, the domain is characterized as S1 motif 12.
+At position 1335 to 1407, the domain is characterized as S1 motif 13.
+At position 706 to 1048, the domain is characterized as PUM-HD.
+At position 240 to 362, the domain is characterized as MsrB.
+At position 287 to 336, the domain is characterized as SOCS box.
+At position 9 to 228, the domain is characterized as Radical SAM core.
+At position 15 to 178, the domain is characterized as PPIase cyclophilin-type.
+At position 61 to 168, the domain is characterized as DM10 1.
+At position 212 to 354, the domain is characterized as DM10 2.
+At position 416 to 523, the domain is characterized as DM10 3.
+At position 39 to 158, the domain is characterized as FZ.
+At position 2 to 193, the domain is characterized as Glutamine amidotransferase type-2.
+At position 239 to 519, the domain is characterized as Asparagine synthetase.
+At position 130 to 392, the domain is characterized as Protein kinase.
+At position 202 to 328, the domain is characterized as Rhodanese.
+At position 525 to 885, the domain is characterized as USP.
+At position 617 to 675, the domain is characterized as FYR N-terminal.
+At position 677 to 756, the domain is characterized as FYR C-terminal.
+At position 73 to 183, the domain is characterized as Expansin-like EG45.
+At position 193 to 272, the domain is characterized as Expansin-like CBD.
+At position 107 to 172, the domain is characterized as CBS 1.
+At position 199 to 259, the domain is characterized as CBS 2.
+At position 18 to 93, the domain is characterized as H15.
+At position 193 to 356, the domain is characterized as NIDO.
+At position 648 to 829, the domain is characterized as AMOP.
+At position 39 to 259, the domain is characterized as ABC transporter.
+At position 359 to 606, the domain is characterized as Clu.
+At position 106 to 354, the domain is characterized as GS catalytic.
+At position 42 to 364, the domain is characterized as G-alpha.
+At position 79 to 159, the domain is characterized as GS beta-grasp.
+At position 166 to 432, the domain is characterized as GS catalytic.
+At position 38 to 315, the domain is characterized as Deacetylase sirtuin-type.
+At position 445 to 640, the domain is characterized as PNPLA.
+At position 50 to 131, the domain is characterized as GST N-terminal.
+At position 139 to 263, the domain is characterized as GST C-terminal.
+At position 415 to 474, the domain is characterized as LIM zinc-binding 1.
+At position 475 to 535, the domain is characterized as LIM zinc-binding 2.
+At position 536 to 604, the domain is characterized as LIM zinc-binding 3.
+At position 9 to 189, the domain is characterized as Ku.
+At position 290 to 368, the domain is characterized as B5.
+At position 295 to 360, the domain is characterized as Mop.
+At position 37 to 106, the domain is characterized as Chitin-binding type R&R.
+At position 889 to 974, the domain is characterized as Toprim.
+At position 215 to 408, the domain is characterized as Rab-GAP TBC.
+At position 42 to 289, the domain is characterized as Cupin type-1 1.
+At position 346 to 495, the domain is characterized as Cupin type-1 2.
+At position 41 to 133, the domain is characterized as Ig-like C2-type.
+At position 583 to 683, the domain is characterized as tRNA-binding.
+At position 66 to 385, the domain is characterized as Kinesin motor.
+At position 11 to 96, the domain is characterized as Acylphosphatase-like.
+At position 1069 to 1188, the domain is characterized as PH.
+At position 1214 to 1486, the domain is characterized as CNH.
+At position 1558 to 1571, the domain is characterized as CRIB.
+At position 622 to 810, the domain is characterized as GATase cobBQ-type.
+At position 3 to 124, the domain is characterized as MSP.
+At position 35 to 113, the domain is characterized as RRM.
+At position 34 to 143, the domain is characterized as Thioredoxin.
+At position 581 to 600, the domain is characterized as UIM 1.
+At position 646 to 662, the domain is characterized as UIM 2.
+At position 118 to 429, the domain is characterized as IF rod.
+At position 9 to 105, the domain is characterized as DMAP1-binding.
+At position 211 to 561, the domain is characterized as TTL.
+At position 37 to 118, the domain is characterized as Inhibitor I9.
+At position 135 to 407, the domain is characterized as Peptidase S8.
+At position 223 to 467, the domain is characterized as Peptidase M12B.
+At position 468 to 559, the domain is characterized as Disintegrin.
+At position 236 to 296, the domain is characterized as SH3.
+At position 290 to 435, the domain is characterized as C-CAP/cofactor C-like.
+At position 56 to 210, the domain is characterized as Nudix hydrolase.
+At position 158 to 476, the domain is characterized as IF rod.
+At position 223 to 292, the domain is characterized as PWWP.
+At position 901 to 1018, the domain is characterized as SET.
+At position 1027 to 1043, the domain is characterized as Post-SET.
+At position 382 to 529, the domain is characterized as Exonuclease.
+At position 392 to 495, the domain is characterized as Thioredoxin.
+At position 6 to 83, the domain is characterized as RRM.
+At position 17 to 189, the domain is characterized as PITH.
+At position 291 to 436, the domain is characterized as Helicase C-terminal.
+At position 433 to 566, the domain is characterized as C2 2.
+At position 571 to 930, the domain is characterized as TTL.
+At position 6 to 72, the domain is characterized as Ubiquitin-like.
+At position 109 to 190, the domain is characterized as BAG.
+At position 197 to 389, the domain is characterized as Glutamine amidotransferase type-1.
+At position 48 to 125, the domain is characterized as GST N-terminal.
+At position 127 to 249, the domain is characterized as GST C-terminal.
+At position 416 to 613, the domain is characterized as FtsK.
+At position 131 to 243, the domain is characterized as TBDR plug.
+At position 249 to 1038, the domain is characterized as TBDR beta-barrel.
+At position 79 to 315, the domain is characterized as ABC transporter 1.
+At position 342 to 562, the domain is characterized as ABC transporter 2.
+At position 585 to 618, the domain is characterized as EF-hand 1.
+At position 615 to 650, the domain is characterized as EF-hand 2.
+At position 680 to 714, the domain is characterized as EF-hand 3.
+At position 677 to 706, the domain is characterized as IQ.
+At position 5 to 230, the domain is characterized as ABC transporter.
+At position 796 to 870, the domain is characterized as RRM.
+At position 423 to 452, the domain is characterized as EF-hand 1.
+At position 453 to 484, the domain is characterized as EF-hand 2.
+At position 162 to 383, the domain is characterized as Radical SAM core.
+At position 134 to 254, the domain is characterized as PilZ.
+At position 78 to 219, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 139 to 261, the domain is characterized as Fe2OG dioxygenase.
+At position 274 to 314, the domain is characterized as ShKT.
+At position 89 to 156, the domain is characterized as POTRA.
+At position 207 to 382, the domain is characterized as PCI.
+At position 45 to 100, the domain is characterized as SAM.
+At position 152 to 277, the domain is characterized as HD.
+At position 9 to 209, the domain is characterized as DarT.
+At position 88 to 274, the domain is characterized as N-acetyltransferase.
+At position 2 to 330, the domain is characterized as GBD/FH3.
+At position 554 to 946, the domain is characterized as FH2.
+At position 974 to 989, the domain is characterized as WH2.
+At position 114 to 384, the domain is characterized as Protein kinase.
+At position 2 to 129, the domain is characterized as PINc.
+At position 144 to 684, the domain is characterized as USP.
+At position 686 to 779, the domain is characterized as DUSP 1.
+At position 20 to 149, the domain is characterized as VHS.
+At position 1 to 108, the domain is characterized as Tyrosine-protein phosphatase.
+At position 22 to 102, the domain is characterized as Lipoyl-binding.
+At position 177 to 445, the domain is characterized as Protein kinase.
+At position 223 to 289, the domain is characterized as KH.
+At position 349 to 442, the domain is characterized as HD.
+At position 15 to 245, the domain is characterized as ABC transporter.
+At position 36 to 72, the domain is characterized as EGF-like.
+At position 79 to 158, the domain is characterized as Kringle.
+At position 173 to 421, the domain is characterized as Peptidase S1.
+At position 578 to 653, the domain is characterized as PUA.
+At position 116 to 245, the domain is characterized as RCK N-terminal.
+At position 1 to 124, the domain is characterized as C2 1.
+At position 318 to 440, the domain is characterized as C2 2.
+At position 477 to 605, the domain is characterized as C2 3.
+At position 652 to 778, the domain is characterized as C2 4.
+At position 248 to 414, the domain is characterized as W2.
+At position 262 to 463, the domain is characterized as MIF4G.
+At position 565 to 689, the domain is characterized as MI.
+At position 7 to 96, the domain is characterized as GLUE N-terminal.
+At position 255 to 288, the domain is characterized as GLUE C-terminal.
+At position 141 to 215, the domain is characterized as UPAR/Ly6.
+At position 28 to 143, the domain is characterized as Ig-like V-type.
+At position 5 to 142, the domain is characterized as MPN.
+At position 244 to 430, the domain is characterized as GATase cobBQ-type.
+At position 529 to 712, the domain is characterized as Helicase ATP-binding 1.
+At position 723 to 956, the domain is characterized as Helicase C-terminal 1.
+At position 1019 to 1324, the domain is characterized as SEC63 1.
+At position 1374 to 1550, the domain is characterized as Helicase ATP-binding 2.
+At position 1587 to 1771, the domain is characterized as Helicase C-terminal 2.
+At position 1848 to 2162, the domain is characterized as SEC63 2.
+At position 31 to 114, the domain is characterized as RRM 1.
+At position 182 to 267, the domain is characterized as RRM 2.
+At position 148 to 316, the domain is characterized as JmjC.
+At position 888 to 935, the domain is characterized as F-box.
+At position 162 to 225, the domain is characterized as Myb-like.
+At position 324 to 523, the domain is characterized as Rho-GAP.
+At position 70 to 402, the domain is characterized as Calpain catalytic.
+At position 905 to 934, the domain is characterized as IQ.
+At position 129 to 313, the domain is characterized as ATP-grasp.
+At position 280 to 414, the domain is characterized as Ferric oxidoreductase.
+At position 415 to 534, the domain is characterized as FAD-binding FR-type.
+At position 41 to 105, the domain is characterized as S4 RNA-binding.
+At position 187 to 278, the domain is characterized as HTH La-type RNA-binding.
+At position 285 to 383, the domain is characterized as RRM.
+At position 78 to 199, the domain is characterized as Barwin.
+At position 273 to 306, the domain is characterized as KOW 1.
+At position 420 to 451, the domain is characterized as KOW 2.
+At position 472 to 503, the domain is characterized as KOW 3.
+At position 594 to 627, the domain is characterized as KOW 4.
+At position 704 to 737, the domain is characterized as KOW 5.
+At position 535 to 632, the domain is characterized as tRNA-binding.
+At position 76 to 142, the domain is characterized as FHA.
+At position 3 to 91, the domain is characterized as HPr.
+At position 51 to 209, the domain is characterized as Tyrosine-protein phosphatase.
+At position 56 to 93, the domain is characterized as EF-hand 1.
+At position 12 to 256, the domain is characterized as Lon N-terminal.
+At position 690 to 875, the domain is characterized as Lon proteolytic.
+At position 232 to 261, the domain is characterized as KH 1.
+At position 295 to 324, the domain is characterized as KH 2.
+At position 431 to 600, the domain is characterized as tr-type G.
+At position 794 to 858, the domain is characterized as SAM.
+At position 464 to 660, the domain is characterized as ABC transporter.
+At position 12 to 138, the domain is characterized as Peptidase C39.
+At position 483 to 705, the domain is characterized as ABC transporter.
+At position 38 to 95, the domain is characterized as Ubiquitin-like; degenerate.
+At position 158 to 459, the domain is characterized as PI3K/PI4K catalytic.
+At position 280 to 435, the domain is characterized as Helicase C-terminal.
+At position 30 to 203, the domain is characterized as BPL/LPL catalytic.
+At position 1 to 151, the domain is characterized as Radical SAM core.
+At position 42 to 126, the domain is characterized as Rieske.
+At position 214 to 277, the domain is characterized as bZIP.
+At position 524 to 665, the domain is characterized as DOD-type homing endonuclease 1.
+At position 1047 to 1186, the domain is characterized as DOD-type homing endonuclease 2.
+At position 142 to 240, the domain is characterized as Rhodanese.
+At position 393 to 553, the domain is characterized as TIR.
+At position 200 to 385, the domain is characterized as YrdC-like.
+At position 21 to 469, the domain is characterized as Hexokinase.
+At position 52 to 88, the domain is characterized as EF-hand 2.
+At position 47 to 91, the domain is characterized as TSP type-1 1.
+At position 681 to 740, the domain is characterized as TSP type-1 2.
+At position 741 to 800, the domain is characterized as TSP type-1 3.
+At position 803 to 865, the domain is characterized as TSP type-1 4.
+At position 866 to 925, the domain is characterized as TSP type-1 5.
+At position 926 to 982, the domain is characterized as TSP type-1 6.
+At position 985 to 1022, the domain is characterized as PLAC.
+At position 149 to 234, the domain is characterized as PDZ.
+At position 100 to 257, the domain is characterized as CP-type G.
+At position 1 to 259, the domain is characterized as ABC transporter.
+At position 898 to 1015, the domain is characterized as SET.
+At position 1024 to 1040, the domain is characterized as Post-SET.
+At position 215 to 278, the domain is characterized as bZIP.
+At position 9 to 378, the domain is characterized as Protein kinase.
+At position 420 to 591, the domain is characterized as tr-type G.
+At position 307 to 450, the domain is characterized as C-CAP/cofactor C-like.
+At position 6 to 140, the domain is characterized as HTH marR-type.
+At position 202 to 289, the domain is characterized as PDZ 1.
+At position 361 to 448, the domain is characterized as PDZ 2.
+At position 510 to 591, the domain is characterized as PDZ 3.
+At position 619 to 690, the domain is characterized as SH3.
+At position 769 to 955, the domain is characterized as Guanylate kinase-like.
+At position 20 to 214, the domain is characterized as RNase H type-2.
+At position 15 to 164, the domain is characterized as UBC core.
+At position 198 to 372, the domain is characterized as Helicase ATP-binding.
+At position 402 to 546, the domain is characterized as Helicase C-terminal.
+At position 222 to 535, the domain is characterized as Protein kinase.
+At position 573 to 661, the domain is characterized as GED.
+At position 1618 to 1695, the domain is characterized as Carrier 1.
+At position 1739 to 1816, the domain is characterized as Carrier 2.
+At position 153 to 205, the domain is characterized as KH.
+At position 70 to 332, the domain is characterized as Protein kinase.
+At position 161 to 308, the domain is characterized as N-acetyltransferase.
+At position 59 to 235, the domain is characterized as BPL/LPL catalytic.
+At position 163 to 248, the domain is characterized as RRM.
+At position 227 to 331, the domain is characterized as RNase III.
+At position 369 to 437, the domain is characterized as DRBM.
+At position 86 to 238, the domain is characterized as Cupin type-1 1.
+At position 329 to 480, the domain is characterized as Cupin type-1 2.
+At position 59 to 316, the domain is characterized as Alpha-carbonic anhydrase 1.
+At position 321 to 585, the domain is characterized as Alpha-carbonic anhydrase 2.
+At position 517 to 739, the domain is characterized as STAS.
+At position 25 to 161, the domain is characterized as Ephrin RBD.
+At position 133 to 231, the domain is characterized as Rhodanese.
+At position 17 to 235, the domain is characterized as Radical SAM core.
+At position 225 to 283, the domain is characterized as PWWP.
+At position 423 to 555, the domain is characterized as ADD.
+At position 575 to 853, the domain is characterized as SAM-dependent MTase C5-type.
+At position 1 to 79, the domain is characterized as GST N-terminal.
+At position 85 to 234, the domain is characterized as GST C-terminal.
+At position 35 to 103, the domain is characterized as Bromo 1.
+At position 295 to 365, the domain is characterized as Bromo 2.
+At position 408 to 526, the domain is characterized as BAH.
+At position 713 to 978, the domain is characterized as Autotransporter.
+At position 2 to 78, the domain is characterized as Carrier.
+At position 238 to 329, the domain is characterized as Ig-like 3.
+At position 6 to 123, the domain is characterized as MATH.
+At position 292 to 350, the domain is characterized as PWWP.
+At position 482 to 614, the domain is characterized as ADD.
+At position 634 to 912, the domain is characterized as SAM-dependent MTase C5-type.
+At position 129 to 401, the domain is characterized as Peptidase S8.
+At position 59 to 156, the domain is characterized as Cytochrome c 1.
+At position 180 to 265, the domain is characterized as Cytochrome c 2.
+At position 18 to 130, the domain is characterized as PH.
+At position 133 to 248, the domain is characterized as SH2.
+At position 216 to 303, the domain is characterized as PDZ 1.
+At position 330 to 421, the domain is characterized as PDZ 2.
+At position 506 to 587, the domain is characterized as PDZ 3.
+At position 620 to 690, the domain is characterized as SH3.
+At position 780 to 955, the domain is characterized as Guanylate kinase-like.
+At position 45 to 275, the domain is characterized as Radical SAM core.
+At position 274 to 494, the domain is characterized as Fibrinogen C-terminal.
+At position 243 to 387, the domain is characterized as FCP1 homology.
+At position 10 to 482, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 509 to 799, the domain is characterized as UvrD-like helicase C-terminal.
+At position 32 to 70, the domain is characterized as LRRNT.
+At position 291 to 511, the domain is characterized as Helicase ATP-binding.
+At position 727 to 895, the domain is characterized as Helicase C-terminal.
+At position 567 to 766, the domain is characterized as Flavodoxin-like.
+At position 795 to 1065, the domain is characterized as FAD-binding FR-type.
+At position 679 to 741, the domain is characterized as LIM zinc-binding.
+At position 905 to 1047, the domain is characterized as bMERB.
+At position 86 to 187, the domain is characterized as PH.
+At position 266 to 442, the domain is characterized as BTB 1.
+At position 229 to 412, the domain is characterized as Integrase catalytic.
+At position 160 to 243, the domain is characterized as PPIase FKBP-type.
+At position 40 to 198, the domain is characterized as Thioredoxin.
+At position 28 to 355, the domain is characterized as G-alpha.
+At position 41 to 259, the domain is characterized as PPM-type phosphatase.
+At position 21 to 53, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 748 to 921, the domain is characterized as PNPLA.
+At position 90 to 246, the domain is characterized as Cytochrome c.
+At position 13 to 101, the domain is characterized as GS beta-grasp.
+At position 108 to 472, the domain is characterized as GS catalytic.
+At position 28 to 134, the domain is characterized as CBM2.
+At position 158 to 296, the domain is characterized as PA.
+At position 327 to 402, the domain is characterized as B5.
+At position 123 to 351, the domain is characterized as Radical SAM core.
+At position 34 to 230, the domain is characterized as Macro.
+At position 376 to 445, the domain is characterized as TRAM.
+At position 139 to 278, the domain is characterized as VPS9.
+At position 29 to 300, the domain is characterized as CN hydrolase.
+At position 12 to 73, the domain is characterized as J.
+At position 198 to 272, the domain is characterized as Toprim.
+At position 132 to 316, the domain is characterized as UmuC.
+At position 2 to 111, the domain is characterized as MTTase N-terminal.
+At position 133 to 364, the domain is characterized as Radical SAM core.
+At position 367 to 428, the domain is characterized as TRAM.
+At position 29 to 230, the domain is characterized as GH16.
+At position 15 to 221, the domain is characterized as AIG1-type G.
+At position 143 to 185, the domain is characterized as CAP-Gly 1.
+At position 260 to 302, the domain is characterized as CAP-Gly 2.
+At position 228 to 287, the domain is characterized as OVATE.
+At position 588 to 746, the domain is characterized as JmjC.
+At position 595 to 863, the domain is characterized as Autotransporter.
+At position 1 to 51, the domain is characterized as CSD 9.
+At position 64 to 105, the domain is characterized as SUZ-C.
+At position 255 to 487, the domain is characterized as Protein kinase.
+At position 121 to 178, the domain is characterized as L27 1.
+At position 180 to 236, the domain is characterized as L27 2.
+At position 258 to 338, the domain is characterized as PDZ.
+At position 347 to 419, the domain is characterized as SH3.
+At position 481 to 662, the domain is characterized as Guanylate kinase-like.
+At position 439 to 477, the domain is characterized as Ubiquitin-like.
+At position 252 to 444, the domain is characterized as Helicase ATP-binding.
+At position 455 to 616, the domain is characterized as Helicase C-terminal.
+At position 19 to 298, the domain is characterized as PH 1.
+At position 112 to 195, the domain is characterized as PDZ.
+At position 322 to 433, the domain is characterized as PH 2.
+At position 482 to 538, the domain is characterized as SU.
+At position 5 to 89, the domain is characterized as Cytochrome b5 heme-binding.
+At position 592 to 859, the domain is characterized as Ras-GEF.
+At position 1846 to 1948, the domain is characterized as PH.
+At position 1967 to 2165, the domain is characterized as Rho-GAP.
+At position 33 to 134, the domain is characterized as SRCR 1.
+At position 160 to 288, the domain is characterized as SRCR 2.
+At position 312 to 412, the domain is characterized as SRCR 3.
+At position 422 to 530, the domain is characterized as SRCR 4.
+At position 21 to 369, the domain is characterized as GH18.
+At position 256 to 450, the domain is characterized as PCI.
+At position 1 to 190, the domain is characterized as EngB-type G.
+At position 439 to 486, the domain is characterized as SARAH.
+At position 213 to 267, the domain is characterized as HAMP.
+At position 272 to 508, the domain is characterized as Methyl-accepting transducer.
+At position 568 to 682, the domain is characterized as SMC hinge.
+At position 20 to 112, the domain is characterized as Ig-like C2-type.
+At position 5 to 52, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 283 to 378, the domain is characterized as PAZ.
+At position 542 to 883, the domain is characterized as Piwi.
+At position 45 to 287, the domain is characterized as HBM.
+At position 314 to 370, the domain is characterized as HAMP.
+At position 88 to 226, the domain is characterized as GST C-terminal.
+At position 26 to 154, the domain is characterized as RabBD.
+At position 590 to 676, the domain is characterized as PDZ.
+At position 743 to 866, the domain is characterized as C2 1.
+At position 1401 to 1519, the domain is characterized as C2 2.
+At position 569 to 773, the domain is characterized as Rho-GAP.
+At position 805 to 1013, the domain is characterized as START.
+At position 439 to 500, the domain is characterized as SH3 3.
+At position 781 to 840, the domain is characterized as SH3 4.
+At position 697 to 791, the domain is characterized as FDX-ACB.
+At position 901 to 1056, the domain is characterized as Guanylate cyclase.
+At position 53 to 299, the domain is characterized as CN hydrolase.
+At position 188 to 217, the domain is characterized as IQ.
+At position 32 to 843, the domain is characterized as Protein kinase.
+At position 844 to 887, the domain is characterized as AGC-kinase C-terminal.
+At position 193 to 387, the domain is characterized as CheB-type methylesterase.
+At position 278 to 478, the domain is characterized as PCI.
+At position 185 to 379, the domain is characterized as CheB-type methylesterase.
+At position 79 to 305, the domain is characterized as Radical SAM core.
+At position 138 to 165, the domain is characterized as HhH.
+At position 54 to 215, the domain is characterized as Integrase catalytic.
+At position 1 to 242, the domain is characterized as ABC transporter 1.
+At position 359 to 597, the domain is characterized as ABC transporter 2.
+At position 610 to 935, the domain is characterized as ABC transporter 3.
+At position 96 to 325, the domain is characterized as Radical SAM core.
+At position 7 to 64, the domain is characterized as Ig-like.
+At position 119 to 147, the domain is characterized as ITAM.
+At position 3 to 233, the domain is characterized as DPCK.
+At position 316 to 402, the domain is characterized as BRCT.
+At position 6 to 62, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 2 to 105, the domain is characterized as FAD-binding FR-type.
+At position 276 to 416, the domain is characterized as SIS 1.
+At position 449 to 587, the domain is characterized as SIS 2.
+At position 400 to 1117, the domain is characterized as GH81.
+At position 155 to 404, the domain is characterized as ABC transporter 1.
+At position 507 to 753, the domain is characterized as ABC transmembrane type-2 1.
+At position 842 to 1087, the domain is characterized as ABC transporter 2.
+At position 1180 to 1404, the domain is characterized as ABC transmembrane type-2 2.
+At position 197 to 542, the domain is characterized as SEC63 1.
+At position 638 to 715, the domain is characterized as SEC63 2.
+At position 269 to 424, the domain is characterized as Guanylate cyclase.
+At position 9 to 304, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 305 to 597, the domain is characterized as UvrD-like helicase C-terminal.
+At position 56 to 133, the domain is characterized as EMI.
+At position 867 to 1014, the domain is characterized as C1q.
+At position 7 to 262, the domain is characterized as NodB homology.
+At position 283 to 338, the domain is characterized as LRRCT.
+At position 338 to 499, the domain is characterized as NTF2.
+At position 543 to 596, the domain is characterized as TAP-C.
+At position 106 to 143, the domain is characterized as LRRNT.
+At position 44 to 339, the domain is characterized as USP.
+At position 25 to 215, the domain is characterized as GH16.
+At position 64 to 356, the domain is characterized as Protein kinase.
+At position 27 to 227, the domain is characterized as AB hydrolase-1.
+At position 18 to 65, the domain is characterized as F-box.
+At position 6 to 43, the domain is characterized as KOW.
+At position 6 to 263, the domain is characterized as PH 1.
+At position 81 to 164, the domain is characterized as PDZ.
+At position 287 to 399, the domain is characterized as PH 2.
+At position 447 to 503, the domain is characterized as SU.
+At position 150 to 185, the domain is characterized as EF-hand 1.
+At position 1328 to 1511, the domain is characterized as Roc.
+At position 1879 to 2146, the domain is characterized as Protein kinase.
+At position 310 to 542, the domain is characterized as Glutamine amidotransferase type-1.
+At position 42 to 283, the domain is characterized as ABC transporter.
+At position 204 to 436, the domain is characterized as Fibrinogen C-terminal.
+At position 316 to 413, the domain is characterized as STAS.
+At position 39 to 102, the domain is characterized as S4 RNA-binding.
+At position 293 to 352, the domain is characterized as LIM zinc-binding.
+At position 86 to 134, the domain is characterized as UMA.
+At position 1 to 118, the domain is characterized as PINc.
+At position 7 to 96, the domain is characterized as CARD.
+At position 122 to 151, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 161 to 190, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 21 to 66, the domain is characterized as F-box.
+At position 185 to 427, the domain is characterized as ABC transporter 1.
+At position 879 to 1117, the domain is characterized as ABC transporter 2.
+At position 259 to 503, the domain is characterized as ABC transporter 2.
+At position 20 to 161, the domain is characterized as Tyrosine-protein phosphatase.
+At position 109 to 205, the domain is characterized as WSC.
+At position 2 to 460, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 487 to 771, the domain is characterized as UvrD-like helicase C-terminal.
+At position 2 to 219, the domain is characterized as ThyX.
+At position 585 to 836, the domain is characterized as Protein kinase.
+At position 5 to 202, the domain is characterized as ABC transporter.
+At position 36 to 77, the domain is characterized as CHCH.
+At position 90 to 166, the domain is characterized as Biotinyl-binding.
+At position 55 to 121, the domain is characterized as Death.
+At position 213 to 499, the domain is characterized as Protein kinase.
+At position 185 to 262, the domain is characterized as Kringle 2.
+At position 480 to 559, the domain is characterized as Kringle 5.
+At position 580 to 807, the domain is characterized as Peptidase S1.
+At position 27 to 128, the domain is characterized as Cadherin 1.
+At position 133 to 237, the domain is characterized as Cadherin 2.
+At position 244 to 338, the domain is characterized as Cadherin 3.
+At position 343 to 451, the domain is characterized as Cadherin 4.
+At position 571 to 667, the domain is characterized as Cadherin 6.
+At position 700 to 793, the domain is characterized as BRCT 1.
+At position 857 to 956, the domain is characterized as BRCT 2.
+At position 259 to 386, the domain is characterized as PH.
+At position 42 to 156, the domain is characterized as sHSP.
+At position 146 to 391, the domain is characterized as NR LBD.
+At position 69 to 246, the domain is characterized as FAD-binding PCMH-type.
+At position 139 to 271, the domain is characterized as RUN.
+At position 407 to 621, the domain is characterized as BURP.
+At position 49 to 124, the domain is characterized as J.
+At position 34 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 531 to 703, the domain is characterized as tr-type G.
+At position 246 to 306, the domain is characterized as SH3.
+At position 129 to 168, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 6 to 98, the domain is characterized as ASCH.
+At position 464 to 513, the domain is characterized as bHLH.
+At position 7 to 82, the domain is characterized as GST N-terminal.
+At position 118 to 238, the domain is characterized as GST C-terminal.
+At position 2 to 203, the domain is characterized as RNase H type-2.
+At position 25 to 88, the domain is characterized as HMA.
+At position 7 to 274, the domain is characterized as YjeF C-terminal.
+At position 207 to 514, the domain is characterized as Tyrosine-protein phosphatase.
+At position 406 to 436, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 14 to 135, the domain is characterized as RGS.
+At position 544 to 625, the domain is characterized as DIX.
+At position 203 to 273, the domain is characterized as PAS 2.
+At position 278 to 317, the domain is characterized as PAC.
+At position 172 to 298, the domain is characterized as C-type lectin.
+At position 262 to 445, the domain is characterized as GATase cobBQ-type.
+At position 14 to 119, the domain is characterized as AB hydrolase-1.
+At position 181 to 290, the domain is characterized as PH.
+At position 672 to 850, the domain is characterized as C2 DOCK-type.
+At position 1690 to 2150, the domain is characterized as DOCKER.
+At position 151 to 254, the domain is characterized as Ig-like C2-type 1.
+At position 358 to 448, the domain is characterized as Ig-like C2-type 2.
+At position 449 to 539, the domain is characterized as Ig-like C2-type 3.
+At position 540 to 629, the domain is characterized as Ig-like C2-type 4.
+At position 641 to 767, the domain is characterized as Ig-like C2-type 5.
+At position 770 to 866, the domain is characterized as Fibronectin type-III 1.
+At position 868 to 963, the domain is characterized as Fibronectin type-III 2.
+At position 967 to 1061, the domain is characterized as Ig-like C2-type 6.
+At position 1064 to 1159, the domain is characterized as Fibronectin type-III 3.
+At position 1177 to 1270, the domain is characterized as Ig-like C2-type 7.
+At position 307 to 359, the domain is characterized as Collagen-like.
+At position 398 to 498, the domain is characterized as SRCR.
+At position 1 to 97, the domain is characterized as Ig-like.
+At position 39 to 129, the domain is characterized as CTCK.
+At position 76 to 105, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 201 to 284, the domain is characterized as TFIIS N-terminal.
+At position 207 to 293, the domain is characterized as Cytochrome c 2.
+At position 35 to 124, the domain is characterized as Link.
+At position 190 to 368, the domain is characterized as EngA-type G 2.
+At position 369 to 461, the domain is characterized as KH-like.
+At position 251 to 517, the domain is characterized as Protein kinase.
+At position 518 to 589, the domain is characterized as AGC-kinase C-terminal.
+At position 65 to 110, the domain is characterized as LysM.
+At position 108 to 203, the domain is characterized as AB hydrolase-1.
+At position 297 to 369, the domain is characterized as RRM 1.
+At position 371 to 452, the domain is characterized as RRM 2.
+At position 44 to 119, the domain is characterized as KH type-2.
+At position 81 to 241, the domain is characterized as TNase-like.
+At position 23 to 140, the domain is characterized as C-type lectin.
+At position 141 to 176, the domain is characterized as EGF-like.
+At position 179 to 239, the domain is characterized as Sushi 1.
+At position 302 to 364, the domain is characterized as Sushi 3.
+At position 365 to 423, the domain is characterized as Sushi 4.
+At position 554 to 655, the domain is characterized as CBM20.
+At position 220 to 323, the domain is characterized as Rhodanese.
+At position 506 to 696, the domain is characterized as B30.2/SPRY.
+At position 605 to 694, the domain is characterized as BRCT.
+At position 132 to 280, the domain is characterized as Tyrosine-protein phosphatase.
+At position 38 to 156, the domain is characterized as EamA.
+At position 189 to 357, the domain is characterized as SSD.
+At position 19 to 181, the domain is characterized as Exonuclease.
+At position 31 to 140, the domain is characterized as Bulb-type lectin.
+At position 38 to 109, the domain is characterized as S4 RNA-binding.
+At position 2 to 224, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 294 to 538, the domain is characterized as Glutamine amidotransferase type-1.
+At position 351 to 504, the domain is characterized as Helicase C-terminal.
+At position 407 to 729, the domain is characterized as Kinesin motor.
+At position 30 to 206, the domain is characterized as Laminin G-like 1.
+At position 732 to 907, the domain is characterized as Laminin G-like 4.
+At position 921 to 1096, the domain is characterized as Laminin G-like 5.
+At position 1099 to 1136, the domain is characterized as EGF-like 3.
+At position 1140 to 1348, the domain is characterized as Laminin G-like 6.
+At position 429 to 547, the domain is characterized as LTD.
+At position 202 to 308, the domain is characterized as RRM.
+At position 356 to 433, the domain is characterized as ACT.
+At position 393 to 461, the domain is characterized as J.
+At position 64 to 225, the domain is characterized as CP-type G.
+At position 476 to 647, the domain is characterized as tr-type G.
+At position 95 to 172, the domain is characterized as PDZ.
+At position 629 to 1009, the domain is characterized as FH2.
+At position 662 to 916, the domain is characterized as Protein kinase.
+At position 62 to 114, the domain is characterized as bHLH.
+At position 154 to 375, the domain is characterized as TRUD.
+At position 17 to 102, the domain is characterized as PDZ 1.
+At position 110 to 284, the domain is characterized as Guanylate kinase-like.
+At position 289 to 322, the domain is characterized as WW 1.
+At position 335 to 368, the domain is characterized as WW 2.
+At position 407 to 489, the domain is characterized as PDZ 2.
+At position 577 to 653, the domain is characterized as PDZ 3.
+At position 727 to 809, the domain is characterized as PDZ 4.
+At position 853 to 940, the domain is characterized as PDZ 5.
+At position 1003 to 1085, the domain is characterized as PDZ 6.
+At position 1 to 202, the domain is characterized as Laminin N-terminal.
+At position 203 to 266, the domain is characterized as Laminin EGF-like 1.
+At position 267 to 303, the domain is characterized as Laminin EGF-like 2.
+At position 76 to 277, the domain is characterized as MAGE.
+At position 52 to 98, the domain is characterized as F-box.
+At position 31 to 224, the domain is characterized as RNase H type-2.
+At position 112 to 172, the domain is characterized as OVATE.
+At position 149 to 205, the domain is characterized as KH.
+At position 19 to 152, the domain is characterized as Galectin 1.
+At position 187 to 317, the domain is characterized as Galectin 2.
+At position 102 to 169, the domain is characterized as MaoC-like.
+At position 29 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 18 to 167, the domain is characterized as TNase-like 1.
+At position 194 to 329, the domain is characterized as TNase-like 2.
+At position 342 to 499, the domain is characterized as TNase-like 3.
+At position 528 to 663, the domain is characterized as TNase-like 4.
+At position 732 to 790, the domain is characterized as Tudor.
+At position 19 to 238, the domain is characterized as YjeF N-terminal.
+At position 251 to 534, the domain is characterized as YjeF C-terminal.
+At position 1 to 158, the domain is characterized as N-acetyltransferase.
+At position 300 to 417, the domain is characterized as OmpA-like.
+At position 152 to 307, the domain is characterized as CheB-type methylesterase.
+At position 277 to 329, the domain is characterized as TSP type-1.
+At position 59 to 338, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 246 to 493, the domain is characterized as ABC transporter 2.
+At position 645 to 900, the domain is characterized as Protein kinase.
+At position 933 to 997, the domain is characterized as SAM.
+At position 187 to 239, the domain is characterized as bHLH.
+At position 636 to 801, the domain is characterized as MAM.
+At position 60 to 145, the domain is characterized as ACB.
+At position 302 to 374, the domain is characterized as RRM 1.
+At position 376 to 457, the domain is characterized as RRM 2.
+At position 1 to 44, the domain is characterized as B12-binding N-terminal.
+At position 45 to 167, the domain is characterized as B12-binding.
+At position 156 to 423, the domain is characterized as ABC transporter 1.
+At position 501 to 714, the domain is characterized as ABC transmembrane type-2 1.
+At position 808 to 1059, the domain is characterized as ABC transporter 2.
+At position 1132 to 1346, the domain is characterized as ABC transmembrane type-2 2.
+At position 79 to 174, the domain is characterized as Fibronectin type-III 1.
+At position 178 to 266, the domain is characterized as Ig-like C2-type 1.
+At position 275 to 370, the domain is characterized as Fibronectin type-III 2.
+At position 388 to 472, the domain is characterized as Ig-like C2-type 2.
+At position 128 to 206, the domain is characterized as RRM 1.
+At position 225 to 303, the domain is characterized as RRM 2.
+At position 461 to 548, the domain is characterized as RRM 3; atypical.
+At position 306 to 441, the domain is characterized as Fido.
+At position 512 to 681, the domain is characterized as N-acetyltransferase.
+At position 114 to 403, the domain is characterized as FAE.
+At position 382 to 798, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1285 to 1596, the domain is characterized as PKS/mFAS DH.
+At position 1665 to 1739, the domain is characterized as Carrier.
+At position 169 to 344, the domain is characterized as tr-type G.
+At position 21 to 231, the domain is characterized as PARP catalytic.
+At position 141 to 240, the domain is characterized as Gnk2-homologous 2.
+At position 134 to 641, the domain is characterized as Biotin carboxylation.
+At position 287 to 481, the domain is characterized as ATP-grasp.
+At position 768 to 842, the domain is characterized as Biotinyl-binding.
+At position 1568 to 1909, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1913 to 2227, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 1 to 187, the domain is characterized as PRELI/MSF1.
+At position 437 to 589, the domain is characterized as RNase NYN.
+At position 142 to 233, the domain is characterized as Ig-like C2-type 1.
+At position 254 to 359, the domain is characterized as Ig-like C2-type 2.
+At position 373 to 468, the domain is characterized as Fibronectin type-III 1.
+At position 501 to 596, the domain is characterized as Fibronectin type-III 2.
+At position 602 to 695, the domain is characterized as Fibronectin type-III 3.
+At position 698 to 800, the domain is characterized as Fibronectin type-III 4.
+At position 803 to 900, the domain is characterized as Fibronectin type-III 5.
+At position 899 to 995, the domain is characterized as Ig-like C2-type 3.
+At position 1002 to 1115, the domain is characterized as Ig-like C2-type 4.
+At position 1118 to 1204, the domain is characterized as Ig-like C2-type 5.
+At position 1225 to 1322, the domain is characterized as Ig-like C2-type 6.
+At position 1333 to 1422, the domain is characterized as Ig-like C2-type 7.
+At position 190 to 278, the domain is characterized as Ras-associating.
+At position 285 to 332, the domain is characterized as SARAH.
+At position 166 to 230, the domain is characterized as SoHo.
+At position 943 to 1002, the domain is characterized as SH3 1.
+At position 1018 to 1079, the domain is characterized as SH3 2.
+At position 1121 to 1180, the domain is characterized as SH3 3.
+At position 29 to 83, the domain is characterized as Clip.
+At position 101 to 370, the domain is characterized as Peptidase S1.
+At position 49 to 133, the domain is characterized as RRM.
+At position 1 to 106, the domain is characterized as Peptidase M12B.
+At position 113 to 202, the domain is characterized as Disintegrin.
+At position 342 to 376, the domain is characterized as EGF-like.
+At position 220 to 476, the domain is characterized as Fibrinogen C-terminal.
+At position 20 to 98, the domain is characterized as Ig-like C2-type 1.
+At position 109 to 187, the domain is characterized as Ig-like C2-type 2.
+At position 201 to 290, the domain is characterized as Ig-like C2-type 3.
+At position 300 to 387, the domain is characterized as Ig-like C2-type 4.
+At position 123 to 324, the domain is characterized as ATP-grasp.
+At position 206 to 273, the domain is characterized as KH.
+At position 115 to 342, the domain is characterized as tr-type G.
+At position 7 to 85, the domain is characterized as KRAB.
+At position 31 to 221, the domain is characterized as Spondin.
+At position 277 to 331, the domain is characterized as TSP type-1.
+At position 51 to 152, the domain is characterized as THUMP.
+At position 93 to 265, the domain is characterized as JmjC.
+At position 327 to 609, the domain is characterized as Protein kinase.
+At position 132 to 361, the domain is characterized as Sigma-54 factor interaction.
+At position 316 to 432, the domain is characterized as Rhodanese.
+At position 8 to 72, the domain is characterized as J.
+At position 205 to 255, the domain is characterized as HAMP.
+At position 262 to 473, the domain is characterized as Histidine kinase.
+At position 34 to 112, the domain is characterized as RRM 1.
+At position 120 to 200, the domain is characterized as RRM 2.
+At position 265 to 343, the domain is characterized as RRM 3.
+At position 6 to 102, the domain is characterized as Rieske.
+At position 40 to 122, the domain is characterized as EMI.
+At position 123 to 163, the domain is characterized as EGF-like 1; calcium-binding.
+At position 205 to 246, the domain is characterized as EGF-like 3.
+At position 247 to 287, the domain is characterized as EGF-like 4.
+At position 288 to 328, the domain is characterized as EGF-like 5; calcium-binding.
+At position 334 to 374, the domain is characterized as EGF-like 6.
+At position 375 to 412, the domain is characterized as EGF-like 7.
+At position 415 to 455, the domain is characterized as EGF-like 8; calcium-binding.
+At position 520 to 556, the domain is characterized as EGF-like 9.
+At position 564 to 599, the domain is characterized as EGF-like 10.
+At position 607 to 642, the domain is characterized as EGF-like 11.
+At position 650 to 687, the domain is characterized as EGF-like 12.
+At position 695 to 732, the domain is characterized as EGF-like 13.
+At position 740 to 774, the domain is characterized as EGF-like 14.
+At position 782 to 818, the domain is characterized as EGF-like 15.
+At position 826 to 861, the domain is characterized as EGF-like 16.
+At position 869 to 905, the domain is characterized as EGF-like 17.
+At position 913 to 948, the domain is characterized as EGF-like 18.
+At position 956 to 991, the domain is characterized as EGF-like 19.
+At position 999 to 1034, the domain is characterized as EGF-like 20.
+At position 1042 to 1077, the domain is characterized as EGF-like 21.
+At position 1085 to 1120, the domain is characterized as EGF-like 22.
+At position 1128 to 1163, the domain is characterized as EGF-like 23.
+At position 1171 to 1206, the domain is characterized as EGF-like 24.
+At position 1214 to 1250, the domain is characterized as EGF-like 25.
+At position 1258 to 1293, the domain is characterized as EGF-like 26.
+At position 1301 to 1336, the domain is characterized as EGF-like 27.
+At position 1344 to 1379, the domain is characterized as EGF-like 28.
+At position 1387 to 1422, the domain is characterized as EGF-like 29.
+At position 1430 to 1465, the domain is characterized as EGF-like 30.
+At position 1473 to 1508, the domain is characterized as EGF-like 31.
+At position 1516 to 1551, the domain is characterized as EGF-like 32.
+At position 1889 to 1918, the domain is characterized as IQ.
+At position 64 to 120, the domain is characterized as HAMP.
+At position 128 to 156, the domain is characterized as Histidine kinase; first part.
+At position 44 to 107, the domain is characterized as SAM.
+At position 161 to 321, the domain is characterized as HD.
+At position 52 to 309, the domain is characterized as Protein kinase.
+At position 158 to 533, the domain is characterized as SAC.
+At position 34 to 102, the domain is characterized as POTRA.
+At position 621 to 683, the domain is characterized as R3H.
+At position 748 to 795, the domain is characterized as G-patch.
+At position 214 to 372, the domain is characterized as TrmE-type G.
+At position 2128 to 2261, the domain is characterized as MPN.
+At position 4 to 99, the domain is characterized as HTH arsR-type.
+At position 288 to 354, the domain is characterized as SAM.
+At position 369 to 482, the domain is characterized as PAZ.
+At position 666 to 965, the domain is characterized as Piwi.
+At position 38 to 78, the domain is characterized as Chaplin.
+At position 53 to 90, the domain is characterized as LDL-receptor class A 1.
+At position 131 to 168, the domain is characterized as LDL-receptor class A 2.
+At position 31 to 169, the domain is characterized as Nudix hydrolase.
+At position 80 to 321, the domain is characterized as Lon N-terminal.
+At position 83 to 205, the domain is characterized as EamA 1.
+At position 236 to 360, the domain is characterized as EamA 2.
+At position 126 to 490, the domain is characterized as Protein kinase.
+At position 120 to 323, the domain is characterized as ATP-grasp.
+At position 27 to 237, the domain is characterized as ThyX.
+At position 946 to 1063, the domain is characterized as SET.
+At position 1072 to 1088, the domain is characterized as Post-SET.
+At position 80 to 334, the domain is characterized as Protein kinase.
+At position 1 to 73, the domain is characterized as S4 RNA-binding.
+At position 525 to 758, the domain is characterized as ABC transporter 1.
+At position 1369 to 1602, the domain is characterized as ABC transporter 2.
+At position 33 to 287, the domain is characterized as Radical SAM core.
+At position 62 to 96, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 25 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 20 to 48, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 139 to 170, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 172 to 201, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 522 to 695, the domain is characterized as Jacalin-type lectin.
+At position 2 to 59, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 12 to 133, the domain is characterized as EamA 1.
+At position 150 to 274, the domain is characterized as EamA 2.
+At position 83 to 146, the domain is characterized as bZIP.
+At position 27 to 202, the domain is characterized as EngB-type G.
+At position 504 to 631, the domain is characterized as Ricin B-type lectin.
+At position 759 to 841, the domain is characterized as DIX.
+At position 20 to 275, the domain is characterized as Protein kinase.
+At position 313 to 337, the domain is characterized as NAF.
+At position 177 to 242, the domain is characterized as HTH luxR-type.
+At position 20 to 171, the domain is characterized as NAC.
+At position 6 to 234, the domain is characterized as Glutamine amidotransferase type-1.
+At position 9 to 80, the domain is characterized as BTB.
+At position 129 to 165, the domain is characterized as Pentapeptide repeat 1.
+At position 166 to 203, the domain is characterized as Pentapeptide repeat 2.
+At position 216 to 255, the domain is characterized as Pentapeptide repeat 3.
+At position 256 to 295, the domain is characterized as Pentapeptide repeat 4.
+At position 1 to 299, the domain is characterized as SPX.
+At position 558 to 751, the domain is characterized as EXS.
+At position 18 to 249, the domain is characterized as ABC transporter.
+At position 1 to 148, the domain is characterized as N-acetyltransferase 1.
+At position 151 to 296, the domain is characterized as N-acetyltransferase 2.
+At position 47 to 326, the domain is characterized as ABC transmembrane type-1 1.
+At position 386 to 663, the domain is characterized as ABC transporter 1.
+At position 743 to 1031, the domain is characterized as ABC transmembrane type-1 2.
+At position 1084 to 1323, the domain is characterized as ABC transporter 2.
+At position 314 to 525, the domain is characterized as GT92.
+At position 249 to 486, the domain is characterized as ABC transporter 2.
+At position 227 to 291, the domain is characterized as SEP.
+At position 389 to 466, the domain is characterized as UBX.
+At position 371 to 443, the domain is characterized as PAS.
+At position 90 to 400, the domain is characterized as IF rod.
+At position 95 to 163, the domain is characterized as S4 RNA-binding.
+At position 12 to 254, the domain is characterized as Radical SAM core.
+At position 62 to 133, the domain is characterized as KRAB.
+At position 154 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 450, the domain is characterized as TRAM.
+At position 147 to 318, the domain is characterized as Helicase ATP-binding.
+At position 334 to 496, the domain is characterized as Helicase C-terminal.
+At position 434 to 463, the domain is characterized as EF-hand 1.
+At position 464 to 495, the domain is characterized as EF-hand 2.
+At position 70 to 328, the domain is characterized as Protein kinase.
+At position 423 to 458, the domain is characterized as EF-hand 2.
+At position 498 to 528, the domain is characterized as EF-hand 4.
+At position 463 to 704, the domain is characterized as Peptidase S1.
+At position 421 to 530, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 96 to 466, the domain is characterized as SAM-dependent MTase C5-type.
+At position 223 to 396, the domain is characterized as CP-type G.
+At position 359 to 565, the domain is characterized as Rho-GAP.
+At position 177 to 437, the domain is characterized as MHD.
+At position 28 to 216, the domain is characterized as GH11.
+At position 921 to 968, the domain is characterized as Myb-like.
+At position 969 to 1023, the domain is characterized as HTH myb-type.
+At position 4 to 247, the domain is characterized as ABC transporter.
+At position 392 to 427, the domain is characterized as EF-hand 1.
+At position 464 to 499, the domain is characterized as EF-hand 3.
+At position 500 to 534, the domain is characterized as EF-hand 4.
+At position 35 to 121, the domain is characterized as PAN.
+At position 126 to 204, the domain is characterized as Kringle 1.
+At position 209 to 286, the domain is characterized as Kringle 2.
+At position 303 to 381, the domain is characterized as Kringle 3.
+At position 389 to 467, the domain is characterized as Kringle 4.
+At position 493 to 721, the domain is characterized as Peptidase S1.
+At position 15 to 198, the domain is characterized as YrdC-like.
+At position 3 to 113, the domain is characterized as VWFA.
+At position 347 to 624, the domain is characterized as Protein kinase.
+At position 460 to 559, the domain is characterized as Tudor; atypical.
+At position 309 to 462, the domain is characterized as Helicase C-terminal.
+At position 91 to 146, the domain is characterized as F-box.
+At position 130 to 572, the domain is characterized as Urease.
+At position 39 to 81, the domain is characterized as CAP-Gly.
+At position 287 to 367, the domain is characterized as PB1.
+At position 49 to 328, the domain is characterized as AB hydrolase-1.
+At position 662 to 793, the domain is characterized as P/Homo B.
+At position 477 to 640, the domain is characterized as Helicase ATP-binding.
+At position 665 to 838, the domain is characterized as Helicase C-terminal.
+At position 128 to 412, the domain is characterized as ABC transmembrane type-1 1.
+At position 543 to 766, the domain is characterized as ABC transporter 1.
+At position 865 to 1155, the domain is characterized as ABC transmembrane type-1 2.
+At position 1193 to 1426, the domain is characterized as ABC transporter 2.
+At position 35 to 72, the domain is characterized as LDL-receptor class A 1.
+At position 81 to 118, the domain is characterized as LDL-receptor class A 2.
+At position 122 to 157, the domain is characterized as LDL-receptor class A 3.
+At position 166 to 205, the domain is characterized as LDL-receptor class A 4.
+At position 208 to 243, the domain is characterized as EGF-like 1.
+At position 244 to 283, the domain is characterized as EGF-like; calcium-binding.
+At position 552 to 588, the domain is characterized as EGF-like 2.
+At position 889 to 927, the domain is characterized as EGF-like 3.
+At position 931 to 969, the domain is characterized as LDL-receptor class A 5.
+At position 973 to 1009, the domain is characterized as LDL-receptor class A 6.
+At position 1012 to 1049, the domain is characterized as LDL-receptor class A 7.
+At position 1052 to 1090, the domain is characterized as LDL-receptor class A 8.
+At position 1094 to 1131, the domain is characterized as LDL-receptor class A 9.
+At position 1140 to 1177, the domain is characterized as LDL-receptor class A 10.
+At position 1178 to 1214, the domain is characterized as LDL-receptor class A 11.
+At position 1225 to 1260, the domain is characterized as LDL-receptor class A 12.
+At position 1262 to 1298, the domain is characterized as EGF-like 4.
+At position 244 to 429, the domain is characterized as Tyr recombinase.
+At position 402 to 568, the domain is characterized as UBC core.
+At position 26 to 139, the domain is characterized as Ig-like V-type.
+At position 121 to 320, the domain is characterized as ATP-grasp.
+At position 114 to 361, the domain is characterized as Radical SAM core.
+At position 35 to 214, the domain is characterized as FAD-binding PCMH-type.
+At position 159 to 246, the domain is characterized as PB1.
+At position 427 to 683, the domain is characterized as Protein kinase.
+At position 541 to 627, the domain is characterized as GED.
+At position 68 to 96, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 8 to 481, the domain is characterized as PTS EIIC type-3.
+At position 53 to 89, the domain is characterized as BetaSPN-type CS-alpha/beta.
+At position 37 to 269, the domain is characterized as AB hydrolase-1.
+At position 1 to 63, the domain is characterized as PTS EIIC type-1.
+At position 78 to 159, the domain is characterized as PTS EIIB type-1.
+At position 194 to 298, the domain is characterized as PTS EIIA type-1.
+At position 78 to 188, the domain is characterized as TBDR plug.
+At position 193 to 735, the domain is characterized as TBDR beta-barrel.
+At position 80 to 155, the domain is characterized as PAS 1.
+At position 159 to 241, the domain is characterized as RRM 1.
+At position 243 to 320, the domain is characterized as RRM 2.
+At position 227 to 280, the domain is characterized as CVC.
+At position 50 to 214, the domain is characterized as PPIase cyclophilin-type.
+At position 391 to 623, the domain is characterized as Rab-GAP TBC.
+At position 19 to 423, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 42 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 10 to 162, the domain is characterized as F-box.
+At position 886 to 974, the domain is characterized as VRR-NUC.
+At position 138 to 334, the domain is characterized as ATP-grasp 1.
+At position 101 to 285, the domain is characterized as Helicase ATP-binding.
+At position 320 to 551, the domain is characterized as Helicase C-terminal.
+At position 21 to 228, the domain is characterized as MARVEL.
+At position 807 to 1072, the domain is characterized as Protein kinase.
+At position 399 to 430, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 20 to 79, the domain is characterized as HTH IS21-type.
+At position 140 to 315, the domain is characterized as Integrase catalytic.
+At position 366 to 797, the domain is characterized as PIPK.
+At position 111 to 182, the domain is characterized as PRC barrel.
+At position 1 to 402, the domain is characterized as SMP-LTD.
+At position 31 to 185, the domain is characterized as uDENN.
+At position 211 to 365, the domain is characterized as cDENN.
+At position 367 to 513, the domain is characterized as dDENN.
+At position 117 to 165, the domain is characterized as bZIP 1.
+At position 279 to 333, the domain is characterized as bZIP 2.
+At position 465 to 587, the domain is characterized as HD.
+At position 706 to 786, the domain is characterized as ACT 1.
+At position 813 to 887, the domain is characterized as ACT 2.
+At position 231 to 306, the domain is characterized as MIT.
+At position 33 to 155, the domain is characterized as Bulb-type lectin.
+At position 157 to 385, the domain is characterized as START.
+At position 505 to 674, the domain is characterized as N-acetyltransferase.
+At position 50 to 136, the domain is characterized as Lipoyl-binding.
+At position 67 to 194, the domain is characterized as SCP.
+At position 399 to 421, the domain is characterized as Follistatin-like 1.
+At position 471 to 494, the domain is characterized as Follistatin-like 2.
+At position 596 to 618, the domain is characterized as Follistatin-like 3.
+At position 660 to 682, the domain is characterized as Follistatin-like 4.
+At position 687 to 710, the domain is characterized as Follistatin-like 5.
+At position 434 to 602, the domain is characterized as tr-type G.
+At position 147 to 264, the domain is characterized as FAD-binding FR-type.
+At position 76 to 130, the domain is characterized as bHLH.
+At position 299 to 382, the domain is characterized as IPT/TIG.
+At position 193 to 386, the domain is characterized as MARVEL.
+At position 86 to 138, the domain is characterized as bHLH.
+At position 2 to 156, the domain is characterized as N-acetyltransferase.
+At position 616 to 686, the domain is characterized as PAS 1.
+At position 689 to 745, the domain is characterized as PAC.
+At position 749 to 823, the domain is characterized as PAS 2.
+At position 900 to 1119, the domain is characterized as Histidine kinase.
+At position 45 to 149, the domain is characterized as Rieske.
+At position 141 to 340, the domain is characterized as CheB-type methylesterase.
+At position 1 to 77, the domain is characterized as Peptidase A1.
+At position 84 to 376, the domain is characterized as YjeF C-terminal.
+At position 280 to 441, the domain is characterized as Helicase ATP-binding.
+At position 462 to 621, the domain is characterized as Helicase C-terminal.
+At position 76 to 154, the domain is characterized as RRM 1.
+At position 177 to 253, the domain is characterized as RRM 2.
+At position 487 to 603, the domain is characterized as RGS.
+At position 842 to 1097, the domain is characterized as Protein kinase.
+At position 184 to 375, the domain is characterized as Glutamine amidotransferase type-1.
+At position 123 to 364, the domain is characterized as ABC transporter.
+At position 527 to 785, the domain is characterized as ABC transmembrane type-2.
+At position 56 to 214, the domain is characterized as Thioredoxin.
+At position 2 to 220, the domain is characterized as Glutamine amidotransferase type-1.
+At position 47 to 150, the domain is characterized as sHSP.
+At position 315 to 435, the domain is characterized as Ricin B-type lectin 1.
+At position 437 to 565, the domain is characterized as Ricin B-type lectin 2.
+At position 21 to 66, the domain is characterized as MADS-box.
+At position 19 to 98, the domain is characterized as IGFBP N-terminal.
+At position 93 to 270, the domain is characterized as FAD-binding PCMH-type.
+At position 305 to 347, the domain is characterized as CUE.
+At position 117 to 151, the domain is characterized as EF-hand 4.
+At position 30 to 290, the domain is characterized as AB hydrolase-1.
+At position 1 to 121, the domain is characterized as Velvet.
+At position 32 to 483, the domain is characterized as Hexokinase.
+At position 358 to 556, the domain is characterized as Helicase ATP-binding.
+At position 567 to 730, the domain is characterized as Helicase C-terminal.
+At position 46 to 357, the domain is characterized as PPM-type phosphatase.
+At position 194 to 252, the domain is characterized as TRAM.
+At position 335 to 348, the domain is characterized as CRIB.
+At position 1 to 99, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 99 to 138, the domain is characterized as 4Fe-4S His(Cys)3-ligated-type.
+At position 249 to 305, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 197 to 276, the domain is characterized as RRM.
+At position 438 to 567, the domain is characterized as C2 2.
+At position 256 to 328, the domain is characterized as KH.
+At position 480 to 558, the domain is characterized as RRM.
+At position 246 to 266, the domain is characterized as ELK.
+At position 1555 to 1778, the domain is characterized as Collagen IV NC1.
+At position 32 to 317, the domain is characterized as Protein kinase.
+At position 5 to 180, the domain is characterized as Prephenate dehydratase.
+At position 194 to 272, the domain is characterized as ACT.
+At position 25 to 214, the domain is characterized as GH16.
+At position 237 to 367, the domain is characterized as DOD-type homing endonuclease.
+At position 561 to 781, the domain is characterized as tr-type G.
+At position 43 to 331, the domain is characterized as Protein kinase.
+At position 241 to 338, the domain is characterized as HTH araC/xylS-type.
+At position 596 to 671, the domain is characterized as PUA.
+At position 233 to 350, the domain is characterized as CUB 1.
+At position 355 to 471, the domain is characterized as CUB 2.
+At position 473 to 509, the domain is characterized as LDL-receptor class A 1.
+At position 548 to 585, the domain is characterized as LDL-receptor class A 2.
+At position 596 to 830, the domain is characterized as Peptidase S1.
+At position 62 to 345, the domain is characterized as Lon N-terminal.
+At position 815 to 1001, the domain is characterized as Lon proteolytic.
+At position 48 to 305, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 321 to 570, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 14 to 446, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 967 to 1284, the domain is characterized as PKS/mFAS DH.
+At position 2355 to 2431, the domain is characterized as Carrier.
+At position 1 to 118, the domain is characterized as PX.
+At position 293 to 360, the domain is characterized as Mop.
+At position 270 to 470, the domain is characterized as GATase cobBQ-type.
+At position 77 to 110, the domain is characterized as WW.
+At position 196 to 456, the domain is characterized as F-BAR.
+At position 480 to 639, the domain is characterized as CBM3.
+At position 664 to 737, the domain is characterized as Dockerin.
+At position 276 to 403, the domain is characterized as MATH.
+At position 310 to 360, the domain is characterized as bHLH.
+At position 647 to 707, the domain is characterized as Tudor.
+At position 208 to 401, the domain is characterized as GMPS ATP-PPase.
+At position 2 to 66, the domain is characterized as HMA 1.
+At position 81 to 145, the domain is characterized as HMA 2.
+At position 5 to 74, the domain is characterized as ACT.
+At position 4 to 100, the domain is characterized as Toprim.
+At position 290 to 386, the domain is characterized as TAFH.
+At position 78 to 195, the domain is characterized as CBM20.
+At position 401 to 711, the domain is characterized as GP-PDE.
+At position 29 to 214, the domain is characterized as PID.
+At position 379 to 470, the domain is characterized as SH2.
+At position 47 to 174, the domain is characterized as TBDR plug.
+At position 179 to 746, the domain is characterized as TBDR beta-barrel.
+At position 73 to 283, the domain is characterized as ABC transmembrane type-1.
+At position 83 to 176, the domain is characterized as Ig-like.
+At position 312 to 641, the domain is characterized as PDEase.
+At position 183 to 242, the domain is characterized as bZIP.
+At position 121 to 292, the domain is characterized as Helicase ATP-binding.
+At position 316 to 464, the domain is characterized as Helicase C-terminal.
+At position 421 to 756, the domain is characterized as Kinesin motor.
+At position 195 to 254, the domain is characterized as CBS 1.
+At position 256 to 314, the domain is characterized as CBS 2.
+At position 32 to 273, the domain is characterized as ABC transporter.
+At position 14 to 214, the domain is characterized as YjeF N-terminal.
+At position 226 to 500, the domain is characterized as YjeF C-terminal.
+At position 228 to 454, the domain is characterized as Lon N-terminal.
+At position 453 to 562, the domain is characterized as CULT.
+At position 170 to 234, the domain is characterized as KH.
+At position 11 to 215, the domain is characterized as Glutamine amidotransferase type-1.
+At position 12 to 720, the domain is characterized as Myosin motor.
+At position 723 to 744, the domain is characterized as IQ 1.
+At position 745 to 774, the domain is characterized as IQ 2.
+At position 782 to 970, the domain is characterized as TH1.
+At position 150 to 326, the domain is characterized as Helicase ATP-binding.
+At position 340 to 510, the domain is characterized as Helicase C-terminal.
+At position 431 to 585, the domain is characterized as MATH.
+At position 2 to 157, the domain is characterized as Obg.
+At position 158 to 325, the domain is characterized as OBG-type G.
+At position 334 to 420, the domain is characterized as OCT.
+At position 220 to 279, the domain is characterized as SH3 1.
+At position 280 to 337, the domain is characterized as SH3 2.
+At position 36 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 2 to 285, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 7 to 289, the domain is characterized as YjeF C-terminal.
+At position 113 to 239, the domain is characterized as C-type lectin.
+At position 268 to 331, the domain is characterized as VWFC.
+At position 98 to 178, the domain is characterized as S4 RNA-binding.
+At position 1022 to 1061, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 1062 to 1117, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 1123 to 1163, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 1164 to 1206, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 1218 to 1270, the domain is characterized as Beta/gamma crystallin 'Greek key' 5.
+At position 1271 to 1313, the domain is characterized as Beta/gamma crystallin 'Greek key' 6.
+At position 1319 to 1361, the domain is characterized as Beta/gamma crystallin 'Greek key' 7.
+At position 1362 to 1404, the domain is characterized as Beta/gamma crystallin 'Greek key' 8.
+At position 1415 to 1452, the domain is characterized as Beta/gamma crystallin 'Greek key' 9.
+At position 1453 to 1496, the domain is characterized as Beta/gamma crystallin 'Greek key' 10.
+At position 1502 to 1542, the domain is characterized as Beta/gamma crystallin 'Greek key' 11.
+At position 1543 to 1584, the domain is characterized as Beta/gamma crystallin 'Greek key' 12.
+At position 1586 to 1719, the domain is characterized as Ricin B-type lectin.
+At position 415 to 686, the domain is characterized as Protein kinase.
+At position 149 to 393, the domain is characterized as Radical SAM core.
+At position 396 to 467, the domain is characterized as TRAM.
+At position 278 to 418, the domain is characterized as Sox C-terminal.
+At position 79 to 224, the domain is characterized as N-acetyltransferase.
+At position 145 to 323, the domain is characterized as CNNM transmembrane.
+At position 344 to 408, the domain is characterized as CBS 1.
+At position 444 to 514, the domain is characterized as CBS 2.
+At position 335 to 429, the domain is characterized as HD.
+At position 37 to 82, the domain is characterized as Gla.
+At position 91 to 126, the domain is characterized as EGF-like 1.
+At position 130 to 170, the domain is characterized as EGF-like 2.
+At position 210 to 447, the domain is characterized as Peptidase S1.
+At position 77 to 149, the domain is characterized as PAS 1.
+At position 336 to 667, the domain is characterized as Single-minded C-terminal.
+At position 336 to 590, the domain is characterized as Protein kinase.
+At position 591 to 648, the domain is characterized as AGC-kinase C-terminal.
+At position 214 to 308, the domain is characterized as Fe2OG dioxygenase.
+At position 167 to 241, the domain is characterized as POU-specific.
+At position 13 to 84, the domain is characterized as Sm.
+At position 123 to 403, the domain is characterized as ABC transmembrane type-1 1.
+At position 467 to 701, the domain is characterized as ABC transporter 1.
+At position 795 to 1082, the domain is characterized as ABC transmembrane type-1 2.
+At position 1120 to 1354, the domain is characterized as ABC transporter 2.
+At position 328 to 378, the domain is characterized as bHLH.
+At position 117 to 179, the domain is characterized as FHA.
+At position 224 to 490, the domain is characterized as Protein kinase.
+At position 3 to 244, the domain is characterized as Alpha-carbonic anhydrase.
+At position 184 to 263, the domain is characterized as Ubiquitin-like 2.
+At position 46 to 80, the domain is characterized as EF-hand 1.
+At position 81 to 118, the domain is characterized as EF-hand 2.
+At position 155 to 190, the domain is characterized as EF-hand 4.
+At position 17 to 134, the domain is characterized as Response regulatory.
+At position 45 to 174, the domain is characterized as VIT.
+At position 297 to 457, the domain is characterized as VWFA.
+At position 94 to 265, the domain is characterized as Helicase ATP-binding.
+At position 414 to 528, the domain is characterized as Toprim.
+At position 170 to 202, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 4 to 116, the domain is characterized as CMP/dCMP-type deaminase.
+At position 59 to 146, the domain is characterized as RRM.
+At position 29 to 174, the domain is characterized as UBC core.
+At position 142 to 234, the domain is characterized as EH 2.
+At position 55 to 267, the domain is characterized as DCUN1.
+At position 63 to 249, the domain is characterized as tr-type G.
+At position 175 to 401, the domain is characterized as tr-type G.
+At position 175 to 242, the domain is characterized as PAS 1.
+At position 315 to 381, the domain is characterized as PAS 2.
+At position 389 to 432, the domain is characterized as PAC.
+At position 1 to 76, the domain is characterized as GST N-terminal.
+At position 64 to 276, the domain is characterized as Radical SAM core.
+At position 145 to 226, the domain is characterized as PRC barrel.
+At position 1044 to 1307, the domain is characterized as Protein kinase.
+At position 546 to 587, the domain is characterized as JmjN.
+At position 610 to 702, the domain is characterized as ARID.
+At position 873 to 1037, the domain is characterized as JmjC.
+At position 78 to 318, the domain is characterized as Peptidase S1.
+At position 106 to 177, the domain is characterized as SUI1.
+At position 721 to 824, the domain is characterized as PH.
+At position 10 to 82, the domain is characterized as ZAD.
+At position 420 to 508, the domain is characterized as PTS EIIB type-2.
+At position 133 to 165, the domain is characterized as LisH.
+At position 171 to 228, the domain is characterized as CTLH.
+At position 136 to 455, the domain is characterized as Peptidase S8.
+At position 463 to 603, the domain is characterized as P/Homo B.
+At position 271 to 432, the domain is characterized as Helicase ATP-binding.
+At position 451 to 611, the domain is characterized as Helicase C-terminal.
+At position 277 to 355, the domain is characterized as RRM 3.
+At position 163 to 271, the domain is characterized as MaoC-like.
+At position 414 to 748, the domain is characterized as HECT.
+At position 201 to 396, the domain is characterized as Peptidase M12B.
+At position 417 to 478, the domain is characterized as Disintegrin.
+At position 2 to 148, the domain is characterized as CYTH.
+At position 15 to 147, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 1 to 158, the domain is characterized as MGS-like.
+At position 31 to 319, the domain is characterized as GH16.
+At position 14 to 160, the domain is characterized as NAC.
+At position 7 to 106, the domain is characterized as HTH arsR-type.
+At position 27 to 303, the domain is characterized as EndoU.
+At position 134 to 394, the domain is characterized as NR LBD.
+At position 56 to 167, the domain is characterized as THUMP.
+At position 260 to 499, the domain is characterized as NR LBD.
+At position 105 to 417, the domain is characterized as IF rod.
+At position 252 to 430, the domain is characterized as GATase cobBQ-type.
+At position 30 to 59, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 61 to 90, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 105 to 136, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 136 to 163, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 388 to 539, the domain is characterized as Helicase C-terminal.
+At position 279 to 392, the domain is characterized as PAZ.
+At position 556 to 848, the domain is characterized as Piwi.
+At position 157 to 379, the domain is characterized as Helicase ATP-binding.
+At position 413 to 573, the domain is characterized as Helicase C-terminal.
+At position 468 to 614, the domain is characterized as DOD-type homing endonuclease.
+At position 210 to 296, the domain is characterized as Disintegrin.
+At position 40 to 140, the domain is characterized as SRCR 1.
+At position 143 to 245, the domain is characterized as SRCR 2.
+At position 248 to 348, the domain is characterized as SRCR 3.
+At position 351 to 450, the domain is characterized as SRCR 4.
+At position 453 to 553, the domain is characterized as SRCR 5.
+At position 555 to 654, the domain is characterized as SRCR 6.
+At position 657 to 757, the domain is characterized as SRCR 7.
+At position 759 to 866, the domain is characterized as SRCR 8.
+At position 868 to 968, the domain is characterized as SRCR 9.
+At position 969 to 1028, the domain is characterized as Sushi.
+At position 49 to 333, the domain is characterized as CN hydrolase.
+At position 154 to 433, the domain is characterized as Protein kinase.
+At position 330 to 390, the domain is characterized as S4 RNA-binding.
+At position 25 to 184, the domain is characterized as ENTH.
+At position 1 to 209, the domain is characterized as SPX.
+At position 972 to 1311, the domain is characterized as GP-PDE.
+At position 308 to 488, the domain is characterized as Helicase ATP-binding.
+At position 539 to 685, the domain is characterized as Helicase C-terminal.
+At position 121 to 329, the domain is characterized as ATP-grasp.
+At position 38 to 163, the domain is characterized as PLAT.
+At position 166 to 857, the domain is characterized as Lipoxygenase.
+At position 930 to 1024, the domain is characterized as MGS-like.
+At position 1 to 87, the domain is characterized as IF rod.
+At position 44 to 155, the domain is characterized as AB hydrolase-1.
+At position 181 to 274, the domain is characterized as Fibronectin type-III.
+At position 27 to 230, the domain is characterized as Velvet.
+At position 26 to 126, the domain is characterized as Ig-like V-type.
+At position 44 to 286, the domain is characterized as ABC transporter.
+At position 1 to 243, the domain is characterized as ABC transporter.
+At position 39 to 90, the domain is characterized as Tudor-knot.
+At position 192 to 509, the domain is characterized as MYST-type HAT.
+At position 3 to 220, the domain is characterized as Glutamine amidotransferase type-1.
+At position 350 to 414, the domain is characterized as S4 RNA-binding.
+At position 789 to 1072, the domain is characterized as FIIND.
+At position 1106 to 1189, the domain is characterized as CARD.
+At position 4 to 59, the domain is characterized as HTH deoR-type.
+At position 95 to 177, the domain is characterized as RRM 1.
+At position 12 to 218, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 231, the domain is characterized as Deacetylase sirtuin-type.
+At position 14 to 338, the domain is characterized as G-alpha.
+At position 628 to 665, the domain is characterized as SANT 2.
+At position 345 to 756, the domain is characterized as Peptidase S8.
+At position 897 to 962, the domain is characterized as HP.
+At position 151 to 210, the domain is characterized as v-SNARE coiled-coil homology.
+At position 26 to 121, the domain is characterized as Chorein N-terminal.
+At position 628 to 678, the domain is characterized as PAP-associated 1.
+At position 1184 to 1237, the domain is characterized as PAP-associated 2.
+At position 69 to 168, the domain is characterized as Mis18.
+At position 280 to 485, the domain is characterized as Ku.
+At position 54 to 222, the domain is characterized as Helicase ATP-binding.
+At position 245 to 447, the domain is characterized as Helicase C-terminal.
+At position 221 to 280, the domain is characterized as LIM zinc-binding 1.
+At position 281 to 338, the domain is characterized as LIM zinc-binding 2.
+At position 339 to 398, the domain is characterized as LIM zinc-binding 3.
+At position 399 to 456, the domain is characterized as LIM zinc-binding 4.
+At position 499 to 551, the domain is characterized as PSI.
+At position 556 to 644, the domain is characterized as Ig-like C2-type.
+At position 176 to 398, the domain is characterized as Histidine kinase.
+At position 7 to 381, the domain is characterized as Trm1 methyltransferase.
+At position 510 to 804, the domain is characterized as UvrD-like helicase C-terminal.
+At position 174 to 298, the domain is characterized as AB hydrolase-1.
+At position 98 to 205, the domain is characterized as S4 RNA-binding.
+At position 595 to 654, the domain is characterized as PASTA 1.
+At position 655 to 711, the domain is characterized as PASTA 2.
+At position 23 to 77, the domain is characterized as Kazal-like 1.
+At position 85 to 140, the domain is characterized as Kazal-like 2.
+At position 148 to 202, the domain is characterized as Kazal-like 3.
+At position 72 to 192, the domain is characterized as B12-binding.
+At position 24 to 132, the domain is characterized as Cadherin 1.
+At position 462 to 570, the domain is characterized as Cadherin 5.
+At position 567 to 693, the domain is characterized as Cadherin 6.
+At position 22 to 141, the domain is characterized as CBM6.
+At position 165 to 459, the domain is characterized as GH26.
+At position 534 to 571, the domain is characterized as CBM10 2.
+At position 317 to 427, the domain is characterized as PAZ.
+At position 594 to 885, the domain is characterized as Piwi.
+At position 1 to 228, the domain is characterized as Helicase ATP-binding.
+At position 102 to 351, the domain is characterized as Protein kinase.
+At position 387 to 422, the domain is characterized as EF-hand 2.
+At position 24 to 73, the domain is characterized as LCN-type CS-alpha/beta.
+At position 64 to 170, the domain is characterized as Expansin-like EG45.
+At position 183 to 270, the domain is characterized as Expansin-like CBD.
+At position 208 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 30 to 181, the domain is characterized as FZ.
+At position 352 to 508, the domain is characterized as N-acetyltransferase.
+At position 173 to 202, the domain is characterized as GS.
+At position 311 to 373, the domain is characterized as CBS 1.
+At position 205 to 323, the domain is characterized as C2 2.
+At position 1138 to 1264, the domain is characterized as C2 4.
+At position 1312 to 1440, the domain is characterized as C2 5.
+At position 1588 to 1706, the domain is characterized as C2 6.
+At position 1822 to 1970, the domain is characterized as C2 7.
+At position 18 to 301, the domain is characterized as ABC transmembrane type-1.
+At position 566 to 669, the domain is characterized as tRNA-binding.
+At position 55 to 221, the domain is characterized as FAD-binding PCMH-type.
+At position 222 to 446, the domain is characterized as Rab-GAP TBC.
+At position 65 to 433, the domain is characterized as PIPK.
+At position 272 to 471, the domain is characterized as Reticulon.
+At position 62 to 242, the domain is characterized as FAD-binding PCMH-type.
+At position 70 to 325, the domain is characterized as Protein kinase.
+At position 28 to 38, the domain is characterized as EF-hand 1.
+At position 39 to 63, the domain is characterized as EF-hand 2.
+At position 45 to 77, the domain is characterized as EF-hand 2.
+At position 59 to 108, the domain is characterized as WAP.
+At position 40 to 166, the domain is characterized as Ricin B-type lectin.
+At position 15 to 97, the domain is characterized as Core-binding (CB).
+At position 115 to 288, the domain is characterized as Tyr recombinase.
+At position 296 to 493, the domain is characterized as Peptidase M12B.
+At position 499 to 585, the domain is characterized as Disintegrin.
+At position 729 to 766, the domain is characterized as EGF-like.
+At position 78 to 171, the domain is characterized as Cytochrome c.
+At position 7 to 185, the domain is characterized as YrdC-like.
+At position 24 to 275, the domain is characterized as Pyruvate carboxyltransferase.
+At position 140 to 203, the domain is characterized as bZIP.
+At position 35 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 143 to 252, the domain is characterized as Gnk2-homologous 2.
+At position 758 to 835, the domain is characterized as PKD 1.
+At position 855 to 918, the domain is characterized as PKD 2.
+At position 528 to 823, the domain is characterized as UvrD-like helicase C-terminal.
+At position 410 to 631, the domain is characterized as B30.2/SPRY.
+At position 47 to 320, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 49 to 277, the domain is characterized as Radical SAM core.
+At position 209 to 406, the domain is characterized as DH.
+At position 446 to 545, the domain is characterized as PH.
+At position 18 to 272, the domain is characterized as Protein kinase.
+At position 46 to 163, the domain is characterized as SEA.
+At position 187 to 417, the domain is characterized as Peptidase S1.
+At position 366 to 463, the domain is characterized as Fibronectin type-III.
+At position 238 to 370, the domain is characterized as Plus3.
+At position 23 to 276, the domain is characterized as Pyruvate carboxyltransferase.
+At position 177 to 269, the domain is characterized as 5'-3' exonuclease.
+At position 340 to 522, the domain is characterized as 3'-5' exonuclease.
+At position 2 to 144, the domain is characterized as Jacalin-type lectin.
+At position 249 to 751, the domain is characterized as Biotin carboxylation.
+At position 408 to 599, the domain is characterized as ATP-grasp.
+At position 878 to 952, the domain is characterized as Biotinyl-binding.
+At position 1685 to 2015, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 2019 to 2335, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 46 to 266, the domain is characterized as Peptidase S1.
+At position 504 to 781, the domain is characterized as Protein kinase.
+At position 154 to 547, the domain is characterized as SAC.
+At position 10 to 172, the domain is characterized as TIR.
+At position 261 to 513, the domain is characterized as NB-ARC.
+At position 3 to 261, the domain is characterized as ABC transporter.
+At position 649 to 740, the domain is characterized as GED.
+At position 39 to 112, the domain is characterized as Cytochrome c.
+At position 96 to 312, the domain is characterized as RNase H type-2.
+At position 6 to 123, the domain is characterized as MTTase N-terminal.
+At position 146 to 380, the domain is characterized as Radical SAM core.
+At position 41 to 183, the domain is characterized as SIS.
+At position 209 to 268, the domain is characterized as CBS 1.
+At position 275 to 327, the domain is characterized as CBS 2.
+At position 16 to 158, the domain is characterized as N-acetyltransferase 1.
+At position 166 to 309, the domain is characterized as N-acetyltransferase 2.
+At position 132 to 226, the domain is characterized as BRICHOS.
+At position 246 to 781, the domain is characterized as PLA2c.
+At position 1 to 83, the domain is characterized as Acylphosphatase-like.
+At position 5 to 147, the domain is characterized as Clp R.
+At position 8 to 367, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 1 to 211, the domain is characterized as DegV.
+At position 169 to 492, the domain is characterized as Kinesin motor.
+At position 533 to 671, the domain is characterized as Flavodoxin-like.
+At position 724 to 964, the domain is characterized as FAD-binding FR-type.
+At position 38 to 272, the domain is characterized as Alpha-carbonic anhydrase.
+At position 806 to 1115, the domain is characterized as Bin3-type SAM.
+At position 683 to 965, the domain is characterized as Protein kinase.
+At position 63 to 96, the domain is characterized as KOW.
+At position 418 to 603, the domain is characterized as N-acetyltransferase.
+At position 1 to 73, the domain is characterized as DED 1.
+At position 92 to 170, the domain is characterized as DED 2.
+At position 60 to 175, the domain is characterized as THUMP.
+At position 185 to 292, the domain is characterized as PH.
+At position 649 to 827, the domain is characterized as C2 DOCK-type.
+At position 1614 to 2055, the domain is characterized as DOCKER.
+At position 55 to 236, the domain is characterized as FAD-binding PCMH-type.
+At position 65 to 356, the domain is characterized as ABC transmembrane type-1 1.
+At position 393 to 638, the domain is characterized as ABC transporter 1.
+At position 727 to 1016, the domain is characterized as ABC transmembrane type-1 2.
+At position 1053 to 1293, the domain is characterized as ABC transporter 2.
+At position 1 to 426, the domain is characterized as SMP-LTD.
+At position 7 to 270, the domain is characterized as ABC transporter 1.
+At position 287 to 533, the domain is characterized as ABC transporter 2.
+At position 297 to 374, the domain is characterized as RRM 1.
+At position 401 to 481, the domain is characterized as RRM 2.
+At position 27 to 452, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 960 to 1270, the domain is characterized as PKS/mFAS DH.
+At position 7 to 160, the domain is characterized as Nudix hydrolase.
+At position 549 to 650, the domain is characterized as tRNA-binding.
+At position 423 to 473, the domain is characterized as LRRCT.
+At position 344 to 411, the domain is characterized as ACT 2.
+At position 25 to 103, the domain is characterized as GIY-YIG.
+At position 627 to 1061, the domain is characterized as PDEase.
+At position 1017 to 1088, the domain is characterized as S1 motif.
+At position 309 to 363, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 365 to 412, the domain is characterized as WR1 1.
+At position 434 to 484, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 487 to 525, the domain is characterized as WR1 2.
+At position 531 to 581, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 588 to 629, the domain is characterized as WR1 3.
+At position 635 to 687, the domain is characterized as BPTI/Kunitz inhibitor 4.
+At position 690 to 737, the domain is characterized as WR1 4.
+At position 743 to 795, the domain is characterized as BPTI/Kunitz inhibitor 5.
+At position 798 to 845, the domain is characterized as WR1 5.
+At position 850 to 897, the domain is characterized as WR1 6.
+At position 902 to 950, the domain is characterized as WR1 7.
+At position 953 to 1000, the domain is characterized as WR1 8.
+At position 1012 to 1059, the domain is characterized as WR1 9.
+At position 1071 to 1115, the domain is characterized as WR1 10.
+At position 1118 to 1162, the domain is characterized as WR1 11.
+At position 1177 to 1209, the domain is characterized as WR1 12.
+At position 1223 to 1266, the domain is characterized as WR1 13.
+At position 1295 to 1342, the domain is characterized as WR1 14.
+At position 1376 to 1416, the domain is characterized as WR1 15.
+At position 1443 to 1488, the domain is characterized as WR1 16.
+At position 822 to 1052, the domain is characterized as Histidine kinase.
+At position 1076 to 1199, the domain is characterized as Response regulatory.
+At position 49 to 105, the domain is characterized as AWS.
+At position 107 to 224, the domain is characterized as SET.
+At position 231 to 247, the domain is characterized as Post-SET.
+At position 445 to 477, the domain is characterized as WW.
+At position 121 to 237, the domain is characterized as EamA 1.
+At position 101 to 152, the domain is characterized as bHLH.
+At position 98 to 255, the domain is characterized as C-CAP/cofactor C-like.
+At position 121 to 243, the domain is characterized as TBDR plug.
+At position 248 to 1061, the domain is characterized as TBDR beta-barrel.
+At position 183 to 374, the domain is characterized as CheB-type methylesterase.
+At position 897 to 1168, the domain is characterized as Tyrosine-protein phosphatase.
+At position 151 to 201, the domain is characterized as bHLH.
+At position 56 to 165, the domain is characterized as Rieske.
+At position 360 to 564, the domain is characterized as Helicase C-terminal.
+At position 635 to 860, the domain is characterized as JmjC.
+At position 277 to 436, the domain is characterized as Helicase C-terminal.
+At position 30 to 236, the domain is characterized as BPL/LPL catalytic.
+At position 389 to 434, the domain is characterized as UBA.
+At position 564 to 644, the domain is characterized as BTB 1.
+At position 768 to 836, the domain is characterized as BTB 2.
+At position 159 to 221, the domain is characterized as t-SNARE coiled-coil homology.
+At position 74 to 356, the domain is characterized as tr-type G.
+At position 8 to 191, the domain is characterized as Guanylate kinase-like.
+At position 189 to 389, the domain is characterized as HIN-200 1.
+At position 562 to 761, the domain is characterized as HIN-200 2.
+At position 52 to 210, the domain is characterized as TNase-like.
+At position 9 to 68, the domain is characterized as CHORD 1.
+At position 152 to 210, the domain is characterized as CHORD 2.
+At position 218 to 308, the domain is characterized as CS.
+At position 1 to 131, the domain is characterized as ADF-H 1.
+At position 169 to 305, the domain is characterized as ADF-H 2.
+At position 477 to 748, the domain is characterized as Protein kinase.
+At position 7 to 283, the domain is characterized as CheR-type methyltransferase.
+At position 9 to 288, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 622 to 668, the domain is characterized as SANT 2.
+At position 5 to 108, the domain is characterized as AB hydrolase-1.
+At position 47 to 137, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 11 to 73, the domain is characterized as S4 RNA-binding.
+At position 23 to 143, the domain is characterized as EamA 1.
+At position 195 to 322, the domain is characterized as EamA 2.
+At position 3 to 235, the domain is characterized as ABC transporter.
+At position 2 to 174, the domain is characterized as Glutamine amidotransferase type-1.
+At position 598 to 772, the domain is characterized as PCI.
+At position 1 to 165, the domain is characterized as PPIase cyclophilin-type.
+At position 242 to 320, the domain is characterized as RRM.
+At position 6 to 118, the domain is characterized as Longin.
+At position 4 to 79, the domain is characterized as ZAD.
+At position 37 to 89, the domain is characterized as Collagen-like.
+At position 144 to 239, the domain is characterized as C-type lectin.
+At position 482 to 762, the domain is characterized as Protein kinase.
+At position 35 to 150, the domain is characterized as Response regulatory.
+At position 1 to 81, the domain is characterized as Core-binding (CB).
+At position 102 to 281, the domain is characterized as Tyr recombinase.
+At position 38 to 171, the domain is characterized as MPN.
+At position 70 to 314, the domain is characterized as Peptidase S1.
+At position 36 to 117, the domain is characterized as KRAB.
+At position 247 to 415, the domain is characterized as Integrase catalytic.
+At position 340 to 403, the domain is characterized as S4 RNA-binding.
+At position 54 to 208, the domain is characterized as Upf1 CH-rich.
+At position 78 to 396, the domain is characterized as Peptidase A1.
+At position 227 to 302, the domain is characterized as RRM.
+At position 21 to 130, the domain is characterized as Rhodanese.
+At position 433 to 698, the domain is characterized as Tyrosine-protein phosphatase.
+At position 132 to 367, the domain is characterized as Radical SAM core.
+At position 6 to 264, the domain is characterized as Protein kinase.
+At position 9 to 103, the domain is characterized as PH.
+At position 593 to 758, the domain is characterized as Helicase ATP-binding.
+At position 779 to 933, the domain is characterized as Helicase C-terminal.
+At position 566 to 939, the domain is characterized as Rab-GAP TBC.
+At position 430 to 480, the domain is characterized as DHHC.
+At position 19 to 113, the domain is characterized as PPIase FKBP-type.
+At position 60 to 90, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 146 to 219, the domain is characterized as DEP 2.
+At position 52 to 121, the domain is characterized as BTB.
+At position 211 to 487, the domain is characterized as NPH3.
+At position 103 to 183, the domain is characterized as Core-binding (CB).
+At position 206 to 381, the domain is characterized as Tyr recombinase.
+At position 46 to 243, the domain is characterized as TNase-like.
+At position 206 to 440, the domain is characterized as NR LBD.
+At position 89 to 259, the domain is characterized as Cytochrome c.
+At position 23 to 73, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 29 to 235, the domain is characterized as Ch-type lysozyme.
+At position 49 to 219, the domain is characterized as Helicase ATP-binding.
+At position 230 to 391, the domain is characterized as Helicase C-terminal.
+At position 678 to 767, the domain is characterized as BRCT.
+At position 78 to 199, the domain is characterized as PH.
+At position 231 to 335, the domain is characterized as IRS-type PTB.
+At position 15 to 179, the domain is characterized as MOSC.
+At position 1 to 208, the domain is characterized as PPM-type phosphatase.
+At position 3 to 187, the domain is characterized as Prephenate dehydratase.
+At position 201 to 278, the domain is characterized as ACT.
+At position 40 to 122, the domain is characterized as Lipoyl-binding.
+At position 270 to 303, the domain is characterized as KOW 1.
+At position 417 to 448, the domain is characterized as KOW 2.
+At position 469 to 500, the domain is characterized as KOW 3.
+At position 591 to 624, the domain is characterized as KOW 4.
+At position 696 to 729, the domain is characterized as KOW 5.
+At position 919 to 963, the domain is characterized as LRRCT.
+At position 157 to 179, the domain is characterized as Follistatin-like 1.
+At position 250 to 272, the domain is characterized as Follistatin-like 2.
+At position 278 to 296, the domain is characterized as Follistatin-like 3.
+At position 358 to 380, the domain is characterized as Follistatin-like 4.
+At position 389 to 415, the domain is characterized as Follistatin-like 5.
+At position 745 to 868, the domain is characterized as OmpA-like.
+At position 162 to 253, the domain is characterized as 5'-3' exonuclease.
+At position 3 to 110, the domain is characterized as DMAP1-binding.
+At position 562 to 756, the domain is characterized as EXS.
+At position 23 to 98, the domain is characterized as Ig-like.
+At position 395 to 640, the domain is characterized as Rab-GAP TBC.
+At position 48 to 473, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1000 to 1307, the domain is characterized as PKS/mFAS DH.
+At position 2359 to 2441, the domain is characterized as Carrier.
+At position 2 to 105, the domain is characterized as Glutaredoxin.
+At position 88 to 147, the domain is characterized as HTH cro/C1-type.
+At position 5 to 162, the domain is characterized as N-acetyltransferase.
+At position 25 to 209, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 48, the domain is characterized as LDL-receptor class A.
+At position 704 to 753, the domain is characterized as KA1.
+At position 790 to 857, the domain is characterized as KHA.
+At position 448 to 507, the domain is characterized as SH3 3.
+At position 840 to 899, the domain is characterized as SH3 4.
+At position 1072 to 1133, the domain is characterized as SH3 5.
+At position 164 to 245, the domain is characterized as PPIase FKBP-type.
+At position 90 to 329, the domain is characterized as Radical SAM core.
+At position 74 to 403, the domain is characterized as Asparaginase/glutaminase.
+At position 118 to 219, the domain is characterized as ATP-cone 2.
+At position 237 to 327, the domain is characterized as ATP-cone 3.
+At position 52 to 104, the domain is characterized as LIM zinc-binding 1.
+At position 114 to 167, the domain is characterized as LIM zinc-binding 2.
+At position 43 to 214, the domain is characterized as VWFD 1.
+At position 302 to 357, the domain is characterized as TIL.
+At position 395 to 579, the domain is characterized as VWFD 2.
+At position 866 to 1038, the domain is characterized as VWFD 3.
+At position 2349 to 2438, the domain is characterized as CTCK.
+At position 41 to 95, the domain is characterized as Clip.
+At position 137 to 404, the domain is characterized as Peptidase S1.
+At position 2 to 199, the domain is characterized as ABC transporter.
+At position 421 to 465, the domain is characterized as LysM.
+At position 137 to 306, the domain is characterized as PCI.
+At position 70 to 786, the domain is characterized as Myosin motor.
+At position 789 to 818, the domain is characterized as IQ 1.
+At position 812 to 836, the domain is characterized as IQ 2.
+At position 837 to 859, the domain is characterized as IQ 3.
+At position 860 to 884, the domain is characterized as IQ 4.
+At position 885 to 907, the domain is characterized as IQ 5.
+At position 908 to 937, the domain is characterized as IQ 6.
+At position 1230 to 1505, the domain is characterized as Dilute.
+At position 222 to 284, the domain is characterized as t-SNARE coiled-coil homology.
+At position 401 to 602, the domain is characterized as Rho-GAP.
+At position 29 to 182, the domain is characterized as Cohesin 1.
+At position 183 to 322, the domain is characterized as Cohesin 2.
+At position 365 to 523, the domain is characterized as CBM3.
+At position 560 to 704, the domain is characterized as Cohesin 3.
+At position 724 to 866, the domain is characterized as Cohesin 4.
+At position 889 to 1031, the domain is characterized as Cohesin 5.
+At position 1054 to 1196, the domain is characterized as Cohesin 6.
+At position 1219 to 1361, the domain is characterized as Cohesin 7.
+At position 1384 to 1526, the domain is characterized as Cohesin 8.
+At position 1548 to 1690, the domain is characterized as Cohesin 9.
+At position 1785 to 1852, the domain is characterized as Dockerin.
+At position 268 to 442, the domain is characterized as NodB homology.
+At position 116 to 378, the domain is characterized as ABC transporter 1.
+At position 813 to 1055, the domain is characterized as ABC transporter 2.
+At position 365 to 432, the domain is characterized as TRAM.
+At position 20 to 61, the domain is characterized as LRRNT.
+At position 350 to 429, the domain is characterized as Ubiquitin-like 1.
+At position 430 to 506, the domain is characterized as Ubiquitin-like 2.
+At position 93 to 125, the domain is characterized as LisH.
+At position 635 to 739, the domain is characterized as Cytochrome c.
+At position 136 to 238, the domain is characterized as BACK.
+At position 384 to 460, the domain is characterized as RRM 1.
+At position 479 to 558, the domain is characterized as RRM 2.
+At position 114 to 172, the domain is characterized as J.
+At position 26 to 294, the domain is characterized as Peptidase S6.
+At position 1156 to 1409, the domain is characterized as Autotransporter.
+At position 94 to 398, the domain is characterized as Peptidase A1.
+At position 112 to 359, the domain is characterized as Radical SAM core.
+At position 28 to 262, the domain is characterized as Alpha-carbonic anhydrase.
+At position 889 to 1043, the domain is characterized as Guanylate cyclase.
+At position 40 to 98, the domain is characterized as Myb-like 1.
+At position 390 to 454, the domain is characterized as Myb-like 2.
+At position 25 to 233, the domain is characterized as Velvet.
+At position 194 to 382, the domain is characterized as MIF4G.
+At position 485 to 601, the domain is characterized as MI.
+At position 206 to 382, the domain is characterized as EngA-type G 2.
+At position 581 to 929, the domain is characterized as GBD/FH3.
+At position 1019 to 1081, the domain is characterized as FH1.
+At position 1086 to 1475, the domain is characterized as FH2.
+At position 1488 to 1518, the domain is characterized as DAD.
+At position 45 to 102, the domain is characterized as CTLH.
+At position 25 to 195, the domain is characterized as Reelin.
+At position 245 to 368, the domain is characterized as DOMON.
+At position 372 to 570, the domain is characterized as Cytochrome b561.
+At position 110 to 173, the domain is characterized as S5 DRBM.
+At position 719 to 1001, the domain is characterized as Protein kinase.
+At position 180 to 348, the domain is characterized as JmjC.
+At position 136 to 217, the domain is characterized as RCK C-terminal.
+At position 14 to 192, the domain is characterized as Guanylate kinase-like.
+At position 402 to 480, the domain is characterized as B5.
+At position 426 to 540, the domain is characterized as Toprim.
+At position 77 to 157, the domain is characterized as KH 1.
+At position 210 to 292, the domain is characterized as KH 2.
+At position 55 to 118, the domain is characterized as HMA 1.
+At position 144 to 208, the domain is characterized as HMA 2.
+At position 153 to 366, the domain is characterized as ATP-grasp.
+At position 358 to 552, the domain is characterized as PCI.
+At position 38 to 126, the domain is characterized as Cystatin 1.
+At position 145 to 215, the domain is characterized as Cystatin 2.
+At position 1 to 294, the domain is characterized as SPX.
+At position 248 to 428, the domain is characterized as PCI.
+At position 172 to 543, the domain is characterized as TTL.
+At position 97 to 255, the domain is characterized as FCP1 homology.
+At position 44 to 364, the domain is characterized as USP.
+At position 161 to 399, the domain is characterized as Radical SAM core.
+At position 4 to 367, the domain is characterized as SAM-dependent MTase C5-type.
+At position 39 to 144, the domain is characterized as HPt.
+At position 3 to 248, the domain is characterized as ABC transporter.
+At position 253 to 429, the domain is characterized as Helicase ATP-binding.
+At position 337 to 614, the domain is characterized as BEACH.
+At position 263 to 410, the domain is characterized as Flavodoxin-like.
+At position 98 to 234, the domain is characterized as Fatty acid hydroxylase.
+At position 106 to 160, the domain is characterized as bHLH.
+At position 566 to 670, the domain is characterized as ARID.
+At position 8 to 126, the domain is characterized as Longin.
+At position 296 to 381, the domain is characterized as RCK C-terminal.
+At position 597 to 662, the domain is characterized as SAM.
+At position 66 to 224, the domain is characterized as Thioredoxin.
+At position 161 to 256, the domain is characterized as Rieske.
+At position 727 to 1020, the domain is characterized as Peptidase S8.
+At position 24 to 108, the domain is characterized as SAM.
+At position 233 to 327, the domain is characterized as Ras-associating.
+At position 104 to 393, the domain is characterized as FAE.
+At position 421 to 598, the domain is characterized as C2 DOCK-type.
+At position 1225 to 1632, the domain is characterized as DOCKER.
+At position 45 to 326, the domain is characterized as GH10.
+At position 638 to 727, the domain is characterized as BRCT.
+At position 173 to 321, the domain is characterized as GAF.
+At position 364 to 601, the domain is characterized as Histidine kinase.
+At position 629 to 746, the domain is characterized as Response regulatory.
+At position 265 to 356, the domain is characterized as PDZ 1.
+At position 362 to 468, the domain is characterized as PDZ 2.
+At position 97 to 138, the domain is characterized as UBA.
+At position 626 to 931, the domain is characterized as Protein kinase.
+At position 932 to 1010, the domain is characterized as AGC-kinase C-terminal.
+At position 67 to 143, the domain is characterized as BTB.
+At position 1 to 346, the domain is characterized as SPX.
+At position 606 to 800, the domain is characterized as EXS.
+At position 30 to 318, the domain is characterized as ABC transmembrane type-1 1.
+At position 353 to 589, the domain is characterized as ABC transporter 1.
+At position 663 to 950, the domain is characterized as ABC transmembrane type-1 2.
+At position 985 to 1223, the domain is characterized as ABC transporter 2.
+At position 440 to 534, the domain is characterized as BTB 1.
+At position 664 to 733, the domain is characterized as BTB 2.
+At position 1 to 20, the domain is characterized as EF-hand 1.
+At position 22 to 43, the domain is characterized as EF-hand 2.
+At position 118 to 304, the domain is characterized as CP-type G.
+At position 411 to 791, the domain is characterized as USP.
+At position 78 to 135, the domain is characterized as CTLH.
+At position 622 to 814, the domain is characterized as Rab-GAP TBC.
+At position 68 to 234, the domain is characterized as Helicase ATP-binding.
+At position 292 to 468, the domain is characterized as Helicase C-terminal.
+At position 885 to 950, the domain is characterized as Tudor.
+At position 34 to 118, the domain is characterized as Inhibitor I9.
+At position 133 to 405, the domain is characterized as Peptidase S8.
+At position 5 to 182, the domain is characterized as UmuC.
+At position 20 to 339, the domain is characterized as Septin-type G.
+At position 80 to 305, the domain is characterized as Radical SAM core.
+At position 210 to 338, the domain is characterized as OmpA-like.
+At position 12 to 158, the domain is characterized as Jacalin-type lectin 1.
+At position 161 to 303, the domain is characterized as Jacalin-type lectin 2.
+At position 304 to 447, the domain is characterized as Jacalin-type lectin 3.
+At position 454 to 597, the domain is characterized as Jacalin-type lectin 4.
+At position 63 to 754, the domain is characterized as Peptidase M13.
+At position 74 to 175, the domain is characterized as Cyclin N-terminal.
+At position 28 to 255, the domain is characterized as PARP catalytic.
+At position 243 to 314, the domain is characterized as RST.
+At position 53 to 280, the domain is characterized as ABC transmembrane type-2.
+At position 53 to 275, the domain is characterized as Saposin B-type.
+At position 101 to 183, the domain is characterized as RRM 1.
+At position 197 to 276, the domain is characterized as RRM 2.
+At position 304 to 376, the domain is characterized as RRM 3.
+At position 201 to 254, the domain is characterized as LRRCT.
+At position 267 to 336, the domain is characterized as Ig-like C2-type.
+At position 431 to 519, the domain is characterized as Fibronectin type-III.
+At position 178 to 238, the domain is characterized as PAP-associated.
+At position 532 to 635, the domain is characterized as PH.
+At position 708 to 798, the domain is characterized as FDX-ACB.
+At position 6 to 134, the domain is characterized as N-acetyltransferase 1.
+At position 20 to 271, the domain is characterized as Radical SAM core.
+At position 113 to 151, the domain is characterized as Sin.
+At position 615 to 767, the domain is characterized as RNase NYN.
+At position 1 to 47, the domain is characterized as ClpX-type ZB.
+At position 4 to 442, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 945 to 1233, the domain is characterized as PKS/mFAS DH.
+At position 2350 to 2425, the domain is characterized as Carrier.
+At position 8 to 202, the domain is characterized as AMMECR1.
+At position 1845 to 1922, the domain is characterized as Carrier 2.
+At position 13 to 133, the domain is characterized as MPN.
+At position 51 to 353, the domain is characterized as GP-PDE 1.
+At position 369 to 670, the domain is characterized as GP-PDE 2.
+At position 805 to 1094, the domain is characterized as Protein kinase.
+At position 10 to 208, the domain is characterized as YjeF N-terminal.
+At position 112 to 334, the domain is characterized as GB1/RHD3-type G.
+At position 9 to 117, the domain is characterized as Calponin-homology (CH) 1.
+At position 126 to 231, the domain is characterized as Calponin-homology (CH) 2.
+At position 48 to 468, the domain is characterized as FERM.
+At position 383 to 798, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1293 to 1605, the domain is characterized as PKS/mFAS DH.
+At position 1657 to 1731, the domain is characterized as Carrier.
+At position 1642 to 1729, the domain is characterized as BRCT 1.
+At position 1749 to 1848, the domain is characterized as BRCT 2.
+At position 75 to 141, the domain is characterized as SAM.
+At position 1086 to 1146, the domain is characterized as v-SNARE coiled-coil homology.
+At position 28 to 288, the domain is characterized as Protein kinase.
+At position 171 to 405, the domain is characterized as Radical SAM core.
+At position 4 to 66, the domain is characterized as HTH iclR-type.
+At position 81 to 250, the domain is characterized as IclR-ED.
+At position 12 to 181, the domain is characterized as FAD-binding PCMH-type.
+At position 130 to 435, the domain is characterized as AB hydrolase-1.
+At position 696 to 914, the domain is characterized as Helicase C-terminal 1.
+At position 18 to 138, the domain is characterized as MTTase N-terminal.
+At position 165 to 397, the domain is characterized as Radical SAM core.
+At position 400 to 462, the domain is characterized as TRAM.
+At position 272 to 384, the domain is characterized as PAZ.
+At position 546 to 838, the domain is characterized as Piwi.
+At position 345 to 610, the domain is characterized as Protein kinase.
+At position 13 to 249, the domain is characterized as PABS.
+At position 37 to 217, the domain is characterized as KIND 1.
+At position 456 to 620, the domain is characterized as KIND 2.
+At position 1239 to 1367, the domain is characterized as N-terminal Ras-GEF.
+At position 1461 to 1712, the domain is characterized as Ras-GEF.
+At position 23 to 102, the domain is characterized as ACT.
+At position 1 to 142, the domain is characterized as TIR.
+At position 397 to 507, the domain is characterized as Toprim.
+At position 9 to 260, the domain is characterized as Deacetylase sirtuin-type.
+At position 239 to 274, the domain is characterized as EF-hand 2.
+At position 355 to 512, the domain is characterized as Ferric oxidoreductase.
+At position 552 to 686, the domain is characterized as FAD-binding FR-type.
+At position 229 to 264, the domain is characterized as EF-hand.
+At position 116 to 324, the domain is characterized as TLC.
+At position 88 to 262, the domain is characterized as Helicase ATP-binding.
+At position 288 to 443, the domain is characterized as Helicase C-terminal.
+At position 542 to 713, the domain is characterized as N-acetyltransferase.
+At position 399 to 472, the domain is characterized as B5.
+At position 47 to 229, the domain is characterized as FAD-binding PCMH-type.
+At position 131 to 203, the domain is characterized as Bromo.
+At position 298 to 379, the domain is characterized as NET.
+At position 116 to 231, the domain is characterized as C2 2.
+At position 300 to 510, the domain is characterized as Ras-GAP.
+At position 38 to 153, the domain is characterized as BAH.
+At position 195 to 406, the domain is characterized as Helicase ATP-binding.
+At position 453 to 625, the domain is characterized as Helicase C-terminal.
+At position 347 to 517, the domain is characterized as tr-type G.
+At position 44 to 156, the domain is characterized as Expansin-like EG45.
+At position 55 to 335, the domain is characterized as Deacetylase sirtuin-type.
+At position 422 to 488, the domain is characterized as DDT.
+At position 1445 to 1515, the domain is characterized as Bromo.
+At position 82 to 214, the domain is characterized as Plastocyanin-like 1.
+At position 423 to 530, the domain is characterized as Plastocyanin-like 2.
+At position 382 to 415, the domain is characterized as KOW 1.
+At position 533 to 560, the domain is characterized as KOW 2.
+At position 584 to 615, the domain is characterized as KOW 3.
+At position 799 to 832, the domain is characterized as KOW 4.
+At position 422 to 647, the domain is characterized as ABC transporter 1.
+At position 880 to 1163, the domain is characterized as ABC transmembrane type-1 2.
+At position 16 to 57, the domain is characterized as JmjN.
+At position 262 to 428, the domain is characterized as JmjC.
+At position 49 to 141, the domain is characterized as PPIase FKBP-type.
+At position 185 to 218, the domain is characterized as EF-hand 2.
+At position 15 to 196, the domain is characterized as RNase H type-2.
+At position 320 to 589, the domain is characterized as Radical SAM core.
+At position 137 to 239, the domain is characterized as C-type lectin.
+At position 142 to 482, the domain is characterized as SAC.
+At position 60 to 239, the domain is characterized as uDENN.
+At position 265 to 390, the domain is characterized as cDENN.
+At position 392 to 525, the domain is characterized as dDENN.
+At position 171 to 269, the domain is characterized as ELM2.
+At position 274 to 326, the domain is characterized as SANT.
+At position 164 to 294, the domain is characterized as Galectin.
+At position 824 to 1101, the domain is characterized as Protein kinase.
+At position 941 to 1215, the domain is characterized as PKS/mFAS DH.
+At position 2010 to 2085, the domain is characterized as Carrier.
+At position 518 to 694, the domain is characterized as FH1.
+At position 595 to 1042, the domain is characterized as FH2.
+At position 174 to 231, the domain is characterized as BSD 1.
+At position 255 to 307, the domain is characterized as BSD 2.
+At position 22 to 307, the domain is characterized as Septin-type G.
+At position 132 to 166, the domain is characterized as EF-hand 4.
+At position 36 to 163, the domain is characterized as C-type lectin.
+At position 16 to 211, the domain is characterized as Lon N-terminal.
+At position 207 to 269, the domain is characterized as HAMP.
+At position 284 to 502, the domain is characterized as Histidine kinase.
+At position 237 to 391, the domain is characterized as TrmE-type G.
+At position 132 to 202, the domain is characterized as PAS 1.
+At position 206 to 257, the domain is characterized as PAC 1.
+At position 332 to 383, the domain is characterized as PAC 2.
+At position 384 to 456, the domain is characterized as PAS 2.
+At position 460 to 512, the domain is characterized as PAC 3.
+At position 594 to 646, the domain is characterized as PAC 4.
+At position 669 to 885, the domain is characterized as Histidine kinase.
+At position 54 to 245, the domain is characterized as PNPLA.
+At position 312 to 352, the domain is characterized as EGF-like 1.
+At position 353 to 393, the domain is characterized as EGF-like 2; calcium-binding.
+At position 394 to 434, the domain is characterized as EGF-like 3.
+At position 432 to 474, the domain is characterized as EGF-like 4.
+At position 738 to 778, the domain is characterized as EGF-like 5.
+At position 830 to 868, the domain is characterized as EGF-like 6.
+At position 869 to 910, the domain is characterized as EGF-like 7; calcium-binding.
+At position 911 to 951, the domain is characterized as EGF-like 8; calcium-binding.
+At position 970 to 1011, the domain is characterized as EGF-like 9.
+At position 682 to 935, the domain is characterized as MOSC.
+At position 40 to 141, the domain is characterized as Collagen-like.
+At position 145 to 281, the domain is characterized as C1q.
+At position 127 to 220, the domain is characterized as PDZ 1.
+At position 222 to 309, the domain is characterized as PDZ 2.
+At position 19 to 119, the domain is characterized as Glutaredoxin.
+At position 688 to 766, the domain is characterized as RRM 1.
+At position 785 to 862, the domain is characterized as RRM 2.
+At position 288 to 377, the domain is characterized as Rhodanese.
+At position 159 to 198, the domain is characterized as UBA.
+At position 505 to 647, the domain is characterized as Response regulatory.
+At position 58 to 108, the domain is characterized as EGF-like 2; calcium-binding.
+At position 367 to 418, the domain is characterized as GPS.
+At position 152 to 224, the domain is characterized as HTH crp-type.
+At position 143 to 218, the domain is characterized as Ubiquitin-like.
+At position 74 to 309, the domain is characterized as Radical SAM core.
+At position 106 to 442, the domain is characterized as USP.
+At position 503 to 595, the domain is characterized as DUSP 1.
+At position 610 to 711, the domain is characterized as DUSP 2.
+At position 738 to 861, the domain is characterized as DUSP 3.
+At position 948 to 1031, the domain is characterized as Ubiquitin-like.
+At position 120 to 262, the domain is characterized as B12-binding.
+At position 176 to 524, the domain is characterized as Reverse transcriptase.
+At position 25 to 224, the domain is characterized as Glutamine amidotransferase type-1.
+At position 10 to 77, the domain is characterized as HTH gntR-type.
+At position 420 to 561, the domain is characterized as MAM.
+At position 67 to 105, the domain is characterized as LDL-receptor class A 2.
+At position 147 to 185, the domain is characterized as LDL-receptor class A 4.
+At position 198 to 234, the domain is characterized as LDL-receptor class A 5.
+At position 237 to 273, the domain is characterized as LDL-receptor class A 6.
+At position 277 to 316, the domain is characterized as LDL-receptor class A 7.
+At position 316 to 355, the domain is characterized as EGF-like 1.
+At position 356 to 388, the domain is characterized as EGF-like 2; calcium-binding.
+At position 54 to 182, the domain is characterized as Runt.
+At position 533 to 793, the domain is characterized as PUL.
+At position 201 to 214, the domain is characterized as ShKT.
+At position 473 to 565, the domain is characterized as BLUF 2.
+At position 620 to 748, the domain is characterized as Guanylate cyclase.
+At position 331 to 500, the domain is characterized as tr-type G.
+At position 430 to 627, the domain is characterized as MCM.
+At position 102 to 261, the domain is characterized as N-acetyltransferase.
+At position 121 to 156, the domain is characterized as Tify.
+At position 182 to 224, the domain is characterized as CCT.
+At position 22 to 109, the domain is characterized as Ig-like 1.
+At position 110 to 227, the domain is characterized as Ig-like 2.
+At position 258 to 357, the domain is characterized as Ig-like 3.
+At position 80 to 176, the domain is characterized as Fibronectin type-III.
+At position 614 to 678, the domain is characterized as SAM 1.
+At position 684 to 750, the domain is characterized as SAM 2.
+At position 760 to 857, the domain is characterized as TIR.
+At position 316 to 357, the domain is characterized as EGF-like 1.
+At position 358 to 398, the domain is characterized as EGF-like 2; calcium-binding.
+At position 399 to 439, the domain is characterized as EGF-like 3.
+At position 437 to 479, the domain is characterized as EGF-like 4.
+At position 834 to 872, the domain is characterized as EGF-like 6.
+At position 873 to 914, the domain is characterized as EGF-like 7; calcium-binding.
+At position 915 to 955, the domain is characterized as EGF-like 8; calcium-binding.
+At position 974 to 1015, the domain is characterized as EGF-like 9.
+At position 26 to 145, the domain is characterized as Thioredoxin 1.
+At position 150 to 272, the domain is characterized as Thioredoxin 2.
+At position 293 to 412, the domain is characterized as Thioredoxin 3.
+At position 77 to 153, the domain is characterized as Lipoyl-binding.
+At position 221 to 258, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 7 to 147, the domain is characterized as PTS EIIA type-2.
+At position 161 to 253, the domain is characterized as HPr.
+At position 1 to 119, the domain is characterized as GS catalytic.
+At position 1 to 80, the domain is characterized as Pyruvate carboxyltransferase.
+At position 81 to 176, the domain is characterized as Core-binding (CB).
+At position 197 to 404, the domain is characterized as Tyr recombinase.
+At position 335 to 384, the domain is characterized as bHLH.
+At position 424 to 600, the domain is characterized as N-acetyltransferase.
+At position 13 to 65, the domain is characterized as HTH myb-type 1.
+At position 66 to 120, the domain is characterized as HTH myb-type 2.
+At position 219 to 338, the domain is characterized as PAZ.
+At position 509 to 820, the domain is characterized as Piwi.
+At position 121 to 185, the domain is characterized as PAC.
+At position 189 to 407, the domain is characterized as Histidine kinase.
+At position 69 to 368, the domain is characterized as FAE.
+At position 25 to 326, the domain is characterized as Protein kinase.
+At position 126 to 197, the domain is characterized as PDZ.
+At position 161 to 282, the domain is characterized as MI 1.
+At position 324 to 447, the domain is characterized as MI 2.
+At position 54 to 171, the domain is characterized as DOMON.
+At position 183 to 379, the domain is characterized as Cytochrome b561.
+At position 324 to 602, the domain is characterized as Protein kinase.
+At position 12 to 175, the domain is characterized as TIR.
+At position 230 to 402, the domain is characterized as Helicase ATP-binding.
+At position 35 to 128, the domain is characterized as Ig-like C2-type 1.
+At position 919 to 1014, the domain is characterized as Fibronectin type-III 4.
+At position 1016 to 1116, the domain is characterized as Fibronectin type-III 5.
+At position 116 to 221, the domain is characterized as Ig-like C2-type 2.
+At position 222 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 313 to 409, the domain is characterized as Ig-like C2-type 4.
+At position 121 to 254, the domain is characterized as Ferric oxidoreductase.
+At position 255 to 410, the domain is characterized as FAD-binding FR-type.
+At position 48 to 101, the domain is characterized as Tudor-knot.
+At position 429 to 625, the domain is characterized as B30.2/SPRY.
+At position 231 to 296, the domain is characterized as J.
+At position 95 to 300, the domain is characterized as Bin3-type SAM.
+At position 27 to 140, the domain is characterized as SET.
+At position 251 to 452, the domain is characterized as GATase cobBQ-type.
+At position 28 to 64, the domain is characterized as LDL-receptor class A 1.
+At position 108 to 146, the domain is characterized as LDL-receptor class A 3.
+At position 148 to 184, the domain is characterized as LDL-receptor class A 4.
+At position 187 to 225, the domain is characterized as LDL-receptor class A 5.
+At position 272 to 308, the domain is characterized as LDL-receptor class A 6.
+At position 312 to 351, the domain is characterized as LDL-receptor class A 7.
+At position 346 to 390, the domain is characterized as EGF-like 1.
+At position 391 to 430, the domain is characterized as EGF-like 2; calcium-binding.
+At position 113 to 153, the domain is characterized as CHCH.
+At position 7 to 275, the domain is characterized as YjeF C-terminal.
+At position 178 to 450, the domain is characterized as ABC transporter 1.
+At position 528 to 741, the domain is characterized as ABC transmembrane type-2 1.
+At position 871 to 1123, the domain is characterized as ABC transporter 2.
+At position 1196 to 1410, the domain is characterized as ABC transmembrane type-2 2.
+At position 423 to 751, the domain is characterized as PDEase.
+At position 7 to 105, the domain is characterized as PINc.
+At position 51 to 130, the domain is characterized as TBDR plug.
+At position 283 to 326, the domain is characterized as AWS.
+At position 326 to 443, the domain is characterized as SET.
+At position 449 to 465, the domain is characterized as Post-SET.
+At position 239 to 301, the domain is characterized as t-SNARE coiled-coil homology.
+At position 20 to 176, the domain is characterized as ABC transporter.
+At position 35 to 104, the domain is characterized as DRBM 1.
+At position 120 to 187, the domain is characterized as DRBM 2.
+At position 648 to 879, the domain is characterized as FAD-binding FR-type.
+At position 24 to 291, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 77 to 200, the domain is characterized as GST C-terminal.
+At position 27 to 133, the domain is characterized as Rieske.
+At position 335 to 394, the domain is characterized as CBS 1.
+At position 398 to 453, the domain is characterized as CBS 2.
+At position 2 to 60, the domain is characterized as LCN-type CS-alpha/beta.
+At position 24 to 105, the domain is characterized as IGFBP N-terminal.
+At position 177 to 259, the domain is characterized as Thyroglobulin type-1.
+At position 459 to 494, the domain is characterized as EF-hand 2.
+At position 70 to 781, the domain is characterized as Myosin motor.
+At position 784 to 806, the domain is characterized as IQ 1.
+At position 807 to 831, the domain is characterized as IQ 2.
+At position 832 to 855, the domain is characterized as IQ 3.
+At position 856 to 879, the domain is characterized as IQ 4.
+At position 880 to 902, the domain is characterized as IQ 5.
+At position 903 to 932, the domain is characterized as IQ 6.
+At position 1226 to 1501, the domain is characterized as Dilute.
+At position 61 to 96, the domain is characterized as EF-hand 1.
+At position 547 to 824, the domain is characterized as Protein kinase.
+At position 1 to 309, the domain is characterized as Protein kinase.
+At position 75 to 243, the domain is characterized as Helicase ATP-binding.
+At position 271 to 441, the domain is characterized as Helicase C-terminal.
+At position 89 to 510, the domain is characterized as Peptidase A1.
+At position 26 to 124, the domain is characterized as Ig-like V-type.
+At position 125 to 211, the domain is characterized as Ig-like C2-type 1.
+At position 212 to 321, the domain is characterized as Ig-like C2-type 2.
+At position 322 to 378, the domain is characterized as Ig-like C2-type 3.
+At position 56 to 129, the domain is characterized as J.
+At position 323 to 377, the domain is characterized as SANT 1.
+At position 490 to 545, the domain is characterized as SANT 2.
+At position 39 to 188, the domain is characterized as PADR1 zinc-binding.
+At position 71 to 105, the domain is characterized as SAP.
+At position 189 to 261, the domain is characterized as BRCT.
+At position 309 to 409, the domain is characterized as WGR.
+At position 436 to 555, the domain is characterized as PARP alpha-helical.
+At position 564 to 795, the domain is characterized as PARP catalytic.
+At position 20 to 110, the domain is characterized as Ig-like.
+At position 236 to 375, the domain is characterized as PADR1 zinc-binding.
+At position 394 to 484, the domain is characterized as BRCT.
+At position 511 to 611, the domain is characterized as WGR.
+At position 633 to 751, the domain is characterized as PARP alpha-helical.
+At position 758 to 983, the domain is characterized as PARP catalytic.
+At position 911 to 1250, the domain is characterized as TTL.
+At position 1320 to 1349, the domain is characterized as IQ 1.
+At position 1348 to 1377, the domain is characterized as IQ 2.
+At position 236 to 311, the domain is characterized as MIT.
+At position 1 to 238, the domain is characterized as GP-PDE.
+At position 34 to 333, the domain is characterized as Calpain catalytic.
+At position 538 to 573, the domain is characterized as EF-hand 1.
+At position 636 to 669, the domain is characterized as EF-hand 2.
+At position 13 to 298, the domain is characterized as Protein kinase.
+At position 289 to 361, the domain is characterized as RRM 1.
+At position 363 to 444, the domain is characterized as RRM 2.
+At position 22 to 150, the domain is characterized as RNase III.
+At position 45 to 162, the domain is characterized as TBDR plug.
+At position 167 to 652, the domain is characterized as TBDR beta-barrel.
+At position 512 to 619, the domain is characterized as Toprim.
+At position 84 to 255, the domain is characterized as Helicase ATP-binding.
+At position 283 to 427, the domain is characterized as Helicase C-terminal.
+At position 18 to 57, the domain is characterized as S1-like.
+At position 42 to 179, the domain is characterized as Thioredoxin.
+At position 1 to 186, the domain is characterized as Glutamine amidotransferase type-1.
+At position 34 to 138, the domain is characterized as Gnk2-homologous 1.
+At position 143 to 242, the domain is characterized as Gnk2-homologous 2.
+At position 20 to 149, the domain is characterized as Thioredoxin.
+At position 151 to 352, the domain is characterized as CHASE.
+At position 445 to 715, the domain is characterized as Histidine kinase.
+At position 732 to 854, the domain is characterized as Response regulatory 1.
+At position 880 to 1016, the domain is characterized as Response regulatory 2.
+At position 16 to 51, the domain is characterized as QLQ.
+At position 81 to 125, the domain is characterized as WRC.
+At position 1 to 205, the domain is characterized as AIG1-type G.
+At position 342 to 525, the domain is characterized as Helicase C-terminal.
+At position 107 to 224, the domain is characterized as PX.
+At position 605 to 1075, the domain is characterized as FH2.
+At position 1025 to 1075, the domain is characterized as DAD.
+At position 26 to 506, the domain is characterized as PPM-type phosphatase.
+At position 399 to 835, the domain is characterized as Urease.
+At position 80 to 186, the domain is characterized as C-type lectin.
+At position 4 to 140, the domain is characterized as DegV.
+At position 25 to 63, the domain is characterized as Collagen-like.
+At position 67 to 196, the domain is characterized as C1q.
+At position 348 to 415, the domain is characterized as S4 RNA-binding.
+At position 29 to 150, the domain is characterized as OTU.
+At position 336 to 396, the domain is characterized as Tudor.
+At position 63 to 286, the domain is characterized as Fibrinogen C-terminal.
+At position 66 to 129, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 13 to 128, the domain is characterized as HotDog ACOT-type.
+At position 338 to 572, the domain is characterized as ABC transporter.
+At position 22 to 205, the domain is characterized as RNase H type-2.
+At position 84 to 216, the domain is characterized as GGDEF.
+At position 333 to 608, the domain is characterized as MYST-type HAT.
+At position 158 to 207, the domain is characterized as KH.
+At position 223 to 303, the domain is characterized as bHLH.
+At position 112 to 209, the domain is characterized as HTH araC/xylS-type.
+At position 758 to 834, the domain is characterized as RRM 4.
+At position 202 to 276, the domain is characterized as POU-specific.
+At position 31 to 198, the domain is characterized as FAD-binding PCMH-type.
+At position 19 to 126, the domain is characterized as sHSP.
+At position 46 to 281, the domain is characterized as ABC transporter.
+At position 183 to 385, the domain is characterized as Histidine kinase.
+At position 25 to 75, the domain is characterized as WAP.
+At position 56 to 218, the domain is characterized as BUB1 N-terminal.
+At position 23 to 146, the domain is characterized as Bulb-type lectin.
+At position 286 to 322, the domain is characterized as EGF-like.
+At position 341 to 422, the domain is characterized as PAN.
+At position 493 to 770, the domain is characterized as Protein kinase.
+At position 232 to 338, the domain is characterized as CUB.
+At position 38 to 338, the domain is characterized as Protein kinase.
+At position 8 to 245, the domain is characterized as tr-type G.
+At position 60 to 207, the domain is characterized as N-acetyltransferase.
+At position 198 to 369, the domain is characterized as EngA-type G 2.
+At position 172 to 214, the domain is characterized as LDL-receptor class A.
+At position 184 to 358, the domain is characterized as tr-type G.
+At position 29 to 63, the domain is characterized as Anaphylatoxin-like 1.
+At position 68 to 107, the domain is characterized as Anaphylatoxin-like 2.
+At position 108 to 139, the domain is characterized as Anaphylatoxin-like 3.
+At position 158 to 192, the domain is characterized as EGF-like 1.
+At position 193 to 238, the domain is characterized as EGF-like 2; calcium-binding.
+At position 239 to 284, the domain is characterized as EGF-like 3; calcium-binding.
+At position 285 to 331, the domain is characterized as EGF-like 4; calcium-binding.
+At position 332 to 373, the domain is characterized as EGF-like 5; calcium-binding.
+At position 374 to 415, the domain is characterized as EGF-like 6; calcium-binding.
+At position 416 to 455, the domain is characterized as EGF-like 7; calcium-binding.
+At position 456 to 499, the domain is characterized as EGF-like 8; calcium-binding.
+At position 500 to 554, the domain is characterized as EGF-like 9; calcium-binding.
+At position 43 to 169, the domain is characterized as Calponin-homology (CH).
+At position 38 to 181, the domain is characterized as SIS.
+At position 207 to 265, the domain is characterized as CBS 1.
+At position 274 to 326, the domain is characterized as CBS 2.
+At position 377 to 438, the domain is characterized as PWWP.
+At position 225 to 375, the domain is characterized as Ferric oxidoreductase.
+At position 404 to 528, the domain is characterized as FAD-binding FR-type.
+At position 24 to 203, the domain is characterized as Reticulon.
+At position 44 to 281, the domain is characterized as PABS.
+At position 233 to 289, the domain is characterized as WHEP-TRS.
+At position 1 to 145, the domain is characterized as CBM3.
+At position 158 to 209, the domain is characterized as HTH bat-type.
+At position 110 to 271, the domain is characterized as Cupin type-1 1.
+At position 312 to 478, the domain is characterized as Cupin type-1 2.
+At position 252 to 493, the domain is characterized as NR LBD.
+At position 238 to 418, the domain is characterized as PBS-linker 1.
+At position 488 to 669, the domain is characterized as PBS-linker 2.
+At position 684 to 861, the domain is characterized as PBS-linker 3.
+At position 185 to 236, the domain is characterized as F-box.
+At position 609 to 869, the domain is characterized as MHD.
+At position 270 to 436, the domain is characterized as Helicase ATP-binding.
+At position 540 to 746, the domain is characterized as Helicase C-terminal.
+At position 8 to 106, the domain is characterized as Acylphosphatase-like.
+At position 65 to 163, the domain is characterized as SH2 1.
+At position 358 to 455, the domain is characterized as SH2 2.
+At position 73 to 261, the domain is characterized as BPL/LPL catalytic.
+At position 66 to 142, the domain is characterized as Cadherin 1.
+At position 143 to 257, the domain is characterized as Cadherin 2.
+At position 142 to 231, the domain is characterized as EH 2.
+At position 52 to 187, the domain is characterized as HD.
+At position 1 to 81, the domain is characterized as Saposin B-type.
+At position 124 to 305, the domain is characterized as Helicase ATP-binding.
+At position 641 to 731, the domain is characterized as Dicer dsRNA-binding fold.
+At position 881 to 1009, the domain is characterized as PAZ.
+At position 1032 to 1192, the domain is characterized as RNase III 1.
+At position 1243 to 1394, the domain is characterized as RNase III 2.
+At position 1428 to 1496, the domain is characterized as DRBM.
+At position 119 to 355, the domain is characterized as Radical SAM core.
+At position 53 to 150, the domain is characterized as Cytochrome b5 heme-binding.
+At position 36 to 212, the domain is characterized as EngB-type G.
+At position 149 to 201, the domain is characterized as TSP type-1.
+At position 309 to 395, the domain is characterized as Ig-like C2-type.
+At position 595 to 872, the domain is characterized as Protein kinase.
+At position 122 to 376, the domain is characterized as PPM-type phosphatase.
+At position 119 to 300, the domain is characterized as Helicase ATP-binding.
+At position 332 to 501, the domain is characterized as Helicase C-terminal.
+At position 162 to 390, the domain is characterized as START.
+At position 291 to 342, the domain is characterized as Chromo 1.
+At position 374 to 438, the domain is characterized as Chromo 2.
+At position 472 to 646, the domain is characterized as Helicase ATP-binding.
+At position 786 to 955, the domain is characterized as Helicase C-terminal.
+At position 1435 to 1489, the domain is characterized as Myb-like.
+At position 169 to 351, the domain is characterized as Helicase ATP-binding.
+At position 361 to 525, the domain is characterized as Helicase C-terminal.
+At position 351 to 461, the domain is characterized as PLAT.
+At position 100 to 210, the domain is characterized as sHSP.
+At position 12 to 179, the domain is characterized as N-acetyltransferase.
+At position 50 to 190, the domain is characterized as Nudix hydrolase.
+At position 411 to 524, the domain is characterized as Toprim.
+At position 3 to 255, the domain is characterized as OBG-type G.
+At position 277 to 360, the domain is characterized as TGS.
+At position 1 to 87, the domain is characterized as BMV.
+At position 526 to 747, the domain is characterized as B30.2/SPRY.
+At position 108 to 430, the domain is characterized as USP.
+At position 314 to 558, the domain is characterized as START.
+At position 19 to 471, the domain is characterized as Biotin carboxylation.
+At position 141 to 338, the domain is characterized as ATP-grasp.
+At position 558 to 825, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1095 to 1170, the domain is characterized as Biotinyl-binding.
+At position 152 to 215, the domain is characterized as bZIP.
+At position 1 to 251, the domain is characterized as Deacetylase sirtuin-type.
+At position 20 to 85, the domain is characterized as Chitin-binding type R&R.
+At position 22 to 212, the domain is characterized as EngB-type G.
+At position 173 to 335, the domain is characterized as SUN.
+At position 238 to 387, the domain is characterized as Helicase C-terminal.
+At position 489 to 511, the domain is characterized as GoLoco 1.
+At position 544 to 566, the domain is characterized as GoLoco 2.
+At position 781 to 873, the domain is characterized as Smr.
+At position 46 to 98, the domain is characterized as PISA.
+At position 631 to 709, the domain is characterized as TFIIS N-terminal.
+At position 332 to 368, the domain is characterized as CBM1.
+At position 101 to 183, the domain is characterized as RRM.
+At position 274 to 457, the domain is characterized as VWFA.
+At position 128 to 300, the domain is characterized as Helicase ATP-binding.
+At position 369 to 529, the domain is characterized as Helicase C-terminal.
+At position 25 to 103, the domain is characterized as EMI.
+At position 102 to 132, the domain is characterized as EGF-like 1.
+At position 225 to 260, the domain is characterized as EGF-like 2.
+At position 268 to 303, the domain is characterized as EGF-like 3.
+At position 311 to 346, the domain is characterized as EGF-like 4.
+At position 400 to 435, the domain is characterized as EGF-like 5.
+At position 486 to 521, the domain is characterized as EGF-like 6.
+At position 577 to 607, the domain is characterized as EGF-like 7.
+At position 615 to 649, the domain is characterized as EGF-like 8.
+At position 657 to 692, the domain is characterized as EGF-like 9.
+At position 203 to 497, the domain is characterized as Protein kinase.
+At position 315 to 564, the domain is characterized as ABC transporter 2.
+At position 160 to 215, the domain is characterized as PQ-loop 2.
+At position 538 to 616, the domain is characterized as Carrier.
+At position 675 to 734, the domain is characterized as S1 motif.
+At position 239 to 307, the domain is characterized as BTB.
+At position 533 to 605, the domain is characterized as Bromo.
+At position 727 to 806, the domain is characterized as NET.
+At position 155 to 193, the domain is characterized as KASH.
+At position 18 to 280, the domain is characterized as Pyruvate carboxyltransferase.
+At position 525 to 797, the domain is characterized as Protein kinase.
+At position 214 to 466, the domain is characterized as NR LBD.
+At position 6 to 130, the domain is characterized as Peptidase C39.
+At position 158 to 434, the domain is characterized as ABC transmembrane type-1.
+At position 464 to 689, the domain is characterized as ABC transporter.
+At position 1 to 151, the domain is characterized as HTH marR-type.
+At position 629 to 719, the domain is characterized as BRCT.
+At position 47 to 162, the domain is characterized as DOMON.
+At position 176 to 371, the domain is characterized as Cytochrome b561.
+At position 198 to 225, the domain is characterized as PLD phosphodiesterase 1.
+At position 413 to 439, the domain is characterized as PLD phosphodiesterase 2.
+At position 8 to 265, the domain is characterized as Protein kinase.
+At position 234 to 300, the domain is characterized as PAS.
+At position 357 to 575, the domain is characterized as Histidine kinase.
+At position 18 to 301, the domain is characterized as Protein kinase.
+At position 415 to 466, the domain is characterized as SANT.
+At position 301 to 382, the domain is characterized as PDZ.
+At position 705 to 798, the domain is characterized as FDX-ACB.
+At position 336 to 765, the domain is characterized as Single-minded C-terminal.
+At position 35 to 230, the domain is characterized as YjeF N-terminal.
+At position 232 to 490, the domain is characterized as YjeF C-terminal.
+At position 57 to 359, the domain is characterized as ABC transmembrane type-1 1.
+At position 394 to 630, the domain is characterized as ABC transporter 1.
+At position 711 to 999, the domain is characterized as ABC transmembrane type-1 2.
+At position 1034 to 1279, the domain is characterized as ABC transporter 2.
+At position 175 to 211, the domain is characterized as UBA.
+At position 84 to 221, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 104 to 205, the domain is characterized as SRCR.
+At position 217 to 448, the domain is characterized as Peptidase S1.
+At position 32 to 105, the domain is characterized as S4 RNA-binding.
+At position 99 to 633, the domain is characterized as Protein kinase.
+At position 538 to 807, the domain is characterized as Protein kinase.
+At position 1 to 76, the domain is characterized as S1-like.
+At position 21 to 55, the domain is characterized as WW.
+At position 211 to 385, the domain is characterized as Helicase ATP-binding.
+At position 414 to 558, the domain is characterized as Helicase C-terminal.
+At position 195 to 360, the domain is characterized as Helicase ATP-binding.
+At position 490 to 653, the domain is characterized as Helicase C-terminal.
+At position 855 to 907, the domain is characterized as SANT 1.
+At position 958 to 1022, the domain is characterized as SANT 2.
+At position 319 to 348, the domain is characterized as IQ.
+At position 73 to 108, the domain is characterized as Tify.
+At position 219 to 420, the domain is characterized as Pentraxin (PTX).
+At position 1 to 58, the domain is characterized as ClpX-type ZB.
+At position 159 to 341, the domain is characterized as VWFA.
+At position 1 to 339, the domain is characterized as SPX.
+At position 596 to 798, the domain is characterized as EXS.
+At position 24 to 132, the domain is characterized as Ig-like V-type 1.
+At position 139 to 245, the domain is characterized as Ig-like V-type 2.
+At position 251 to 356, the domain is characterized as Ig-like C2-type.
+At position 31 to 165, the domain is characterized as MPN.
+At position 692 to 882, the domain is characterized as SEC7.
+At position 378 to 583, the domain is characterized as Helicase ATP-binding.
+At position 1363 to 1531, the domain is characterized as Helicase C-terminal.
+At position 536 to 586, the domain is characterized as DHHC.
+At position 157 to 380, the domain is characterized as Histidine kinase.
+At position 8 to 127, the domain is characterized as ERCC4.
+At position 98 to 474, the domain is characterized as GT44.
+At position 574 to 787, the domain is characterized as Peptidase C80.
+At position 68 to 135, the domain is characterized as S1 motif.
+At position 192 to 361, the domain is characterized as tr-type G.
+At position 17 to 109, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 122 to 190, the domain is characterized as H15.
+At position 59 to 155, the domain is characterized as Plastocyanin-like.
+At position 144 to 347, the domain is characterized as ATP-grasp.
+At position 25 to 140, the domain is characterized as Thioredoxin 1.
+At position 336 to 480, the domain is characterized as Thioredoxin 2.
+At position 143 to 275, the domain is characterized as RUN.
+At position 37 to 484, the domain is characterized as Biotin carboxylation.
+At position 156 to 354, the domain is characterized as ATP-grasp.
+At position 657 to 733, the domain is characterized as Biotinyl-binding.
+At position 156 to 511, the domain is characterized as Protein kinase.
+At position 53 to 105, the domain is characterized as PISA.
+At position 579 to 631, the domain is characterized as LRRCT.
+At position 691 to 836, the domain is characterized as TIR.
+At position 128 to 253, the domain is characterized as NEAT 1.
+At position 325 to 442, the domain is characterized as NEAT 2.
+At position 1 to 83, the domain is characterized as Phosphagen kinase N-terminal.
+At position 111 to 347, the domain is characterized as Phosphagen kinase C-terminal.
+At position 10 to 214, the domain is characterized as YjeF N-terminal.
+At position 17 to 140, the domain is characterized as EamA 1.
+At position 27 to 143, the domain is characterized as Ig-like V-type.
+At position 446 to 537, the domain is characterized as Cache.
+At position 22 to 76, the domain is characterized as F-box.
+At position 547 to 716, the domain is characterized as N-acetyltransferase.
+At position 630 to 699, the domain is characterized as S1 motif.
+At position 464 to 600, the domain is characterized as Ricin B-type lectin.
+At position 754 to 816, the domain is characterized as SH3.
+At position 137 to 419, the domain is characterized as ABC transporter 1.
+At position 376 to 435, the domain is characterized as LIM zinc-binding 1.
+At position 436 to 495, the domain is characterized as LIM zinc-binding 2.
+At position 496 to 562, the domain is characterized as LIM zinc-binding 3.
+At position 472 to 535, the domain is characterized as bZIP.
+At position 33 to 131, the domain is characterized as Pyrin.
+At position 204 to 527, the domain is characterized as NACHT.
+At position 61 to 219, the domain is characterized as Thioredoxin.
+At position 196 to 383, the domain is characterized as Glutamine amidotransferase type-1.
+At position 184 to 256, the domain is characterized as ACT-like 1.
+At position 278 to 349, the domain is characterized as ACT-like 2.
+At position 314 to 361, the domain is characterized as F-box.
+At position 312 to 548, the domain is characterized as NR LBD.
+At position 329 to 580, the domain is characterized as Clu.
+At position 7 to 240, the domain is characterized as PABS.
+At position 32 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 1006 to 1081, the domain is characterized as Carrier.
+At position 1326 to 1402, the domain is characterized as DEP.
+At position 1 to 215, the domain is characterized as ThyX.
+At position 403 to 529, the domain is characterized as Thioredoxin.
+At position 61 to 215, the domain is characterized as CP-type G.
+At position 53 to 190, the domain is characterized as MPN.
+At position 870 to 961, the domain is characterized as FDX-ACB.
+At position 308 to 568, the domain is characterized as ABC transporter 1.
+At position 588 to 916, the domain is characterized as ABC transporter 2.
+At position 72 to 327, the domain is characterized as PPM-type phosphatase.
+At position 40 to 250, the domain is characterized as tr-type G.
+At position 288 to 366, the domain is characterized as PUA.
+At position 26 to 153, the domain is characterized as Bulb-type lectin.
+At position 295 to 332, the domain is characterized as EGF-like; atypical.
+At position 346 to 427, the domain is characterized as PAN.
+At position 529 to 814, the domain is characterized as Protein kinase.
+At position 318 to 389, the domain is characterized as PAS.
+At position 607 to 830, the domain is characterized as Histidine kinase.
+At position 1550 to 1641, the domain is characterized as Olduvai.
+At position 633 to 732, the domain is characterized as CXC.
+At position 11 to 70, the domain is characterized as HTH tetR-type.
+At position 1354 to 1419, the domain is characterized as NAC-A/B.
+At position 77 to 381, the domain is characterized as ABC transmembrane type-1 1.
+At position 416 to 652, the domain is characterized as ABC transporter 1.
+At position 754 to 1043, the domain is characterized as ABC transmembrane type-1 2.
+At position 1077 to 1315, the domain is characterized as ABC transporter 2.
+At position 7 to 257, the domain is characterized as ABC transporter.
+At position 10 to 42, the domain is characterized as EF-hand 1.
+At position 43 to 72, the domain is characterized as EF-hand 2.
+At position 73 to 107, the domain is characterized as EF-hand 3.
+At position 108 to 141, the domain is characterized as EF-hand 4.
+At position 101 to 367, the domain is characterized as Protein kinase.
+At position 816 to 995, the domain is characterized as MOSC.
+At position 3 to 113, the domain is characterized as PH.
+At position 1 to 72, the domain is characterized as U-box.
+At position 274 to 359, the domain is characterized as PDZ 1.
+At position 381 to 464, the domain is characterized as PDZ 2.
+At position 507 to 593, the domain is characterized as PDZ 3.
+At position 638 to 724, the domain is characterized as PDZ 4.
+At position 65 to 206, the domain is characterized as Tyrosine-protein phosphatase.
+At position 11 to 246, the domain is characterized as ABC transporter.
+At position 717 to 794, the domain is characterized as BRCT.
+At position 1 to 284, the domain is characterized as Protein kinase.
+At position 218 to 414, the domain is characterized as CNNM transmembrane.
+At position 433 to 495, the domain is characterized as CBS 1.
+At position 502 to 568, the domain is characterized as CBS 2.
+At position 16 to 127, the domain is characterized as HIT.
+At position 147 to 206, the domain is characterized as HTH myb-type.
+At position 234 to 288, the domain is characterized as Myb-like.
+At position 61 to 148, the domain is characterized as UPAR/Ly6.
+At position 476 to 524, the domain is characterized as GYF.
+At position 359 to 587, the domain is characterized as TLDc.
+At position 14 to 341, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 353 to 680, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 661 to 892, the domain is characterized as NR LBD.
+At position 67 to 352, the domain is characterized as Protein kinase.
+At position 6 to 231, the domain is characterized as Radical SAM core.
+At position 307 to 344, the domain is characterized as Fibronectin type-I 6.
+At position 356 to 404, the domain is characterized as Fibronectin type-II 1.
+At position 416 to 464, the domain is characterized as Fibronectin type-II 2.
+At position 469 to 517, the domain is characterized as Fibronectin type-I 7.
+At position 517 to 559, the domain is characterized as Fibronectin type-I 8.
+At position 560 to 603, the domain is characterized as Fibronectin type-I 9.
+At position 611 to 706, the domain is characterized as Fibronectin type-III 1.
+At position 718 to 813, the domain is characterized as Fibronectin type-III 2.
+At position 814 to 903, the domain is characterized as Fibronectin type-III 3.
+At position 910 to 1001, the domain is characterized as Fibronectin type-III 4.
+At position 1002 to 1089, the domain is characterized as Fibronectin type-III 5.
+At position 1090 to 1176, the domain is characterized as Fibronectin type-III 6.
+At position 1177 to 1271, the domain is characterized as Fibronectin type-III 7.
+At position 1272 to 1360, the domain is characterized as Fibronectin type-III 8; extra domain B.
+At position 1361 to 1452, the domain is characterized as Fibronectin type-III 9.
+At position 1453 to 1541, the domain is characterized as Fibronectin type-III 10.
+At position 1542 to 1635, the domain is characterized as Fibronectin type-III 11.
+At position 1636 to 1727, the domain is characterized as Fibronectin type-III 12.
+At position 1728 to 1815, the domain is characterized as Fibronectin type-III 13; extra domain A.
+At position 1816 to 1909, the domain is characterized as Fibronectin type-III 14.
+At position 1910 to 1996, the domain is characterized as Fibronectin type-III 15.
+At position 1997 to 2087, the domain is characterized as Fibronectin type-III 16.
+At position 2195 to 2289, the domain is characterized as Fibronectin type-III 17.
+At position 2296 to 2340, the domain is characterized as Fibronectin type-I 10.
+At position 2341 to 2383, the domain is characterized as Fibronectin type-I 11.
+At position 2385 to 2428, the domain is characterized as Fibronectin type-I 12.
+At position 206 to 316, the domain is characterized as PX.
+At position 347 to 550, the domain is characterized as BAR.
+At position 271 to 346, the domain is characterized as B5.
+At position 89 to 205, the domain is characterized as GST C-terminal.
+At position 680 to 742, the domain is characterized as CBS 2.
+At position 406 to 613, the domain is characterized as Helicase C-terminal.
+At position 25 to 317, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 18 to 165, the domain is characterized as Reelin.
+At position 15 to 293, the domain is characterized as Protein kinase.
+At position 55 to 167, the domain is characterized as THUMP.
+At position 270 to 380, the domain is characterized as OmpA-like.
+At position 242 to 532, the domain is characterized as Protein kinase.
+At position 202 to 302, the domain is characterized as Fe2OG dioxygenase.
+At position 158 to 240, the domain is characterized as SCAN box.
+At position 280 to 370, the domain is characterized as KRAB 2.
+At position 435 to 606, the domain is characterized as Helicase ATP-binding.
+At position 837 to 996, the domain is characterized as Helicase C-terminal.
+At position 64 to 251, the domain is characterized as TR mART core.
+At position 489 to 864, the domain is characterized as USP.
+At position 909 to 1074, the domain is characterized as Exonuclease.
+At position 130 to 189, the domain is characterized as SANT.
+At position 563 to 614, the domain is characterized as GPS.
+At position 613 to 672, the domain is characterized as KH.
+At position 684 to 753, the domain is characterized as S1 motif.
+At position 23 to 129, the domain is characterized as Ig-like.
+At position 163 to 315, the domain is characterized as Plastocyanin-like 2.
+At position 417 to 553, the domain is characterized as Plastocyanin-like 3.
+At position 6 to 315, the domain is characterized as Protein kinase.
+At position 188 to 388, the domain is characterized as CheB-type methylesterase.
+At position 121 to 241, the domain is characterized as PX.
+At position 761 to 987, the domain is characterized as PPM-type phosphatase.
+At position 215 to 275, the domain is characterized as SH3.
+At position 49 to 96, the domain is characterized as SMB.
+At position 9 to 275, the domain is characterized as Protein kinase.
+At position 114 to 330, the domain is characterized as SMP-LTD.
+At position 1 to 306, the domain is characterized as Teneurin N-terminal.
+At position 508 to 539, the domain is characterized as EGF-like 1.
+At position 540 to 570, the domain is characterized as EGF-like 2.
+At position 572 to 604, the domain is characterized as EGF-like 3.
+At position 605 to 636, the domain is characterized as EGF-like 4.
+At position 638 to 671, the domain is characterized as EGF-like 5.
+At position 672 to 703, the domain is characterized as EGF-like 6.
+At position 704 to 733, the domain is characterized as EGF-like 7.
+At position 734 to 768, the domain is characterized as EGF-like 8.
+At position 440 to 526, the domain is characterized as PDZ.
+At position 577 to 700, the domain is characterized as C2 1.
+At position 1309 to 1427, the domain is characterized as C2 2.
+At position 114 to 291, the domain is characterized as SMP-LTD.
+At position 291 to 408, the domain is characterized as C2 1.
+At position 426 to 566, the domain is characterized as C2 2.
+At position 754 to 876, the domain is characterized as C2 3.
+At position 88 to 306, the domain is characterized as Radical SAM core.
+At position 67 to 177, the domain is characterized as MTTase N-terminal.
+At position 202 to 443, the domain is characterized as Radical SAM core.
+At position 446 to 519, the domain is characterized as TRAM.
+At position 651 to 905, the domain is characterized as Protein kinase.
+At position 170 to 397, the domain is characterized as Starter acyltransferase (SAT).
+At position 1544 to 1662, the domain is characterized as MaoC-like.
+At position 1682 to 2046, the domain is characterized as Malonyl-CoA:ACP transacylase (MAT).
+At position 49 to 374, the domain is characterized as Protein kinase.
+At position 785 to 872, the domain is characterized as LRRCT.
+At position 1510 to 1569, the domain is characterized as MucBP 1.
+At position 1575 to 1634, the domain is characterized as MucBP 2.
+At position 1644 to 1705, the domain is characterized as MucBP 3.
+At position 32 to 107, the domain is characterized as DEP.
+At position 219 to 282, the domain is characterized as G protein gamma.
+At position 53 to 749, the domain is characterized as Peptidase M13.
+At position 277 to 555, the domain is characterized as Protein kinase.
+At position 137 to 316, the domain is characterized as Helicase ATP-binding.
+At position 348 to 498, the domain is characterized as Helicase C-terminal.
+At position 221 to 422, the domain is characterized as Pentraxin (PTX).
+At position 163 to 469, the domain is characterized as USP.
+At position 38 to 326, the domain is characterized as GP-PDE.
+At position 60 to 363, the domain is characterized as PPM-type phosphatase.
+At position 1 to 63, the domain is characterized as BTB.
+At position 149 to 409, the domain is characterized as NPH3.
+At position 75 to 347, the domain is characterized as Protein kinase.
+At position 25 to 82, the domain is characterized as bHLH.
+At position 110 to 180, the domain is characterized as PAS.
+At position 215 to 481, the domain is characterized as NR LBD.
+At position 26 to 284, the domain is characterized as Protein kinase.
+At position 327 to 362, the domain is characterized as EF-hand 1.
+At position 399 to 434, the domain is characterized as EF-hand 3.
+At position 438 to 468, the domain is characterized as EF-hand 4.
+At position 440 to 502, the domain is characterized as EGF-like 1.
+At position 503 to 555, the domain is characterized as EGF-like 2.
+At position 556 to 592, the domain is characterized as EGF-like 3.
+At position 593 to 636, the domain is characterized as EGF-like 4.
+At position 162 to 433, the domain is characterized as MYST-type HAT.
+At position 402 to 657, the domain is characterized as Protein kinase.
+At position 385 to 466, the domain is characterized as Disintegrin.
+At position 517 to 621, the domain is characterized as PTS EIIA type-1.
+At position 32 to 92, the domain is characterized as HTH myb-type.
+At position 14 to 105, the domain is characterized as BRCT.
+At position 3 to 259, the domain is characterized as Protein kinase.
+At position 93 to 145, the domain is characterized as Kazal-like 1.
+At position 184 to 237, the domain is characterized as Kazal-like 2.
+At position 271 to 311, the domain is characterized as EGF-like.
+At position 2 to 138, the domain is characterized as CID.
+At position 1 to 103, the domain is characterized as Glutaredoxin.
+At position 622 to 673, the domain is characterized as SANT 2.
+At position 280 to 503, the domain is characterized as TLDc.
+At position 108 to 188, the domain is characterized as RRM 1.
+At position 202 to 281, the domain is characterized as RRM 2.
+At position 321 to 393, the domain is characterized as RRM 3.
+At position 46 to 219, the domain is characterized as PCI.
+At position 199 to 232, the domain is characterized as WW 1.
+At position 234 to 267, the domain is characterized as WW 2.
+At position 321 to 368, the domain is characterized as SARAH.
+At position 187 to 223, the domain is characterized as DFDF.
+At position 280 to 484, the domain is characterized as YjeF N-terminal.
+At position 206 to 440, the domain is characterized as START.
+At position 1 to 277, the domain is characterized as IF rod.
+At position 310 to 427, the domain is characterized as LTD.
+At position 239 to 332, the domain is characterized as Fibronectin type-III 1.
+At position 642 to 736, the domain is characterized as Fibronectin type-III 3.
+At position 740 to 834, the domain is characterized as Fibronectin type-III 4.
+At position 25 to 177, the domain is characterized as Saposin B-type.
+At position 61 to 174, the domain is characterized as TBDR plug.
+At position 181 to 710, the domain is characterized as TBDR beta-barrel.
+At position 671 to 970, the domain is characterized as Protein kinase.
+At position 185 to 455, the domain is characterized as SF4 helicase.
+At position 389 to 517, the domain is characterized as CUB.
+At position 722 to 989, the domain is characterized as Protein kinase.
+At position 13 to 84, the domain is characterized as KRAB 1.
+At position 110 to 181, the domain is characterized as KRAB 2.
+At position 166 to 227, the domain is characterized as SoHo.
+At position 959 to 1018, the domain is characterized as SH3 1.
+At position 1034 to 1095, the domain is characterized as SH3 2.
+At position 1137 to 1196, the domain is characterized as SH3 3.
+At position 272 to 321, the domain is characterized as bHLH.
+At position 506 to 558, the domain is characterized as PAC 1.
+At position 559 to 622, the domain is characterized as PAS.
+At position 632 to 684, the domain is characterized as PAC 2.
+At position 697 to 916, the domain is characterized as Histidine kinase.
+At position 64 to 292, the domain is characterized as OBG-type G.
+At position 292 to 367, the domain is characterized as TGS.
+At position 450 to 530, the domain is characterized as RRM 3.
+At position 1 to 93, the domain is characterized as HIG1.
+At position 38 to 235, the domain is characterized as Helicase ATP-binding.
+At position 284 to 462, the domain is characterized as Helicase C-terminal.
+At position 556 to 624, the domain is characterized as PUA.
+At position 651 to 921, the domain is characterized as Protein kinase.
+At position 505 to 780, the domain is characterized as Reverse transcriptase.
+At position 1247 to 1266, the domain is characterized as DUF1725.
+At position 1 to 141, the domain is characterized as Ferritin-like diiron.
+At position 698 to 762, the domain is characterized as SAM 1.
+At position 770 to 833, the domain is characterized as SAM 2.
+At position 858 to 930, the domain is characterized as SAM 3.
+At position 32 to 109, the domain is characterized as Ubiquitin-like 1.
+At position 110 to 188, the domain is characterized as Ubiquitin-like 2.
+At position 257 to 555, the domain is characterized as PI3K/PI4K catalytic.
+At position 25 to 213, the domain is characterized as RNase H type-2.
+At position 1268 to 1584, the domain is characterized as PKS/mFAS DH.
+At position 7 to 391, the domain is characterized as DhaK.
+At position 433 to 645, the domain is characterized as DhaL.
+At position 606 to 663, the domain is characterized as CBS 1.
+At position 808 to 869, the domain is characterized as CBS 2.
+At position 212 to 271, the domain is characterized as Nudix hydrolase.
+At position 115 to 185, the domain is characterized as PAS 1.
+At position 234 to 305, the domain is characterized as PAS 2.
+At position 368 to 598, the domain is characterized as Sigma-54 factor interaction.
+At position 10 to 275, the domain is characterized as Protein kinase.
+At position 376 to 440, the domain is characterized as PASTA 1.
+At position 441 to 508, the domain is characterized as PASTA 2.
+At position 513 to 581, the domain is characterized as PASTA 3.
+At position 589 to 648, the domain is characterized as PASTA 4.
+At position 32 to 182, the domain is characterized as 6-Cys 1.
+At position 283 to 415, the domain is characterized as 6-Cys 2.
+At position 89 to 304, the domain is characterized as ABC transmembrane type-1.
+At position 127 to 299, the domain is characterized as Helicase ATP-binding.
+At position 326 to 473, the domain is characterized as Helicase C-terminal.
+At position 94 to 392, the domain is characterized as ABC transmembrane type-1 1.
+At position 428 to 666, the domain is characterized as ABC transporter 1.
+At position 761 to 1049, the domain is characterized as ABC transmembrane type-1 2.
+At position 1086 to 1325, the domain is characterized as ABC transporter 2.
+At position 30 to 117, the domain is characterized as Ig-like 1.
+At position 122 to 208, the domain is characterized as Ig-like 2.
+At position 221 to 308, the domain is characterized as Ig-like 3.
+At position 312 to 396, the domain is characterized as Ig-like 4.
+At position 406 to 500, the domain is characterized as Fibronectin type-III 1.
+At position 502 to 601, the domain is characterized as Fibronectin type-III 2.
+At position 608 to 701, the domain is characterized as Fibronectin type-III 3.
+At position 711 to 804, the domain is characterized as Fibronectin type-III 4.
+At position 809 to 904, the domain is characterized as Fibronectin type-III 5.
+At position 508 to 666, the domain is characterized as C2 1.
+At position 751 to 888, the domain is characterized as C2 2.
+At position 952 to 1112, the domain is characterized as C2 3.
+At position 1136 to 1303, the domain is characterized as C2 4.
+At position 1370 to 1505, the domain is characterized as C2 5.
+At position 1581 to 1713, the domain is characterized as C2 6.
+At position 48 to 289, the domain is characterized as ABC transporter.
+At position 114 to 254, the domain is characterized as Nudix hydrolase.
+At position 9 to 102, the domain is characterized as Core-binding (CB).
+At position 115 to 279, the domain is characterized as Tyr recombinase.
+At position 60 to 296, the domain is characterized as Grh/CP2 DB.
+At position 63 to 131, the domain is characterized as CBS 1.
+At position 185 to 244, the domain is characterized as CBS 2.
+At position 263 to 324, the domain is characterized as CBS 3.
+At position 350 to 408, the domain is characterized as CBS 4.
+At position 1 to 248, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 1 to 273, the domain is characterized as Deacetylase sirtuin-type.
+At position 171 to 298, the domain is characterized as C2.
+At position 813 to 846, the domain is characterized as WW 1.
+At position 991 to 1024, the domain is characterized as WW 2.
+At position 1243 to 1578, the domain is characterized as HECT.
+At position 118 to 283, the domain is characterized as CRAL-TRIO.
+At position 20 to 54, the domain is characterized as SAP.
+At position 82 to 277, the domain is characterized as Exonuclease.
+At position 106 to 365, the domain is characterized as Septin-type G.
+At position 55 to 130, the domain is characterized as Biotinyl-binding.
+At position 84 to 365, the domain is characterized as tr-type G.
+At position 25 to 188, the domain is characterized as EXPERA.
+At position 468 to 529, the domain is characterized as LIM zinc-binding 1.
+At position 533 to 593, the domain is characterized as LIM zinc-binding 2.
+At position 594 to 662, the domain is characterized as LIM zinc-binding 3.
+At position 38 to 97, the domain is characterized as TRAM 1.
+At position 127 to 186, the domain is characterized as TRAM 2.
+At position 197 to 260, the domain is characterized as TRAM 3.
+At position 1 to 114, the domain is characterized as Pru.
+At position 178 to 290, the domain is characterized as DEUBAD.
+At position 183 to 325, the domain is characterized as KARI C-terminal knotted.
+At position 2 to 77, the domain is characterized as REM-1 1.
+At position 86 to 165, the domain is characterized as REM-1 2.
+At position 169 to 238, the domain is characterized as REM-1 3.
+At position 548 to 807, the domain is characterized as Protein kinase.
+At position 808 to 878, the domain is characterized as AGC-kinase C-terminal.
+At position 25 to 298, the domain is characterized as Septin-type G.
+At position 305 to 451, the domain is characterized as N-acetyltransferase.
+At position 34 to 205, the domain is characterized as Helicase ATP-binding.
+At position 233 to 383, the domain is characterized as Helicase C-terminal.
+At position 28 to 106, the domain is characterized as RRM.
+At position 227 to 353, the domain is characterized as PAZ.
+At position 515 to 815, the domain is characterized as Piwi.
+At position 141 to 409, the domain is characterized as NR LBD.
+At position 166 to 229, the domain is characterized as KH 1.
+At position 236 to 328, the domain is characterized as KH 2.
+At position 339 to 405, the domain is characterized as KH 3.
+At position 416 to 486, the domain is characterized as KH 4.
+At position 575 to 644, the domain is characterized as KH 5.
+At position 658 to 726, the domain is characterized as KH 6.
+At position 741 to 798, the domain is characterized as KH 7.
+At position 808 to 883, the domain is characterized as KH 8.
+At position 894 to 957, the domain is characterized as KH 9.
+At position 967 to 1040, the domain is characterized as KH 10.
+At position 1050 to 1114, the domain is characterized as KH 11.
+At position 1219 to 1280, the domain is characterized as KH 12.
+At position 1 to 46, the domain is characterized as Sigma-54 factor interaction.
+At position 362 to 508, the domain is characterized as Helicase C-terminal.
+At position 54 to 130, the domain is characterized as BTB.
+At position 714 to 789, the domain is characterized as Smr.
+At position 64 to 109, the domain is characterized as CARD.
+At position 30 to 290, the domain is characterized as GH18.
+At position 1 to 105, the domain is characterized as HTH arsR-type.
+At position 1 to 53, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 61 to 116, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 167 to 487, the domain is characterized as Peptidase S8.
+At position 224 to 299, the domain is characterized as MIT.
+At position 1 to 85, the domain is characterized as Ubiquitin-like.
+At position 326 to 609, the domain is characterized as ABC transmembrane type-1 1.
+At position 645 to 869, the domain is characterized as ABC transporter 1.
+At position 975 to 1257, the domain is characterized as ABC transmembrane type-1 2.
+At position 1294 to 1528, the domain is characterized as ABC transporter 2.
+At position 65 to 183, the domain is characterized as Plastocyanin-like 1.
+At position 189 to 347, the domain is characterized as Plastocyanin-like 2.
+At position 424 to 567, the domain is characterized as Plastocyanin-like 3.
+At position 74 to 144, the domain is characterized as HTH iclR-type.
+At position 188 to 363, the domain is characterized as CRAL-TRIO.
+At position 116 to 340, the domain is characterized as ATP-grasp.
+At position 555 to 596, the domain is characterized as JmjN.
+At position 619 to 711, the domain is characterized as ARID.
+At position 882 to 1046, the domain is characterized as JmjC.
+At position 532 to 608, the domain is characterized as IPT/TIG.
+At position 609 to 719, the domain is characterized as CBM20.
+At position 356 to 440, the domain is characterized as OCT.
+At position 330 to 394, the domain is characterized as SAM.
+At position 401 to 474, the domain is characterized as U-box.
+At position 12 to 296, the domain is characterized as GH18.
+At position 20 to 191, the domain is characterized as NAC.
+At position 710 to 992, the domain is characterized as Protein kinase.
+At position 385 to 553, the domain is characterized as tr-type G.
+At position 411 to 471, the domain is characterized as LIM zinc-binding 2.
+At position 472 to 540, the domain is characterized as LIM zinc-binding 3.
+At position 49 to 138, the domain is characterized as Fibronectin type-III 1.
+At position 335 to 434, the domain is characterized as Fibronectin type-III 2.
+At position 110 to 197, the domain is characterized as RRM 2.
+At position 243 to 323, the domain is characterized as RRM 3.
+At position 354 to 419, the domain is characterized as Death.
+At position 44 to 107, the domain is characterized as S4 RNA-binding.
+At position 27 to 118, the domain is characterized as UPAR/Ly6.
+At position 373 to 535, the domain is characterized as Helicase ATP-binding.
+At position 589 to 743, the domain is characterized as Helicase C-terminal.
+At position 11 to 225, the domain is characterized as tr-type G.
+At position 286 to 379, the domain is characterized as SH2.
+At position 95 to 165, the domain is characterized as PAH 2.
+At position 292 to 367, the domain is characterized as PAH 3.
+At position 605 to 690, the domain is characterized as Ig-like C2-type.
+At position 134 to 472, the domain is characterized as TTL.
+At position 157 to 264, the domain is characterized as Cadherin 1.
+At position 265 to 377, the domain is characterized as Cadherin 2.
+At position 378 to 488, the domain is characterized as Cadherin 3.
+At position 489 to 595, the domain is characterized as Cadherin 4.
+At position 596 to 699, the domain is characterized as Cadherin 5.
+At position 15 to 209, the domain is characterized as Glutamine amidotransferase type-1.
+At position 210 to 416, the domain is characterized as GMPS ATP-PPase.
+At position 226 to 343, the domain is characterized as PX.
+At position 3 to 97, the domain is characterized as TGS.
+At position 63 to 351, the domain is characterized as ABC transmembrane type-1.
+At position 492 to 729, the domain is characterized as ABC transporter.
+At position 42 to 137, the domain is characterized as RAMA.
+At position 229 to 364, the domain is characterized as MPN.
+At position 90 to 209, the domain is characterized as GST C-terminal.
+At position 182 to 367, the domain is characterized as Glutamine amidotransferase type-1.
+At position 280 to 382, the domain is characterized as RAMA.
+At position 15 to 321, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 140 to 178, the domain is characterized as LRRCT.
+At position 547 to 663, the domain is characterized as PI-PLC Y-box.
+At position 666 to 791, the domain is characterized as C2.
+At position 171 to 262, the domain is characterized as 5'-3' exonuclease.
+At position 7 to 687, the domain is characterized as Myosin motor.
+At position 725 to 919, the domain is characterized as TH1.
+At position 958 to 1017, the domain is characterized as SH3.
+At position 47 to 269, the domain is characterized as Saposin B-type.
+At position 147 to 237, the domain is characterized as Rhodanese.
+At position 484 to 578, the domain is characterized as Fibronectin type-III.
+At position 257 to 498, the domain is characterized as ABC transporter 2.
+At position 2 to 45, the domain is characterized as LysM 1.
+At position 48 to 92, the domain is characterized as LysM 2.
+At position 100 to 420, the domain is characterized as GH18.
+At position 435 to 493, the domain is characterized as COS.
+At position 498 to 592, the domain is characterized as Fibronectin type-III.
+At position 574 to 765, the domain is characterized as B30.2/SPRY.
+At position 547 to 757, the domain is characterized as Lon N-terminal.
+At position 177 to 256, the domain is characterized as BCNT-C.
+At position 116 to 577, the domain is characterized as Peptidase S8.
+At position 352 to 433, the domain is characterized as PA.
+At position 102 to 300, the domain is characterized as KARI N-terminal Rossmann.
+At position 301 to 449, the domain is characterized as KARI C-terminal knotted 1.
+At position 450 to 586, the domain is characterized as KARI C-terminal knotted 2.
+At position 199 to 393, the domain is characterized as Peptidase M12B.
+At position 13 to 176, the domain is characterized as TIR.
+At position 225 to 478, the domain is characterized as NB-ARC.
+At position 5 to 99, the domain is characterized as RH1.
+At position 289 to 358, the domain is characterized as RH2.
+At position 35 to 102, the domain is characterized as Histone-fold; involved in forming hexamer structure in TFIID complex.
+At position 34 to 331, the domain is characterized as Calpain catalytic.
+At position 537 to 572, the domain is characterized as EF-hand 1.
+At position 635 to 668, the domain is characterized as EF-hand 2.
+At position 27 to 166, the domain is characterized as FZ.
+At position 21 to 285, the domain is characterized as Alpha-carbonic anhydrase.
+At position 527 to 696, the domain is characterized as N-acetyltransferase.
+At position 27 to 63, the domain is characterized as ATP-grasp.
+At position 66 to 135, the domain is characterized as BTB.
+At position 170 to 271, the domain is characterized as BACK.
+At position 17 to 112, the domain is characterized as G.
+At position 293 to 377, the domain is characterized as Ig-like C2-type.
+At position 583 to 658, the domain is characterized as PUA.
+At position 143 to 388, the domain is characterized as NR LBD.
+At position 323 to 502, the domain is characterized as PCI.
+At position 392 to 525, the domain is characterized as DOD-type homing endonuclease.
+At position 502 to 776, the domain is characterized as MYST-type HAT.
+At position 672 to 947, the domain is characterized as Autotransporter.
+At position 88 to 342, the domain is characterized as Protein kinase.
+At position 343 to 398, the domain is characterized as AGC-kinase C-terminal.
+At position 16 to 273, the domain is characterized as Alpha-carbonic anhydrase.
+At position 527 to 641, the domain is characterized as SMC hinge.
+At position 4 to 84, the domain is characterized as Ubiquitin-like.
+At position 402 to 442, the domain is characterized as UBA.
+At position 194 to 253, the domain is characterized as SH3 1.
+At position 256 to 319, the domain is characterized as SH3 2.
+At position 464 to 525, the domain is characterized as SH3 3.
+At position 823 to 882, the domain is characterized as SH3 4.
+At position 235 to 350, the domain is characterized as Calponin-homology (CH).
+At position 1465 to 1599, the domain is characterized as CKK.
+At position 20 to 86, the domain is characterized as LCN-type CS-alpha/beta.
+At position 360 to 682, the domain is characterized as Transferrin-like 2.
+At position 1015 to 1085, the domain is characterized as HTH CENPB-type.
+At position 1117 to 1323, the domain is characterized as DDE-1.
+At position 17 to 336, the domain is characterized as tr-type G.
+At position 31 to 284, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 39 to 144, the domain is characterized as Thioredoxin.
+At position 79 to 196, the domain is characterized as HD.
+At position 146 to 302, the domain is characterized as Helicase ATP-binding.
+At position 403 to 575, the domain is characterized as Helicase C-terminal.
+At position 38 to 142, the domain is characterized as SSB.
+At position 444 to 539, the domain is characterized as Fibronectin type-III 1.
+At position 543 to 635, the domain is characterized as Fibronectin type-III 2.
+At position 640 to 733, the domain is characterized as Fibronectin type-III 3.
+At position 822 to 1094, the domain is characterized as Protein kinase.
+At position 8 to 110, the domain is characterized as Rieske.
+At position 443 to 766, the domain is characterized as Kinesin motor.
+At position 1 to 227, the domain is characterized as Deacetylase sirtuin-type.
+At position 24 to 86, the domain is characterized as KH; atypical.
+At position 73 to 146, the domain is characterized as RRM.
+At position 6 to 133, the domain is characterized as Thioredoxin.
+At position 187 to 563, the domain is characterized as USP.
+At position 27 to 135, the domain is characterized as Rieske.
+At position 585 to 687, the domain is characterized as tRNA-binding.
+At position 123 to 527, the domain is characterized as Protein kinase.
+At position 9 to 285, the domain is characterized as tr-type G.
+At position 58 to 105, the domain is characterized as F-box.
+At position 22 to 138, the domain is characterized as C-type lectin.
+At position 139 to 174, the domain is characterized as EGF-like.
+At position 177 to 238, the domain is characterized as Sushi 1.
+At position 239 to 300, the domain is characterized as Sushi 2.
+At position 314 to 363, the domain is characterized as Sushi 3.
+At position 365 to 426, the domain is characterized as Sushi 4.
+At position 428 to 489, the domain is characterized as Sushi 5.
+At position 490 to 548, the domain is characterized as Sushi 6.
+At position 11 to 63, the domain is characterized as Peptidase S8.
+At position 77 to 164, the domain is characterized as PB1.
+At position 535 to 564, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 583 to 664, the domain is characterized as BRCT.
+At position 59 to 118, the domain is characterized as CBS 1.
+At position 125 to 183, the domain is characterized as CBS 2.
+At position 225 to 285, the domain is characterized as CBS 3.
+At position 293 to 350, the domain is characterized as CBS 4.
+At position 402 to 489, the domain is characterized as PB1.
+At position 13 to 245, the domain is characterized as ABC transporter.
+At position 56 to 287, the domain is characterized as Peptidase S1.
+At position 68 to 391, the domain is characterized as Asparaginase/glutaminase.
+At position 174 to 262, the domain is characterized as EH 1.
+At position 206 to 241, the domain is characterized as EF-hand 1.
+At position 1452 to 1469, the domain is characterized as WH2.
+At position 52 to 304, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 161 to 245, the domain is characterized as PPIase FKBP-type.
+At position 38 to 242, the domain is characterized as PNPLA.
+At position 66 to 130, the domain is characterized as KH 1.
+At position 148 to 213, the domain is characterized as KH 2.
+At position 330 to 394, the domain is characterized as KH 3.
+At position 409 to 587, the domain is characterized as Helicase ATP-binding.
+At position 614 to 762, the domain is characterized as Helicase C-terminal.
+At position 80 to 309, the domain is characterized as ABC transmembrane type-1.
+At position 48 to 116, the domain is characterized as POTRA.
+At position 74 to 152, the domain is characterized as Ubiquitin-like.
+At position 46 to 315, the domain is characterized as Septin-type G.
+At position 1091 to 1428, the domain is characterized as PUM-HD.
+At position 1 to 66, the domain is characterized as Calpain catalytic.
+At position 294 to 327, the domain is characterized as EF-hand 1.
+At position 324 to 359, the domain is characterized as EF-hand 2.
+At position 389 to 422, the domain is characterized as EF-hand 3.
+At position 45 to 81, the domain is characterized as EGF-like 1.
+At position 82 to 117, the domain is characterized as EGF-like 2.
+At position 118 to 154, the domain is characterized as EGF-like 3.
+At position 155 to 191, the domain is characterized as EGF-like 4.
+At position 192 to 228, the domain is characterized as EGF-like 5.
+At position 229 to 265, the domain is characterized as EGF-like 6.
+At position 266 to 301, the domain is characterized as EGF-like 7.
+At position 302 to 340, the domain is characterized as EGF-like 8.
+At position 342 to 378, the domain is characterized as EGF-like 9.
+At position 383 to 420, the domain is characterized as EGF-like 10.
+At position 425 to 461, the domain is characterized as EGF-like 11.
+At position 37 to 226, the domain is characterized as GH11.
+At position 76 to 265, the domain is characterized as Thioredoxin.
+At position 118 to 290, the domain is characterized as 3'-5' exonuclease.
+At position 33 to 134, the domain is characterized as HD.
+At position 74 to 249, the domain is characterized as FAD-binding PCMH-type.
+At position 552 to 632, the domain is characterized as Carrier.
+At position 104 to 325, the domain is characterized as Radical SAM core.
+At position 617 to 697, the domain is characterized as BRCT.
+At position 20 to 123, the domain is characterized as Ig-like.
+At position 1 to 87, the domain is characterized as Jacalin-type lectin 1.
+At position 90 to 232, the domain is characterized as Jacalin-type lectin 2.
+At position 235 to 378, the domain is characterized as Jacalin-type lectin 3.
+At position 385 to 528, the domain is characterized as Jacalin-type lectin 4.
+At position 313 to 396, the domain is characterized as SWIB/MDM2.
+At position 453 to 586, the domain is characterized as Plus3.
+At position 716 to 770, the domain is characterized as GYF.
+At position 77 to 188, the domain is characterized as Rieske.
+At position 31 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 38 to 209, the domain is characterized as Helicase ATP-binding.
+At position 237 to 386, the domain is characterized as Helicase C-terminal.
+At position 352 to 406, the domain is characterized as LRRCT.
+At position 407 to 496, the domain is characterized as Ig-like C2-type.
+At position 168 to 251, the domain is characterized as RRM.
+At position 946 to 1065, the domain is characterized as PH.
+At position 1091 to 1365, the domain is characterized as CNH.
+At position 1436 to 1449, the domain is characterized as CRIB.
+At position 566 to 705, the domain is characterized as JmjC.
+At position 329 to 603, the domain is characterized as Clu.
+At position 236 to 299, the domain is characterized as bZIP.
+At position 95 to 406, the domain is characterized as IF rod.
+At position 1 to 151, the domain is characterized as Protein kinase.
+At position 117 to 536, the domain is characterized as Peptidase S8.
+At position 354 to 396, the domain is characterized as PA.
+At position 230 to 290, the domain is characterized as HTH myb-type.
+At position 323 to 781, the domain is characterized as USP.
+At position 576 to 626, the domain is characterized as UBA 1.
+At position 649 to 689, the domain is characterized as UBA 2.
+At position 2 to 360, the domain is characterized as SAM-dependent MTase C5-type.
+At position 1174 to 1358, the domain is characterized as DH.
+At position 1390 to 1502, the domain is characterized as PH.
+At position 1510 to 1571, the domain is characterized as SH3.
+At position 88 to 774, the domain is characterized as Myosin motor.
+At position 777 to 806, the domain is characterized as IQ.
+At position 47 to 277, the domain is characterized as GB1/RHD3-type G.
+At position 35 to 75, the domain is characterized as EGF-like.
+At position 113 to 175, the domain is characterized as FHA.
+At position 220 to 486, the domain is characterized as Protein kinase.
+At position 335 to 436, the domain is characterized as Rhodanese.
+At position 39 to 125, the domain is characterized as RRM.
+At position 1 to 86, the domain is characterized as Phosphagen kinase N-terminal.
+At position 113 to 355, the domain is characterized as Phosphagen kinase C-terminal.
+At position 174 to 480, the domain is characterized as USP.
+At position 90 to 223, the domain is characterized as Guanylate cyclase.
+At position 737 to 819, the domain is characterized as ACT 1.
+At position 348 to 629, the domain is characterized as Protein kinase.
+At position 700 to 883, the domain is characterized as F5/8 type C.
+At position 316 to 541, the domain is characterized as tr-type G.
+At position 26 to 191, the domain is characterized as Thioredoxin.
+At position 7 to 219, the domain is characterized as tr-type G.
+At position 84 to 143, the domain is characterized as CTLH.
+At position 133 to 210, the domain is characterized as UPAR/Ly6 1.
+At position 325 to 377, the domain is characterized as UPAR/Ly6 2.
+At position 601 to 664, the domain is characterized as bZIP.
+At position 174 to 366, the domain is characterized as ATP-grasp.
+At position 1559 to 1958, the domain is characterized as USP.
+At position 3 to 81, the domain is characterized as Lipoyl-binding.
+At position 112 to 150, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 112 to 184, the domain is characterized as PRC barrel.
+At position 7 to 69, the domain is characterized as t-SNARE coiled-coil homology.
+At position 6 to 94, the domain is characterized as PPIase FKBP-type.
+At position 32 to 108, the domain is characterized as Lipoyl-binding.
+At position 169 to 210, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 31 to 197, the domain is characterized as Tyrosine-protein phosphatase.
+At position 117 to 181, the domain is characterized as CBS 1.
+At position 190 to 255, the domain is characterized as CBS 2.
+At position 148 to 358, the domain is characterized as ATP-grasp.
+At position 484 to 556, the domain is characterized as RRM 3.
+At position 597 to 680, the domain is characterized as RRM 4.
+At position 702 to 779, the domain is characterized as RRM 5.
+At position 146 to 480, the domain is characterized as Protein kinase.
+At position 481 to 555, the domain is characterized as AGC-kinase C-terminal.
+At position 35 to 180, the domain is characterized as N-acetyltransferase.
+At position 124 to 216, the domain is characterized as BRCT.
+At position 3 to 186, the domain is characterized as Glutamine amidotransferase type-1.
+At position 188 to 229, the domain is characterized as GRAM 1.
+At position 239 to 342, the domain is characterized as PH.
+At position 602 to 668, the domain is characterized as GRAM 2.
+At position 198 to 324, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 1 to 288, the domain is characterized as Peptidase M60.
+At position 463 to 615, the domain is characterized as PA14.
+At position 311 to 437, the domain is characterized as MATH.
+At position 144 to 269, the domain is characterized as OTU.
+At position 204 to 288, the domain is characterized as RCK C-terminal 1.
+At position 290 to 377, the domain is characterized as RCK C-terminal 2.
+At position 204 to 365, the domain is characterized as CP-type G.
+At position 272 to 327, the domain is characterized as HTH myb-type 1.
+At position 328 to 378, the domain is characterized as HTH myb-type 2.
+At position 26 to 375, the domain is characterized as BRO1.
+At position 412 to 490, the domain is characterized as PDZ.
+At position 74 to 139, the domain is characterized as NAC-A/B.
+At position 290 to 382, the domain is characterized as PB1.
+At position 63 to 217, the domain is characterized as N-acetyltransferase.
+At position 48 to 98, the domain is characterized as F-box.
+At position 70 to 273, the domain is characterized as Peptidase M12A.
+At position 267 to 306, the domain is characterized as EGF-like.
+At position 324 to 475, the domain is characterized as VPS9.
+At position 414 to 626, the domain is characterized as NEL.
+At position 1 to 96, the domain is characterized as Pyrin.
+At position 167 to 484, the domain is characterized as NACHT.
+At position 467 to 601, the domain is characterized as Thioredoxin.
+At position 2 to 246, the domain is characterized as KaiC.
+At position 1 to 226, the domain is characterized as Deacetylase sirtuin-type.
+At position 63 to 92, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 122 to 151, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 145 to 174, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 179 to 209, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 274 to 408, the domain is characterized as Ferric oxidoreductase.
+At position 409 to 528, the domain is characterized as FAD-binding FR-type.
+At position 245 to 334, the domain is characterized as EH 2.
+At position 278 to 313, the domain is characterized as EF-hand 2.
+At position 718 to 779, the domain is characterized as SH3 1.
+At position 852 to 910, the domain is characterized as SH3 2.
+At position 942 to 1000, the domain is characterized as SH3 3.
+At position 1014 to 1078, the domain is characterized as SH3 4.
+At position 1088 to 1147, the domain is characterized as SH3 5.
+At position 1170 to 1357, the domain is characterized as DH.
+At position 1396 to 1506, the domain is characterized as PH.
+At position 1514 to 1630, the domain is characterized as C2.
+At position 166 to 252, the domain is characterized as Ig-like C1-type.
+At position 446 to 867, the domain is characterized as FH2.
+At position 120 to 350, the domain is characterized as Radical SAM core.
+At position 353 to 422, the domain is characterized as TRAM.
+At position 1 to 187, the domain is characterized as SPX.
+At position 650 to 903, the domain is characterized as Protein kinase.
+At position 195 to 273, the domain is characterized as RRM 1.
+At position 295 to 418, the domain is characterized as RRM 2.
+At position 540 to 638, the domain is characterized as RRM 3.
+At position 22 to 415, the domain is characterized as Glutamine amidotransferase type-2.
+At position 46 to 212, the domain is characterized as Helicase ATP-binding.
+At position 265 to 447, the domain is characterized as Helicase C-terminal.
+At position 866 to 931, the domain is characterized as Tudor.
+At position 253 to 311, the domain is characterized as CNA-B.
+At position 18 to 216, the domain is characterized as ABC transporter.
+At position 8 to 137, the domain is characterized as TsaA-like.
+At position 224 to 302, the domain is characterized as Ig-like C2-type 3.
+At position 309 to 395, the domain is characterized as Ig-like C2-type 4.
+At position 404 to 515, the domain is characterized as Ig-like C2-type 5.
+At position 572 to 673, the domain is characterized as Fibronectin type-III 1.
+At position 719 to 814, the domain is characterized as Fibronectin type-III 2.
+At position 822 to 922, the domain is characterized as Fibronectin type-III 3.
+At position 18 to 167, the domain is characterized as NAC.
+At position 32 to 154, the domain is characterized as NlpC/P60.
+At position 9 to 159, the domain is characterized as PPIase cyclophilin-type.
+At position 18 to 261, the domain is characterized as ATP-grasp.
+At position 215 to 394, the domain is characterized as GAF.
+At position 609 to 680, the domain is characterized as PAS.
+At position 683 to 739, the domain is characterized as PAC.
+At position 1004 to 1307, the domain is characterized as Protein kinase.
+At position 3 to 68, the domain is characterized as G protein gamma.
+At position 12 to 106, the domain is characterized as ACB.
+At position 563 to 676, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 677 to 791, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 857 to 935, the domain is characterized as POLO box.
+At position 223 to 469, the domain is characterized as CN hydrolase.
+At position 229 to 408, the domain is characterized as GAF.
+At position 622 to 693, the domain is characterized as PAS 1.
+At position 756 to 808, the domain is characterized as PAS 2.
+At position 1 to 42, the domain is characterized as C-type lectin.
+At position 1 to 32, the domain is characterized as Peptidase S8.
+At position 443 to 555, the domain is characterized as VRR-NUC.
+At position 9 to 133, the domain is characterized as VOC.
+At position 333 to 426, the domain is characterized as Fibronectin type-III 2.
+At position 428 to 527, the domain is characterized as Fibronectin type-III 3.
+At position 528 to 621, the domain is characterized as Fibronectin type-III 4.
+At position 623 to 734, the domain is characterized as Fibronectin type-III 5.
+At position 417 to 572, the domain is characterized as DOD-type homing endonuclease.
+At position 904 to 1083, the domain is characterized as Lon proteolytic.
+At position 90 to 301, the domain is characterized as RNase H type-2.
+At position 1 to 94, the domain is characterized as PPIase FKBP-type.
+At position 5 to 94, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 104 to 205, the domain is characterized as FAD-binding FR-type.
+At position 3 to 277, the domain is characterized as DegV.
+At position 206 to 395, the domain is characterized as Helicase ATP-binding.
+At position 406 to 566, the domain is characterized as Helicase C-terminal.
+At position 26 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 169 to 366, the domain is characterized as ABC transmembrane type-1.
+At position 290 to 345, the domain is characterized as SOCS box.
+At position 219 to 457, the domain is characterized as CN hydrolase.
+At position 425 to 569, the domain is characterized as JmjC.
+At position 332 to 410, the domain is characterized as WWE.
+At position 234 to 269, the domain is characterized as EF-hand 4.
+At position 10 to 113, the domain is characterized as SH2 1.
+At position 134 to 232, the domain is characterized as SH2 2.
+At position 264 to 580, the domain is characterized as Tyrosine-protein phosphatase.
+At position 75 to 185, the domain is characterized as SET.
+At position 1 to 141, the domain is characterized as MGS-like.
+At position 131 to 313, the domain is characterized as FAD-binding PCMH-type.
+At position 72 to 135, the domain is characterized as S5 DRBM.
+At position 123 to 228, the domain is characterized as EamA.
+At position 1 to 137, the domain is characterized as PTS EIIA type-4.
+At position 2 to 86, the domain is characterized as ACB.
+At position 369 to 504, the domain is characterized as C-CAP/cofactor C-like.
+At position 4 to 160, the domain is characterized as Thioredoxin.
+At position 156 to 201, the domain is characterized as F-box.
+At position 49 to 151, the domain is characterized as AB hydrolase-1.
+At position 1 to 30, the domain is characterized as Tudor 1.
+At position 215 to 279, the domain is characterized as Tudor 2.
+At position 435 to 491, the domain is characterized as Tudor 3.
+At position 853 to 910, the domain is characterized as Tudor 4.
+At position 1060 to 1118, the domain is characterized as Tudor 5.
+At position 30 to 279, the domain is characterized as Peptidase S1.
+At position 217 to 261, the domain is characterized as PCI.
+At position 218 to 392, the domain is characterized as Helicase ATP-binding.
+At position 426 to 572, the domain is characterized as Helicase C-terminal.
+At position 515 to 625, the domain is characterized as PH.
+At position 7 to 155, the domain is characterized as RWD.
+At position 30 to 80, the domain is characterized as HTH myb-type 1.
+At position 81 to 136, the domain is characterized as HTH myb-type 2.
+At position 137 to 187, the domain is characterized as HTH myb-type 3.
+At position 26 to 399, the domain is characterized as FERM.
+At position 11 to 118, the domain is characterized as Response regulatory.
+At position 146 to 208, the domain is characterized as HTH luxR-type.
+At position 4 to 134, the domain is characterized as VOC.
+At position 191 to 351, the domain is characterized as Hflx-type G.
+At position 167 to 256, the domain is characterized as TonB C-terminal.
+At position 4 to 85, the domain is characterized as GS beta-grasp.
+At position 83 to 326, the domain is characterized as GS catalytic.
+At position 23 to 301, the domain is characterized as ABC transmembrane type-1.
+At position 474 to 643, the domain is characterized as tr-type G.
+At position 145 to 347, the domain is characterized as ATP-grasp.
+At position 40 to 154, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 76 to 289, the domain is characterized as TLC.
+At position 173 to 269, the domain is characterized as 5'-3' exonuclease.
+At position 161 to 443, the domain is characterized as Deacetylase sirtuin-type.
+At position 607 to 783, the domain is characterized as PCI.
+At position 72 to 237, the domain is characterized as Laminin G-like.
+At position 610 to 664, the domain is characterized as Collagen-like 1.
+At position 673 to 732, the domain is characterized as Collagen-like 2.
+At position 742 to 801, the domain is characterized as Collagen-like 3.
+At position 817 to 876, the domain is characterized as Collagen-like 4.
+At position 877 to 936, the domain is characterized as Collagen-like 5.
+At position 937 to 996, the domain is characterized as Collagen-like 6.
+At position 997 to 1038, the domain is characterized as Collagen-like 7.
+At position 1039 to 1096, the domain is characterized as Collagen-like 8.
+At position 1117 to 1176, the domain is characterized as Collagen-like 9.
+At position 1177 to 1236, the domain is characterized as Collagen-like 10.
+At position 1240 to 1299, the domain is characterized as Collagen-like 11.
+At position 1325 to 1384, the domain is characterized as Collagen-like 12.
+At position 1424 to 1483, the domain is characterized as Collagen-like 13.
+At position 1484 to 1543, the domain is characterized as Collagen-like 14.
+At position 1544 to 1603, the domain is characterized as Collagen-like 15.
+At position 1645 to 1845, the domain is characterized as Fibrillar collagen NC1.
+At position 39 to 186, the domain is characterized as C2 PI3K-type.
+At position 275 to 460, the domain is characterized as PIK helical.
+At position 532 to 800, the domain is characterized as PI3K/PI4K catalytic.
+At position 38 to 147, the domain is characterized as tRNA-binding.
+At position 708 to 799, the domain is characterized as FDX-ACB.
+At position 189 to 405, the domain is characterized as Histidine kinase.
+At position 272 to 399, the domain is characterized as Ricin B-type lectin 1.
+At position 402 to 526, the domain is characterized as Ricin B-type lectin 2.
+At position 164 to 227, the domain is characterized as Histone-fold.
+At position 186 to 247, the domain is characterized as bZIP.
+At position 137 to 225, the domain is characterized as Ig-like C2-type 2.
+At position 233 to 315, the domain is characterized as Ig-like C2-type 3.
+At position 322 to 412, the domain is characterized as Fibronectin type-III 1.
+At position 417 to 511, the domain is characterized as Fibronectin type-III 2.
+At position 515 to 604, the domain is characterized as Fibronectin type-III 3.
+At position 918 to 1013, the domain is characterized as Fibronectin type-III 7.
+At position 1354 to 1609, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1641 to 1900, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 182 to 351, the domain is characterized as tr-type G.
+At position 139 to 434, the domain is characterized as NB-ARC.
+At position 66 to 201, the domain is characterized as C1q.
+At position 21 to 144, the domain is characterized as Thioredoxin 1.
+At position 365 to 485, the domain is characterized as Thioredoxin 2.
+At position 124 to 223, the domain is characterized as Ig-like 2.
+At position 232 to 328, the domain is characterized as Ig-like 3.
+At position 102 to 238, the domain is characterized as PPC.
+At position 99 to 177, the domain is characterized as RRM.
+At position 38 to 122, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 312, the domain is characterized as Ig-like C2-type 3.
+At position 321 to 408, the domain is characterized as Ig-like C2-type 4.
+At position 419 to 500, the domain is characterized as Ig-like C2-type 5.
+At position 589 to 677, the domain is characterized as Ig-like C2-type 6.
+At position 686 to 760, the domain is characterized as Ig-like C2-type 7.
+At position 777 to 869, the domain is characterized as Ig-like C2-type 8.
+At position 873 to 958, the domain is characterized as Ig-like C2-type 9.
+At position 965 to 1060, the domain is characterized as Ig-like C2-type 10.
+At position 1065 to 1150, the domain is characterized as Ig-like C2-type 11.
+At position 1161 to 1242, the domain is characterized as Ig-like C2-type 12.
+At position 176 to 228, the domain is characterized as BSD.
+At position 1 to 107, the domain is characterized as C2 1.
+At position 232 to 352, the domain is characterized as C2 2.
+At position 384 to 507, the domain is characterized as C2 3.
+At position 543 to 669, the domain is characterized as C2 4.
+At position 4 to 218, the domain is characterized as ABC transporter.
+At position 346 to 591, the domain is characterized as PH.
+At position 612 to 732, the domain is characterized as Arf-GAP.
+At position 163 to 355, the domain is characterized as CheB-type methylesterase.
+At position 666 to 959, the domain is characterized as Protein kinase.
+At position 222 to 291, the domain is characterized as HTH OST-type 2.
+At position 325 to 394, the domain is characterized as HTH OST-type 3.
+At position 501 to 558, the domain is characterized as Tudor 1.
+At position 691 to 748, the domain is characterized as Tudor 2.
+At position 19 to 55, the domain is characterized as F-box.
+At position 192 to 424, the domain is characterized as Protein kinase.
+At position 42 to 109, the domain is characterized as BTB.
+At position 215 to 330, the domain is characterized as Calponin-homology (CH).
+At position 1443 to 1576, the domain is characterized as CKK.
+At position 187 to 335, the domain is characterized as MOSC.
+At position 99 to 154, the domain is characterized as BSD 1.
+At position 380 to 418, the domain is characterized as UBA.
+At position 93 to 189, the domain is characterized as Plastocyanin-like 1.
+At position 254 to 355, the domain is characterized as Plastocyanin-like 2.
+At position 118 to 285, the domain is characterized as tr-type G.
+At position 1 to 202, the domain is characterized as GRAS.
+At position 43 to 354, the domain is characterized as AB hydrolase-1.
+At position 14 to 90, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 578 to 680, the domain is characterized as tRNA-binding.
+At position 34 to 112, the domain is characterized as Inhibitor I9.
+At position 117 to 560, the domain is characterized as Peptidase S8.
+At position 356 to 415, the domain is characterized as PA.
+At position 116 to 198, the domain is characterized as RRM.
+At position 291 to 469, the domain is characterized as VWFA.
+At position 485 to 574, the domain is characterized as Cache.
+At position 19 to 113, the domain is characterized as Ig-like.
+At position 28 to 189, the domain is characterized as HD.
+At position 260 to 455, the domain is characterized as HD-GYP.
+At position 79 to 111, the domain is characterized as EF-hand 2.
+At position 47 to 192, the domain is characterized as Tyrosine-protein phosphatase.
+At position 393 to 501, the domain is characterized as Fe2OG dioxygenase.
+At position 4 to 125, the domain is characterized as MTTase N-terminal.
+At position 366 to 610, the domain is characterized as TLDc.
+At position 4 to 45, the domain is characterized as UBA.
+At position 231 to 295, the domain is characterized as SEP.
+At position 343 to 420, the domain is characterized as UBX.
+At position 16 to 105, the domain is characterized as F-box.
+At position 76 to 251, the domain is characterized as PCI.
+At position 1 to 157, the domain is characterized as Peptidase S1.
+At position 89 to 153, the domain is characterized as J.
+At position 19 to 147, the domain is characterized as RNase III.
+At position 174 to 242, the domain is characterized as DRBM.
+At position 2 to 262, the domain is characterized as Glutamine amidotransferase type-2.
+At position 44 to 73, the domain is characterized as ShKT.
+At position 294 to 316, the domain is characterized as RRM.
+At position 21 to 465, the domain is characterized as Hexokinase.
+At position 23 to 138, the domain is characterized as Rhodanese.
+At position 160 to 302, the domain is characterized as Tyrosine-protein phosphatase.
+At position 574 to 847, the domain is characterized as Protein kinase.
+At position 173 to 408, the domain is characterized as NR LBD.
+At position 394 to 429, the domain is characterized as CBM1.
+At position 247 to 391, the domain is characterized as FCP1 homology.
+At position 1669 to 1698, the domain is characterized as IQ.
+At position 243 to 424, the domain is characterized as PCI.
+At position 132 to 200, the domain is characterized as SAM.
+At position 1 to 38, the domain is characterized as Sin.
+At position 297 to 382, the domain is characterized as RCK C-terminal 2.
+At position 33 to 307, the domain is characterized as F-BAR.
+At position 506 to 692, the domain is characterized as Rho-GAP.
+At position 110 to 293, the domain is characterized as Helicase ATP-binding.
+At position 327 to 478, the domain is characterized as Helicase C-terminal.
+At position 152 to 221, the domain is characterized as HTH OST-type.
+At position 1 to 211, the domain is characterized as ABC transporter.
+At position 37 to 318, the domain is characterized as ABC transmembrane type-1.
+At position 350 to 584, the domain is characterized as ABC transporter.
+At position 279 to 440, the domain is characterized as EF-1-gamma C-terminal.
+At position 212 to 381, the domain is characterized as PCI.
+At position 425 to 497, the domain is characterized as ACT-like 1.
+At position 519 to 590, the domain is characterized as ACT-like 2.
+At position 131 to 571, the domain is characterized as Urease.
+At position 130 to 158, the domain is characterized as ITAM 3.
+At position 2 to 145, the domain is characterized as Thioredoxin.
+At position 87 to 295, the domain is characterized as Rab-GAP TBC.
+At position 110 to 182, the domain is characterized as HTH crp-type.
+At position 154 to 202, the domain is characterized as G-patch.
+At position 221 to 248, the domain is characterized as KOW 1.
+At position 47 to 109, the domain is characterized as TGS.
+At position 15 to 217, the domain is characterized as YjeF N-terminal.
+At position 232 to 506, the domain is characterized as YjeF C-terminal.
+At position 232 to 390, the domain is characterized as TrmE-type G.
+At position 285 to 371, the domain is characterized as RRM.
+At position 4 to 117, the domain is characterized as PH.
+At position 177 to 237, the domain is characterized as SH3.
+At position 245 to 343, the domain is characterized as SH2.
+At position 368 to 620, the domain is characterized as Protein kinase.
+At position 28 to 110, the domain is characterized as GOLD.
+At position 264 to 448, the domain is characterized as DH.
+At position 480 to 592, the domain is characterized as PH.
+At position 603 to 664, the domain is characterized as SH3.
+At position 88 to 151, the domain is characterized as S5 DRBM.
+At position 33 to 135, the domain is characterized as HD.
+At position 3 to 120, the domain is characterized as N-acetyltransferase.
+At position 50 to 154, the domain is characterized as FAD-binding FR-type.
+At position 108 to 307, the domain is characterized as ATP-grasp.
+At position 98 to 377, the domain is characterized as Protein kinase.
+At position 183 to 263, the domain is characterized as PPIase FKBP-type.
+At position 295 to 400, the domain is characterized as Glutaredoxin.
+At position 30 to 99, the domain is characterized as Ubiquitin-like.
+At position 575 to 671, the domain is characterized as PilZ.
+At position 88 to 166, the domain is characterized as RRM 1.
+At position 174 to 257, the domain is characterized as RRM 2.
+At position 328 to 406, the domain is characterized as RRM 3.
+At position 243 to 408, the domain is characterized as Helicase ATP-binding.
+At position 536 to 687, the domain is characterized as Helicase C-terminal.
+At position 877 to 929, the domain is characterized as SANT 1.
+At position 978 to 1039, the domain is characterized as SANT 2.
+At position 253 to 426, the domain is characterized as Helicase ATP-binding.
+At position 593 to 758, the domain is characterized as Helicase C-terminal.
+At position 111 to 193, the domain is characterized as Toprim.
+At position 1 to 178, the domain is characterized as MIF4G.
+At position 322 to 391, the domain is characterized as U-box.
+At position 15 to 257, the domain is characterized as CN hydrolase.
+At position 216 to 368, the domain is characterized as Laminin G-like 1.
+At position 401 to 552, the domain is characterized as Laminin G-like 2.
+At position 963 to 1002, the domain is characterized as EGF-like 2.
+At position 1055 to 1214, the domain is characterized as Laminin G-like 4.
+At position 118 to 248, the domain is characterized as Fatty acid hydroxylase.
+At position 18 to 269, the domain is characterized as Protein kinase.
+At position 182 to 480, the domain is characterized as Lon N-terminal.
+At position 923 to 1109, the domain is characterized as Lon proteolytic.
+At position 6 to 97, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 122 to 392, the domain is characterized as Protein kinase.
+At position 99 to 172, the domain is characterized as BTB.
+At position 2 to 177, the domain is characterized as Thioredoxin.
+At position 1 to 291, the domain is characterized as FERM.
+At position 1 to 229, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 298 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 5 to 87, the domain is characterized as GST N-terminal.
+At position 93 to 220, the domain is characterized as GST C-terminal.
+At position 15 to 182, the domain is characterized as Miro 1.
+At position 319 to 354, the domain is characterized as EF-hand 2.
+At position 427 to 595, the domain is characterized as Miro 2.
+At position 178 to 384, the domain is characterized as Helicase ATP-binding.
+At position 422 to 622, the domain is characterized as Helicase C-terminal.
+At position 40 to 118, the domain is characterized as GIY-YIG.
+At position 228 to 263, the domain is characterized as UVR.
+At position 190 to 349, the domain is characterized as Plastocyanin-like.
+At position 141 to 208, the domain is characterized as KH.
+At position 596 to 683, the domain is characterized as BRCT.
+At position 91 to 229, the domain is characterized as PPC.
+At position 1193 to 1427, the domain is characterized as ABC transporter 2.
+At position 2274 to 2498, the domain is characterized as JmjC.
+At position 4 to 79, the domain is characterized as RRM 1.
+At position 361 to 439, the domain is characterized as RRM 2.
+At position 553 to 625, the domain is characterized as RRM 3.
+At position 678 to 761, the domain is characterized as RRM 4.
+At position 795 to 872, the domain is characterized as RRM 5.
+At position 112 to 310, the domain is characterized as ATP-grasp.
+At position 160 to 564, the domain is characterized as PUM-HD.
+At position 430 to 512, the domain is characterized as RRM.
+At position 59 to 149, the domain is characterized as UPAR/Ly6.
+At position 39 to 158, the domain is characterized as tRNA-binding.
+At position 417 to 492, the domain is characterized as B5.
+At position 106 to 228, the domain is characterized as PLAT.
+At position 231 to 926, the domain is characterized as Lipoxygenase.
+At position 60 to 282, the domain is characterized as BURP.
+At position 103 to 163, the domain is characterized as LIM zinc-binding 2.
+At position 259 to 356, the domain is characterized as Fe2OG dioxygenase.
+At position 1 to 170, the domain is characterized as Kinesin motor.
+At position 27 to 110, the domain is characterized as WSC.
+At position 77 to 154, the domain is characterized as RRM 1.
+At position 179 to 256, the domain is characterized as RRM 2.
+At position 310 to 387, the domain is characterized as RRM 3.
+At position 630 to 808, the domain is characterized as STAS.
+At position 16 to 152, the domain is characterized as N-acetyltransferase 1.
+At position 492 to 550, the domain is characterized as PAP-associated.
+At position 4 to 147, the domain is characterized as RNase H type-1.
+At position 16 to 114, the domain is characterized as Ras-associating.
+At position 148 to 971, the domain is characterized as Myosin motor.
+At position 976 to 996, the domain is characterized as IQ 1.
+At position 1025 to 1054, the domain is characterized as IQ 2.
+At position 1066 to 1095, the domain is characterized as IQ 3.
+At position 1089 to 1118, the domain is characterized as IQ 4.
+At position 1823 to 2011, the domain is characterized as Rho-GAP.
+At position 1 to 207, the domain is characterized as RNase H type-2.
+At position 44 to 129, the domain is characterized as Core-binding (CB).
+At position 155 to 332, the domain is characterized as Tyr recombinase.
+At position 253 to 328, the domain is characterized as H15 2.
+At position 335 to 411, the domain is characterized as H15 3.
+At position 40 to 380, the domain is characterized as TTL.
+At position 86 to 159, the domain is characterized as AB hydrolase-1.
+At position 151 to 296, the domain is characterized as Jacalin-type lectin 2.
+At position 298 to 443, the domain is characterized as Jacalin-type lectin 3.
+At position 6 to 126, the domain is characterized as MSP.
+At position 122 to 269, the domain is characterized as Thioredoxin.
+At position 460 to 632, the domain is characterized as tr-type G.
+At position 69 to 263, the domain is characterized as ABC transmembrane type-1.
+At position 10 to 129, the domain is characterized as C-type lectin.
+At position 80 to 338, the domain is characterized as Protein kinase.
+At position 488 to 522, the domain is characterized as EF-hand 4.
+At position 826 to 999, the domain is characterized as Helicase ATP-binding.
+At position 1198 to 1379, the domain is characterized as Helicase C-terminal.
+At position 124 to 421, the domain is characterized as Protein kinase.
+At position 633 to 710, the domain is characterized as BRCT.
+At position 592 to 681, the domain is characterized as BRCT.
+At position 81 to 149, the domain is characterized as PA.
+At position 238 to 366, the domain is characterized as Cadherin 1.
+At position 367 to 483, the domain is characterized as Cadherin 2.
+At position 484 to 600, the domain is characterized as Cadherin 3.
+At position 601 to 708, the domain is characterized as Cadherin 4.
+At position 709 to 832, the domain is characterized as Cadherin 5.
+At position 547 to 757, the domain is characterized as DDHD.
+At position 171 to 363, the domain is characterized as CheB-type methylesterase.
+At position 105 to 193, the domain is characterized as CARD.
+At position 25 to 153, the domain is characterized as EamA.
+At position 16 to 154, the domain is characterized as CheW-like.
+At position 176 to 302, the domain is characterized as Response regulatory.
+At position 82 to 179, the domain is characterized as AD.
+At position 91 to 208, the domain is characterized as Rhodanese 1.
+At position 259 to 373, the domain is characterized as Rhodanese 2.
+At position 425 to 523, the domain is characterized as Fibronectin type-III.
+At position 166 to 344, the domain is characterized as Galectin.
+At position 301 to 402, the domain is characterized as PH.
+At position 428 to 621, the domain is characterized as Rho-GAP.
+At position 628 to 694, the domain is characterized as SH3.
+At position 13 to 155, the domain is characterized as Jacalin-type lectin 1.
+At position 240 to 382, the domain is characterized as Jacalin-type lectin 2.
+At position 438 to 583, the domain is characterized as Jacalin-type lectin 3.
+At position 299 to 431, the domain is characterized as N-acetyltransferase.
+At position 573 to 777, the domain is characterized as Rho-GAP.
+At position 809 to 1017, the domain is characterized as START.
+At position 95 to 171, the domain is characterized as BTB.
+At position 206 to 308, the domain is characterized as BACK.
+At position 36 to 113, the domain is characterized as Inhibitor I9.
+At position 127 to 405, the domain is characterized as Peptidase S8.
+At position 4 to 152, the domain is characterized as N-acetyltransferase.
+At position 199 to 325, the domain is characterized as FZ 1.
+At position 334 to 371, the domain is characterized as LDL-receptor class A 1.
+At position 371 to 407, the domain is characterized as LDL-receptor class A 2.
+At position 407 to 444, the domain is characterized as LDL-receptor class A 3.
+At position 444 to 481, the domain is characterized as LDL-receptor class A 4.
+At position 516 to 639, the domain is characterized as FZ 2.
+At position 645 to 681, the domain is characterized as LDL-receptor class A 5.
+At position 681 to 719, the domain is characterized as LDL-receptor class A 6.
+At position 720 to 756, the domain is characterized as LDL-receptor class A 7.
+At position 756 to 851, the domain is characterized as SRCR.
+At position 867 to 1100, the domain is characterized as Peptidase S1.
+At position 51 to 81, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 56 to 285, the domain is characterized as Radical SAM core.
+At position 4 to 330, the domain is characterized as Asparaginase/glutaminase.
+At position 107 to 355, the domain is characterized as Protein kinase.
+At position 44 to 127, the domain is characterized as RRM 1.
+At position 136 to 216, the domain is characterized as RRM 2.
+At position 429 to 507, the domain is characterized as RRM 3.
+At position 308 to 597, the domain is characterized as Asparagine synthetase.
+At position 50 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 534 to 582, the domain is characterized as GYF.
+At position 75 to 151, the domain is characterized as BTB.
+At position 190 to 290, the domain is characterized as BACK.
+At position 24 to 689, the domain is characterized as Vitellogenin.
+At position 1310 to 1479, the domain is characterized as VWFD.
+At position 20 to 60, the domain is characterized as EGF-like.
+At position 643 to 897, the domain is characterized as Protein kinase.
+At position 6 to 417, the domain is characterized as Helicase ATP-binding.
+At position 192 to 312, the domain is characterized as C2 1.
+At position 325 to 458, the domain is characterized as C2 2.
+At position 4 to 122, the domain is characterized as Response regulatory.
+At position 323 to 555, the domain is characterized as Peptidase S1 2.
+At position 590 to 808, the domain is characterized as Peptidase S1 3.
+At position 73 to 147, the domain is characterized as U-box.
+At position 133 to 199, the domain is characterized as Z-binding 1.
+At position 293 to 357, the domain is characterized as Z-binding 2.
+At position 503 to 571, the domain is characterized as DRBM 1.
+At position 614 to 682, the domain is characterized as DRBM 2.
+At position 726 to 794, the domain is characterized as DRBM 3.
+At position 886 to 1221, the domain is characterized as A to I editase.
+At position 120 to 242, the domain is characterized as MPN.
+At position 101 to 359, the domain is characterized as Protein kinase.
+At position 510 to 545, the domain is characterized as EF-hand 4.
+At position 899 to 1131, the domain is characterized as ABC transporter 1.
+At position 1912 to 2144, the domain is characterized as ABC transporter 2.
+At position 159 to 229, the domain is characterized as Sushi 3.
+At position 231 to 290, the domain is characterized as Sushi 4.
+At position 292 to 354, the domain is characterized as Sushi 5.
+At position 355 to 415, the domain is characterized as Sushi 6.
+At position 417 to 477, the domain is characterized as Sushi 7.
+At position 2196 to 2306, the domain is characterized as PH.
+At position 566 to 614, the domain is characterized as GYF.
+At position 1 to 324, the domain is characterized as Protein kinase.
+At position 87 to 137, the domain is characterized as DHHC.
+At position 201 to 260, the domain is characterized as SH3.
+At position 358 to 375, the domain is characterized as ITAM.
+At position 52 to 177, the domain is characterized as MSP.
+At position 164 to 250, the domain is characterized as PPIase FKBP-type.
+At position 30 to 179, the domain is characterized as Nudix hydrolase.
+At position 87 to 316, the domain is characterized as Radical SAM core.
+At position 93 to 276, the domain is characterized as ATP-grasp.
+At position 65 to 181, the domain is characterized as FZ.
+At position 257 to 292, the domain is characterized as EF-hand.
+At position 51 to 214, the domain is characterized as SIS.
+At position 228 to 486, the domain is characterized as CN hydrolase.
+At position 424 to 697, the domain is characterized as Protein kinase.
+At position 26 to 209, the domain is characterized as RNase H type-2.
+At position 161 to 202, the domain is characterized as JmjN.
+At position 226 to 316, the domain is characterized as ARID.
+At position 591 to 757, the domain is characterized as JmjC.
+At position 25 to 206, the domain is characterized as Laminin G-like 1.
+At position 196 to 234, the domain is characterized as EGF-like 1.
+At position 251 to 441, the domain is characterized as Laminin G-like 2.
+At position 448 to 641, the domain is characterized as Laminin G-like 3.
+At position 645 to 682, the domain is characterized as EGF-like 2.
+At position 687 to 881, the domain is characterized as Laminin G-like 4.
+At position 874 to 1049, the domain is characterized as Laminin G-like 5.
+At position 1052 to 1089, the domain is characterized as EGF-like 3.
+At position 1093 to 1291, the domain is characterized as Laminin G-like 6.
+At position 68 to 326, the domain is characterized as Protein kinase.
+At position 480 to 511, the domain is characterized as EF-hand 4.
+At position 161 to 522, the domain is characterized as PI3K/PI4K catalytic.
+At position 351 to 459, the domain is characterized as PX.
+At position 232 to 262, the domain is characterized as EF-hand 3.
+At position 5 to 162, the domain is characterized as N-acetyltransferase 1.
+At position 155 to 306, the domain is characterized as N-acetyltransferase 2.
+At position 1 to 219, the domain is characterized as MurNAc-LAA.
+At position 390 to 489, the domain is characterized as Ras-associating.
+At position 579 to 716, the domain is characterized as DAGKc.
+At position 32 to 117, the domain is characterized as Importin N-terminal.
+At position 415 to 558, the domain is characterized as RCK N-terminal.
+At position 24 to 244, the domain is characterized as ABC transporter.
+At position 1 to 133, the domain is characterized as PTS EIIC type-4.
+At position 108 to 149, the domain is characterized as JmjN.
+At position 293 to 454, the domain is characterized as JmjC.
+At position 11 to 65, the domain is characterized as bHLH.
+At position 86 to 153, the domain is characterized as PAS 1.
+At position 222 to 292, the domain is characterized as PAS 2.
+At position 296 to 340, the domain is characterized as PAC.
+At position 60 to 255, the domain is characterized as Helicase ATP-binding.
+At position 286 to 447, the domain is characterized as Helicase C-terminal.
+At position 390 to 592, the domain is characterized as B30.2/SPRY.
+At position 710 to 742, the domain is characterized as LisH.
+At position 769 to 826, the domain is characterized as CTLH.
+At position 19 to 299, the domain is characterized as ABC transmembrane type-1.
+At position 27 to 105, the domain is characterized as GIY-YIG.
+At position 1622 to 1713, the domain is characterized as Ig-like C2-type 3.
+At position 1718 to 1810, the domain is characterized as Ig-like C2-type 4.
+At position 1815 to 1907, the domain is characterized as Ig-like C2-type 5.
+At position 1915 to 2008, the domain is characterized as Ig-like C2-type 6.
+At position 2011 to 2109, the domain is characterized as Ig-like C2-type 7.
+At position 2115 to 2203, the domain is characterized as Ig-like C2-type 8.
+At position 2208 to 2305, the domain is characterized as Ig-like C2-type 9.
+At position 2311 to 2401, the domain is characterized as Ig-like C2-type 10.
+At position 2406 to 2492, the domain is characterized as Ig-like C2-type 11.
+At position 2502 to 2597, the domain is characterized as Ig-like C2-type 12.
+At position 30 to 206, the domain is characterized as EngB-type G.
+At position 4 to 126, the domain is characterized as VOC.
+At position 35 to 226, the domain is characterized as RNase H type-2.
+At position 18 to 116, the domain is characterized as Ig-like V-type.
+At position 139 to 224, the domain is characterized as Ig-like C2-type 1.
+At position 229 to 324, the domain is characterized as Ig-like C2-type 2.
+At position 6 to 140, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 112 to 237, the domain is characterized as EamA 1.
+At position 261 to 389, the domain is characterized as EamA 2.
+At position 197 to 311, the domain is characterized as SCP.
+At position 188 to 304, the domain is characterized as TFIIS central.
+At position 384 to 470, the domain is characterized as Disintegrin.
+At position 610 to 643, the domain is characterized as EGF-like.
+At position 7 to 73, the domain is characterized as HMA.
+At position 162 to 344, the domain is characterized as CheB-type methylesterase.
+At position 37 to 117, the domain is characterized as MANSC.
+At position 138 to 476, the domain is characterized as TTL.
+At position 9 to 65, the domain is characterized as WHEP-TRS.
+At position 111 to 232, the domain is characterized as Rhodanese.
+At position 502 to 878, the domain is characterized as Tyrosine-protein phosphatase.
+At position 27 to 158, the domain is characterized as Nudix hydrolase.
+At position 257 to 378, the domain is characterized as SET.
+At position 102 to 318, the domain is characterized as HD Cas3-type.
+At position 16 to 117, the domain is characterized as PilZ.
+At position 964 to 1122, the domain is characterized as MGS-like.
+At position 100 to 309, the domain is characterized as Lon N-terminal.
+At position 751 to 935, the domain is characterized as Lon proteolytic.
+At position 195 to 385, the domain is characterized as Reticulon.
+At position 314 to 357, the domain is characterized as LysM 3.
+At position 67 to 175, the domain is characterized as PA.
+At position 639 to 780, the domain is characterized as TIR.
+At position 288 to 324, the domain is characterized as DFDF.
+At position 40 to 109, the domain is characterized as POTRA.
+At position 97 to 342, the domain is characterized as Radical SAM core.
+At position 2 to 186, the domain is characterized as GMPS ATP-PPase.
+At position 306 to 559, the domain is characterized as START.
+At position 61 to 321, the domain is characterized as Protein kinase.
+At position 3 to 140, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 1974 to 2087, the domain is characterized as C2.
+At position 32 to 231, the domain is characterized as GH16.
+At position 19 to 120, the domain is characterized as Ig-like V-type.
+At position 79 to 160, the domain is characterized as GST N-terminal.
+At position 130 to 286, the domain is characterized as GST C-terminal.
+At position 120 to 207, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 323, the domain is characterized as Ig-like C2-type 3.
+At position 379 to 539, the domain is characterized as TIR.
+At position 123 to 169, the domain is characterized as F-box.
+At position 17 to 196, the domain is characterized as Guanylate kinase-like.
+At position 188 to 372, the domain is characterized as Glutamine amidotransferase type-1.
+At position 586 to 670, the domain is characterized as BRCT.
+At position 122 to 464, the domain is characterized as Protein kinase.
+At position 39 to 145, the domain is characterized as Expansin-like EG45.
+At position 159 to 240, the domain is characterized as Expansin-like CBD.
+At position 152 to 222, the domain is characterized as HAMP.
+At position 244 to 480, the domain is characterized as Methyl-accepting transducer.
+At position 26 to 69, the domain is characterized as LysM 1.
+At position 149 to 192, the domain is characterized as LysM 3.
+At position 217 to 334, the domain is characterized as NlpC/P60.
+At position 177 to 212, the domain is characterized as EF-hand 1.
+At position 264 to 299, the domain is characterized as EF-hand 2.
+At position 390 to 425, the domain is characterized as EF-hand 3.
+At position 210 to 276, the domain is characterized as KH.
+At position 142 to 389, the domain is characterized as Radical SAM core.
+At position 555 to 625, the domain is characterized as Dockerin.
+At position 345 to 398, the domain is characterized as bHLH.
+At position 49 to 113, the domain is characterized as Ricin B-type lectin.
+At position 171 to 219, the domain is characterized as Fibronectin type-II.
+At position 227 to 356, the domain is characterized as C-type lectin 1.
+At position 374 to 502, the domain is characterized as C-type lectin 2.
+At position 511 to 645, the domain is characterized as C-type lectin 3.
+At position 660 to 798, the domain is characterized as C-type lectin 4.
+At position 815 to 939, the domain is characterized as C-type lectin 5.
+At position 954 to 1098, the domain is characterized as C-type lectin 6.
+At position 1117 to 1231, the domain is characterized as C-type lectin 7.
+At position 1243 to 1376, the domain is characterized as C-type lectin 8.
+At position 217 to 332, the domain is characterized as C-type lectin.
+At position 486 to 658, the domain is characterized as tr-type G.
+At position 313 to 506, the domain is characterized as VWFA.
+At position 20 to 212, the domain is characterized as Albumin 1.
+At position 405 to 602, the domain is characterized as Albumin 3.
+At position 102 to 156, the domain is characterized as FHA.
+At position 313 to 495, the domain is characterized as VWFA.
+At position 28 to 96, the domain is characterized as KH type-2.
+At position 325 to 409, the domain is characterized as RRM 3.
+At position 477 to 582, the domain is characterized as RRM 4.
+At position 14 to 356, the domain is characterized as YjeF C-terminal.
+At position 19 to 102, the domain is characterized as SWIB/MDM2.
+At position 593 to 651, the domain is characterized as Kazal-like.
+At position 69 to 410, the domain is characterized as Kinesin motor.
+At position 598 to 676, the domain is characterized as BRCT.
+At position 276 to 531, the domain is characterized as Tyrosine-protein phosphatase.
+At position 77 to 507, the domain is characterized as PPM-type phosphatase.
+At position 20 to 168, the domain is characterized as Thioredoxin.
+At position 564 to 662, the domain is characterized as tRNA-binding.
+At position 514 to 691, the domain is characterized as PBS-linker 2.
+At position 63 to 317, the domain is characterized as Protein kinase.
+At position 318 to 385, the domain is characterized as AGC-kinase C-terminal.
+At position 58 to 166, the domain is characterized as PA.
+At position 414 to 464, the domain is characterized as EGF-like 1.
+At position 467 to 513, the domain is characterized as EGF-like 2.
+At position 514 to 556, the domain is characterized as EGF-like 3; calcium-binding.
+At position 29 to 141, the domain is characterized as sHSP.
+At position 4 to 99, the domain is characterized as KRAB.
+At position 2 to 160, the domain is characterized as DHFR.
+At position 1 to 105, the domain is characterized as WH1.
+At position 447 to 816, the domain is characterized as USP.
+At position 10 to 80, the domain is characterized as LCN-type CS-alpha/beta.
+At position 127 to 262, the domain is characterized as DAGKc.
+At position 142 to 252, the domain is characterized as PH.
+At position 427 to 571, the domain is characterized as PI-PLC X-box.
+At position 619 to 735, the domain is characterized as PI-PLC Y-box.
+At position 735 to 864, the domain is characterized as C2.
+At position 27 to 123, the domain is characterized as Glutaredoxin.
+At position 1105 to 1371, the domain is characterized as Autotransporter.
+At position 8 to 84, the domain is characterized as Tudor-knot.
+At position 184 to 356, the domain is characterized as MRG.
+At position 40 to 102, the domain is characterized as t-SNARE coiled-coil homology.
+At position 35 to 135, the domain is characterized as Plastocyanin-like.
+At position 372 to 564, the domain is characterized as DH.
+At position 620 to 720, the domain is characterized as PH.
+At position 66 to 98, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 109 to 138, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 49 to 334, the domain is characterized as Protein kinase.
+At position 45 to 130, the domain is characterized as RRM 1.
+At position 183 to 265, the domain is characterized as RRM 2.
+At position 32 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 152 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 231 to 328, the domain is characterized as Ig-like C2-type 3.
+At position 334 to 429, the domain is characterized as Ig-like C2-type 4.
+At position 430 to 550, the domain is characterized as Ig-like C2-type 5.
+At position 557 to 656, the domain is characterized as Ig-like C2-type 6.
+At position 662 to 748, the domain is characterized as Ig-like C2-type 7.
+At position 828 to 1158, the domain is characterized as Protein kinase.
+At position 637 to 785, the domain is characterized as PCI.
+At position 191 to 352, the domain is characterized as CRAL-TRIO.
+At position 53 to 150, the domain is characterized as HD.
+At position 398 to 459, the domain is characterized as TGS.
+At position 336 to 402, the domain is characterized as KH.
+At position 462 to 555, the domain is characterized as HD.
+At position 78 to 141, the domain is characterized as S5 DRBM.
+At position 156 to 376, the domain is characterized as VWFA.
+At position 8 to 215, the domain is characterized as ABC transporter.
+At position 1082 to 1132, the domain is characterized as GRIP.
+At position 68 to 300, the domain is characterized as Peptidase S1.
+At position 265 to 469, the domain is characterized as Helicase C-terminal.
+At position 364 to 432, the domain is characterized as S4 RNA-binding.
+At position 56 to 329, the domain is characterized as Dynamin-type G.
+At position 560 to 648, the domain is characterized as GED.
+At position 135 to 163, the domain is characterized as ITAM.
+At position 37 to 111, the domain is characterized as POTRA.
+At position 3 to 352, the domain is characterized as BRO1.
+At position 421 to 564, the domain is characterized as FH1.
+At position 589 to 979, the domain is characterized as FH2.
+At position 1007 to 1022, the domain is characterized as WH2.
+At position 4 to 81, the domain is characterized as GIY-YIG.
+At position 617 to 717, the domain is characterized as Fibronectin type-III 1.
+At position 1046 to 1143, the domain is characterized as Fibronectin type-III 2.
+At position 1443 to 1540, the domain is characterized as Fibronectin type-III 3.
+At position 1544 to 1658, the domain is characterized as Fibronectin type-III 4.
+At position 1665 to 1768, the domain is characterized as Fibronectin type-III 5.
+At position 1775 to 1881, the domain is characterized as Fibronectin type-III 6.
+At position 1966 to 2235, the domain is characterized as Protein kinase.
+At position 29 to 232, the domain is characterized as HORMA.
+At position 1507 to 1783, the domain is characterized as Dilute.
+At position 1076 to 1153, the domain is characterized as SH3.
+At position 1433 to 1758, the domain is characterized as PIPK.
+At position 660 to 766, the domain is characterized as PA.
+At position 7 to 130, the domain is characterized as PINc.
+At position 1245 to 1396, the domain is characterized as PINc.
+At position 9 to 45, the domain is characterized as ATP-grasp.
+At position 381 to 483, the domain is characterized as PDZ 1.
+At position 515 to 599, the domain is characterized as PDZ 2.
+At position 659 to 750, the domain is characterized as PDZ 3.
+At position 200 to 233, the domain is characterized as WW 1.
+At position 235 to 268, the domain is characterized as WW 2.
+At position 322 to 369, the domain is characterized as SARAH.
+At position 242 to 266, the domain is characterized as Myb-like 1.
+At position 268 to 320, the domain is characterized as Myb-like 2.
+At position 328 to 381, the domain is characterized as Myb-like 3.
+At position 70 to 248, the domain is characterized as Helicase ATP-binding.
+At position 262 to 429, the domain is characterized as Helicase C-terminal.
+At position 11 to 270, the domain is characterized as SET.
+At position 19 to 187, the domain is characterized as FAD-binding PCMH-type.
+At position 108 to 306, the domain is characterized as KARI N-terminal Rossmann.
+At position 307 to 455, the domain is characterized as KARI C-terminal knotted 1.
+At position 456 to 592, the domain is characterized as KARI C-terminal knotted 2.
+At position 119 to 230, the domain is characterized as C-type lectin.
+At position 210 to 291, the domain is characterized as SAND.
+At position 69 to 334, the domain is characterized as AB hydrolase-1.
+At position 84 to 274, the domain is characterized as B30.2/SPRY.
+At position 121 to 326, the domain is characterized as Histidine kinase.
+At position 16 to 75, the domain is characterized as KID.
+At position 266 to 317, the domain is characterized as bZIP.
+At position 471 to 722, the domain is characterized as STAS.
+At position 162 to 317, the domain is characterized as MARVEL 2.
+At position 7 to 135, the domain is characterized as CMP/dCMP-type deaminase.
+At position 31 to 148, the domain is characterized as Plastocyanin-like 1.
+At position 159 to 322, the domain is characterized as Plastocyanin-like 2.
+At position 425 to 563, the domain is characterized as Plastocyanin-like 3.
+At position 412 to 621, the domain is characterized as Histidine kinase.
+At position 149 to 184, the domain is characterized as PH.
+At position 175 to 473, the domain is characterized as Peptidase S8.
+At position 236 to 270, the domain is characterized as SAP.
+At position 460 to 911, the domain is characterized as USP.
+At position 23 to 286, the domain is characterized as PPM-type phosphatase.
+At position 116 to 258, the domain is characterized as DAGKc.
+At position 593 to 676, the domain is characterized as BRCT.
+At position 472 to 862, the domain is characterized as USP.
+At position 911 to 1079, the domain is characterized as Exonuclease.
+At position 1 to 368, the domain is characterized as SPX.
+At position 627 to 823, the domain is characterized as EXS.
+At position 134 to 368, the domain is characterized as Radical SAM core.
+At position 371 to 431, the domain is characterized as TRAM.
+At position 265 to 437, the domain is characterized as Helicase C-terminal.
+At position 165 to 478, the domain is characterized as NACHT.
+At position 24 to 276, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 141 to 328, the domain is characterized as JmjC.
+At position 7 to 68, the domain is characterized as PWWP.
+At position 80 to 147, the domain is characterized as RRM 1.
+At position 576 to 692, the domain is characterized as Calponin-homology (CH).
+At position 243 to 433, the domain is characterized as PCI.
+At position 406 to 541, the domain is characterized as STAS.
+At position 125 to 224, the domain is characterized as Fibronectin type-III.
+At position 334 to 406, the domain is characterized as Plastocyanin-like.
+At position 578 to 659, the domain is characterized as RWP-RK.
+At position 863 to 945, the domain is characterized as PB1.
+At position 228 to 434, the domain is characterized as Rab-GAP TBC.
+At position 39 to 112, the domain is characterized as S4 RNA-binding.
+At position 10 to 101, the domain is characterized as Core-binding (CB).
+At position 368 to 475, the domain is characterized as SEA.
+At position 176 to 280, the domain is characterized as Fe2OG dioxygenase.
+At position 38 to 104, the domain is characterized as CSD.
+At position 615 to 723, the domain is characterized as Cadherin 6.
+At position 79 to 133, the domain is characterized as bHLH.
+At position 238 to 337, the domain is characterized as CBM20.
+At position 49 to 278, the domain is characterized as Radical SAM core.
+At position 38 to 145, the domain is characterized as HTH La-type RNA-binding.
+At position 279 to 397, the domain is characterized as xRRM.
+At position 327 to 392, the domain is characterized as SAM.
+At position 5 to 229, the domain is characterized as ABC transporter.
+At position 60 to 228, the domain is characterized as 3'-5' exonuclease.
+At position 558 to 724, the domain is characterized as Helicase ATP-binding.
+At position 749 to 899, the domain is characterized as Helicase C-terminal.
+At position 1150 to 1229, the domain is characterized as HRDC.
+At position 383 to 672, the domain is characterized as Protein kinase.
+At position 31 to 100, the domain is characterized as S1 motif 1.
+At position 118 to 182, the domain is characterized as S1 motif 2.
+At position 196 to 264, the domain is characterized as S1 motif 3.
+At position 225 to 270, the domain is characterized as EGF-like 2; calcium-binding.
+At position 271 to 320, the domain is characterized as EGF-like 3; calcium-binding.
+At position 44 to 161, the domain is characterized as SEA.
+At position 22 to 214, the domain is characterized as PBC.
+At position 325 to 389, the domain is characterized as Ig-like C2-type 4.
+At position 423 to 476, the domain is characterized as Ig-like C2-type 5.
+At position 192 to 365, the domain is characterized as Helicase ATP-binding.
+At position 402 to 551, the domain is characterized as Helicase C-terminal.
+At position 557 to 752, the domain is characterized as SEC7.
+At position 215 to 300, the domain is characterized as KH.
+At position 341 to 433, the domain is characterized as HD.
+At position 15 to 296, the domain is characterized as Lon N-terminal.
+At position 773 to 987, the domain is characterized as Lon proteolytic.
+At position 22 to 327, the domain is characterized as PPM-type phosphatase.
+At position 230 to 405, the domain is characterized as EngA-type G 2.
+At position 406 to 490, the domain is characterized as KH-like.
+At position 25 to 163, the domain is characterized as FZ.
+At position 92 to 218, the domain is characterized as GST C-terminal.
+At position 111 to 357, the domain is characterized as PPM-type phosphatase.
+At position 7 to 204, the domain is characterized as DPCK.
+At position 80 to 126, the domain is characterized as F-box.
+At position 279 to 439, the domain is characterized as JmjC.
+At position 338 to 465, the domain is characterized as Ricin B-type lectin.
+At position 24 to 62, the domain is characterized as LRRNT.
+At position 336 to 388, the domain is characterized as LRRCT.
+At position 357 to 479, the domain is characterized as C2 1.
+At position 508 to 634, the domain is characterized as C2 2.
+At position 214 to 531, the domain is characterized as DOT1.
+At position 517 to 603, the domain is characterized as RWP-RK.
+At position 792 to 875, the domain is characterized as PB1.
+At position 18 to 398, the domain is characterized as ABC transmembrane type-1.
+At position 430 to 664, the domain is characterized as ABC transporter.
+At position 58 to 192, the domain is characterized as Cytochrome c 1.
+At position 185 to 270, the domain is characterized as Cytochrome c 2.
+At position 1 to 65, the domain is characterized as START.
+At position 5 to 121, the domain is characterized as WH1.
+At position 199 to 253, the domain is characterized as KBD.
+At position 299 to 407, the domain is characterized as SPR.
+At position 6 to 194, the domain is characterized as DhaL.
+At position 227 to 393, the domain is characterized as TrmE-type G.
+At position 117 to 459, the domain is characterized as Kinesin motor.
+At position 165 to 254, the domain is characterized as CS.
+At position 277 to 367, the domain is characterized as SGS.
+At position 301 to 506, the domain is characterized as MCM.
+At position 532 to 657, the domain is characterized as STAS.
+At position 47 to 121, the domain is characterized as PAS.
+At position 89 to 297, the domain is characterized as ABC transmembrane type-1.
+At position 166 to 259, the domain is characterized as RRM Nup35-type.
+At position 435 to 517, the domain is characterized as RRM.
+At position 27 to 134, the domain is characterized as EamA 1.
+At position 196 to 325, the domain is characterized as EamA 2.
+At position 137 to 359, the domain is characterized as GB1/RHD3-type G.
+At position 734 to 809, the domain is characterized as Carrier.
+At position 8 to 423, the domain is characterized as PTS EIIC type-3.
+At position 113 to 265, the domain is characterized as Exonuclease.
+At position 91 to 239, the domain is characterized as FAS1.
+At position 295 to 459, the domain is characterized as Hflx-type G.
+At position 17 to 51, the domain is characterized as WW.
+At position 189 to 363, the domain is characterized as Helicase ATP-binding.
+At position 205 to 331, the domain is characterized as C2.
+At position 46 to 80, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 494 to 765, the domain is characterized as Reverse transcriptase.
+At position 389 to 450, the domain is characterized as TRAM.
+At position 82 to 146, the domain is characterized as FHA.
+At position 176 to 238, the domain is characterized as Chromo.
+At position 210 to 389, the domain is characterized as Helicase ATP-binding.
+At position 422 to 566, the domain is characterized as Helicase C-terminal.
+At position 567 to 634, the domain is characterized as KH.
+At position 637 to 712, the domain is characterized as S1 motif.
+At position 21 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 132 to 230, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 343, the domain is characterized as Ig-like C2-type 3.
+At position 346 to 419, the domain is characterized as Ig-like C2-type 4.
+At position 430 to 530, the domain is characterized as Ig-like C2-type 5.
+At position 287 to 398, the domain is characterized as SCP2.
+At position 6 to 217, the domain is characterized as AIG1-type G.
+At position 19 to 141, the domain is characterized as Rhodanese.
+At position 178 to 319, the domain is characterized as Tyrosine-protein phosphatase.
+At position 185 to 382, the domain is characterized as Peptidase M12B.
+At position 396 to 485, the domain is characterized as Disintegrin.
+At position 633 to 667, the domain is characterized as EGF-like.
+At position 128 to 213, the domain is characterized as VPS37 C-terminal.
+At position 213 to 336, the domain is characterized as MsrB.
+At position 3 to 128, the domain is characterized as NTR.
+At position 462 to 836, the domain is characterized as USP.
+At position 888 to 1058, the domain is characterized as Exonuclease.
+At position 271 to 390, the domain is characterized as C2 1.
+At position 403 to 532, the domain is characterized as C2 2.
+At position 126 to 303, the domain is characterized as Prephenate dehydratase.
+At position 319 to 410, the domain is characterized as ACT.
+At position 426 to 592, the domain is characterized as Helicase C-terminal.
+At position 48 to 154, the domain is characterized as AB hydrolase-1.
+At position 23 to 85, the domain is characterized as HTH iclR-type.
+At position 100 to 272, the domain is characterized as IclR-ED.
+At position 293 to 421, the domain is characterized as DOD-type homing endonuclease.
+At position 145 to 240, the domain is characterized as Ig-like C2-type.
+At position 249 to 290, the domain is characterized as EGF-like.
+At position 31 to 170, the domain is characterized as C2.
+At position 371 to 406, the domain is characterized as PLD phosphodiesterase 1.
+At position 712 to 739, the domain is characterized as PLD phosphodiesterase 2.
+At position 148 to 225, the domain is characterized as Cache.
+At position 298 to 350, the domain is characterized as HAMP.
+At position 369 to 619, the domain is characterized as Methyl-accepting transducer.
+At position 8 to 146, the domain is characterized as TIR.
+At position 182 to 318, the domain is characterized as DBB.
+At position 315 to 452, the domain is characterized as ZU5.
+At position 652 to 722, the domain is characterized as SH3 2.
+At position 25 to 125, the domain is characterized as Ig-like V-type 1.
+At position 128 to 217, the domain is characterized as Ig-like V-type 2.
+At position 67 to 200, the domain is characterized as N-terminal Ras-GEF.
+At position 344 to 579, the domain is characterized as Ras-GEF.
+At position 52 to 142, the domain is characterized as CTCK.
+At position 537 to 612, the domain is characterized as Cytochrome b5 heme-binding.
+At position 637 to 751, the domain is characterized as FAD-binding FR-type.
+At position 171 to 276, the domain is characterized as Fe2OG dioxygenase.
+At position 173 to 234, the domain is characterized as PWWP.
+At position 15 to 132, the domain is characterized as Pru.
+At position 132 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 521 to 639, the domain is characterized as SMC hinge.
+At position 1 to 77, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 630 to 665, the domain is characterized as EF-hand.
+At position 413 to 490, the domain is characterized as Histone-fold.
+At position 612 to 729, the domain is characterized as Response regulatory.
+At position 949 to 1023, the domain is characterized as U-box.
+At position 14 to 264, the domain is characterized as CN hydrolase.
+At position 297 to 405, the domain is characterized as HIT.
+At position 1618 to 1902, the domain is characterized as Autotransporter.
+At position 10 to 116, the domain is characterized as FAD-binding FR-type.
+At position 264 to 351, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 146 to 175, the domain is characterized as IQ.
+At position 694 to 971, the domain is characterized as Protein kinase.
+At position 663 to 753, the domain is characterized as EH.
+At position 697 to 732, the domain is characterized as EF-hand.
+At position 122 to 342, the domain is characterized as VWFA.
+At position 571 to 657, the domain is characterized as BRCT.
+At position 1668 to 2104, the domain is characterized as DOCKER.
+At position 766 to 852, the domain is characterized as SUEL-type lectin.
+At position 209 to 382, the domain is characterized as Helicase ATP-binding.
+At position 10 to 235, the domain is characterized as ABC transporter.
+At position 94 to 352, the domain is characterized as Protein kinase.
+At position 395 to 430, the domain is characterized as EF-hand 1.
+At position 431 to 466, the domain is characterized as EF-hand 2.
+At position 467 to 502, the domain is characterized as EF-hand 3.
+At position 506 to 536, the domain is characterized as EF-hand 4.
+At position 485 to 662, the domain is characterized as DOD-type homing endonuclease.
+At position 100 to 175, the domain is characterized as RRM.
+At position 2 to 136, the domain is characterized as ENTH.
+At position 266 to 295, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 69 to 241, the domain is characterized as Helicase ATP-binding.
+At position 252 to 425, the domain is characterized as Helicase C-terminal.
+At position 39 to 121, the domain is characterized as Lipoyl-binding.
+At position 121 to 342, the domain is characterized as Radical SAM core.
+At position 496 to 551, the domain is characterized as Kazal-like.
+At position 642 to 805, the domain is characterized as Toprim.
+At position 1160 to 1287, the domain is characterized as DOD-type homing endonuclease.
+At position 89 to 226, the domain is characterized as GST C-terminal.
+At position 265 to 338, the domain is characterized as Myb-like.
+At position 157 to 229, the domain is characterized as MBD.
+At position 291 to 364, the domain is characterized as Pre-SET.
+At position 367 to 694, the domain is characterized as SET.
+At position 301 to 365, the domain is characterized as Ig-like C2-type 2.
+At position 391 to 504, the domain is characterized as PAZ.
+At position 688 to 989, the domain is characterized as Piwi.
+At position 230 to 569, the domain is characterized as SET.
+At position 653 to 702, the domain is characterized as Histone-fold.
+At position 18 to 116, the domain is characterized as SAND.
+At position 42 to 107, the domain is characterized as Inhibitor I9.
+At position 115 to 387, the domain is characterized as Peptidase S8.
+At position 145 to 288, the domain is characterized as FCP1 homology.
+At position 35 to 714, the domain is characterized as Myosin motor.
+At position 718 to 738, the domain is characterized as IQ 1.
+At position 739 to 764, the domain is characterized as IQ 2.
+At position 770 to 960, the domain is characterized as TH1.
+At position 1157 to 1219, the domain is characterized as SH3.
+At position 109 to 228, the domain is characterized as RGS.
+At position 87 to 150, the domain is characterized as S5 DRBM.
+At position 19 to 66, the domain is characterized as F-box; degenerate.
+At position 281 to 456, the domain is characterized as Helicase ATP-binding.
+At position 484 to 629, the domain is characterized as Helicase C-terminal.
+At position 5 to 147, the domain is characterized as PTS EIIA type-2.
+At position 92 to 180, the domain is characterized as RRM.
+At position 1846 to 1963, the domain is characterized as SET.
+At position 1969 to 1985, the domain is characterized as Post-SET.
+At position 340 to 433, the domain is characterized as HD.
+At position 190 to 385, the domain is characterized as Histidine kinase.
+At position 179 to 276, the domain is characterized as WGR.
+At position 301 to 419, the domain is characterized as PARP alpha-helical.
+At position 427 to 653, the domain is characterized as PARP catalytic.
+At position 72 to 514, the domain is characterized as Hexokinase 1.
+At position 520 to 962, the domain is characterized as Hexokinase 2.
+At position 56 to 391, the domain is characterized as Kinesin motor.
+At position 1 to 153, the domain is characterized as CID.
+At position 339 to 409, the domain is characterized as RRM.
+At position 168 to 409, the domain is characterized as Protein kinase.
+At position 6 to 89, the domain is characterized as Ig-like 1.
+At position 103 to 201, the domain is characterized as Ig-like 2.
+At position 205 to 305, the domain is characterized as Ig-like 3.
+At position 314 to 414, the domain is characterized as Ig-like 4.
+At position 16 to 128, the domain is characterized as HotDog ACOT-type.
+At position 190 to 241, the domain is characterized as LRRCT.
+At position 708 to 756, the domain is characterized as GPS.
+At position 227 to 311, the domain is characterized as Death.
+At position 229 to 323, the domain is characterized as RRM.
+At position 181 to 277, the domain is characterized as PH 1.
+At position 359 to 453, the domain is characterized as PH 2.
+At position 107 to 136, the domain is characterized as EF-hand 2.
+At position 137 to 172, the domain is characterized as EF-hand 3.
+At position 173 to 208, the domain is characterized as EF-hand 4.
+At position 65 to 164, the domain is characterized as PINc.
+At position 233 to 402, the domain is characterized as tr-type G.
+At position 16 to 237, the domain is characterized as ABC transporter.
+At position 56 to 148, the domain is characterized as CARD.
+At position 119 to 245, the domain is characterized as Thioredoxin.
+At position 212 to 588, the domain is characterized as GRAS.
+At position 1 to 91, the domain is characterized as PE.
+At position 739 to 828, the domain is characterized as EH.
+At position 590 to 771, the domain is characterized as Lon proteolytic.
+At position 540 to 749, the domain is characterized as Lon N-terminal.
+At position 302 to 356, the domain is characterized as bHLH.
+At position 19 to 126, the domain is characterized as HIT.
+At position 131 to 244, the domain is characterized as Calponin-homology (CH).
+At position 78 to 121, the domain is characterized as LysM 2.
+At position 46 to 170, the domain is characterized as C2.
+At position 324 to 856, the domain is characterized as PLA2c.
+At position 7 to 84, the domain is characterized as GIY-YIG.
+At position 28 to 238, the domain is characterized as DHFR.
+At position 595 to 719, the domain is characterized as C2 2.
+At position 1024 to 1168, the domain is characterized as MHD1.
+At position 1430 to 1557, the domain is characterized as C2 3.
+At position 35 to 192, the domain is characterized as FZ.
+At position 47 to 282, the domain is characterized as ABC transporter.
+At position 1 to 73, the domain is characterized as HIG1.
+At position 28 to 66, the domain is characterized as SMB.
+At position 285 to 433, the domain is characterized as AMOP.
+At position 445 to 639, the domain is characterized as VWFD.
+At position 723 to 780, the domain is characterized as Sushi.
+At position 131 to 181, the domain is characterized as DHHC.
+At position 436 to 577, the domain is characterized as Thioredoxin.
+At position 168 to 355, the domain is characterized as Reticulon.
+At position 413 to 634, the domain is characterized as B30.2/SPRY.
+At position 43 to 125, the domain is characterized as SCAN box.
+At position 178 to 355, the domain is characterized as EngA-type G 2.
+At position 865 to 1182, the domain is characterized as Protein kinase.
+At position 215 to 418, the domain is characterized as Rab-GAP TBC.
+At position 519 to 689, the domain is characterized as tr-type G.
+At position 1243 to 1508, the domain is characterized as Protein kinase.
+At position 1 to 108, the domain is characterized as Ig-like 1.
+At position 117 to 211, the domain is characterized as Ig-like 2.
+At position 225 to 286, the domain is characterized as KH 1.
+At position 319 to 380, the domain is characterized as KH 2.
+At position 187 to 292, the domain is characterized as PRD 1.
+At position 297 to 404, the domain is characterized as PRD 2.
+At position 409 to 500, the domain is characterized as PTS EIIB type-2.
+At position 510 to 648, the domain is characterized as PTS EIIA type-2.
+At position 114 to 311, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 75 to 104, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 114 to 143, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 66 to 254, the domain is characterized as BPL/LPL catalytic.
+At position 167 to 263, the domain is characterized as CRM 1.
+At position 371 to 468, the domain is characterized as CRM 2.
+At position 582 to 682, the domain is characterized as CRM 3.
+At position 20 to 217, the domain is characterized as GH11.
+At position 361 to 477, the domain is characterized as BRCT.
+At position 19 to 189, the domain is characterized as N-acetyltransferase.
+At position 123 to 298, the domain is characterized as Helicase ATP-binding.
+At position 386 to 556, the domain is characterized as tr-type G.
+At position 39 to 114, the domain is characterized as Lipoyl-binding.
+At position 184 to 221, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 50 to 209, the domain is characterized as SIS.
+At position 26 to 97, the domain is characterized as Ig-like.
+At position 228 to 485, the domain is characterized as GP-PDE.
+At position 2 to 175, the domain is characterized as Era-type G.
+At position 131 to 443, the domain is characterized as IF rod.
+At position 441 to 747, the domain is characterized as USP.
+At position 287 to 362, the domain is characterized as Rho RNA-BD.
+At position 156 to 199, the domain is characterized as UBA 1.
+At position 260 to 303, the domain is characterized as STI1.
+At position 342 to 382, the domain is characterized as UBA 2.
+At position 76 to 150, the domain is characterized as RRM 1.
+At position 166 to 244, the domain is characterized as RRM 2.
+At position 335 to 409, the domain is characterized as RRM 3.
+At position 5 to 149, the domain is characterized as PTS EIIA type-2.
+At position 172 to 267, the domain is characterized as PTS EIIB type-2.
+At position 301 to 635, the domain is characterized as PTS EIIC type-2.
+At position 178 to 400, the domain is characterized as Fibrinogen C-terminal.
+At position 249 to 653, the domain is characterized as PPM-type phosphatase.
+At position 38 to 139, the domain is characterized as SRCR 1.
+At position 166 to 272, the domain is characterized as SRCR 2.
+At position 293 to 393, the domain is characterized as SRCR 3.
+At position 403 to 511, the domain is characterized as SRCR 4.
+At position 409 to 470, the domain is characterized as LIM zinc-binding 1.
+At position 471 to 529, the domain is characterized as LIM zinc-binding 2.
+At position 530 to 601, the domain is characterized as LIM zinc-binding 3.
+At position 536 to 627, the domain is characterized as BRCT 2.
+At position 133 to 285, the domain is characterized as Thioredoxin 2.
+At position 2 to 65, the domain is characterized as SH3.
+At position 250 to 313, the domain is characterized as SAM.
+At position 698 to 808, the domain is characterized as PH.
+At position 62 to 220, the domain is characterized as TNase-like.
+At position 357 to 517, the domain is characterized as Helicase C-terminal.
+At position 21 to 139, the domain is characterized as DSCP-N.
+At position 178 to 201, the domain is characterized as Follistatin-like 1.
+At position 213 to 237, the domain is characterized as Follistatin-like 2.
+At position 272 to 295, the domain is characterized as Follistatin-like 3.
+At position 324 to 348, the domain is characterized as Follistatin-like 4.
+At position 368 to 391, the domain is characterized as Follistatin-like 5.
+At position 416 to 439, the domain is characterized as Follistatin-like 6.
+At position 121 to 481, the domain is characterized as PTS EIIC type-1.
+At position 510 to 614, the domain is characterized as PTS EIIA type-1.
+At position 4 to 167, the domain is characterized as N-acetyltransferase.
+At position 154 to 179, the domain is characterized as EF-hand 2.
+At position 230 to 414, the domain is characterized as Reverse transcriptase.
+At position 812 to 967, the domain is characterized as Integrase catalytic.
+At position 64 to 169, the domain is characterized as PRD 1.
+At position 170 to 280, the domain is characterized as PRD 2.
+At position 320 to 487, the domain is characterized as Helicase ATP-binding.
+At position 653 to 817, the domain is characterized as Helicase C-terminal.
+At position 770 to 1053, the domain is characterized as Protein kinase.
+At position 82 to 280, the domain is characterized as IF rod.
+At position 37 to 150, the domain is characterized as Plastocyanin-like 1.
+At position 414 to 550, the domain is characterized as Plastocyanin-like 3.
+At position 269 to 325, the domain is characterized as Collagen-like 1.
+At position 326 to 356, the domain is characterized as Collagen-like 2.
+At position 473 to 512, the domain is characterized as Collagen-like 5.
+At position 604 to 656, the domain is characterized as Collagen-like 6.
+At position 657 to 711, the domain is characterized as Collagen-like 7.
+At position 712 to 755, the domain is characterized as Collagen-like 8.
+At position 875 to 953, the domain is characterized as IPT/TIG.
+At position 1547 to 1576, the domain is characterized as IQ 1.
+At position 1577 to 1599, the domain is characterized as IQ 2.
+At position 1600 to 1622, the domain is characterized as IQ 3.
+At position 1393 to 1504, the domain is characterized as PH.
+At position 56 to 298, the domain is characterized as ABC transporter.
+At position 5 to 36, the domain is characterized as KOW.
+At position 876 to 1027, the domain is characterized as CBM3.
+At position 31 to 97, the domain is characterized as Chitin-binding type R&R.
+At position 259 to 321, the domain is characterized as t-SNARE coiled-coil homology.
+At position 253 to 341, the domain is characterized as Ig-like.
+At position 361 to 451, the domain is characterized as Fibronectin type-III.
+At position 35 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 145 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 328 to 404, the domain is characterized as Ig-like C2-type 4.
+At position 425 to 494, the domain is characterized as Ig-like C2-type 5.
+At position 500 to 592, the domain is characterized as Ig-like C2-type 6.
+At position 76 to 127, the domain is characterized as WAP 2.
+At position 450 to 563, the domain is characterized as xRRM.
+At position 46 to 109, the domain is characterized as KH 1.
+At position 119 to 185, the domain is characterized as KH 2.
+At position 297 to 362, the domain is characterized as Tudor.
+At position 208 to 347, the domain is characterized as Fe2OG dioxygenase.
+At position 292 to 361, the domain is characterized as Mop.
+At position 29 to 119, the domain is characterized as CTCK.
+At position 168 to 315, the domain is characterized as N-acetyltransferase.
+At position 415 to 486, the domain is characterized as Bromo.
+At position 323 to 472, the domain is characterized as Helicase C-terminal.
+At position 126 to 381, the domain is characterized as Protein kinase.
+At position 180 to 493, the domain is characterized as IF rod.
+At position 39 to 296, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 68 to 353, the domain is characterized as Protein kinase.
+At position 225 to 288, the domain is characterized as S5 DRBM.
+At position 14 to 190, the domain is characterized as N-acetyltransferase.
+At position 14 to 161, the domain is characterized as N-acetyltransferase.
+At position 27 to 77, the domain is characterized as F-box.
+At position 277 to 354, the domain is characterized as TFIIS N-terminal.
+At position 1093 to 1499, the domain is characterized as Histidine kinase.
+At position 1541 to 1656, the domain is characterized as Response regulatory 1.
+At position 2262 to 2383, the domain is characterized as Response regulatory 2.
+At position 144 to 214, the domain is characterized as S1 motif.
+At position 319 to 386, the domain is characterized as KH.
+At position 285 to 327, the domain is characterized as CCT.
+At position 12 to 280, the domain is characterized as F-BAR.
+At position 466 to 527, the domain is characterized as SH3 1.
+At position 544 to 607, the domain is characterized as SH3 2.
+At position 1 to 30, the domain is characterized as Chitin-binding type-1.
+At position 164 to 373, the domain is characterized as ATP-grasp.
+At position 58 to 204, the domain is characterized as Nudix hydrolase.
+At position 197 to 264, the domain is characterized as GRAM.
+At position 432 to 598, the domain is characterized as VASt.
+At position 853 to 1087, the domain is characterized as AIG1-type G.
+At position 42 to 219, the domain is characterized as BPL/LPL catalytic.
+At position 348 to 502, the domain is characterized as Helicase C-terminal.
+At position 59 to 162, the domain is characterized as FAD-binding FR-type.
+At position 871 to 1060, the domain is characterized as DH.
+At position 1089 to 1183, the domain is characterized as PH 1.
+At position 1333 to 1429, the domain is characterized as PH 2.
+At position 75 to 148, the domain is characterized as S1 motif.
+At position 57 to 128, the domain is characterized as KRAB.
+At position 53 to 315, the domain is characterized as Deacetylase sirtuin-type.
+At position 232 to 290, the domain is characterized as PWWP.
+At position 428 to 560, the domain is characterized as ADD.
+At position 581 to 859, the domain is characterized as SAM-dependent MTase C5-type.
+At position 586 to 665, the domain is characterized as BRCT.
+At position 2 to 40, the domain is characterized as ACB.
+At position 29 to 89, the domain is characterized as CBS 1.
+At position 115 to 177, the domain is characterized as CBS 2.
+At position 187 to 247, the domain is characterized as CBS 3.
+At position 262 to 319, the domain is characterized as CBS 4.
+At position 4 to 440, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 936 to 1228, the domain is characterized as PKS/mFAS DH.
+At position 2356 to 2431, the domain is characterized as Carrier.
+At position 274 to 584, the domain is characterized as UvrD-like helicase C-terminal.
+At position 231 to 309, the domain is characterized as Rho RNA-BD.
+At position 354 to 411, the domain is characterized as S4 RNA-binding.
+At position 4 to 74, the domain is characterized as MBD.
+At position 227 to 402, the domain is characterized as Helicase ATP-binding.
+At position 414 to 581, the domain is characterized as Helicase C-terminal.
+At position 23 to 103, the domain is characterized as GS beta-grasp.
+At position 110 to 361, the domain is characterized as GS catalytic.
+At position 68 to 281, the domain is characterized as Lon N-terminal.
+At position 687 to 878, the domain is characterized as Lon proteolytic.
+At position 19 to 339, the domain is characterized as GH10.
+At position 138 to 388, the domain is characterized as Radical SAM core.
+At position 359 to 775, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1256 to 1565, the domain is characterized as PKS/mFAS DH.
+At position 1610 to 1684, the domain is characterized as Carrier.
+At position 119 to 362, the domain is characterized as Radical SAM core.
+At position 167 to 227, the domain is characterized as S1 motif.
+At position 1 to 258, the domain is characterized as Peptidase S8.
+At position 176 to 239, the domain is characterized as SH3 1.
+At position 267 to 330, the domain is characterized as SH3 2.
+At position 156 to 220, the domain is characterized as Sushi 3.
+At position 221 to 280, the domain is characterized as Sushi 4.
+At position 281 to 347, the domain is characterized as Sushi 5.
+At position 348 to 413, the domain is characterized as Sushi 6.
+At position 454 to 511, the domain is characterized as Sushi 7.
+At position 453 to 619, the domain is characterized as Helicase ATP-binding.
+At position 751 to 912, the domain is characterized as Helicase C-terminal.
+At position 21 to 97, the domain is characterized as PDZ.
+At position 227 to 339, the domain is characterized as PID.
+At position 108 to 419, the domain is characterized as Peptidase A1.
+At position 31 to 356, the domain is characterized as G-alpha.
+At position 429 to 486, the domain is characterized as SH3.
+At position 4 to 196, the domain is characterized as Glutamine amidotransferase type-1.
+At position 246 to 342, the domain is characterized as RRM 1.
+At position 347 to 427, the domain is characterized as RRM 2.
+At position 464 to 544, the domain is characterized as RRM 3.
+At position 571 to 720, the domain is characterized as 6-Cys.
+At position 63 to 291, the domain is characterized as GB1/RHD3-type G.
+At position 136 to 393, the domain is characterized as Protein kinase.
+At position 394 to 464, the domain is characterized as AGC-kinase C-terminal.
+At position 119 to 274, the domain is characterized as RNase NYN.
+At position 104 to 256, the domain is characterized as Nudix hydrolase.
+At position 152 to 209, the domain is characterized as KH.
+At position 46 to 123, the domain is characterized as Biotinyl-binding.
+At position 43 to 146, the domain is characterized as Ig-like C2-type 1.
+At position 162 to 245, the domain is characterized as Ig-like C2-type 2.
+At position 156 to 208, the domain is characterized as bHLH.
+At position 8 to 108, the domain is characterized as Fibronectin type-III.
+At position 26 to 364, the domain is characterized as GH18 1.
+At position 372 to 727, the domain is characterized as GH18 2.
+At position 743 to 1067, the domain is characterized as GH18 3.
+At position 2 to 110, the domain is characterized as FAD-binding FR-type.
+At position 297 to 346, the domain is characterized as FBD.
+At position 93 to 186, the domain is characterized as PH.
+At position 361 to 497, the domain is characterized as DAGKc.
+At position 1878 to 1941, the domain is characterized as SAM.
+At position 486 to 653, the domain is characterized as tr-type G.
+At position 9 to 195, the domain is characterized as RNase H type-2.
+At position 202 to 426, the domain is characterized as Rab-GAP TBC.
+At position 726 to 1019, the domain is characterized as Peptidase S8.
+At position 159 to 471, the domain is characterized as Peptidase S8.
+At position 208 to 298, the domain is characterized as Death.
+At position 71 to 185, the domain is characterized as Expansin-like EG45.
+At position 195 to 279, the domain is characterized as Expansin-like CBD.
+At position 67 to 163, the domain is characterized as HTH araC/xylS-type.
+At position 79 to 248, the domain is characterized as PCI.
+At position 713 to 1001, the domain is characterized as ABC transmembrane type-1 2.
+At position 194 to 458, the domain is characterized as SF4 helicase.
+At position 7 to 83, the domain is characterized as KRAB.
+At position 29 to 608, the domain is characterized as Lipoxygenase.
+At position 412 to 576, the domain is characterized as Helicase ATP-binding.
+At position 601 to 774, the domain is characterized as Helicase C-terminal.
+At position 221 to 329, the domain is characterized as CUB 1.
+At position 331 to 390, the domain is characterized as Sushi 1.
+At position 392 to 502, the domain is characterized as CUB 2.
+At position 505 to 566, the domain is characterized as Sushi 2.
+At position 568 to 679, the domain is characterized as CUB 3.
+At position 683 to 742, the domain is characterized as Sushi 3.
+At position 744 to 807, the domain is characterized as Sushi 4.
+At position 811 to 872, the domain is characterized as Sushi 5.
+At position 25 to 105, the domain is characterized as BTB.
+At position 114 to 388, the domain is characterized as Peptidase S8.
+At position 1 to 110, the domain is characterized as N-acetyltransferase 1.
+At position 118 to 265, the domain is characterized as N-acetyltransferase 2.
+At position 338 to 479, the domain is characterized as DAGKc.
+At position 7 to 92, the domain is characterized as Acylphosphatase-like.
+At position 34 to 66, the domain is characterized as LisH.
+At position 87 to 341, the domain is characterized as Protein kinase.
+At position 342 to 397, the domain is characterized as AGC-kinase C-terminal.
+At position 66 to 326, the domain is characterized as PPM-type phosphatase.
+At position 16 to 129, the domain is characterized as C2.
+At position 156 to 191, the domain is characterized as EF-hand 1.
+At position 192 to 227, the domain is characterized as EF-hand 2.
+At position 2 to 24, the domain is characterized as LCN-type CS-alpha/beta.
+At position 10 to 130, the domain is characterized as MTTase N-terminal.
+At position 157 to 389, the domain is characterized as Radical SAM core.
+At position 392 to 454, the domain is characterized as TRAM.
+At position 7 to 355, the domain is characterized as Kinesin motor.
+At position 410 to 472, the domain is characterized as FHA.
+At position 365 to 643, the domain is characterized as Protein kinase.
+At position 22 to 130, the domain is characterized as HIT.
+At position 209 to 496, the domain is characterized as GT23.
+At position 505 to 566, the domain is characterized as SH3.
+At position 191 to 392, the domain is characterized as Galectin.
+At position 441 to 529, the domain is characterized as ABM.
+At position 88 to 212, the domain is characterized as VOC 1.
+At position 218 to 342, the domain is characterized as VOC 2.
+At position 93 to 282, the domain is characterized as ABC transmembrane type-1.
+At position 144 to 265, the domain is characterized as THUMP.
+At position 288 to 365, the domain is characterized as TGS.
+At position 95 to 320, the domain is characterized as ABC transmembrane type-1.
+At position 210 to 385, the domain is characterized as Helicase ATP-binding.
+At position 399 to 569, the domain is characterized as Helicase C-terminal.
+At position 21 to 175, the domain is characterized as CP-type G.
+At position 11 to 386, the domain is characterized as SAM-dependent MTase C5-type.
+At position 194 to 461, the domain is characterized as Protein kinase.
+At position 249 to 495, the domain is characterized as Protein kinase.
+At position 15 to 135, the domain is characterized as MTTase N-terminal.
+At position 163 to 395, the domain is characterized as Radical SAM core.
+At position 398 to 461, the domain is characterized as TRAM.
+At position 201 to 502, the domain is characterized as Protein kinase.
+At position 86 to 257, the domain is characterized as Helicase ATP-binding.
+At position 282 to 462, the domain is characterized as Helicase C-terminal.
+At position 243 to 416, the domain is characterized as Helicase ATP-binding.
+At position 464 to 666, the domain is characterized as Helicase C-terminal.
+At position 173 to 210, the domain is characterized as UBA.
+At position 90 to 139, the domain is characterized as bHLH.
+At position 16 to 113, the domain is characterized as SCP2.
+At position 17 to 162, the domain is characterized as Thioredoxin.
+At position 145 to 197, the domain is characterized as BSD.
+At position 366 to 469, the domain is characterized as SoHo.
+At position 793 to 852, the domain is characterized as SH3 1.
+At position 867 to 928, the domain is characterized as SH3 2.
+At position 1231 to 1292, the domain is characterized as SH3 3.
+At position 310 to 401, the domain is characterized as PKD 1.
+At position 877 to 934, the domain is characterized as Tudor 1.
+At position 935 to 991, the domain is characterized as Tudor 2.
+At position 13 to 246, the domain is characterized as ABC transporter.
+At position 429 to 826, the domain is characterized as G-alpha.
+At position 21 to 268, the domain is characterized as KaiC 1.
+At position 282 to 541, the domain is characterized as KaiC 2.
+At position 7 to 50, the domain is characterized as SMB 1.
+At position 51 to 95, the domain is characterized as SMB 2.
+At position 181 to 213, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 234 to 263, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 126 to 321, the domain is characterized as Peptidase M12A.
+At position 316 to 357, the domain is characterized as EGF-like.
+At position 367 to 481, the domain is characterized as CUB.
+At position 506 to 555, the domain is characterized as TSP type-1.
+At position 138 to 337, the domain is characterized as HIN-200.
+At position 54 to 355, the domain is characterized as AB hydrolase-1.
+At position 154 to 306, the domain is characterized as TRUD.
+At position 56 to 99, the domain is characterized as Inhibitor I9.
+At position 111 to 382, the domain is characterized as Peptidase S8.
+At position 13 to 77, the domain is characterized as HMA.
+At position 23 to 253, the domain is characterized as Radical SAM core.
+At position 611 to 644, the domain is characterized as EGF-like.
+At position 26 to 177, the domain is characterized as PPIase cyclophilin-type.
+At position 100 to 157, the domain is characterized as VWFC.
+At position 288 to 325, the domain is characterized as LRRNT.
+At position 105 to 230, the domain is characterized as OTU.
+At position 96 to 168, the domain is characterized as S4 RNA-binding.
+At position 19 to 279, the domain is characterized as Protein kinase.
+At position 297 to 328, the domain is characterized as NAF.
+At position 116 to 273, the domain is characterized as N-acetyltransferase.
+At position 141 to 165, the domain is characterized as KOW.
+At position 213 to 292, the domain is characterized as Peptidase A2.
+At position 374 to 414, the domain is characterized as UBA.
+At position 23 to 198, the domain is characterized as EngB-type G.
+At position 295 to 380, the domain is characterized as RCK C-terminal.
+At position 113 to 236, the domain is characterized as OmpA-like.
+At position 67 to 347, the domain is characterized as GH16.
+At position 360 to 642, the domain is characterized as Protein kinase.
+At position 137 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 47 to 337, the domain is characterized as PPM-type phosphatase.
+At position 366 to 466, the domain is characterized as Fibronectin type-III 1.
+At position 1797 to 1888, the domain is characterized as Fibronectin type-III 2.
+At position 1890 to 2006, the domain is characterized as Fibronectin type-III 3.
+At position 45 to 318, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 38 to 117, the domain is characterized as Tudor-knot.
+At position 284 to 553, the domain is characterized as MYST-type HAT.
+At position 17 to 128, the domain is characterized as MTTase N-terminal.
+At position 152 to 381, the domain is characterized as Radical SAM core.
+At position 384 to 450, the domain is characterized as TRAM.
+At position 69 to 212, the domain is characterized as N-acetyltransferase.
+At position 957 to 1106, the domain is characterized as MGS-like.
+At position 137 to 231, the domain is characterized as GS beta-grasp.
+At position 238 to 563, the domain is characterized as GS catalytic.
+At position 106 to 353, the domain is characterized as Deacetylase sirtuin-type.
+At position 160 to 377, the domain is characterized as TRUD.
+At position 63 to 310, the domain is characterized as Dynamin-type G.
+At position 118 to 372, the domain is characterized as ABC transporter 1.
+At position 813 to 1056, the domain is characterized as ABC transporter 2.
+At position 510 to 794, the domain is characterized as UvrD-like helicase C-terminal.
+At position 622 to 816, the domain is characterized as FtsK.
+At position 428 to 486, the domain is characterized as SH3.
+At position 491 to 786, the domain is characterized as UvrD-like helicase C-terminal.
+At position 425 to 560, the domain is characterized as GGDEF.
+At position 136 to 422, the domain is characterized as ABC transmembrane type-1.
+At position 457 to 696, the domain is characterized as ABC transporter.
+At position 158 to 309, the domain is characterized as VOC 2.
+At position 159 to 344, the domain is characterized as OBG-type G.
+At position 678 to 876, the domain is characterized as ATP-grasp 2.
+At position 957 to 1102, the domain is characterized as MGS-like.
+At position 148 to 267, the domain is characterized as C2 1.
+At position 279 to 400, the domain is characterized as C2 2.
+At position 559 to 605, the domain is characterized as EGF-like.
+At position 27 to 132, the domain is characterized as Plastocyanin-like.
+At position 258 to 320, the domain is characterized as CBS 1.
+At position 322 to 373, the domain is characterized as CBS 2.
+At position 91 to 289, the domain is characterized as Laminin G-like.
+At position 6 to 137, the domain is characterized as RNase III.
+At position 374 to 531, the domain is characterized as F5/8 type C.
+At position 497 to 572, the domain is characterized as Cytochrome b5 heme-binding.
+At position 606 to 718, the domain is characterized as FAD-binding FR-type.
+At position 11 to 434, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 616 to 926, the domain is characterized as PKS/mFAS DH.
+At position 1802 to 1879, the domain is characterized as Carrier.
+At position 48 to 344, the domain is characterized as Velvet.
+At position 169 to 268, the domain is characterized as PH.
+At position 13 to 45, the domain is characterized as LisH.
+At position 9 to 445, the domain is characterized as Helicase ATP-binding.
+At position 415 to 523, the domain is characterized as OCEL.
+At position 418 to 493, the domain is characterized as HSA.
+At position 957 to 1122, the domain is characterized as Helicase ATP-binding.
+At position 1510 to 1660, the domain is characterized as Helicase C-terminal.
+At position 40 to 162, the domain is characterized as tRNA-binding.
+At position 412 to 486, the domain is characterized as B5.
+At position 210 to 296, the domain is characterized as Ig-like C1-type.
+At position 347 to 462, the domain is characterized as C2.
+At position 488 to 591, the domain is characterized as PH.
+At position 891 to 1068, the domain is characterized as MHD1.
+At position 474 to 628, the domain is characterized as PPIase cyclophilin-type.
+At position 121 to 269, the domain is characterized as N-acetyltransferase.
+At position 147 to 352, the domain is characterized as ATP-grasp.
+At position 164 to 392, the domain is characterized as START.
+At position 347 to 431, the domain is characterized as Fibronectin type-III.
+At position 23 to 96, the domain is characterized as Importin N-terminal.
+At position 1217 to 1286, the domain is characterized as S1 motif.
+At position 1329 to 1440, the domain is characterized as SH2.
+At position 8 to 107, the domain is characterized as HTH araC/xylS-type.
+At position 131 to 307, the domain is characterized as Helicase ATP-binding.
+At position 656 to 748, the domain is characterized as Dicer dsRNA-binding fold.
+At position 932 to 1054, the domain is characterized as PAZ.
+At position 1083 to 1251, the domain is characterized as RNase III 1.
+At position 1292 to 1436, the domain is characterized as RNase III 2.
+At position 1462 to 1528, the domain is characterized as DRBM 1.
+At position 1621 to 1697, the domain is characterized as DRBM 2.
+At position 448 to 497, the domain is characterized as bHLH.
+At position 192 to 267, the domain is characterized as EMI.
+At position 1023 to 1059, the domain is characterized as EGF-like.
+At position 1078 to 1210, the domain is characterized as C1q.
+At position 192 to 464, the domain is characterized as Olfactomedin-like.
+At position 483 to 543, the domain is characterized as Kazal-like.
+At position 101 to 256, the domain is characterized as CP-type G.
+At position 5 to 358, the domain is characterized as Kinesin motor.
+At position 453 to 659, the domain is characterized as MCM.
+At position 47 to 134, the domain is characterized as BRCT.
+At position 423 to 664, the domain is characterized as UmuC.
+At position 50 to 292, the domain is characterized as ABC transporter.
+At position 295 to 542, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 31 to 93, the domain is characterized as t-SNARE coiled-coil homology.
+At position 272 to 373, the domain is characterized as Ig-like C2-type 2.
+At position 91 to 381, the domain is characterized as Radical SAM core.
+At position 405 to 557, the domain is characterized as N-acetyltransferase.
+At position 23 to 151, the domain is characterized as ENTH.
+At position 22 to 149, the domain is characterized as EamA.
+At position 1476 to 1511, the domain is characterized as EF-hand.
+At position 183 to 313, the domain is characterized as DOD-type homing endonuclease.
+At position 31 to 261, the domain is characterized as AB hydrolase-1.
+At position 39 to 138, the domain is characterized as Cadherin 1.
+At position 139 to 250, the domain is characterized as Cadherin 2.
+At position 251 to 357, the domain is characterized as Cadherin 3.
+At position 363 to 476, the domain is characterized as Cadherin 4.
+At position 477 to 580, the domain is characterized as Cadherin 5.
+At position 572 to 692, the domain is characterized as Cadherin 6.
+At position 60 to 138, the domain is characterized as RRM 1.
+At position 148 to 225, the domain is characterized as RRM 2.
+At position 241 to 318, the domain is characterized as RRM 3.
+At position 344 to 462, the domain is characterized as RRM 4.
+At position 657 to 734, the domain is characterized as PABC.
+At position 1112 to 1246, the domain is characterized as CKK.
+At position 218 to 400, the domain is characterized as GAF.
+At position 749 to 820, the domain is characterized as PAS 2.
+At position 14 to 100, the domain is characterized as MtN3/slv 1.
+At position 29 to 194, the domain is characterized as Laminin G-like.
+At position 288 to 327, the domain is characterized as EGF-like 1.
+At position 328 to 365, the domain is characterized as EGF-like 2; calcium-binding.
+At position 381 to 418, the domain is characterized as EGF-like 3; calcium-binding.
+At position 422 to 464, the domain is characterized as EGF-like 4.
+At position 733 to 947, the domain is characterized as TSP C-terminal.
+At position 1465 to 1690, the domain is characterized as Collagen IV NC1.
+At position 11 to 281, the domain is characterized as PTS EIID.
+At position 61 to 334, the domain is characterized as Pyruvate carboxyltransferase.
+At position 436 to 486, the domain is characterized as DHHC.
+At position 71 to 286, the domain is characterized as ABC transmembrane type-1.
+At position 29 to 199, the domain is characterized as Helicase ATP-binding.
+At position 209 to 379, the domain is characterized as Helicase C-terminal.
+At position 29 to 201, the domain is characterized as EngB-type G.
+At position 4 to 41, the domain is characterized as UBA-like.
+At position 58 to 291, the domain is characterized as DCUN1.
+At position 15 to 74, the domain is characterized as S4 RNA-binding.
+At position 60 to 212, the domain is characterized as Cytochrome c.
+At position 448 to 644, the domain is characterized as FtsK.
+At position 622 to 707, the domain is characterized as BRCT.
+At position 14 to 86, the domain is characterized as J.
+At position 1 to 187, the domain is characterized as ATP-grasp.
+At position 254 to 395, the domain is characterized as MGS-like.
+At position 43 to 157, the domain is characterized as THUMP.
+At position 407 to 667, the domain is characterized as Protein kinase.
+At position 668 to 736, the domain is characterized as AGC-kinase C-terminal.
+At position 237 to 467, the domain is characterized as Ku.
+At position 162 to 308, the domain is characterized as TRUD.
+At position 103 to 398, the domain is characterized as ABC transmembrane type-1.
+At position 432 to 673, the domain is characterized as ABC transporter.
+At position 929 to 1095, the domain is characterized as PNPLA.
+At position 5 to 218, the domain is characterized as Radical SAM core.
+At position 87 to 479, the domain is characterized as Kinesin motor.
+At position 102 to 277, the domain is characterized as Helicase ATP-binding.
+At position 303 to 461, the domain is characterized as Helicase C-terminal.
+At position 307 to 357, the domain is characterized as bHLH.
+At position 47 to 325, the domain is characterized as Pyruvate carboxyltransferase.
+At position 2 to 404, the domain is characterized as Rtt109-type HAT.
+At position 1 to 232, the domain is characterized as Autotransporter.
+At position 194 to 221, the domain is characterized as PLD phosphodiesterase 1.
+At position 409 to 435, the domain is characterized as PLD phosphodiesterase 2.
+At position 300 to 469, the domain is characterized as tr-type G.
+At position 413 to 596, the domain is characterized as Helicase ATP-binding.
+At position 630 to 777, the domain is characterized as Helicase C-terminal.
+At position 115 to 188, the domain is characterized as RRM 1.
+At position 206 to 277, the domain is characterized as RRM 2.
+At position 323 to 396, the domain is characterized as RRM 3.
+At position 414 to 485, the domain is characterized as RRM 4.
+At position 20 to 256, the domain is characterized as ABC transporter 1.
+At position 266 to 510, the domain is characterized as ABC transporter 2.
+At position 84 to 249, the domain is characterized as CP-type G.
+At position 12 to 333, the domain is characterized as Hcy-binding.
+At position 1 to 99, the domain is characterized as Glutamine amidotransferase type-1.
+At position 93 to 230, the domain is characterized as GST C-terminal.
+At position 22 to 60, the domain is characterized as Saposin A-type.
+At position 2 to 20, the domain is characterized as IGFBP N-terminal.
+At position 212 to 287, the domain is characterized as Thyroglobulin type-1.
+At position 1 to 282, the domain is characterized as FERM.
+At position 621 to 680, the domain is characterized as KH.
+At position 692 to 761, the domain is characterized as S1 motif.
+At position 30 to 74, the domain is characterized as Histone-fold.
+At position 74 to 167, the domain is characterized as Ig-like C2-type 1.
+At position 175 to 267, the domain is characterized as Ig-like C2-type 2.
+At position 377 to 660, the domain is characterized as Protein kinase.
+At position 903 to 1166, the domain is characterized as Protein kinase.
+At position 1169 to 1346, the domain is characterized as KEN.
+At position 193 to 526, the domain is characterized as Kinesin motor.
+At position 210 to 393, the domain is characterized as MIF4G.
+At position 501 to 617, the domain is characterized as MI.
+At position 18 to 266, the domain is characterized as Glutamine amidotransferase type-2.
+At position 600 to 676, the domain is characterized as BRCT.
+At position 34 to 248, the domain is characterized as Reverse transcriptase.
+At position 420 to 527, the domain is characterized as Rhodanese.
+At position 4 to 276, the domain is characterized as CheR-type methyltransferase.
+At position 20 to 157, the domain is characterized as TIR.
+At position 278 to 422, the domain is characterized as Helicase C-terminal.
+At position 15 to 120, the domain is characterized as Calponin-homology (CH).
+At position 139 to 200, the domain is characterized as LIM zinc-binding 1.
+At position 219 to 279, the domain is characterized as LIM zinc-binding 2.
+At position 373 to 435, the domain is characterized as LIM zinc-binding 3.
+At position 437 to 495, the domain is characterized as LIM zinc-binding 4.
+At position 519 to 579, the domain is characterized as LIM zinc-binding 5.
+At position 583 to 658, the domain is characterized as LIM zinc-binding 6.
+At position 216 to 383, the domain is characterized as TrmE-type G.
+At position 232 to 409, the domain is characterized as tr-type G.
+At position 114 to 191, the domain is characterized as DRBM.
+At position 1 to 102, the domain is characterized as FAD-binding FR-type.
+At position 214 to 274, the domain is characterized as KRAB.
+At position 47 to 93, the domain is characterized as RPE1 insert.
+At position 268 to 392, the domain is characterized as Cadherin 2.
+At position 393 to 497, the domain is characterized as Cadherin 3.
+At position 92 to 381, the domain is characterized as FAE.
+At position 234 to 332, the domain is characterized as PH.
+At position 658 to 793, the domain is characterized as GRAM 1.
+At position 881 to 948, the domain is characterized as GRAM 2.
+At position 77 to 174, the domain is characterized as HD.
+At position 418 to 479, the domain is characterized as TGS.
+At position 684 to 758, the domain is characterized as ACT.
+At position 809 to 934, the domain is characterized as DBINO.
+At position 1057 to 1229, the domain is characterized as Helicase ATP-binding.
+At position 1630 to 1789, the domain is characterized as Helicase C-terminal.
+At position 16 to 242, the domain is characterized as Radical SAM core.
+At position 4 to 86, the domain is characterized as GS beta-grasp.
+At position 89 to 329, the domain is characterized as GS catalytic.
+At position 1 to 148, the domain is characterized as CYTH.
+At position 739 to 810, the domain is characterized as MBD.
+At position 1087 to 1152, the domain is characterized as DDT.
+At position 2077 to 2147, the domain is characterized as Bromo.
+At position 21 to 250, the domain is characterized as Radical SAM core.
+At position 34 to 211, the domain is characterized as CP-type G.
+At position 42 to 159, the domain is characterized as Cytochrome c.
+At position 11 to 184, the domain is characterized as PITH.
+At position 24 to 127, the domain is characterized as Phytocyanin.
+At position 247 to 310, the domain is characterized as bZIP.
+At position 3 to 129, the domain is characterized as Thioredoxin.
+At position 149 to 358, the domain is characterized as ATP-grasp.
+At position 100 to 220, the domain is characterized as MTTase N-terminal.
+At position 244 to 512, the domain is characterized as Radical SAM core.
+At position 515 to 590, the domain is characterized as TRAM.
+At position 327 to 380, the domain is characterized as HAMP.
+At position 385 to 621, the domain is characterized as Methyl-accepting transducer.
+At position 199 to 388, the domain is characterized as CheB-type methylesterase.
+At position 29 to 90, the domain is characterized as PUB.
+At position 450 to 651, the domain is characterized as PAW.
+At position 726 to 964, the domain is characterized as NR LBD.
+At position 54 to 163, the domain is characterized as PH.
+At position 207 to 227, the domain is characterized as ELK.
+At position 5 to 53, the domain is characterized as F-box.
+At position 346 to 384, the domain is characterized as FBD.
+At position 965 to 1040, the domain is characterized as Carrier 1.
+At position 2006 to 2080, the domain is characterized as Carrier 2.
+At position 111 to 148, the domain is characterized as LRRNT.
+At position 271 to 346, the domain is characterized as PUA.
+At position 18 to 307, the domain is characterized as FERM.
+At position 60 to 437, the domain is characterized as YcaO.
+At position 27 to 300, the domain is characterized as Deacetylase sirtuin-type.
+At position 2 to 310, the domain is characterized as IF rod.
+At position 361 to 423, the domain is characterized as STI1.
+At position 39 to 493, the domain is characterized as Hexokinase.
+At position 42 to 265, the domain is characterized as Radical SAM core.
+At position 10 to 73, the domain is characterized as HMA.
+At position 9 to 355, the domain is characterized as Kinesin motor.
+At position 79 to 125, the domain is characterized as G-patch.
+At position 223 to 442, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 745 to 779, the domain is characterized as WW.
+At position 614 to 886, the domain is characterized as Protein kinase.
+At position 105 to 352, the domain is characterized as GS catalytic.
+At position 134 to 586, the domain is characterized as Urease.
+At position 189 to 217, the domain is characterized as STI1 1.
+At position 219 to 258, the domain is characterized as STI1 2.
+At position 589 to 635, the domain is characterized as UBA.
+At position 38 to 266, the domain is characterized as SET.
+At position 37 to 150, the domain is characterized as OmpA-like.
+At position 50 to 142, the domain is characterized as ARID.
+At position 32 to 303, the domain is characterized as EndoU.
+At position 193 to 421, the domain is characterized as NR LBD.
+At position 341 to 394, the domain is characterized as TSP type-1.
+At position 325 to 531, the domain is characterized as MCM.
+At position 264 to 421, the domain is characterized as SSD.
+At position 342 to 384, the domain is characterized as LRRCT.
+At position 127 to 162, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 237 to 264, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 127 to 423, the domain is characterized as NR LBD.
+At position 353 to 430, the domain is characterized as OCT.
+At position 169 to 403, the domain is characterized as Radical SAM core.
+At position 10 to 84, the domain is characterized as HTH HARE-type.
+At position 254 to 363, the domain is characterized as DEUBAD.
+At position 29 to 251, the domain is characterized as BPL/LPL catalytic.
+At position 15 to 117, the domain is characterized as LOB.
+At position 109 to 361, the domain is characterized as Protein kinase.
+At position 488 to 528, the domain is characterized as UBA.
+At position 1008 to 1057, the domain is characterized as KA1.
+At position 1090 to 1526, the domain is characterized as CBP/p300-type HAT.
+At position 297 to 322, the domain is characterized as NAF.
+At position 255 to 424, the domain is characterized as PCI.
+At position 822 to 1004, the domain is characterized as B30.2/SPRY 1.
+At position 1020 to 1209, the domain is characterized as B30.2/SPRY 2.
+At position 1481 to 1703, the domain is characterized as B30.2/SPRY 3.
+At position 1734 to 1798, the domain is characterized as SAM.
+At position 2115 to 2387, the domain is characterized as Protein kinase.
+At position 78 to 124, the domain is characterized as F-box; degenerate.
+At position 752 to 824, the domain is characterized as Bromo.
+At position 957 to 1039, the domain is characterized as NET.
+At position 529 to 629, the domain is characterized as tRNA-binding.
+At position 33 to 231, the domain is characterized as Eph LBD.
+At position 363 to 478, the domain is characterized as Fibronectin type-III 1.
+At position 479 to 574, the domain is characterized as Fibronectin type-III 2.
+At position 662 to 911, the domain is characterized as Protein kinase.
+At position 940 to 1004, the domain is characterized as SAM.
+At position 145 to 384, the domain is characterized as NR LBD.
+At position 144 to 356, the domain is characterized as NR LBD.
+At position 17 to 101, the domain is characterized as PDZ.
+At position 302 to 335, the domain is characterized as WW 1.
+At position 348 to 381, the domain is characterized as WW 2.
+At position 426 to 510, the domain is characterized as PDZ 1.
+At position 605 to 683, the domain is characterized as PDZ 2.
+At position 778 to 860, the domain is characterized as PDZ 3.
+At position 920 to 1010, the domain is characterized as PDZ 4.
+At position 1141 to 1223, the domain is characterized as PDZ 5.
+At position 28 to 658, the domain is characterized as Vitellogenin.
+At position 304 to 346, the domain is characterized as CUE.
+At position 153 to 225, the domain is characterized as PAS.
+At position 286 to 516, the domain is characterized as NR LBD.
+At position 196 to 354, the domain is characterized as Tyrosine-protein phosphatase.
+At position 85 to 174, the domain is characterized as GS beta-grasp.
+At position 179 to 615, the domain is characterized as GS catalytic.
+At position 39 to 230, the domain is characterized as RGSL.
+At position 414 to 603, the domain is characterized as DH.
+At position 645 to 758, the domain is characterized as PH.
+At position 525 to 587, the domain is characterized as R3H.
+At position 652 to 695, the domain is characterized as G-patch.
+At position 376 to 563, the domain is characterized as FtsK.
+At position 22 to 404, the domain is characterized as Lon N-terminal.
+At position 990 to 1241, the domain is characterized as Lon proteolytic.
+At position 61 to 172, the domain is characterized as Thioredoxin.
+At position 231 to 356, the domain is characterized as SEA 1.
+At position 735 to 848, the domain is characterized as SEA 2.
+At position 31 to 214, the domain is characterized as EngB-type G.
+At position 147 to 321, the domain is characterized as Helicase ATP-binding.
+At position 350 to 494, the domain is characterized as Helicase C-terminal.
+At position 32 to 165, the domain is characterized as MPN.
+At position 31 to 257, the domain is characterized as Peptidase S1.
+At position 1418 to 1453, the domain is characterized as EF-hand.
+At position 50 to 417, the domain is characterized as A to I editase.
+At position 302 to 589, the domain is characterized as Protein kinase.
+At position 42 to 101, the domain is characterized as SH3.
+At position 111 to 414, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 267 to 289, the domain is characterized as Follistatin-like 1.
+At position 335 to 359, the domain is characterized as Follistatin-like 2.
+At position 400 to 423, the domain is characterized as Follistatin-like 3.
+At position 430 to 452, the domain is characterized as Follistatin-like 4.
+At position 1 to 90, the domain is characterized as FAD-binding FR-type.
+At position 455 to 592, the domain is characterized as SIS 2.
+At position 27 to 364, the domain is characterized as Kinesin motor.
+At position 1418 to 1611, the domain is characterized as Calpain catalytic 1.
+At position 1706 to 2008, the domain is characterized as Calpain catalytic 2.
+At position 555 to 878, the domain is characterized as Piwi.
+At position 72 to 186, the domain is characterized as CUB.
+At position 187 to 285, the domain is characterized as LCCL.
+At position 292 to 449, the domain is characterized as F5/8 type C.
+At position 88 to 381, the domain is characterized as ABC transmembrane type-1 1.
+At position 414 to 649, the domain is characterized as ABC transporter 1.
+At position 836 to 1124, the domain is characterized as ABC transmembrane type-1 2.
+At position 1159 to 1396, the domain is characterized as ABC transporter 2.
+At position 51 to 159, the domain is characterized as C-type lectin.
+At position 102 to 163, the domain is characterized as LIM zinc-binding 2.
+At position 27 to 148, the domain is characterized as Thioredoxin.
+At position 20 to 51, the domain is characterized as LRRNT.
+At position 233 to 372, the domain is characterized as Ig-like.
+At position 312 to 490, the domain is characterized as 3'-5' exonuclease.
+At position 800 to 871, the domain is characterized as Olduvai 4.
+At position 872 to 963, the domain is characterized as Olduvai 5.
+At position 966 to 1021, the domain is characterized as Olduvai 6.
+At position 1022 to 1114, the domain is characterized as Olduvai 7.
+At position 1115 to 1207, the domain is characterized as Olduvai 8.
+At position 1210 to 1265, the domain is characterized as Olduvai 9.
+At position 1266 to 1358, the domain is characterized as Olduvai 10.
+At position 1359 to 1457, the domain is characterized as Olduvai 11.
+At position 21 to 235, the domain is characterized as ABC transporter.
+At position 110 to 299, the domain is characterized as ATP-grasp.
+At position 157 to 222, the domain is characterized as TGS.
+At position 446 to 493, the domain is characterized as SARAH.
+At position 88 to 269, the domain is characterized as Guanylate kinase-like.
+At position 53 to 304, the domain is characterized as PABS.
+At position 44 to 73, the domain is characterized as LRRNT.
+At position 371 to 425, the domain is characterized as LRRCT.
+At position 413 to 515, the domain is characterized as Ig-like C2-type.
+At position 1250 to 1437, the domain is characterized as Rho-GAP.
+At position 288 to 472, the domain is characterized as DH.
+At position 505 to 624, the domain is characterized as PH.
+At position 633 to 693, the domain is characterized as SH3.
+At position 29 to 163, the domain is characterized as TIR.
+At position 677 to 709, the domain is characterized as EGF-like.
+At position 612 to 698, the domain is characterized as BRCT.
+At position 161 to 221, the domain is characterized as HTH myb-type.
+At position 273 to 406, the domain is characterized as Nudix hydrolase.
+At position 99 to 366, the domain is characterized as Protein kinase.
+At position 461 to 572, the domain is characterized as PH.
+At position 32 to 88, the domain is characterized as F-box.
+At position 3 to 173, the domain is characterized as MurNAc-LAA.
+At position 307 to 390, the domain is characterized as Rho RNA-BD.
+At position 147 to 224, the domain is characterized as RRM.
+At position 448 to 615, the domain is characterized as tr-type G.
+At position 7 to 150, the domain is characterized as N-acetyltransferase 1.
+At position 152 to 301, the domain is characterized as N-acetyltransferase 2.
+At position 245 to 434, the domain is characterized as FAD-binding PCMH-type.
+At position 4 to 59, the domain is characterized as TIL.
+At position 118 to 166, the domain is characterized as Fibronectin type-II.
+At position 508 to 582, the domain is characterized as RRM.
+At position 10 to 104, the domain is characterized as Ig-like.
+At position 83 to 212, the domain is characterized as Helicase ATP-binding.
+At position 213 to 399, the domain is characterized as Helicase C-terminal.
+At position 179 to 373, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 342 to 397, the domain is characterized as MIR 1.
+At position 412 to 468, the domain is characterized as MIR 2.
+At position 474 to 534, the domain is characterized as MIR 3.
+At position 263 to 420, the domain is characterized as SSD.
+At position 698 to 761, the domain is characterized as KH 1.
+At position 775 to 839, the domain is characterized as KH 2.
+At position 19 to 74, the domain is characterized as HTH myb-type.
+At position 305 to 406, the domain is characterized as CS.
+At position 87 to 113, the domain is characterized as EF-hand.
+At position 31 to 522, the domain is characterized as Sema.
+At position 569 to 671, the domain is characterized as IPT/TIG 1.
+At position 684 to 767, the domain is characterized as IPT/TIG 2.
+At position 770 to 860, the domain is characterized as IPT/TIG 3.
+At position 1082 to 1345, the domain is characterized as Protein kinase.
+At position 33 to 185, the domain is characterized as N-acetyltransferase.
+At position 67 to 130, the domain is characterized as BTB.
+At position 224 to 307, the domain is characterized as NPH3.
+At position 489 to 547, the domain is characterized as PAP-associated.
+At position 113 to 281, the domain is characterized as CRAL-TRIO.
+At position 83 to 353, the domain is characterized as ABC transmembrane type-1 1.
+At position 424 to 645, the domain is characterized as ABC transporter 1.
+At position 860 to 1163, the domain is characterized as ABC transmembrane type-1 2.
+At position 4 to 140, the domain is characterized as HTH marR-type.
+At position 72 to 253, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 102 to 199, the domain is characterized as HD.
+At position 447 to 508, the domain is characterized as TGS.
+At position 711 to 785, the domain is characterized as ACT.
+At position 28 to 125, the domain is characterized as Ig-like V-type 1.
+At position 135 to 228, the domain is characterized as Ig-like V-type 2.
+At position 1417 to 1609, the domain is characterized as Calpain catalytic 1.
+At position 1703 to 2005, the domain is characterized as Calpain catalytic 2.
+At position 118 to 218, the domain is characterized as PB1.
+At position 205 to 389, the domain is characterized as Helicase ATP-binding.
+At position 416 to 567, the domain is characterized as Helicase C-terminal.
+At position 47 to 169, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 63 to 286, the domain is characterized as RNase H type-2.
+At position 319 to 659, the domain is characterized as PUM-HD.
+At position 97 to 407, the domain is characterized as ABC transmembrane type-1.
+At position 440 to 680, the domain is characterized as ABC transporter.
+At position 419 to 534, the domain is characterized as CBM21.
+At position 234 to 360, the domain is characterized as Sox C-terminal.
+At position 69 to 251, the domain is characterized as ABC transmembrane type-1.
+At position 13 to 152, the domain is characterized as Nudix hydrolase.
+At position 8 to 242, the domain is characterized as SET.
+At position 35 to 147, the domain is characterized as FAD-binding FR-type.
+At position 187 to 217, the domain is characterized as EGF-like 2.
+At position 218 to 249, the domain is characterized as EGF-like 3.
+At position 250 to 280, the domain is characterized as EGF-like 4.
+At position 281 to 311, the domain is characterized as EGF-like 5.
+At position 312 to 342, the domain is characterized as EGF-like 6.
+At position 343 to 373, the domain is characterized as EGF-like 7.
+At position 374 to 404, the domain is characterized as EGF-like 8.
+At position 405 to 435, the domain is characterized as EGF-like 9.
+At position 436 to 466, the domain is characterized as EGF-like 10.
+At position 467 to 497, the domain is characterized as EGF-like 11.
+At position 498 to 528, the domain is characterized as EGF-like 12.
+At position 529 to 559, the domain is characterized as EGF-like 13.
+At position 560 to 589, the domain is characterized as EGF-like 14.
+At position 590 to 620, the domain is characterized as EGF-like 15.
+At position 625 to 717, the domain is characterized as Fibronectin type-III 1.
+At position 718 to 801, the domain is characterized as Fibronectin type-III 2.
+At position 989 to 1075, the domain is characterized as Fibronectin type-III 5.
+At position 1076 to 1166, the domain is characterized as Fibronectin type-III 6.
+At position 1257 to 1346, the domain is characterized as Fibronectin type-III 8.
+At position 1347 to 1433, the domain is characterized as Fibronectin type-III 9.
+At position 1434 to 1522, the domain is characterized as Fibronectin type-III 10.
+At position 1520 to 1735, the domain is characterized as Fibrinogen C-terminal.
+At position 20 to 108, the domain is characterized as Acylphosphatase-like.
+At position 79 to 197, the domain is characterized as Response regulatory.
+At position 669 to 711, the domain is characterized as CCT.
+At position 38 to 296, the domain is characterized as Peptidase S1 1.
+At position 284 to 410, the domain is characterized as CUB 1.
+At position 419 to 531, the domain is characterized as CUB 2.
+At position 575 to 812, the domain is characterized as Peptidase S1 2.
+At position 846 to 957, the domain is characterized as CUB 3.
+At position 7 to 136, the domain is characterized as MATH.
+At position 160 to 227, the domain is characterized as BTB.
+At position 37 to 195, the domain is characterized as PPIase cyclophilin-type.
+At position 22 to 274, the domain is characterized as SET.
+At position 58 to 167, the domain is characterized as THUMP.
+At position 11 to 262, the domain is characterized as Pyruvate carboxyltransferase.
+At position 22 to 113, the domain is characterized as Ig-like C1-type.
+At position 62 to 252, the domain is characterized as TR mART core.
+At position 137 to 256, the domain is characterized as C2.
+At position 299 to 376, the domain is characterized as PDZ.
+At position 1073 to 1198, the domain is characterized as RGS.
+At position 135 to 202, the domain is characterized as PAS.
+At position 93 to 163, the domain is characterized as C-type lectin.
+At position 19 to 138, the domain is characterized as AB hydrolase-1.
+At position 8 to 45, the domain is characterized as Kazal-like.
+At position 254 to 365, the domain is characterized as TFIIS central.
+At position 351 to 429, the domain is characterized as PB1.
+At position 457 to 516, the domain is characterized as SH3 2.
+At position 14 to 82, the domain is characterized as HTH HARE-type.
+At position 67 to 248, the domain is characterized as NodB homology.
+At position 86 to 128, the domain is characterized as Agouti.
+At position 119 to 287, the domain is characterized as 3'-5' exonuclease.
+At position 350 to 436, the domain is characterized as HRDC.
+At position 496 to 619, the domain is characterized as HD.
+At position 848 to 922, the domain is characterized as ACT 2.
+At position 16 to 48, the domain is characterized as EF-hand 1.
+At position 607 to 685, the domain is characterized as BRCT.
+At position 155 to 337, the domain is characterized as FAD-binding PCMH-type.
+At position 336 to 531, the domain is characterized as SET.
+At position 8 to 171, the domain is characterized as N-acetyltransferase.
+At position 428 to 623, the domain is characterized as Thioredoxin.
+At position 637 to 727, the domain is characterized as Ras-associating.
+At position 1432 to 1709, the domain is characterized as PPM-type phosphatase.
+At position 1773 to 1910, the domain is characterized as Guanylate cyclase.
+At position 1027 to 1293, the domain is characterized as Protein kinase.
+At position 1296 to 1448, the domain is characterized as KEN.
+At position 1 to 264, the domain is characterized as BAR.
+At position 299 to 358, the domain is characterized as SH3.
+At position 95 to 324, the domain is characterized as ATP-grasp.
+At position 5 to 189, the domain is characterized as DhaL.
+At position 205 to 268, the domain is characterized as bZIP.
+At position 149 to 392, the domain is characterized as NR LBD.
+At position 309 to 423, the domain is characterized as PH.
+At position 771 to 976, the domain is characterized as VASt.
+At position 80 to 296, the domain is characterized as RNase H type-2.
+At position 103 to 135, the domain is characterized as LisH.
+At position 136 to 211, the domain is characterized as CTLH.
+At position 254 to 391, the domain is characterized as YTH.
+At position 58 to 164, the domain is characterized as PA.
+At position 412 to 462, the domain is characterized as EGF-like 1.
+At position 465 to 511, the domain is characterized as EGF-like 2.
+At position 145 to 407, the domain is characterized as Peptidase M66.
+At position 152 to 399, the domain is characterized as NR LBD.
+At position 185 to 378, the domain is characterized as Peptidase M12B.
+At position 388 to 476, the domain is characterized as Disintegrin.
+At position 623 to 657, the domain is characterized as EGF-like.
+At position 1335 to 1353, the domain is characterized as WH2.
+At position 521 to 785, the domain is characterized as Protein kinase.
+At position 118 to 302, the domain is characterized as FAD-binding PCMH-type.
+At position 1136 to 1283, the domain is characterized as SHD.
+At position 1287 to 1606, the domain is characterized as MHD.
+At position 264 to 662, the domain is characterized as PIPK.
+At position 18 to 107, the domain is characterized as CFEM.
+At position 217 to 270, the domain is characterized as CVC.
+At position 22 to 146, the domain is characterized as EamA 1.
+At position 182 to 308, the domain is characterized as EamA 2.
+At position 863 to 1023, the domain is characterized as VWFA.
+At position 126 to 270, the domain is characterized as JmjC.
+At position 81 to 208, the domain is characterized as PID.
+At position 130 to 228, the domain is characterized as Rhodanese.
+At position 306 to 693, the domain is characterized as GRAS.
+At position 8 to 101, the domain is characterized as KRAB.
+At position 124 to 222, the domain is characterized as PH.
+At position 1527 to 1851, the domain is characterized as Protein kinase.
+At position 1852 to 1911, the domain is characterized as AGC-kinase C-terminal.
+At position 245 to 602, the domain is characterized as PUM-HD.
+At position 7 to 54, the domain is characterized as F-box.
+At position 8 to 220, the domain is characterized as Radical SAM core.
+At position 371 to 725, the domain is characterized as Kinesin motor.
+At position 5 to 138, the domain is characterized as UBC core.
+At position 1523 to 1599, the domain is characterized as RRM.
+At position 404 to 432, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 442 to 473, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1025 to 1203, the domain is characterized as C2.
+At position 31 to 64, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 578 to 644, the domain is characterized as KH.
+At position 24 to 301, the domain is characterized as GH16.
+At position 313 to 453, the domain is characterized as Ricin B-type lectin.
+At position 37 to 89, the domain is characterized as Kazal-like.
+At position 92 to 158, the domain is characterized as Thyroglobulin type-1 1.
+At position 224 to 292, the domain is characterized as Thyroglobulin type-1 2.
+At position 359 to 394, the domain is characterized as EF-hand 1.
+At position 117 to 436, the domain is characterized as Protein kinase 1.
+At position 532 to 819, the domain is characterized as Protein kinase 2.
+At position 20 to 243, the domain is characterized as Peptidase S1.
+At position 203 to 265, the domain is characterized as t-SNARE coiled-coil homology.
+At position 183 to 406, the domain is characterized as Lon N-terminal.
+At position 871 to 1059, the domain is characterized as Lon proteolytic.
+At position 93 to 217, the domain is characterized as CRC.
+At position 8 to 66, the domain is characterized as Chromo.
+At position 64 to 206, the domain is characterized as VWFA.
+At position 4 to 108, the domain is characterized as HTH La-type RNA-binding.
+At position 116 to 193, the domain is characterized as RRM.
+At position 298 to 419, the domain is characterized as xRRM.
+At position 6 to 176, the domain is characterized as Era-type G.
+At position 207 to 283, the domain is characterized as KH type-2.
+At position 26 to 113, the domain is characterized as GS beta-grasp.
+At position 120 to 456, the domain is characterized as GS catalytic.
+At position 26 to 75, the domain is characterized as Clip.
+At position 113 to 368, the domain is characterized as Peptidase S1.
+At position 267 to 344, the domain is characterized as Sm.
+At position 24 to 248, the domain is characterized as L-type lectin-like.
+At position 211 to 276, the domain is characterized as SEP.
+At position 334 to 410, the domain is characterized as UBX.
+At position 24 to 68, the domain is characterized as F-box.
+At position 110 to 174, the domain is characterized as J.
+At position 36 to 102, the domain is characterized as PQ-loop 1.
+At position 186 to 251, the domain is characterized as PQ-loop 2.
+At position 159 to 345, the domain is characterized as OBG-type G.
+At position 524 to 543, the domain is characterized as WH2.
+At position 1 to 240, the domain is characterized as ABC transporter.
+At position 293 to 377, the domain is characterized as RCK C-terminal 2.
+At position 51 to 234, the domain is characterized as IRG-type G.
+At position 94 to 228, the domain is characterized as GST C-terminal.
+At position 456 to 582, the domain is characterized as PH 2.
+At position 629 to 743, the domain is characterized as N-terminal Ras-GEF.
+At position 49 to 276, the domain is characterized as Radical SAM core.
+At position 276 to 450, the domain is characterized as PCI.
+At position 69 to 226, the domain is characterized as Cupin type-1.
+At position 668 to 946, the domain is characterized as Autotransporter.
+At position 626 to 658, the domain is characterized as EGF-like.
+At position 84 to 207, the domain is characterized as HotDog ACOT-type 1.
+At position 287 to 399, the domain is characterized as HotDog ACOT-type 2.
+At position 11 to 98, the domain is characterized as MtN3/slv 1.
+At position 134 to 216, the domain is characterized as MtN3/slv 2.
+At position 299 to 602, the domain is characterized as ABC transmembrane type-1 1.
+At position 679 to 930, the domain is characterized as ABC transporter 1.
+At position 1013 to 1307, the domain is characterized as ABC transmembrane type-1 2.
+At position 1345 to 1579, the domain is characterized as ABC transporter 2.
+At position 1 to 31, the domain is characterized as Peptidase S1.
+At position 669 to 686, the domain is characterized as WH2.
+At position 151 to 211, the domain is characterized as Sushi.
+At position 10 to 133, the domain is characterized as BTB.
+At position 4 to 55, the domain is characterized as Myosin N-terminal SH3-like.
+At position 59 to 886, the domain is characterized as Myosin motor.
+At position 889 to 918, the domain is characterized as IQ 1.
+At position 912 to 941, the domain is characterized as IQ 2.
+At position 1389 to 1572, the domain is characterized as DH.
+At position 1603 to 1714, the domain is characterized as PH.
+At position 482 to 609, the domain is characterized as Guanylate cyclase.
+At position 87 to 233, the domain is characterized as PPC.
+At position 167 to 270, the domain is characterized as Fe2OG dioxygenase.
+At position 271 to 445, the domain is characterized as B30.2/SPRY.
+At position 22 to 117, the domain is characterized as EthD.
+At position 1 to 113, the domain is characterized as Calponin-homology (CH).
+At position 70 to 129, the domain is characterized as OVATE.
+At position 372 to 572, the domain is characterized as DhaL.
+At position 525 to 581, the domain is characterized as FHA.
+At position 1592 to 1690, the domain is characterized as PH.
+At position 220 to 407, the domain is characterized as Glutamine amidotransferase type-1.
+At position 168 to 245, the domain is characterized as RRM.
+At position 2 to 192, the domain is characterized as RNase H type-2.
+At position 41 to 352, the domain is characterized as AB hydrolase-1.
+At position 1 to 74, the domain is characterized as Protein kinase.
+At position 16 to 214, the domain is characterized as Lon N-terminal.
+At position 601 to 781, the domain is characterized as Lon proteolytic.
+At position 283 to 365, the domain is characterized as Death 2.
+At position 170 to 256, the domain is characterized as Toprim.
+At position 421 to 482, the domain is characterized as SH3.
+At position 7 to 203, the domain is characterized as Glutamine amidotransferase type-1.
+At position 204 to 391, the domain is characterized as GMPS ATP-PPase.
+At position 187 to 271, the domain is characterized as RCK C-terminal 1.
+At position 273 to 354, the domain is characterized as RCK C-terminal 2.
+At position 83 to 446, the domain is characterized as PRONE.
+At position 22 to 74, the domain is characterized as Chromo.
+At position 65 to 320, the domain is characterized as Protein kinase.
+At position 666 to 715, the domain is characterized as KA1.
+At position 176 to 277, the domain is characterized as Ig-like C2-type 2.
+At position 14 to 231, the domain is characterized as tr-type G.
+At position 164 to 242, the domain is characterized as Ig-like C2-type.
+At position 12 to 342, the domain is characterized as PTS EIIC type-2.
+At position 378 to 473, the domain is characterized as PTS EIIB type-2.
+At position 494 to 635, the domain is characterized as PTS EIIA type-2.
+At position 12 to 206, the domain is characterized as B30.2/SPRY.
+At position 4 to 151, the domain is characterized as 6-Cys 1.
+At position 152 to 294, the domain is characterized as 6-Cys 2.
+At position 237 to 319, the domain is characterized as Ig-like C2-type 2.
+At position 65 to 177, the domain is characterized as Thioredoxin.
+At position 190 to 339, the domain is characterized as GAF.
+At position 382 to 615, the domain is characterized as Histidine kinase.
+At position 641 to 760, the domain is characterized as Response regulatory.
+At position 69 to 211, the domain is characterized as HD.
+At position 202 to 367, the domain is characterized as Hflx-type G.
+At position 260 to 531, the domain is characterized as Dynamin-type G.
+At position 805 to 898, the domain is characterized as GED.
+At position 54 to 134, the domain is characterized as Cytochrome c 1.
+At position 164 to 242, the domain is characterized as Cytochrome c 2.
+At position 25 to 170, the domain is characterized as FAS1 1.
+At position 184 to 323, the domain is characterized as FAS1 2.
+At position 184 to 384, the domain is characterized as MAGE 1.
+At position 456 to 643, the domain is characterized as MAGE 2.
+At position 41 to 210, the domain is characterized as FAD-binding PCMH-type.
+At position 6 to 89, the domain is characterized as Toprim.
+At position 19 to 90, the domain is characterized as IGFBP N-terminal.
+At position 93 to 159, the domain is characterized as VWFC.
+At position 190 to 235, the domain is characterized as TSP type-1.
+At position 249 to 323, the domain is characterized as CTCK.
+At position 52 to 222, the domain is characterized as Helicase ATP-binding.
+At position 379 to 418, the domain is characterized as RPE3 insert.
+At position 33 to 283, the domain is characterized as GB1/RHD3-type G.
+At position 154 to 260, the domain is characterized as DOD-type homing endonuclease.
+At position 313 to 576, the domain is characterized as SF4 helicase.
+At position 106 to 225, the domain is characterized as FZ.
+At position 5 to 100, the domain is characterized as Ig-like.
+At position 46 to 114, the domain is characterized as POTRA.
+At position 1842 to 1905, the domain is characterized as SAM.
+At position 24 to 234, the domain is characterized as YjeF N-terminal.
+At position 54 to 467, the domain is characterized as USP.
+At position 11 to 40, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 105 to 411, the domain is characterized as Protein kinase.
+At position 189 to 420, the domain is characterized as GB1/RHD3-type G.
+At position 2 to 120, the domain is characterized as CMP/dCMP-type deaminase.
+At position 136 to 254, the domain is characterized as LTD.
+At position 6 to 120, the domain is characterized as Longin.
+At position 135 to 195, the domain is characterized as v-SNARE coiled-coil homology.
+At position 266 to 527, the domain is characterized as Protein kinase.
+At position 528 to 605, the domain is characterized as AGC-kinase C-terminal.
+At position 6 to 204, the domain is characterized as DHFR.
+At position 65 to 363, the domain is characterized as AB hydrolase-1.
+At position 24 to 190, the domain is characterized as FAD-binding PCMH-type.
+At position 122 to 149, the domain is characterized as HhH.
+At position 26 to 263, the domain is characterized as AB hydrolase-1.
+At position 28 to 157, the domain is characterized as GAF.
+At position 192 to 327, the domain is characterized as GGDEF.
+At position 335 to 587, the domain is characterized as EAL.
+At position 53 to 149, the domain is characterized as sHSP.
+At position 150 to 324, the domain is characterized as CRAL-TRIO.
+At position 257 to 322, the domain is characterized as HTH luxR-type.
+At position 259 to 455, the domain is characterized as B30.2/SPRY.
+At position 261 to 281, the domain is characterized as ELK.
+At position 57 to 367, the domain is characterized as tr-type G.
+At position 496 to 784, the domain is characterized as UvrD-like helicase C-terminal.
+At position 20 to 164, the domain is characterized as SprT-like.
+At position 7 to 327, the domain is characterized as DhaK.
+At position 368 to 570, the domain is characterized as DhaL.
+At position 329 to 497, the domain is characterized as tr-type G.
+At position 1 to 155, the domain is characterized as RPW8.
+At position 178 to 305, the domain is characterized as NB-ARC.
+At position 345 to 416, the domain is characterized as LIM zinc-binding.
+At position 82 to 123, the domain is characterized as Collagen-like.
+At position 124 to 263, the domain is characterized as C1q.
+At position 116 to 156, the domain is characterized as EGF-like 1.
+At position 164 to 201, the domain is characterized as EGF-like 2.
+At position 203 to 244, the domain is characterized as EGF-like 3.
+At position 245 to 284, the domain is characterized as EGF-like 4.
+At position 330 to 370, the domain is characterized as EGF-like 5.
+At position 379 to 512, the domain is characterized as FAS1 1.
+At position 522 to 659, the domain is characterized as FAS1 2.
+At position 743 to 783, the domain is characterized as EGF-like 6.
+At position 833 to 873, the domain is characterized as EGF-like 7.
+At position 874 to 917, the domain is characterized as EGF-like 8.
+At position 918 to 960, the domain is characterized as EGF-like 9.
+At position 961 to 1002, the domain is characterized as EGF-like 10.
+At position 1002 to 1135, the domain is characterized as FAS1 3.
+At position 1145 to 1273, the domain is characterized as FAS1 4.
+At position 1350 to 1415, the domain is characterized as Laminin EGF-like 1.
+At position 1439 to 1477, the domain is characterized as EGF-like 11.
+At position 1478 to 1519, the domain is characterized as EGF-like 12.
+At position 1520 to 1561, the domain is characterized as EGF-like 13.
+At position 1562 to 1603, the domain is characterized as EGF-like 14.
+At position 1603 to 1731, the domain is characterized as FAS1 5.
+At position 1747 to 1888, the domain is characterized as FAS1 6.
+At position 1965 to 2030, the domain is characterized as Laminin EGF-like 2.
+At position 2055 to 2089, the domain is characterized as EGF-like 15.
+At position 2090 to 2130, the domain is characterized as EGF-like 16.
+At position 2131 to 2173, the domain is characterized as EGF-like 17.
+At position 2206 to 2298, the domain is characterized as Link.
+At position 2318 to 2452, the domain is characterized as FAS1 7.
+At position 86 to 298, the domain is characterized as RNase H type-2.
+At position 107 to 402, the domain is characterized as AB hydrolase-1.
+At position 58 to 216, the domain is characterized as TNase-like.
+At position 81 to 256, the domain is characterized as Helicase ATP-binding.
+At position 268 to 429, the domain is characterized as Helicase C-terminal.
+At position 16 to 140, the domain is characterized as EamA 1.
+At position 162 to 288, the domain is characterized as EamA 2.
+At position 98 to 170, the domain is characterized as J.
+At position 221 to 488, the domain is characterized as Protein kinase.
+At position 4 to 264, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 224 to 271, the domain is characterized as F-box.
+At position 80 to 230, the domain is characterized as PPC.
+At position 436 to 512, the domain is characterized as SH3.
+At position 99 to 199, the domain is characterized as HD.
+At position 506 to 537, the domain is characterized as EF-hand 2.
+At position 415 to 457, the domain is characterized as Chitin-binding type-3.
+At position 297 to 430, the domain is characterized as Tyrosine-protein phosphatase.
+At position 62 to 109, the domain is characterized as F-box.
+At position 109 to 244, the domain is characterized as SGF29 C-terminal.
+At position 54 to 269, the domain is characterized as Radical SAM core.
+At position 59 to 319, the domain is characterized as PPM-type phosphatase.
+At position 407 to 841, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1335 to 1643, the domain is characterized as PKS/mFAS DH.
+At position 1704 to 1781, the domain is characterized as Carrier.
+At position 22 to 122, the domain is characterized as PH.
+At position 300 to 380, the domain is characterized as PDZ.
+At position 126 to 233, the domain is characterized as C-type lectin.
+At position 167 to 339, the domain is characterized as OBG-type G.
+At position 72 to 263, the domain is characterized as ABC transmembrane type-1.
+At position 850 to 927, the domain is characterized as ACT 2.
+At position 24 to 143, the domain is characterized as Barwin.
+At position 112 to 225, the domain is characterized as RGS 1.
+At position 240 to 359, the domain is characterized as RGS 2.
+At position 142 to 179, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 61 to 287, the domain is characterized as RNase H type-2.
+At position 83 to 145, the domain is characterized as S4 RNA-binding.
+At position 451 to 509, the domain is characterized as SH3.
+At position 19 to 303, the domain is characterized as ABC transmembrane type-1.
+At position 288 to 564, the domain is characterized as Clu.
+At position 165 to 418, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1078 to 1195, the domain is characterized as SET.
+At position 1204 to 1220, the domain is characterized as Post-SET.
+At position 16 to 133, the domain is characterized as MSP.
+At position 48 to 123, the domain is characterized as Carrier.
+At position 48 to 159, the domain is characterized as tRNA-binding.
+At position 411 to 492, the domain is characterized as B5.
+At position 740 to 833, the domain is characterized as FDX-ACB.
+At position 1 to 103, the domain is characterized as tr-type G.
+At position 37 to 132, the domain is characterized as RRM 1.
+At position 223 to 307, the domain is characterized as RRM 2.
+At position 780 to 826, the domain is characterized as G-patch.
+At position 432 to 542, the domain is characterized as STAS.
+At position 311 to 664, the domain is characterized as Kinesin motor.
+At position 8 to 110, the domain is characterized as tRNA-binding.
+At position 306 to 603, the domain is characterized as Protein kinase.
+At position 759 to 779, the domain is characterized as IQ 1.
+At position 72 to 108, the domain is characterized as EGF-like.
+At position 115 to 364, the domain is characterized as ZP.
+At position 12 to 131, the domain is characterized as DMAP1-binding.
+At position 317 to 623, the domain is characterized as Protein kinase.
+At position 1 to 111, the domain is characterized as N-acetyltransferase.
+At position 23 to 314, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 38 to 88, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 201 to 218, the domain is characterized as R.
+At position 147 to 419, the domain is characterized as Collagen-like.
+At position 424 to 519, the domain is characterized as SRCR.
+At position 55 to 162, the domain is characterized as Calponin-homology (CH).
+At position 180 to 382, the domain is characterized as Histidine kinase.
+At position 448 to 585, the domain is characterized as Thioredoxin.
+At position 1 to 135, the domain is characterized as SAM-dependent MTase C5-type.
+At position 192 to 389, the domain is characterized as ATP-grasp.
+At position 154 to 206, the domain is characterized as bHLH.
+At position 90 to 157, the domain is characterized as BTB.
+At position 192 to 294, the domain is characterized as BACK.
+At position 16 to 144, the domain is characterized as C-type lysozyme.
+At position 271 to 510, the domain is characterized as Peptidase M12B.
+At position 519 to 608, the domain is characterized as Disintegrin.
+At position 43 to 307, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 190 to 228, the domain is characterized as F-box.
+At position 52 to 83, the domain is characterized as EF-hand 2.
+At position 15 to 73, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 120 to 259, the domain is characterized as B12-binding.
+At position 32 to 109, the domain is characterized as RRM.
+At position 237 to 383, the domain is characterized as Helicase C-terminal.
+At position 48 to 313, the domain is characterized as Septin-type G.
+At position 231 to 501, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 167 to 239, the domain is characterized as AWS.
+At position 241 to 358, the domain is characterized as SET.
+At position 365 to 381, the domain is characterized as Post-SET.
+At position 630 to 661, the domain is characterized as WW.
+At position 40 to 276, the domain is characterized as Peptidase S1.
+At position 168 to 268, the domain is characterized as PH.
+At position 169 to 253, the domain is characterized as CTCK.
+At position 266 to 415, the domain is characterized as Helicase C-terminal.
+At position 168 to 353, the domain is characterized as NodB homology.
+At position 52 to 108, the domain is characterized as WHEP-TRS.
+At position 391 to 592, the domain is characterized as ERCC4.
+At position 141 to 340, the domain is characterized as PNPLA.
+At position 44 to 189, the domain is characterized as N-acetyltransferase.
+At position 30 to 313, the domain is characterized as ABC transmembrane type-1.
+At position 7 to 20, the domain is characterized as Peptidase M12B.
+At position 1211 to 1316, the domain is characterized as Calponin-homology (CH).
+At position 1542 to 1694, the domain is characterized as bMERB.
+At position 109 to 285, the domain is characterized as Helicase ATP-binding.
+At position 316 to 462, the domain is characterized as Helicase C-terminal.
+At position 52 to 289, the domain is characterized as Zn-dependent PLC.
+At position 205 to 390, the domain is characterized as Reverse transcriptase.
+At position 797 to 956, the domain is characterized as Integrase catalytic.
+At position 2 to 88, the domain is characterized as RRM 1.
+At position 488 to 560, the domain is characterized as RRM 3.
+At position 612 to 695, the domain is characterized as RRM 4.
+At position 712 to 789, the domain is characterized as RRM 5.
+At position 452 to 685, the domain is characterized as NR LBD.
+At position 192 to 216, the domain is characterized as HhH.
+At position 34 to 201, the domain is characterized as Helicase ATP-binding.
+At position 233 to 435, the domain is characterized as Helicase C-terminal.
+At position 156 to 288, the domain is characterized as Ricin B-type lectin 2.
+At position 24 to 154, the domain is characterized as Ig-like.
+At position 34 to 88, the domain is characterized as TIL.
+At position 86 to 348, the domain is characterized as Protein kinase.
+At position 349 to 411, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 270, the domain is characterized as Protein kinase.
+At position 65 to 342, the domain is characterized as Protein kinase.
+At position 5 to 188, the domain is characterized as tr-type G.
+At position 1 to 266, the domain is characterized as SMP-LTD.
+At position 8 to 75, the domain is characterized as J.
+At position 249 to 284, the domain is characterized as DMA.
+At position 158 to 262, the domain is characterized as Fe2OG dioxygenase.
+At position 20 to 170, the domain is characterized as NAC.
+At position 21 to 174, the domain is characterized as N-acetyltransferase.
+At position 1220 to 1384, the domain is characterized as PNPLA.
+At position 105 to 285, the domain is characterized as UmuC.
+At position 225 to 501, the domain is characterized as CN hydrolase.
+At position 2 to 455, the domain is characterized as ADPK.
+At position 216 to 480, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 235 to 361, the domain is characterized as Sox C-terminal.
+At position 415 to 576, the domain is characterized as Miro 2.
+At position 180 to 228, the domain is characterized as LRRCT.
+At position 315 to 401, the domain is characterized as Ig-like C2-type 1.
+At position 408 to 495, the domain is characterized as Ig-like C2-type 2.
+At position 26 to 151, the domain is characterized as AB hydrolase-1.
+At position 1 to 162, the domain is characterized as PPIase cyclophilin-type.
+At position 64 to 148, the domain is characterized as Cadherin 1.
+At position 156 to 258, the domain is characterized as Cadherin 2.
+At position 259 to 416, the domain is characterized as Cadherin 3.
+At position 417 to 527, the domain is characterized as Cadherin 4.
+At position 48 to 162, the domain is characterized as Expansin-like EG45.
+At position 172 to 251, the domain is characterized as Expansin-like CBD.
+At position 18 to 261, the domain is characterized as ABC transporter.
+At position 23 to 214, the domain is characterized as DH.
+At position 245 to 361, the domain is characterized as PH.
+At position 390 to 464, the domain is characterized as DEP 1.
+At position 491 to 566, the domain is characterized as DEP 2.
+At position 592 to 671, the domain is characterized as PDZ 1.
+At position 677 to 754, the domain is characterized as PDZ 2.
+At position 234 to 269, the domain is characterized as DMA.
+At position 623 to 723, the domain is characterized as tRNA-binding.
+At position 85 to 400, the domain is characterized as Peptidase A1.
+At position 4 to 214, the domain is characterized as ABC transporter.
+At position 36 to 157, the domain is characterized as MPN.
+At position 69 to 468, the domain is characterized as AB hydrolase-1.
+At position 78 to 563, the domain is characterized as Protein kinase.
+At position 63 to 115, the domain is characterized as SANT.
+At position 357 to 445, the domain is characterized as SWIRM.
+At position 459 to 645, the domain is characterized as PID.
+At position 658 to 744, the domain is characterized as PDZ 1.
+At position 749 to 824, the domain is characterized as PDZ 2.
+At position 12 to 299, the domain is characterized as YjeF C-terminal.
+At position 128 to 199, the domain is characterized as RRM.
+At position 1368 to 1485, the domain is characterized as SET.
+At position 1491 to 1507, the domain is characterized as Post-SET.
+At position 974 to 1024, the domain is characterized as AWS.
+At position 1026 to 1143, the domain is characterized as SET.
+At position 1151 to 1167, the domain is characterized as Post-SET.
+At position 27 to 252, the domain is characterized as Peptidase S1.
+At position 1181 to 1496, the domain is characterized as Dilute.
+At position 92 to 127, the domain is characterized as QLQ.
+At position 97 to 404, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 597 to 751, the domain is characterized as Exonuclease.
+At position 180 to 355, the domain is characterized as EngA-type G 2.
+At position 31 to 74, the domain is characterized as Histone-fold.
+At position 135 to 293, the domain is characterized as Integrase catalytic.
+At position 5 to 112, the domain is characterized as HIT.
+At position 61 to 125, the domain is characterized as SEP.
+At position 170 to 247, the domain is characterized as UBX.
+At position 39 to 122, the domain is characterized as Inhibitor I9.
+At position 130 to 426, the domain is characterized as Peptidase S8.
+At position 117 to 335, the domain is characterized as Fibrinogen C-terminal.
+At position 35 to 147, the domain is characterized as GOLD.
+At position 55 to 168, the domain is characterized as TBDR plug.
+At position 173 to 702, the domain is characterized as TBDR beta-barrel.
+At position 116 to 305, the domain is characterized as Tyr recombinase.
+At position 243 to 442, the domain is characterized as Peptidase M12B.
+At position 448 to 535, the domain is characterized as Disintegrin.
+At position 681 to 713, the domain is characterized as EGF-like.
+At position 121 to 262, the domain is characterized as Fido.
+At position 140 to 203, the domain is characterized as CBS 1.
+At position 204 to 260, the domain is characterized as CBS 2.
+At position 131 to 266, the domain is characterized as C2.
+At position 617 to 692, the domain is characterized as Cytochrome b5 heme-binding.
+At position 721 to 836, the domain is characterized as FAD-binding FR-type.
+At position 334 to 609, the domain is characterized as MYST-type HAT.
+At position 168 to 280, the domain is characterized as Fe2OG dioxygenase.
+At position 667 to 858, the domain is characterized as ATP-grasp 2.
+At position 940 to 1101, the domain is characterized as MGS-like.
+At position 58 to 326, the domain is characterized as Tyrosine-protein phosphatase.
+At position 310 to 345, the domain is characterized as DMA.
+At position 844 to 986, the domain is characterized as Peptidase S59.
+At position 41 to 224, the domain is characterized as Reticulon.
+At position 127 to 203, the domain is characterized as Ubiquitin-like.
+At position 334 to 363, the domain is characterized as IQ.
+At position 84 to 119, the domain is characterized as EF-hand.
+At position 59 to 223, the domain is characterized as TIR.
+At position 241 to 511, the domain is characterized as NB-ARC.
+At position 336 to 433, the domain is characterized as PDZ.
+At position 140 to 444, the domain is characterized as NB-ARC.
+At position 341 to 390, the domain is characterized as UBX.
+At position 790 to 856, the domain is characterized as HP.
+At position 453 to 570, the domain is characterized as Toprim.
+At position 525 to 654, the domain is characterized as SMC hinge.
+At position 51 to 115, the domain is characterized as TGS.
+At position 136 to 175, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 242 to 491, the domain is characterized as CN hydrolase.
+At position 558 to 727, the domain is characterized as N-acetyltransferase.
+At position 10 to 148, the domain is characterized as N-acetyltransferase.
+At position 18 to 169, the domain is characterized as MARVEL.
+At position 476 to 539, the domain is characterized as SAM 1.
+At position 545 to 609, the domain is characterized as SAM 2.
+At position 212 to 427, the domain is characterized as Helicase ATP-binding.
+At position 438 to 624, the domain is characterized as Helicase C-terminal.
+At position 172 to 235, the domain is characterized as bZIP.
+At position 20 to 152, the domain is characterized as ENTH.
+At position 20 to 130, the domain is characterized as Thioredoxin 1.
+At position 134 to 250, the domain is characterized as Thioredoxin 2.
+At position 60 to 172, the domain is characterized as Thioredoxin.
+At position 1 to 36, the domain is characterized as F-box.
+At position 71 to 238, the domain is characterized as Cyclin N-terminal.
+At position 113 to 192, the domain is characterized as RRM.
+At position 344 to 494, the domain is characterized as NTF2.
+At position 4 to 193, the domain is characterized as Flavodoxin-like.
+At position 48 to 131, the domain is characterized as PDZ 1.
+At position 148 to 234, the domain is characterized as PDZ 2.
+At position 248 to 332, the domain is characterized as PDZ 3.
+At position 456 to 545, the domain is characterized as PDZ 4.
+At position 557 to 641, the domain is characterized as PDZ 5.
+At position 656 to 738, the domain is characterized as PDZ 6.
+At position 941 to 1023, the domain is characterized as PDZ 7.
+At position 12 to 129, the domain is characterized as MTTase N-terminal.
+At position 122 to 206, the domain is characterized as Ig-like C2-type.
+At position 39 to 114, the domain is characterized as TFIIS N-terminal.
+At position 131 to 210, the domain is characterized as TFIIS central.
+At position 43 to 147, the domain is characterized as Calponin-homology (CH) 1.
+At position 156 to 262, the domain is characterized as Calponin-homology (CH) 2.
+At position 758 to 793, the domain is characterized as EF-hand 1.
+At position 799 to 834, the domain is characterized as EF-hand 2.
+At position 58 to 277, the domain is characterized as Laminin G-like.
+At position 136 to 238, the domain is characterized as Rieske.
+At position 184 to 355, the domain is characterized as Hflx-type G.
+At position 210 to 312, the domain is characterized as Fe2OG dioxygenase.
+At position 632 to 773, the domain is characterized as MOSC.
+At position 24 to 94, the domain is characterized as Ig-like.
+At position 145 to 173, the domain is characterized as ITAM.
+At position 141 to 372, the domain is characterized as Radical SAM core.
+At position 375 to 439, the domain is characterized as TRAM.
+At position 1 to 70, the domain is characterized as W2.
+At position 551 to 863, the domain is characterized as Protein kinase.
+At position 174 to 350, the domain is characterized as Helicase ATP-binding.
+At position 364 to 534, the domain is characterized as Helicase C-terminal.
+At position 21 to 137, the domain is characterized as RGS.
+At position 27 to 89, the domain is characterized as LCN-type CS-alpha/beta.
+At position 1237 to 1401, the domain is characterized as PNPLA.
+At position 51 to 228, the domain is characterized as tr-type G.
+At position 77 to 168, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 211 to 241, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 24 to 67, the domain is characterized as CHCH.
+At position 47 to 356, the domain is characterized as PPM-type phosphatase.
+At position 88 to 231, the domain is characterized as N-acetyltransferase.
+At position 47 to 351, the domain is characterized as Cbl-PTB.
+At position 856 to 895, the domain is characterized as UBA.
+At position 25 to 294, the domain is characterized as GH18.
+At position 79 to 179, the domain is characterized as PI3K-ABD.
+At position 272 to 363, the domain is characterized as PI3K-RBD.
+At position 430 to 588, the domain is characterized as C2 PI3K-type.
+At position 607 to 793, the domain is characterized as PIK helical.
+At position 858 to 1159, the domain is characterized as PI3K/PI4K catalytic.
+At position 510 to 798, the domain is characterized as UvrD-like helicase C-terminal.
+At position 134 to 263, the domain is characterized as Fatty acid hydroxylase.
+At position 647 to 728, the domain is characterized as S1 motif.
+At position 36 to 288, the domain is characterized as Protein kinase.
+At position 627 to 708, the domain is characterized as BRCT.
+At position 526 to 600, the domain is characterized as Carrier.
+At position 28 to 60, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 1120 to 1406, the domain is characterized as Protein kinase.
+At position 13 to 145, the domain is characterized as ADF-H.
+At position 27 to 171, the domain is characterized as Toprim.
+At position 48 to 119, the domain is characterized as KH type-2.
+At position 18 to 209, the domain is characterized as NodB homology.
+At position 312 to 546, the domain is characterized as Rho-GAP.
+At position 103 to 189, the domain is characterized as ELM2.
+At position 190 to 241, the domain is characterized as SANT 1.
+At position 381 to 432, the domain is characterized as SANT 2.
+At position 477 to 535, the domain is characterized as RAP.
+At position 43 to 293, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 560 to 618, the domain is characterized as RAP.
+At position 44 to 203, the domain is characterized as Helicase ATP-binding.
+At position 285 to 432, the domain is characterized as Helicase C-terminal.
+At position 31 to 214, the domain is characterized as BPL/LPL catalytic.
+At position 61 to 151, the domain is characterized as WGR.
+At position 183 to 301, the domain is characterized as PARP alpha-helical.
+At position 312 to 526, the domain is characterized as PARP catalytic.
+At position 62 to 160, the domain is characterized as WSC 1.
+At position 195 to 289, the domain is characterized as WSC 2.
+At position 307 to 404, the domain is characterized as WSC 3.
+At position 3 to 155, the domain is characterized as NAC.
+At position 406 to 485, the domain is characterized as Rhodanese.
+At position 63 to 147, the domain is characterized as LITAF.
+At position 24 to 107, the domain is characterized as UPAR/Ly6.
+At position 539 to 650, the domain is characterized as Ig-like 6.
+At position 627 to 744, the domain is characterized as Fibronectin type-III.
+At position 670 to 831, the domain is characterized as Helicase ATP-binding.
+At position 852 to 1006, the domain is characterized as Helicase C-terminal.
+At position 230 to 368, the domain is characterized as PADR1 zinc-binding.
+At position 257 to 291, the domain is characterized as SAP.
+At position 507 to 607, the domain is characterized as WGR.
+At position 629 to 748, the domain is characterized as PARP alpha-helical.
+At position 755 to 980, the domain is characterized as PARP catalytic.
+At position 16 to 258, the domain is characterized as ABC transporter.
+At position 100 to 316, the domain is characterized as ABC transmembrane type-1.
+At position 27 to 298, the domain is characterized as PPM-type phosphatase.
+At position 348 to 543, the domain is characterized as PCI.
+At position 8 to 204, the domain is characterized as Peptidase M12B.
+At position 6 to 173, the domain is characterized as Exonuclease.
+At position 377 to 429, the domain is characterized as FBD.
+At position 157 to 487, the domain is characterized as GH16.
+At position 168 to 266, the domain is characterized as RRM 1.
+At position 274 to 359, the domain is characterized as RRM 2.
+At position 242 to 315, the domain is characterized as SPOR.
+At position 174 to 232, the domain is characterized as LIM zinc-binding 1.
+At position 233 to 292, the domain is characterized as LIM zinc-binding 2.
+At position 293 to 350, the domain is characterized as LIM zinc-binding 3.
+At position 351 to 410, the domain is characterized as LIM zinc-binding 4.
+At position 1284 to 1457, the domain is characterized as Helicase ATP-binding.
+At position 1639 to 1787, the domain is characterized as Helicase C-terminal.
+At position 391 to 407, the domain is characterized as Post-SET.
+At position 959 to 1253, the domain is characterized as PKS/mFAS DH.
+At position 2454 to 2531, the domain is characterized as Carrier.
+At position 1 to 81, the domain is characterized as HTH TFE/IIEalpha-type.
+At position 123 to 156, the domain is characterized as WW.
+At position 16 to 210, the domain is characterized as Lon N-terminal.
+At position 268 to 467, the domain is characterized as B30.2/SPRY.
+At position 817 to 1146, the domain is characterized as GP-PDE.
+At position 139 to 213, the domain is characterized as HTH crp-type.
+At position 208 to 286, the domain is characterized as RRM 2.
+At position 51 to 115, the domain is characterized as J.
+At position 113 to 187, the domain is characterized as POU-specific.
+At position 572 to 666, the domain is characterized as PH 1.
+At position 681 to 790, the domain is characterized as PH 2.
+At position 826 to 980, the domain is characterized as MyTH4.
+At position 991 to 1327, the domain is characterized as FERM.
+At position 112 to 351, the domain is characterized as Radical SAM core.
+At position 111 to 332, the domain is characterized as Radical SAM core.
+At position 34 to 122, the domain is characterized as Importin N-terminal.
+At position 302 to 394, the domain is characterized as Ig-like C2-type 1.
+At position 402 to 487, the domain is characterized as Ig-like C2-type 2.
+At position 22 to 139, the domain is characterized as MTTase N-terminal.
+At position 152 to 386, the domain is characterized as Radical SAM core.
+At position 389 to 449, the domain is characterized as TRAM.
+At position 14 to 356, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 366 to 704, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 624 to 779, the domain is characterized as BAH.
+At position 1510 to 1634, the domain is characterized as BAH.
+At position 252 to 424, the domain is characterized as MRG.
+At position 286 to 445, the domain is characterized as FCP1 homology.
+At position 31 to 136, the domain is characterized as Ig-like V-type.
+At position 147 to 246, the domain is characterized as Ig-like C1-type 1.
+At position 253 to 347, the domain is characterized as Ig-like C1-type 2.
+At position 180 to 270, the domain is characterized as TonB C-terminal.
+At position 85 to 506, the domain is characterized as Peptidase A1.
+At position 315 to 420, the domain is characterized as Saposin B-type.
+At position 85 to 439, the domain is characterized as Peptidase A1.
+At position 19 to 324, the domain is characterized as F-BAR.
+At position 496 to 680, the domain is characterized as Rho-GAP.
+At position 738 to 797, the domain is characterized as SH3.
+At position 885 to 1027, the domain is characterized as Peptidase S59.
+At position 2 to 127, the domain is characterized as VOC.
+At position 530 to 845, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 18 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 237 to 349, the domain is characterized as Ig-like C2-type 3.
+At position 158 to 709, the domain is characterized as TBDR beta-barrel.
+At position 1 to 414, the domain is characterized as Protein kinase 1.
+At position 1397 to 1467, the domain is characterized as Bromo 1.
+At position 1425 to 1872, the domain is characterized as Protein kinase 2.
+At position 1520 to 1590, the domain is characterized as Bromo 2.
+At position 29 to 164, the domain is characterized as RanBD1.
+At position 5 to 264, the domain is characterized as F-BAR.
+At position 358 to 415, the domain is characterized as SH3.
+At position 438 to 489, the domain is characterized as Rubredoxin-like.
+At position 519 to 712, the domain is characterized as Protein kinase.
+At position 130 to 262, the domain is characterized as Fatty acid hydroxylase.
+At position 678 to 912, the domain is characterized as NR LBD.
+At position 42 to 140, the domain is characterized as Ig-like V-type.
+At position 325 to 403, the domain is characterized as Ig-like C2-type 3.
+At position 9 to 114, the domain is characterized as PINc.
+At position 30 to 79, the domain is characterized as FHA-like.
+At position 330 to 527, the domain is characterized as Protein kinase.
+At position 249 to 518, the domain is characterized as Letm1 RBD.
+At position 676 to 711, the domain is characterized as EF-hand.
+At position 220 to 464, the domain is characterized as PABS.
+At position 95 to 194, the domain is characterized as BRICHOS.
+At position 71 to 248, the domain is characterized as Helicase ATP-binding.
+At position 259 to 491, the domain is characterized as Helicase C-terminal.
+At position 19 to 216, the domain is characterized as Lon N-terminal.
+At position 286 to 322, the domain is characterized as EGF-like; atypical.
+At position 519 to 809, the domain is characterized as Protein kinase.
+At position 6 to 27, the domain is characterized as Pentraxin (PTX).
+At position 1163 to 1224, the domain is characterized as PAP-associated.
+At position 31 to 212, the domain is characterized as Laminin G-like 1.
+At position 13 to 107, the domain is characterized as HTH arsR-type.
+At position 591 to 707, the domain is characterized as PI-PLC Y-box.
+At position 708 to 836, the domain is characterized as C2.
+At position 176 to 392, the domain is characterized as Glutamine amidotransferase type-1.
+At position 814 to 888, the domain is characterized as Carrier 1.
+At position 1364 to 1437, the domain is characterized as Carrier 2.
+At position 1917 to 1993, the domain is characterized as Carrier 3.
+At position 61 to 95, the domain is characterized as SAP.
+At position 423 to 602, the domain is characterized as Lon proteolytic.
+At position 61 to 250, the domain is characterized as TLDc.
+At position 153 to 344, the domain is characterized as CheB-type methylesterase.
+At position 335 to 533, the domain is characterized as Cytochrome b561.
+At position 156 to 413, the domain is characterized as PPM-type phosphatase.
+At position 6 to 208, the domain is characterized as AIG1-type G.
+At position 135 to 377, the domain is characterized as Protein kinase.
+At position 255 to 353, the domain is characterized as Fe2OG dioxygenase.
+At position 98 to 317, the domain is characterized as ATP-grasp.
+At position 2 to 355, the domain is characterized as Kinesin motor.
+At position 483 to 595, the domain is characterized as FHA.
+At position 1523 to 1616, the domain is characterized as PH.
+At position 157 to 388, the domain is characterized as Radical SAM core.
+At position 391 to 460, the domain is characterized as TRAM.
+At position 35 to 378, the domain is characterized as FERM.
+At position 399 to 480, the domain is characterized as SH2; atypical.
+At position 542 to 806, the domain is characterized as Protein kinase 1.
+At position 846 to 1118, the domain is characterized as Protein kinase 2.
+At position 334 to 390, the domain is characterized as MIR 1.
+At position 403 to 459, the domain is characterized as MIR 2.
+At position 404 to 473, the domain is characterized as J.
+At position 319 to 365, the domain is characterized as F-box.
+At position 721 to 796, the domain is characterized as Smr.
+At position 5 to 234, the domain is characterized as tr-type G.
+At position 47 to 343, the domain is characterized as PPM-type phosphatase.
+At position 219 to 320, the domain is characterized as Fe2OG dioxygenase.
+At position 39 to 370, the domain is characterized as USP.
+At position 279 to 371, the domain is characterized as RRM.
+At position 89 to 175, the domain is characterized as K-box.
+At position 616 to 722, the domain is characterized as tRNA-binding.
+At position 64 to 314, the domain is characterized as PPM-type phosphatase.
+At position 1 to 59, the domain is characterized as MADS-box.
+At position 148 to 460, the domain is characterized as NB-ARC.
+At position 28 to 466, the domain is characterized as Deacetylase sirtuin-type.
+At position 406 to 557, the domain is characterized as PA14.
+At position 17 to 202, the domain is characterized as YrdC-like.
+At position 252 to 457, the domain is characterized as GATase cobBQ-type.
+At position 185 to 284, the domain is characterized as SWIRM.
+At position 413 to 464, the domain is characterized as SANT.
+At position 208 to 473, the domain is characterized as Protein kinase.
+At position 180 to 503, the domain is characterized as NACHT.
+At position 3 to 234, the domain is characterized as ABC transporter.
+At position 413 to 487, the domain is characterized as B5.
+At position 252 to 370, the domain is characterized as Nop.
+At position 933 to 1087, the domain is characterized as Guanylate cyclase.
+At position 32 to 187, the domain is characterized as SIS.
+At position 179 to 240, the domain is characterized as Sushi 1.
+At position 316 to 365, the domain is characterized as Sushi 3.
+At position 367 to 428, the domain is characterized as Sushi 4.
+At position 43 to 245, the domain is characterized as TLC.
+At position 40 to 118, the domain is characterized as IGFBP N-terminal.
+At position 384 to 476, the domain is characterized as PDZ.
+At position 8 to 69, the domain is characterized as Chromo.
+At position 258 to 325, the domain is characterized as Pre-SET.
+At position 328 to 452, the domain is characterized as SET.
+At position 473 to 489, the domain is characterized as Post-SET.
+At position 940 to 1291, the domain is characterized as Protein kinase.
+At position 74 to 169, the domain is characterized as HPt.
+At position 122 to 209, the domain is characterized as Fibronectin type-III 2.
+At position 210 to 299, the domain is characterized as Fibronectin type-III 3.
+At position 300 to 387, the domain is characterized as Fibronectin type-III 4.
+At position 388 to 477, the domain is characterized as Fibronectin type-III 5.
+At position 478 to 563, the domain is characterized as Fibronectin type-III 6.
+At position 564 to 666, the domain is characterized as Fibronectin type-III 7.
+At position 665 to 749, the domain is characterized as Fibronectin type-III 8.
+At position 820 to 1079, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1 to 250, the domain is characterized as Protein kinase.
+At position 509 to 678, the domain is characterized as N-acetyltransferase.
+At position 83 to 209, the domain is characterized as C2 1.
+At position 243 to 376, the domain is characterized as C2 2.
+At position 306 to 428, the domain is characterized as C2 1.
+At position 462 to 603, the domain is characterized as C2 2.
+At position 126 to 358, the domain is characterized as Radical SAM core.
+At position 11 to 147, the domain is characterized as AB hydrolase-1.
+At position 387 to 808, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1295 to 1602, the domain is characterized as PKS/mFAS DH.
+At position 1652 to 1726, the domain is characterized as Carrier.
+At position 102 to 203, the domain is characterized as Cyclin N-terminal.
+At position 19 to 117, the domain is characterized as Ig-like.
+At position 79 to 204, the domain is characterized as MATH.
+At position 228 to 295, the domain is characterized as BTB.
+At position 821 to 949, the domain is characterized as C1q.
+At position 114 to 345, the domain is characterized as Radical SAM core.
+At position 34 to 382, the domain is characterized as GH10.
+At position 363 to 434, the domain is characterized as EGF-like.
+At position 43 to 269, the domain is characterized as Reverse transcriptase.
+At position 379 to 456, the domain is characterized as Kringle 4.
+At position 482 to 561, the domain is characterized as Kringle 5.
+At position 582 to 808, the domain is characterized as Peptidase S1.
+At position 24 to 66, the domain is characterized as EGF-like 1.
+At position 301 to 350, the domain is characterized as GPS.
+At position 201 to 237, the domain is characterized as ShKT.
+At position 61 to 152, the domain is characterized as Cadherin 1.
+At position 153 to 260, the domain is characterized as Cadherin 2.
+At position 261 to 375, the domain is characterized as Cadherin 3.
+At position 376 to 481, the domain is characterized as Cadherin 4.
+At position 482 to 590, the domain is characterized as Cadherin 5.
+At position 137 to 173, the domain is characterized as EF-hand 3.
+At position 174 to 205, the domain is characterized as EF-hand 4.
+At position 6 to 78, the domain is characterized as DED 1.
+At position 97 to 172, the domain is characterized as DED 2.
+At position 247 to 383, the domain is characterized as DAGKc.
+At position 158 to 210, the domain is characterized as BSD.
+At position 637 to 934, the domain is characterized as FERM.
+At position 7 to 129, the domain is characterized as Thioredoxin.
+At position 480 to 745, the domain is characterized as Protein kinase.
+At position 765 to 835, the domain is characterized as U-box.
+At position 306 to 392, the domain is characterized as PPIase FKBP-type.
+At position 28 to 140, the domain is characterized as SSB.
+At position 27 to 213, the domain is characterized as RNase H type-2.
+At position 189 to 207, the domain is characterized as UIM.
+At position 180 to 357, the domain is characterized as Peptidase M12B.
+At position 179 to 231, the domain is characterized as BSD 2.
+At position 33 to 320, the domain is characterized as GP-PDE 1.
+At position 337 to 645, the domain is characterized as GP-PDE 2.
+At position 61 to 83, the domain is characterized as GoLoco 1.
+At position 103 to 125, the domain is characterized as GoLoco 2.
+At position 131 to 154, the domain is characterized as GoLoco 3.
+At position 267 to 476, the domain is characterized as Peptidase M12B.
+At position 485 to 566, the domain is characterized as Disintegrin.
+At position 567 to 622, the domain is characterized as TSP type-1 1.
+At position 875 to 929, the domain is characterized as TSP type-1 2.
+At position 22 to 204, the domain is characterized as MIF4G.
+At position 290 to 407, the domain is characterized as MI.
+At position 70 to 149, the domain is characterized as SPOR 1.
+At position 150 to 229, the domain is characterized as SPOR 2.
+At position 230 to 311, the domain is characterized as SPOR 3.
+At position 630 to 700, the domain is characterized as SH3b.
+At position 103 to 188, the domain is characterized as PDZ.
+At position 63 to 117, the domain is characterized as TCP.
+At position 41 to 140, the domain is characterized as SCP.
+At position 716 to 818, the domain is characterized as PH.
+At position 29 to 126, the domain is characterized as Ig-like V-type 1.
+At position 134 to 227, the domain is characterized as Ig-like V-type 2.
+At position 16 to 299, the domain is characterized as ABC transmembrane type-1.
+At position 333 to 567, the domain is characterized as ABC transporter.
+At position 23 to 345, the domain is characterized as Protein kinase.
+At position 384 to 437, the domain is characterized as PAP-associated.
+At position 35 to 113, the domain is characterized as ACT.
+At position 482 to 553, the domain is characterized as PAS.
+At position 58 to 203, the domain is characterized as Cupin type-1.
+At position 40 to 144, the domain is characterized as FAD-binding FR-type.
+At position 285 to 885, the domain is characterized as USP.
+At position 7 to 199, the domain is characterized as Glutamine amidotransferase type-1.
+At position 6 to 178, the domain is characterized as Era-type G.
+At position 207 to 282, the domain is characterized as KH type-2.
+At position 60 to 118, the domain is characterized as Myb-like 1.
+At position 401 to 465, the domain is characterized as Myb-like 2.
+At position 743 to 832, the domain is characterized as EH.
+At position 142 to 225, the domain is characterized as BTB.
+At position 861 to 1154, the domain is characterized as ABC transmembrane type-1 2.
+At position 1208 to 1441, the domain is characterized as ABC transporter 2.
+At position 24 to 104, the domain is characterized as Importin N-terminal.
+At position 106 to 224, the domain is characterized as FZ.
+At position 114 to 266, the domain is characterized as PH.
+At position 304 to 504, the domain is characterized as SMP-LTD.
+At position 208 to 291, the domain is characterized as RCK C-terminal 1.
+At position 296 to 376, the domain is characterized as RCK C-terminal 2.
+At position 936 to 1076, the domain is characterized as MGS-like.
+At position 379 to 465, the domain is characterized as KH-like.
+At position 134 to 385, the domain is characterized as FCP1 homology.
+At position 656 to 722, the domain is characterized as DRBM.
+At position 31 to 157, the domain is characterized as RNase III.
+At position 184 to 252, the domain is characterized as DRBM.
+At position 105 to 118, the domain is characterized as CRIB.
+At position 153 to 331, the domain is characterized as Rho-GAP.
+At position 375 to 526, the domain is characterized as N-acetyltransferase.
+At position 248 to 443, the domain is characterized as START.
+At position 263 to 283, the domain is characterized as ELK.
+At position 48 to 234, the domain is characterized as VWFA.
+At position 241 to 287, the domain is characterized as TSP type-1.
+At position 4 to 87, the domain is characterized as KRAB.
+At position 69 to 319, the domain is characterized as Radical SAM core 1.
+At position 528 to 763, the domain is characterized as Radical SAM core 2.
+At position 290 to 364, the domain is characterized as POU-specific.
+At position 332 to 457, the domain is characterized as DUF1170.
+At position 503 to 602, the domain is characterized as PH.
+At position 1 to 291, the domain is characterized as YjeF C-terminal.
+At position 6 to 238, the domain is characterized as ABC transporter 1.
+At position 251 to 494, the domain is characterized as ABC transporter 2.
+At position 116 to 175, the domain is characterized as Collagen-like 1.
+At position 209 to 268, the domain is characterized as Collagen-like 2.
+At position 278 to 337, the domain is characterized as Collagen-like 3.
+At position 338 to 473, the domain is characterized as C1q.
+At position 70 to 319, the domain is characterized as PPM-type phosphatase.
+At position 213 to 449, the domain is characterized as Peptidase S1.
+At position 52 to 497, the domain is characterized as ADPK.
+At position 50 to 284, the domain is characterized as Cache.
+At position 357 to 411, the domain is characterized as HAMP.
+At position 416 to 652, the domain is characterized as Methyl-accepting transducer.
+At position 85 to 209, the domain is characterized as HotDog ACOT-type 1.
+At position 201 to 257, the domain is characterized as SSD.
+At position 18 to 161, the domain is characterized as SprT-like.
+At position 1 to 150, the domain is characterized as Ferritin-like diiron.
+At position 157 to 195, the domain is characterized as Rubredoxin-like.
+At position 9 to 125, the domain is characterized as Response regulatory.
+At position 85 to 298, the domain is characterized as RrmJ-type SAM-dependent 2'-O-MTase.
+At position 3 to 159, the domain is characterized as ADF-H.
+At position 233 to 381, the domain is characterized as Tyrosine-protein phosphatase.
+At position 521 to 775, the domain is characterized as ATP-grasp.
+At position 47 to 126, the domain is characterized as PDZ.
+At position 306 to 486, the domain is characterized as RGSL.
+At position 734 to 923, the domain is characterized as DH.
+At position 965 to 1079, the domain is characterized as PH.
+At position 625 to 727, the domain is characterized as Fibronectin type-III 1.
+At position 754 to 848, the domain is characterized as Fibronectin type-III 2.
+At position 854 to 948, the domain is characterized as Fibronectin type-III 3.
+At position 1024 to 1299, the domain is characterized as Protein kinase.
+At position 150 to 209, the domain is characterized as LIM zinc-binding 1.
+At position 210 to 267, the domain is characterized as LIM zinc-binding 2.
+At position 268 to 327, the domain is characterized as LIM zinc-binding 3.
+At position 328 to 386, the domain is characterized as LIM zinc-binding 4.
+At position 76 to 174, the domain is characterized as BTB.
+At position 22 to 211, the domain is characterized as GH16.
+At position 21 to 493, the domain is characterized as Sema.
+At position 526 to 634, the domain is characterized as Ig-like C2-type.
+At position 139 to 253, the domain is characterized as Response regulatory.
+At position 183 to 380, the domain is characterized as Peptidase M12B.
+At position 630 to 664, the domain is characterized as EGF-like.
+At position 193 to 282, the domain is characterized as CS.
+At position 301 to 387, the domain is characterized as SGS.
+At position 144 to 260, the domain is characterized as PilZ.
+At position 26 to 336, the domain is characterized as Peptidase S6.
+At position 1293 to 1545, the domain is characterized as Autotransporter.
+At position 301 to 545, the domain is characterized as B30.2/SPRY.
+At position 52 to 410, the domain is characterized as Kinesin motor.
+At position 8 to 295, the domain is characterized as CN hydrolase.
+At position 187 to 379, the domain is characterized as Glutamine amidotransferase type-1.
+At position 540 to 718, the domain is characterized as Helicase ATP-binding.
+At position 729 to 890, the domain is characterized as Helicase C-terminal.
+At position 108 to 249, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 47 to 174, the domain is characterized as G8.
+At position 212 to 340, the domain is characterized as OmpA-like.
+At position 143 to 364, the domain is characterized as Radical SAM core.
+At position 274 to 602, the domain is characterized as FERM.
+At position 400 to 508, the domain is characterized as PH.
+At position 155 to 346, the domain is characterized as CheB-type methylesterase.
+At position 227 to 246, the domain is characterized as UIM 1.
+At position 247 to 266, the domain is characterized as UIM 2.
+At position 337 to 356, the domain is characterized as UIM 3.
+At position 104 to 339, the domain is characterized as Radical SAM core.
+At position 696 to 804, the domain is characterized as DMAP1-binding.
+At position 970 to 1005, the domain is characterized as EF-hand.
+At position 405 to 570, the domain is characterized as Helicase ATP-binding.
+At position 939 to 1092, the domain is characterized as Helicase C-terminal.
+At position 427 to 461, the domain is characterized as PLD phosphodiesterase 1.
+At position 584 to 614, the domain is characterized as PLD phosphodiesterase 2.
+At position 8 to 124, the domain is characterized as Calponin-homology (CH).
+At position 324 to 378, the domain is characterized as SAM.
+At position 182 to 361, the domain is characterized as CNNM transmembrane.
+At position 380 to 441, the domain is characterized as CBS 1.
+At position 448 to 515, the domain is characterized as CBS 2.
+At position 136 to 205, the domain is characterized as S1 motif 1.
+At position 248 to 318, the domain is characterized as S1 motif 2.
+At position 280 to 636, the domain is characterized as Rab-GAP TBC.
+At position 397 to 496, the domain is characterized as Ig-like C2-type.
+At position 198 to 321, the domain is characterized as MsrB.
+At position 4 to 199, the domain is characterized as C2 NT-type.
+At position 383 to 645, the domain is characterized as Autotransporter.
+At position 58 to 230, the domain is characterized as FAD-binding PCMH-type.
+At position 56 to 236, the domain is characterized as Guanylate kinase-like.
+At position 411 to 485, the domain is characterized as B5.
+At position 739 to 832, the domain is characterized as FDX-ACB.
+At position 50 to 105, the domain is characterized as VWFC 1.
+At position 108 to 163, the domain is characterized as VWFC 2.
+At position 164 to 225, the domain is characterized as VWFC 3.
+At position 238 to 289, the domain is characterized as VWFC 4.
+At position 299 to 358, the domain is characterized as VWFC 5.
+At position 362 to 535, the domain is characterized as VWFD.
+At position 629 to 682, the domain is characterized as TIL.
+At position 155 to 294, the domain is characterized as CP-type G.
+At position 140 to 196, the domain is characterized as BTB.
+At position 313 to 391, the domain is characterized as UBX.
+At position 6 to 272, the domain is characterized as Pyruvate carboxyltransferase.
+At position 72 to 172, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 77 to 307, the domain is characterized as SET.
+At position 21 to 307, the domain is characterized as tr-type G.
+At position 108 to 296, the domain is characterized as ATP-grasp.
+At position 1 to 115, the domain is characterized as PX.
+At position 278 to 340, the domain is characterized as t-SNARE coiled-coil homology.
+At position 166 to 391, the domain is characterized as TRUD.
+At position 58 to 131, the domain is characterized as RRM 1.
+At position 137 to 222, the domain is characterized as RRM 2.
+At position 74 to 136, the domain is characterized as S4 RNA-binding.
+At position 537 to 706, the domain is characterized as tr-type G.
+At position 106 to 256, the domain is characterized as N-acetyltransferase.
+At position 19 to 151, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 99 to 323, the domain is characterized as Radical SAM core.
+At position 215 to 294, the domain is characterized as Kringle.
+At position 354 to 594, the domain is characterized as Peptidase S1.
+At position 563 to 647, the domain is characterized as Ig-like C2-type 1.
+At position 656 to 731, the domain is characterized as Ig-like C2-type 2.
+At position 803 to 1076, the domain is characterized as Protein kinase.
+At position 300 to 576, the domain is characterized as Protein kinase.
+At position 30 to 177, the domain is characterized as FZ.
+At position 931 to 1070, the domain is characterized as MGS-like.
+At position 88 to 212, the domain is characterized as GST C-terminal.
+At position 41 to 251, the domain is characterized as Sigma-54 factor interaction.
+At position 209 to 592, the domain is characterized as Peptidase S53.
+At position 285 to 354, the domain is characterized as Plastocyanin-like.
+At position 24 to 183, the domain is characterized as ALOG.
+At position 258 to 540, the domain is characterized as Phosphatase tensin-type.
+At position 21 to 149, the domain is characterized as Response regulatory.
+At position 1 to 76, the domain is characterized as PTS EIIA type-1.
+At position 250 to 395, the domain is characterized as JmjC.
+At position 446 to 548, the domain is characterized as CBM20.
+At position 172 to 274, the domain is characterized as BACK.
+At position 57 to 321, the domain is characterized as PPM-type phosphatase.
+At position 40 to 114, the domain is characterized as TFIIS N-terminal.
+At position 131 to 208, the domain is characterized as TFIIS central.
+At position 163 to 281, the domain is characterized as PH.
+At position 149 to 468, the domain is characterized as Protein kinase.
+At position 273 to 361, the domain is characterized as CS.
+At position 41 to 123, the domain is characterized as GOLD.
+At position 32 to 228, the domain is characterized as Peptidase M12B.
+At position 236 to 317, the domain is characterized as Disintegrin.
+At position 381 to 433, the domain is characterized as bHLH.
+At position 36 to 215, the domain is characterized as BPL/LPL catalytic.
+At position 10 to 47, the domain is characterized as EF-hand 1.
+At position 222 to 383, the domain is characterized as CP-type G.
+At position 648 to 906, the domain is characterized as Protein kinase.
+At position 52 to 315, the domain is characterized as AB hydrolase-1.
+At position 1 to 50, the domain is characterized as TRAM.
+At position 68 to 133, the domain is characterized as NAC-A/B.
+At position 174 to 211, the domain is characterized as UBA.
+At position 221 to 390, the domain is characterized as tr-type G.
+At position 144 to 175, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 176 to 205, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 57 to 159, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 198 to 304, the domain is characterized as KH.
+At position 80 to 404, the domain is characterized as HAP1 N-terminal.
+At position 48 to 369, the domain is characterized as ABC transmembrane type-1 1.
+At position 405 to 641, the domain is characterized as ABC transporter 1.
+At position 732 to 1020, the domain is characterized as ABC transmembrane type-1 2.
+At position 1059 to 1298, the domain is characterized as ABC transporter 2.
+At position 46 to 188, the domain is characterized as GAF.
+At position 230 to 458, the domain is characterized as Sigma-54 factor interaction.
+At position 1 to 182, the domain is characterized as PTS EIIC type-5.
+At position 18 to 232, the domain is characterized as tr-type G.
+At position 165 to 217, the domain is characterized as FAF.
+At position 63 to 379, the domain is characterized as tr-type G.
+At position 489 to 660, the domain is characterized as Helicase C-terminal.
+At position 5 to 226, the domain is characterized as tr-type G.
+At position 652 to 854, the domain is characterized as MRH.
+At position 135 to 415, the domain is characterized as Protein kinase.
+At position 165 to 602, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1084 to 1393, the domain is characterized as PKS/mFAS DH.
+At position 1441 to 1518, the domain is characterized as Carrier 1.
+At position 1552 to 1630, the domain is characterized as Carrier 2.
+At position 63 to 473, the domain is characterized as TROVE.
+At position 53 to 116, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 167 to 238, the domain is characterized as RRM.
+At position 168 to 270, the domain is characterized as AB hydrolase-1.
+At position 69 to 144, the domain is characterized as Carrier.
+At position 88 to 397, the domain is characterized as IF rod.
+At position 215 to 913, the domain is characterized as REJ.
+At position 1230 to 1347, the domain is characterized as PLAT.
+At position 287 to 370, the domain is characterized as TFIIS N-terminal.
+At position 33 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 20 to 238, the domain is characterized as Protein kinase.
+At position 281 to 600, the domain is characterized as Peptidase A1.
+At position 214 to 260, the domain is characterized as G-patch.
+At position 283 to 369, the domain is characterized as RRM.
+At position 151 to 264, the domain is characterized as Gnk2-homologous 2.
+At position 50 to 147, the domain is characterized as THUMP.
+At position 534 to 552, the domain is characterized as EF-hand 1.
+At position 880 to 954, the domain is characterized as U-box.
+At position 480 to 663, the domain is characterized as N-acetyltransferase.
+At position 3 to 87, the domain is characterized as GS beta-grasp.
+At position 92 to 343, the domain is characterized as GS catalytic.
+At position 38 to 186, the domain is characterized as SCP.
+At position 102 to 180, the domain is characterized as RRM.
+At position 279 to 319, the domain is characterized as Rho-GAP.
+At position 40 to 69, the domain is characterized as LRRNT.
+At position 584 to 690, the domain is characterized as tRNA-binding.
+At position 116 to 311, the domain is characterized as NR LBD.
+At position 1 to 43, the domain is characterized as Disintegrin.
+At position 66 to 102, the domain is characterized as Laminin EGF-like 1.
+At position 103 to 160, the domain is characterized as Laminin EGF-like 2.
+At position 161 to 171, the domain is characterized as Laminin EGF-like 3.
+At position 1 to 19, the domain is characterized as C-type lectin.
+At position 70 to 215, the domain is characterized as CBM-cenC.
+At position 79 to 159, the domain is characterized as PDZ.
+At position 788 to 877, the domain is characterized as ASD1.
+At position 1427 to 1721, the domain is characterized as ASD2.
+At position 84 to 344, the domain is characterized as PPM-type phosphatase.
+At position 351 to 448, the domain is characterized as BEN.
+At position 46 to 272, the domain is characterized as Peptidase S1.
+At position 33 to 72, the domain is characterized as Pentapeptide repeat 1.
+At position 73 to 112, the domain is characterized as Pentapeptide repeat 2.
+At position 113 to 152, the domain is characterized as Pentapeptide repeat 3.
+At position 8 to 156, the domain is characterized as MPN.
+At position 113 to 229, the domain is characterized as RGS.
+At position 5 to 82, the domain is characterized as GIY-YIG.
+At position 6 to 100, the domain is characterized as Ig-like C1-type.
+At position 182 to 260, the domain is characterized as RRM.
+At position 5 to 251, the domain is characterized as Glutamine amidotransferase type-1.
+At position 39 to 114, the domain is characterized as U-box.
+At position 291 to 450, the domain is characterized as PPIase cyclophilin-type.
+At position 2 to 76, the domain is characterized as J.
+At position 233 to 376, the domain is characterized as FCP1 homology.
+At position 27 to 160, the domain is characterized as Nudix hydrolase.
+At position 331 to 525, the domain is characterized as Protein kinase.
+At position 308 to 354, the domain is characterized as G-patch.
+At position 564 to 649, the domain is characterized as S1 motif.
+At position 28 to 49, the domain is characterized as LDL-receptor class A 1; truncated.
+At position 65 to 223, the domain is characterized as MAM 1.
+At position 229 to 267, the domain is characterized as LDL-receptor class A 2.
+At position 270 to 426, the domain is characterized as MAM 2.
+At position 457 to 492, the domain is characterized as LDL-receptor class A 3.
+At position 492 to 649, the domain is characterized as MAM 3.
+At position 659 to 815, the domain is characterized as MAM 4.
+At position 817 to 975, the domain is characterized as MAM 5.
+At position 977 to 1144, the domain is characterized as MAM 6.
+At position 419 to 582, the domain is characterized as YDG.
+At position 353 to 405, the domain is characterized as FBD.
+At position 606 to 685, the domain is characterized as BRCT.
+At position 444 to 495, the domain is characterized as Rubredoxin-like.
+At position 493 to 618, the domain is characterized as DBINO.
+At position 734 to 906, the domain is characterized as Helicase ATP-binding.
+At position 1299 to 1463, the domain is characterized as Helicase C-terminal.
+At position 25 to 288, the domain is characterized as Protein kinase.
+At position 668 to 716, the domain is characterized as GRIP.
+At position 150 to 369, the domain is characterized as TRUD.
+At position 15 to 383, the domain is characterized as SAM-dependent MTase C5-type.
+At position 354 to 412, the domain is characterized as S4 RNA-binding.
+At position 182 to 290, the domain is characterized as Fe2OG dioxygenase.
+At position 14 to 201, the domain is characterized as YrdC-like.
+At position 41 to 284, the domain is characterized as ABC transporter.
+At position 906 to 979, the domain is characterized as S1 motif.
+At position 331 to 454, the domain is characterized as PLAT.
+At position 560 to 606, the domain is characterized as EGF-like.
+At position 518 to 588, the domain is characterized as Bromo.
+At position 1648 to 1739, the domain is characterized as Ig-like C2-type 3.
+At position 1745 to 1836, the domain is characterized as Ig-like C2-type 4.
+At position 1841 to 1933, the domain is characterized as Ig-like C2-type 5.
+At position 1941 to 2034, the domain is characterized as Ig-like C2-type 6.
+At position 2037 to 2135, the domain is characterized as Ig-like C2-type 7.
+At position 2141 to 2229, the domain is characterized as Ig-like C2-type 8.
+At position 2234 to 2331, the domain is characterized as Ig-like C2-type 9.
+At position 2337 to 2427, the domain is characterized as Ig-like C2-type 10.
+At position 2432 to 2518, the domain is characterized as Ig-like C2-type 11.
+At position 2528 to 2623, the domain is characterized as Ig-like C2-type 12.
+At position 8 to 298, the domain is characterized as FERM.
+At position 115 to 387, the domain is characterized as NR LBD.
+At position 448 to 551, the domain is characterized as CBM20.
+At position 26 to 106, the domain is characterized as Transferrin-like 1; first part.
+At position 107 to 172, the domain is characterized as Thyroglobulin type-1 1.
+At position 177 to 244, the domain is characterized as Thyroglobulin type-1 2.
+At position 245 to 482, the domain is characterized as Transferrin-like 1; second part.
+At position 492 to 828, the domain is characterized as Transferrin-like 2.
+At position 441 to 486, the domain is characterized as PAP-associated.
+At position 36 to 105, the domain is characterized as J.
+At position 259 to 428, the domain is characterized as tr-type G.
+At position 121 to 337, the domain is characterized as SMP-LTD.
+At position 291 to 545, the domain is characterized as Glutamine amidotransferase type-1.
+At position 3 to 91, the domain is characterized as Chorismate mutase.
+At position 92 to 269, the domain is characterized as Prephenate dehydratase.
+At position 281 to 356, the domain is characterized as ACT.
+At position 25 to 308, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 19 to 132, the domain is characterized as Ig-like V-type 1.
+At position 133 to 222, the domain is characterized as Ig-like V-type 2.
+At position 270 to 466, the domain is characterized as B30.2/SPRY.
+At position 265 to 450, the domain is characterized as VWFA 1.
+At position 467 to 640, the domain is characterized as VWFA 2.
+At position 318 to 413, the domain is characterized as Ig-like C2-type 4.
+At position 422 to 508, the domain is characterized as Ig-like C2-type 5.
+At position 528 to 622, the domain is characterized as Fibronectin type-III 1.
+At position 641 to 739, the domain is characterized as Fibronectin type-III 2.
+At position 743 to 840, the domain is characterized as Fibronectin type-III 3.
+At position 800 to 906, the domain is characterized as EH.
+At position 15 to 356, the domain is characterized as Protein kinase.
+At position 98 to 356, the domain is characterized as ABC transporter 1.
+At position 425 to 640, the domain is characterized as ABC transporter 2.
+At position 945 to 1015, the domain is characterized as Bromo.
+At position 113 to 365, the domain is characterized as AB hydrolase-1.
+At position 33 to 133, the domain is characterized as Ig-like C2-type 1.
+At position 146 to 235, the domain is characterized as Ig-like C2-type 2.
+At position 245 to 353, the domain is characterized as Ig-like C2-type 3.
+At position 407 to 563, the domain is characterized as TIR.
+At position 103 to 442, the domain is characterized as GS catalytic.
+At position 584 to 664, the domain is characterized as PB1.
+At position 1 to 98, the domain is characterized as Glutaredoxin.
+At position 41 to 105, the domain is characterized as SH3.
+At position 117 to 379, the domain is characterized as Protein kinase.
+At position 80 to 173, the domain is characterized as Ig-like.
+At position 353 to 429, the domain is characterized as ACT.
+At position 1 to 83, the domain is characterized as VPS9.
+At position 291 to 354, the domain is characterized as bZIP.
+At position 18 to 405, the domain is characterized as GBD/FH3.
+At position 985 to 1016, the domain is characterized as FH1.
+At position 1039 to 1435, the domain is characterized as FH2.
+At position 1515 to 1547, the domain is characterized as DAD.
+At position 427 to 607, the domain is characterized as Helicase ATP-binding.
+At position 100 to 195, the domain is characterized as PRC barrel.
+At position 301 to 548, the domain is characterized as Glutamine amidotransferase type-1.
+At position 264 to 403, the domain is characterized as MPN.
+At position 321 to 565, the domain is characterized as Clu.
+At position 477 to 754, the domain is characterized as Peptidase S1.
+At position 10 to 363, the domain is characterized as Kinesin motor.
+At position 33 to 164, the domain is characterized as N-terminal Ras-GEF.
+At position 208 to 455, the domain is characterized as Ras-GEF.
+At position 151 to 276, the domain is characterized as NEAT 1.
+At position 348 to 465, the domain is characterized as NEAT 2.
+At position 50 to 162, the domain is characterized as Expansin-like EG45.
+At position 306 to 379, the domain is characterized as RRM.
+At position 166 to 273, the domain is characterized as SEA.
+At position 267 to 368, the domain is characterized as Ig-like 1.
+At position 369 to 466, the domain is characterized as Ig-like 2.
+At position 471 to 561, the domain is characterized as Ig-like 3.
+At position 951 to 1002, the domain is characterized as GPS.
+At position 66 to 153, the domain is characterized as ABM.
+At position 88 to 249, the domain is characterized as CP-type G.
+At position 30 to 336, the domain is characterized as Protein kinase.
+At position 185 to 376, the domain is characterized as Glutamine amidotransferase type-1.
+At position 2 to 134, the domain is characterized as HTH marR-type.
+At position 202 to 358, the domain is characterized as YDG.
+At position 434 to 492, the domain is characterized as Pre-SET.
+At position 495 to 638, the domain is characterized as SET.
+At position 232 to 391, the domain is characterized as TrmE-type G.
+At position 314 to 441, the domain is characterized as MATH.
+At position 144 to 259, the domain is characterized as Ras-associating.
+At position 600 to 897, the domain is characterized as Dilute.
+At position 402 to 473, the domain is characterized as TRAM.
+At position 672 to 707, the domain is characterized as Anaphylatoxin-like.
+At position 1496 to 1639, the domain is characterized as NTR.
+At position 241 to 333, the domain is characterized as PA.
+At position 1 to 234, the domain is characterized as GS catalytic.
+At position 463 to 499, the domain is characterized as QLQ.
+At position 993 to 1158, the domain is characterized as Helicase ATP-binding.
+At position 1312 to 1489, the domain is characterized as Helicase C-terminal.
+At position 1918 to 1988, the domain is characterized as Bromo.
+At position 121 to 305, the domain is characterized as FAD-binding PCMH-type.
+At position 554 to 743, the domain is characterized as SEC7.
+At position 17 to 208, the domain is characterized as RNase H type-2.
+At position 1 to 24, the domain is characterized as Gla.
+At position 30 to 76, the domain is characterized as KH.
+At position 333 to 521, the domain is characterized as Helicase ATP-binding.
+At position 665 to 824, the domain is characterized as Helicase C-terminal.
+At position 95 to 220, the domain is characterized as TBDR plug.
+At position 228 to 1084, the domain is characterized as TBDR beta-barrel.
+At position 740 to 806, the domain is characterized as SH3 1.
+At position 913 to 971, the domain is characterized as SH3 2.
+At position 1002 to 1060, the domain is characterized as SH3 3.
+At position 1074 to 1138, the domain is characterized as SH3 4.
+At position 1155 to 1214, the domain is characterized as SH3 5.
+At position 1237 to 1423, the domain is characterized as DH.
+At position 1462 to 1571, the domain is characterized as PH.
+At position 1579 to 1695, the domain is characterized as C2.
+At position 332 to 414, the domain is characterized as PAN.
+At position 489 to 777, the domain is characterized as Protein kinase.
+At position 113 to 231, the domain is characterized as EamA.
+At position 171 to 250, the domain is characterized as Fe2OG dioxygenase.
+At position 180 to 378, the domain is characterized as Peptidase M12B.
+At position 387 to 476, the domain is characterized as Disintegrin.
+At position 616 to 650, the domain is characterized as EGF-like.
+At position 137 to 295, the domain is characterized as N-acetyltransferase.
+At position 11 to 68, the domain is characterized as CBS 1.
+At position 71 to 127, the domain is characterized as CBS 2.
+At position 166 to 643, the domain is characterized as Lipoxygenase.
+At position 145 to 214, the domain is characterized as BTB.
+At position 268 to 360, the domain is characterized as BACK.
+At position 1331 to 1460, the domain is characterized as MSP.
+At position 28 to 326, the domain is characterized as NodB homology.
+At position 333 to 375, the domain is characterized as Chitin-binding type-3 1.
+At position 382 to 419, the domain is characterized as Chitin-binding type-3 2.
+At position 387 to 486, the domain is characterized as Ras-associating.
+At position 576 to 713, the domain is characterized as DAGKc.
+At position 189 to 386, the domain is characterized as N-acetyltransferase.
+At position 151 to 288, the domain is characterized as N-acetyltransferase.
+At position 50 to 231, the domain is characterized as ABC transmembrane type-1.
+At position 539 to 710, the domain is characterized as W2.
+At position 300 to 398, the domain is characterized as GTD-binding.
+At position 90 to 221, the domain is characterized as PH 1.
+At position 254 to 433, the domain is characterized as PH 2.
+At position 42 to 165, the domain is characterized as Ricin B-type lectin.
+At position 176 to 224, the domain is characterized as Fibronectin type-II.
+At position 241 to 357, the domain is characterized as C-type lectin 1.
+At position 387 to 504, the domain is characterized as C-type lectin 2.
+At position 524 to 643, the domain is characterized as C-type lectin 3.
+At position 964 to 1095, the domain is characterized as C-type lectin 6.
+At position 1120 to 1231, the domain is characterized as C-type lectin 7.
+At position 1256 to 1377, the domain is characterized as C-type lectin 8.
+At position 91 to 244, the domain is characterized as Ferritin-like diiron.
+At position 56 to 166, the domain is characterized as Rhodanese 1.
+At position 194 to 315, the domain is characterized as Rhodanese 2.
+At position 315 to 495, the domain is characterized as TR mART core.
+At position 600 to 709, the domain is characterized as Peptidase S72.
+At position 72 to 188, the domain is characterized as Plastocyanin-like 1.
+At position 198 to 331, the domain is characterized as Plastocyanin-like 2.
+At position 431 to 571, the domain is characterized as Plastocyanin-like 3.
+At position 68 to 348, the domain is characterized as Protein kinase.
+At position 14 to 153, the domain is characterized as Nudix hydrolase.
+At position 740 to 820, the domain is characterized as KHA.
+At position 225 to 416, the domain is characterized as Helicase ATP-binding.
+At position 427 to 587, the domain is characterized as Helicase C-terminal.
+At position 716 to 766, the domain is characterized as GRIP.
+At position 355 to 492, the domain is characterized as YTH.
+At position 50 to 356, the domain is characterized as ABC transmembrane type-1 1.
+At position 400 to 468, the domain is characterized as SH3b.
+At position 187 to 419, the domain is characterized as Protein kinase.
+At position 21 to 175, the domain is characterized as NAC.
+At position 91 to 213, the domain is characterized as Thioredoxin 1.
+At position 621 to 771, the domain is characterized as Thioredoxin 2.
+At position 14 to 198, the domain is characterized as tr-type G.
+At position 1 to 53, the domain is characterized as PLAT.
+At position 56 to 741, the domain is characterized as Lipoxygenase.
+At position 560 to 790, the domain is characterized as Reverse transcriptase.
+At position 136 to 303, the domain is characterized as Helicase ATP-binding.
+At position 60 to 242, the domain is characterized as BPL/LPL catalytic.
+At position 188 to 389, the domain is characterized as Helicase ATP-binding.
+At position 430 to 622, the domain is characterized as Helicase C-terminal.
+At position 479 to 646, the domain is characterized as tr-type G.
+At position 707 to 808, the domain is characterized as FDX-ACB.
+At position 38 to 110, the domain is characterized as S4 RNA-binding.
+At position 53 to 187, the domain is characterized as Tyr recombinase.
+At position 20 to 271, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 270 to 520, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 168 to 312, the domain is characterized as Jacalin-type lectin 2.
+At position 5 to 81, the domain is characterized as PUA.
+At position 14 to 77, the domain is characterized as KH 1.
+At position 106 to 163, the domain is characterized as KH 2.
+At position 68 to 166, the domain is characterized as Plastocyanin-like.
+At position 391 to 454, the domain is characterized as bZIP.
+At position 360 to 425, the domain is characterized as TRAM.
+At position 682 to 1037, the domain is characterized as G-alpha.
+At position 99 to 377, the domain is characterized as Protein kinase.
+At position 1098 to 1147, the domain is characterized as KA1.
+At position 21 to 140, the domain is characterized as C-type lysozyme.
+At position 54 to 324, the domain is characterized as Protein kinase.
+At position 61 to 341, the domain is characterized as Pyruvate carboxyltransferase.
+At position 662 to 853, the domain is characterized as ATP-grasp 2.
+At position 919 to 1056, the domain is characterized as MGS-like.
+At position 422 to 508, the domain is characterized as Fibronectin type-III.
+At position 3 to 103, the domain is characterized as FAD-binding FR-type.
+At position 247 to 456, the domain is characterized as Ku.
+At position 564 to 598, the domain is characterized as SAP.
+At position 47 to 140, the domain is characterized as Fibronectin type-III.
+At position 537 to 611, the domain is characterized as RRM 1.
+At position 896 to 965, the domain is characterized as RRM 2.
+At position 159 to 224, the domain is characterized as Olduvai.
+At position 59 to 106, the domain is characterized as Myb-like.
+At position 1 to 432, the domain is characterized as SMP-LTD.
+At position 95 to 178, the domain is characterized as PRC barrel.
+At position 109 to 186, the domain is characterized as Kringle 1.
+At position 190 to 268, the domain is characterized as Kringle 2.
+At position 283 to 362, the domain is characterized as Kringle 3.
+At position 370 to 449, the domain is characterized as Kringle 4.
+At position 485 to 710, the domain is characterized as Peptidase S1.
+At position 296 to 335, the domain is characterized as LIM interaction domain (LID).
+At position 2 to 130, the domain is characterized as RCK N-terminal.
+At position 141 to 223, the domain is characterized as RCK C-terminal.
+At position 33 to 286, the domain is characterized as GH16.
+At position 28 to 275, the domain is characterized as Protein kinase.
+At position 7 to 215, the domain is characterized as RNase H type-2.
+At position 29 to 222, the domain is characterized as Lon N-terminal.
+At position 401 to 458, the domain is characterized as Chromo 1.
+At position 489 to 550, the domain is characterized as Chromo 2.
+At position 614 to 798, the domain is characterized as Helicase ATP-binding.
+At position 930 to 1093, the domain is characterized as Helicase C-terminal.
+At position 48 to 302, the domain is characterized as ABC transporter.
+At position 95 to 174, the domain is characterized as RRM 2.
+At position 17 to 69, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 83 to 129, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 60 to 122, the domain is characterized as t-SNARE coiled-coil homology.
+At position 29 to 110, the domain is characterized as GST N-terminal.
+At position 112 to 232, the domain is characterized as GST C-terminal.
+At position 349 to 428, the domain is characterized as OCT.
+At position 3 to 130, the domain is characterized as CMP/dCMP-type deaminase.
+At position 102 to 247, the domain is characterized as PA14.
+At position 1 to 99, the domain is characterized as N-acetyltransferase.
+At position 169 to 278, the domain is characterized as CBM21.
+At position 1115 to 1185, the domain is characterized as BIG2.
+At position 1438 to 1502, the domain is characterized as SLH.
+At position 135 to 184, the domain is characterized as bHLH.
+At position 186 to 344, the domain is characterized as Cupin type-1 1.
+At position 403 to 569, the domain is characterized as Cupin type-1 2.
+At position 37 to 227, the domain is characterized as Glutamine amidotransferase type-1.
+At position 228 to 426, the domain is characterized as GMPS ATP-PPase.
+At position 126 to 245, the domain is characterized as PX.
+At position 288 to 402, the domain is characterized as xRRM.
+At position 336 to 399, the domain is characterized as bZIP.
+At position 179 to 223, the domain is characterized as bZIP.
+At position 247 to 458, the domain is characterized as DOG1.
+At position 184 to 352, the domain is characterized as tr-type G.
+At position 1 to 128, the domain is characterized as C2.
+At position 573 to 635, the domain is characterized as FIP-RBD.
+At position 220 to 378, the domain is characterized as TrmE-type G.
+At position 492 to 679, the domain is characterized as Helicase C-terminal.
+At position 152 to 337, the domain is characterized as FAD-binding PCMH-type.
+At position 95 to 173, the domain is characterized as PRC barrel.
+At position 5 to 110, the domain is characterized as PH.
+At position 157 to 414, the domain is characterized as Protein kinase.
+At position 415 to 486, the domain is characterized as AGC-kinase C-terminal.
+At position 2 to 183, the domain is characterized as Glutamine amidotransferase type-2.
+At position 277 to 582, the domain is characterized as Asparagine synthetase.
+At position 35 to 422, the domain is characterized as uDENN FNIP1/2-type.
+At position 430 to 772, the domain is characterized as cDENN FNIP1/2-type.
+At position 777 to 842, the domain is characterized as dDENN FNIP1/2-type.
+At position 7 to 629, the domain is characterized as PFL.
+At position 636 to 764, the domain is characterized as Glycine radical.
+At position 47 to 223, the domain is characterized as BPL/LPL catalytic.
+At position 272 to 456, the domain is characterized as DH.
+At position 488 to 600, the domain is characterized as PH.
+At position 611 to 672, the domain is characterized as SH3.
+At position 431 to 448, the domain is characterized as WH2.
+At position 5 to 80, the domain is characterized as REM-1 1.
+At position 93 to 163, the domain is characterized as REM-1 2.
+At position 165 to 245, the domain is characterized as REM-1 3.
+At position 559 to 818, the domain is characterized as Protein kinase.
+At position 819 to 889, the domain is characterized as AGC-kinase C-terminal.
+At position 10 to 242, the domain is characterized as ABC transporter.
+At position 88 to 160, the domain is characterized as ACT 1.
+At position 321 to 395, the domain is characterized as ACT 2.
+At position 179 to 223, the domain is characterized as DSL.
+At position 225 to 257, the domain is characterized as EGF-like 1.
+At position 257 to 288, the domain is characterized as EGF-like 2.
+At position 290 to 328, the domain is characterized as EGF-like 3.
+At position 330 to 366, the domain is characterized as EGF-like 4; calcium-binding.
+At position 368 to 405, the domain is characterized as EGF-like 5.
+At position 407 to 443, the domain is characterized as EGF-like 6.
+At position 445 to 481, the domain is characterized as EGF-like 7.
+At position 483 to 519, the domain is characterized as EGF-like 8.
+At position 153 to 205, the domain is characterized as BSD.
+At position 48 to 273, the domain is characterized as L-type lectin-like.
+At position 71 to 158, the domain is characterized as Ig-like V-type 1.
+At position 159 to 253, the domain is characterized as Ig-like V-type 2.
+At position 5 to 329, the domain is characterized as Kinesin motor.
+At position 375 to 437, the domain is characterized as t-SNARE coiled-coil homology.
+At position 14 to 202, the domain is characterized as RNase H type-2.
+At position 214 to 330, the domain is characterized as C2 2.
+At position 369 to 502, the domain is characterized as C2 3.
+At position 951 to 1078, the domain is characterized as C2 4.
+At position 1126 to 1250, the domain is characterized as C2 5.
+At position 1430 to 1549, the domain is characterized as C2 6.
+At position 1675 to 1824, the domain is characterized as C2 7.
+At position 215 to 446, the domain is characterized as NR LBD.
+At position 57 to 345, the domain is characterized as ABC transmembrane type-1 1.
+At position 378 to 662, the domain is characterized as ABC transporter 1.
+At position 789 to 1089, the domain is characterized as ABC transmembrane type-1 2.
+At position 1126 to 1416, the domain is characterized as ABC transporter 2.
+At position 1 to 136, the domain is characterized as MGS-like.
+At position 233 to 318, the domain is characterized as PDZ 1.
+At position 339 to 422, the domain is characterized as PDZ 2.
+At position 468 to 554, the domain is characterized as PDZ 3.
+At position 600 to 688, the domain is characterized as PDZ 4.
+At position 164 to 339, the domain is characterized as Helicase ATP-binding.
+At position 493 to 647, the domain is characterized as Helicase C-terminal.
+At position 316 to 509, the domain is characterized as Helicase ATP-binding.
+At position 700 to 882, the domain is characterized as Helicase C-terminal.
+At position 79 to 174, the domain is characterized as SH2.
+At position 161 to 210, the domain is characterized as SOCS box.
+At position 9 to 130, the domain is characterized as Response regulatory 1.
+At position 139 to 255, the domain is characterized as Response regulatory 2.
+At position 299 to 432, the domain is characterized as GGDEF.
+At position 443 to 691, the domain is characterized as EAL.
+At position 67 to 254, the domain is characterized as BPL/LPL catalytic.
+At position 686 to 768, the domain is characterized as BRCT 1.
+At position 825 to 935, the domain is characterized as BRCT 2.
+At position 271 to 360, the domain is characterized as Ig-like C2-type 1.
+At position 440 to 539, the domain is characterized as Ig-like C2-type 2.
+At position 1001 to 1085, the domain is characterized as Ig-like C2-type 3.
+At position 1135 to 1226, the domain is characterized as Ig-like C2-type 4.
+At position 1233 to 1324, the domain is characterized as Ig-like C2-type 5.
+At position 525 to 598, the domain is characterized as Histone-fold.
+At position 8 to 107, the domain is characterized as IF rod.
+At position 427 to 477, the domain is characterized as DHHC.
+At position 6 to 88, the domain is characterized as Cystatin.
+At position 20 to 153, the domain is characterized as VHS.
+At position 298 to 317, the domain is characterized as UIM 2.
+At position 85 to 501, the domain is characterized as Peptidase A1.
+At position 311 to 416, the domain is characterized as Saposin B-type.
+At position 103 to 179, the domain is characterized as RRM.
+At position 92 to 441, the domain is characterized as Peptidase A1.
+At position 39 to 424, the domain is characterized as Helicase ATP-binding.
+At position 441 to 604, the domain is characterized as Helicase C-terminal.
+At position 56 to 106, the domain is characterized as LIM zinc-binding 1.
+At position 15 to 250, the domain is characterized as ABC transporter.
+At position 31 to 74, the domain is characterized as WAP 1.
+At position 119 to 167, the domain is characterized as WAP 2.
+At position 61 to 208, the domain is characterized as Tyrosine-protein phosphatase.
+At position 102 to 600, the domain is characterized as Peptidase S8.
+At position 81 to 414, the domain is characterized as SAM-dependent MTase C5-type.
+At position 174 to 275, the domain is characterized as PpiC 1.
+At position 284 to 384, the domain is characterized as PpiC 2.
+At position 217 to 406, the domain is characterized as Helicase ATP-binding.
+At position 417 to 577, the domain is characterized as Helicase C-terminal.
+At position 91 to 330, the domain is characterized as ABC transporter 1.
+At position 401 to 618, the domain is characterized as ABC transporter 2.
+At position 715 to 1005, the domain is characterized as ABC transmembrane type-1 2.
+At position 19 to 196, the domain is characterized as FCP1 homology.
+At position 25 to 175, the domain is characterized as GAF.
+At position 185 to 255, the domain is characterized as PAS.
+At position 263 to 313, the domain is characterized as PAC.
+At position 342 to 464, the domain is characterized as GGDEF.
+At position 472 to 732, the domain is characterized as EAL.
+At position 150 to 285, the domain is characterized as PAS 1.
+At position 303 to 409, the domain is characterized as PAS 2.
+At position 460 to 728, the domain is characterized as Protein kinase.
+At position 748 to 819, the domain is characterized as U-box.
+At position 764 to 840, the domain is characterized as Carrier 1.
+At position 1557 to 1633, the domain is characterized as Carrier 2.
+At position 85 to 779, the domain is characterized as Myosin motor.
+At position 1 to 134, the domain is characterized as ADF-H.
+At position 58 to 131, the domain is characterized as Peptidase A2.
+At position 338 to 523, the domain is characterized as Reverse transcriptase.
+At position 957 to 1119, the domain is characterized as Integrase catalytic.
+At position 719 to 1020, the domain is characterized as Protein kinase.
+At position 309 to 387, the domain is characterized as RRM.
+At position 489 to 637, the domain is characterized as GST C-terminal.
+At position 33 to 143, the domain is characterized as Ig-like V-type 1.
+At position 157 to 258, the domain is characterized as Ig-like V-type 2.
+At position 68 to 177, the domain is characterized as Inhibitor I9.
+At position 200 to 512, the domain is characterized as Peptidase S8.
+At position 6 to 86, the domain is characterized as KRAB.
+At position 157 to 201, the domain is characterized as CHCH.
+At position 81 to 184, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 147 to 265, the domain is characterized as LTD.
+At position 110 to 172, the domain is characterized as S4 RNA-binding.
+At position 287 to 323, the domain is characterized as EGF-like.
+At position 465 to 742, the domain is characterized as Protein kinase.
+At position 175 to 331, the domain is characterized as Exonuclease.
+At position 73 to 168, the domain is characterized as Fibronectin type-III 1.
+At position 172 to 260, the domain is characterized as Ig-like C2-type 1.
+At position 269 to 364, the domain is characterized as Fibronectin type-III 2.
+At position 382 to 466, the domain is characterized as Ig-like C2-type 2.
+At position 138 to 423, the domain is characterized as Protein kinase.
+At position 19 to 150, the domain is characterized as C-type lysozyme.
+At position 84 to 141, the domain is characterized as CBS 2.
+At position 249 to 288, the domain is characterized as GRAM 1.
+At position 289 to 387, the domain is characterized as PH.
+At position 733 to 799, the domain is characterized as GRAM 2.
+At position 59 to 328, the domain is characterized as Protein kinase.
+At position 393 to 491, the domain is characterized as PilZ.
+At position 98 to 770, the domain is characterized as Peptidase M13.
+At position 313 to 394, the domain is characterized as Saposin B-type 3.
+At position 438 to 519, the domain is characterized as Saposin B-type 4.
+At position 521 to 557, the domain is characterized as Saposin A-type 2.
+At position 27 to 249, the domain is characterized as ABC transporter.
+At position 403 to 447, the domain is characterized as LysM.
+At position 387 to 451, the domain is characterized as TRAM.
+At position 62 to 91, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 101 to 130, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 3 to 461, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 473 to 769, the domain is characterized as UvrD-like helicase C-terminal.
+At position 87 to 209, the domain is characterized as FAD-binding FR-type.
+At position 194 to 372, the domain is characterized as Helicase ATP-binding.
+At position 383 to 544, the domain is characterized as Helicase C-terminal.
+At position 316 to 552, the domain is characterized as NR LBD.
+At position 998 to 1286, the domain is characterized as Autotransporter.
+At position 74 to 174, the domain is characterized as PI3K-ABD.
+At position 266 to 358, the domain is characterized as PI3K-RBD.
+At position 425 to 577, the domain is characterized as C2 PI3K-type.
+At position 601 to 788, the domain is characterized as PIK helical.
+At position 853 to 1168, the domain is characterized as PI3K/PI4K catalytic.
+At position 10 to 153, the domain is characterized as RNase H type-1.
+At position 612 to 733, the domain is characterized as STAS.
+At position 88 to 165, the domain is characterized as Cytochrome b5 heme-binding.
+At position 197 to 563, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 24 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 151 to 270, the domain is characterized as Fe2OG dioxygenase.
+At position 198 to 323, the domain is characterized as TFIIS central.
+At position 939 to 1150, the domain is characterized as JmjC.
+At position 162 to 256, the domain is characterized as MaoC-like.
+At position 55 to 346, the domain is characterized as ABC transmembrane type-1 1.
+At position 381 to 626, the domain is characterized as ABC transporter 1.
+At position 1027 to 1280, the domain is characterized as ABC transporter 2.
+At position 186 to 264, the domain is characterized as UBX.
+At position 49 to 79, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 342 to 420, the domain is characterized as OCT.
+At position 121 to 172, the domain is characterized as Myb-like.
+At position 214 to 277, the domain is characterized as KH.
+At position 231 to 503, the domain is characterized as Deacetylase sirtuin-type.
+At position 11 to 337, the domain is characterized as YjeF C-terminal.
+At position 9 to 86, the domain is characterized as RRM.
+At position 553 to 607, the domain is characterized as FHA.
+At position 73 to 159, the domain is characterized as BAG.
+At position 129 to 208, the domain is characterized as PDZ.
+At position 228 to 297, the domain is characterized as SH3.
+At position 351 to 538, the domain is characterized as Guanylate kinase-like.
+At position 15 to 243, the domain is characterized as AB hydrolase-1.
+At position 34 to 68, the domain is characterized as LRRNT.
+At position 149 to 196, the domain is characterized as LRRCT.
+At position 1 to 222, the domain is characterized as Alpha-carbonic anhydrase.
+At position 242 to 410, the domain is characterized as TLDc.
+At position 105 to 290, the domain is characterized as CP-type G.
+At position 58 to 319, the domain is characterized as Rab-GAP TBC.
+At position 78 to 395, the domain is characterized as Peptidase A1.
+At position 160 to 202, the domain is characterized as G-patch.
+At position 193 to 229, the domain is characterized as DFDF.
+At position 95 to 456, the domain is characterized as PRONE.
+At position 297 to 378, the domain is characterized as RRM.
+At position 260 to 504, the domain is characterized as ABC transporter 2.
+At position 24 to 148, the domain is characterized as Barwin.
+At position 76 to 262, the domain is characterized as Rho-GAP.
+At position 260 to 329, the domain is characterized as HTH OST-type 2.
+At position 364 to 433, the domain is characterized as HTH OST-type 3.
+At position 540 to 597, the domain is characterized as Tudor 1.
+At position 730 to 787, the domain is characterized as Tudor 2.
+At position 27 to 117, the domain is characterized as Ig-like 1.
+At position 122 to 209, the domain is characterized as Ig-like 2.
+At position 222 to 309, the domain is characterized as Ig-like 3.
+At position 314 to 399, the domain is characterized as Ig-like 4.
+At position 408 to 502, the domain is characterized as Fibronectin type-III 1.
+At position 504 to 600, the domain is characterized as Fibronectin type-III 2.
+At position 605 to 704, the domain is characterized as Fibronectin type-III 3.
+At position 809 to 905, the domain is characterized as Fibronectin type-III 5.
+At position 553 to 630, the domain is characterized as Carrier.
+At position 174 to 273, the domain is characterized as SWIRM.
+At position 210 to 373, the domain is characterized as Helicase ATP-binding.
+At position 1453 to 1469, the domain is characterized as Post-SET.
+At position 23 to 249, the domain is characterized as Peptidase S1.
+At position 392 to 465, the domain is characterized as PAS.
+At position 523 to 745, the domain is characterized as Histidine kinase.
+At position 436 to 505, the domain is characterized as SH3b.
+At position 326 to 487, the domain is characterized as Helicase ATP-binding.
+At position 541 to 701, the domain is characterized as Helicase C-terminal.
+At position 83 to 250, the domain is characterized as TNase-like.
+At position 145 to 213, the domain is characterized as TSP type-1.
+At position 517 to 881, the domain is characterized as Reverse transcriptase.
+At position 177 to 235, the domain is characterized as CBS 2.
+At position 32 to 275, the domain is characterized as ATP-grasp.
+At position 560 to 643, the domain is characterized as Carrier.
+At position 5 to 100, the domain is characterized as HIG1.
+At position 565 to 615, the domain is characterized as SANT.
+At position 664 to 763, the domain is characterized as CXC.
+At position 778 to 893, the domain is characterized as SET.
+At position 262 to 346, the domain is characterized as Toprim.
+At position 2 to 182, the domain is characterized as UmuC.
+At position 918 to 1067, the domain is characterized as bMERB.
+At position 461 to 614, the domain is characterized as N-acetyltransferase.
+At position 703 to 773, the domain is characterized as Bromo.
+At position 31 to 293, the domain is characterized as GH18.
+At position 186 to 265, the domain is characterized as RRM.
+At position 728 to 876, the domain is characterized as Flavodoxin-like.
+At position 8 to 264, the domain is characterized as Nudix hydrolase.
+At position 248 to 443, the domain is characterized as GATase cobBQ-type.
+At position 38 to 99, the domain is characterized as Ig-like C2-type 1.
+At position 123 to 188, the domain is characterized as Ig-like C2-type 2.
+At position 225 to 292, the domain is characterized as Ig-like C2-type 3.
+At position 320 to 373, the domain is characterized as Ig-like C2-type 4.
+At position 407 to 460, the domain is characterized as Ig-like C2-type 5.
+At position 222 to 439, the domain is characterized as Helicase ATP-binding.
+At position 476 to 644, the domain is characterized as Helicase C-terminal.
+At position 27 to 134, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 258 to 351, the domain is characterized as Ig-like C2-type 3.
+At position 360 to 460, the domain is characterized as Ig-like C2-type 4.
+At position 578 to 866, the domain is characterized as Protein kinase.
+At position 811 to 905, the domain is characterized as Fibronectin type-III 6.
+At position 909 to 1001, the domain is characterized as Fibronectin type-III 7.
+At position 1005 to 1089, the domain is characterized as Fibronectin type-III 8.
+At position 1343 to 1598, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 1630 to 1889, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 89 to 170, the domain is characterized as PA.
+At position 64 to 229, the domain is characterized as Helicase ATP-binding.
+At position 8 to 176, the domain is characterized as 3'-5' exonuclease.
+At position 214 to 294, the domain is characterized as HRDC.
+At position 308 to 361, the domain is characterized as HTH myb-type 1.
+At position 362 to 422, the domain is characterized as HTH myb-type 2.
+At position 515 to 676, the domain is characterized as N-acetyltransferase.
+At position 5 to 167, the domain is characterized as UBC core.
+At position 6 to 149, the domain is characterized as Clp R.
+At position 46 to 241, the domain is characterized as Glutamine amidotransferase type-1.
+At position 122 to 385, the domain is characterized as Protein kinase.
+At position 35 to 119, the domain is characterized as Kringle.
+At position 121 to 215, the domain is characterized as WSC.
+At position 219 to 326, the domain is characterized as CUB.
+At position 54 to 172, the domain is characterized as RGS.
+At position 663 to 745, the domain is characterized as DIX.
+At position 318 to 601, the domain is characterized as ABC transmembrane type-1 1.
+At position 633 to 857, the domain is characterized as ABC transporter 1.
+At position 975 to 1260, the domain is characterized as ABC transmembrane type-1 2.
+At position 1296 to 1530, the domain is characterized as ABC transporter 2.
+At position 5 to 187, the domain is characterized as N-acetyltransferase.
+At position 279 to 417, the domain is characterized as Flavodoxin-like.
+At position 922 to 1206, the domain is characterized as PKS/mFAS DH.
+At position 2426 to 2503, the domain is characterized as Carrier.
+At position 10 to 210, the domain is characterized as YjeF N-terminal.
+At position 283 to 462, the domain is characterized as Helicase ATP-binding.
+At position 490 to 640, the domain is characterized as Helicase C-terminal.
+At position 392 to 427, the domain is characterized as EF-hand 2.
+At position 472 to 499, the domain is characterized as EF-hand 4.
+At position 360 to 589, the domain is characterized as AIG1-type G.
+At position 57 to 142, the domain is characterized as Inhibitor I9.
+At position 158 to 597, the domain is characterized as Peptidase S8.
+At position 383 to 461, the domain is characterized as PA.
+At position 7 to 64, the domain is characterized as CSD.
+At position 147 to 423, the domain is characterized as Protein kinase.
+At position 22 to 55, the domain is characterized as WW.
+At position 141 to 402, the domain is characterized as F-BAR.
+At position 351 to 520, the domain is characterized as Helicase C-terminal.
+At position 622 to 703, the domain is characterized as BRCT.
+At position 38 to 123, the domain is characterized as ELM2.
+At position 124 to 175, the domain is characterized as SANT 1.
+At position 328 to 379, the domain is characterized as SANT 2.
+At position 32 to 252, the domain is characterized as ABC transmembrane type-2.
+At position 132 to 254, the domain is characterized as OmpA-like.
+At position 159 to 219, the domain is characterized as SAM.
+At position 137 to 216, the domain is characterized as RRM.
+At position 425 to 470, the domain is characterized as LEM.
+At position 525 to 635, the domain is characterized as GIY-YIG.
+At position 749 to 822, the domain is characterized as Smr.
+At position 51 to 161, the domain is characterized as Expansin-like EG45.
+At position 174 to 255, the domain is characterized as Expansin-like CBD.
+At position 612 to 723, the domain is characterized as tRNA-binding.
+At position 558 to 622, the domain is characterized as FHA.
+At position 243 to 411, the domain is characterized as PCI.
+At position 902 to 1180, the domain is characterized as PKS/mFAS DH.
+At position 1664 to 1742, the domain is characterized as Carrier.
+At position 112 to 372, the domain is characterized as GS catalytic.
+At position 36 to 286, the domain is characterized as Septin-type G.
+At position 89 to 362, the domain is characterized as Pyruvate carboxyltransferase.
+At position 527 to 640, the domain is characterized as Toprim.
+At position 131 to 355, the domain is characterized as NR LBD.
+At position 696 to 985, the domain is characterized as Protein kinase.
+At position 275 to 294, the domain is characterized as UIM 1.
+At position 300 to 319, the domain is characterized as UIM 2.
+At position 33 to 156, the domain is characterized as C-type lectin.
+At position 1568 to 1685, the domain is characterized as SET.
+At position 1691 to 1707, the domain is characterized as Post-SET.
+At position 28 to 342, the domain is characterized as G-alpha.
+At position 16 to 299, the domain is characterized as Radical SAM core.
+At position 47 to 79, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 80 to 112, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 4 to 89, the domain is characterized as BMC.
+At position 892 to 1084, the domain is characterized as DH.
+At position 1113 to 1207, the domain is characterized as PH 1.
+At position 1363 to 1461, the domain is characterized as PH 2.
+At position 50 to 291, the domain is characterized as Protein kinase.
+At position 19 to 317, the domain is characterized as F-BAR.
+At position 507 to 695, the domain is characterized as Rho-GAP.
+At position 746 to 805, the domain is characterized as SH3.
+At position 384 to 433, the domain is characterized as bHLH.
+At position 270 to 450, the domain is characterized as PCI.
+At position 351 to 430, the domain is characterized as OCT.
+At position 16 to 298, the domain is characterized as Protein kinase.
+At position 212 to 247, the domain is characterized as UVR.
+At position 342 to 406, the domain is characterized as ACT.
+At position 602 to 878, the domain is characterized as Autotransporter.
+At position 656 to 736, the domain is characterized as BRCT.
+At position 105 to 343, the domain is characterized as Reverse transcriptase.
+At position 525 to 571, the domain is characterized as HNH.
+At position 241 to 301, the domain is characterized as GRAM 1.
+At position 292 to 391, the domain is characterized as PH.
+At position 261 to 321, the domain is characterized as EamA.
+At position 228 to 271, the domain is characterized as CUE.
+At position 90 to 327, the domain is characterized as KIND.
+At position 399 to 417, the domain is characterized as WH2 1.
+At position 463 to 480, the domain is characterized as WH2 2.
+At position 756 to 774, the domain is characterized as WH2.
+At position 291 to 390, the domain is characterized as PpiC 2.
+At position 92 to 153, the domain is characterized as SH3.
+At position 159 to 256, the domain is characterized as SH2.
+At position 32 to 90, the domain is characterized as Kazal-like.
+At position 276 to 323, the domain is characterized as F-box.
+At position 177 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 3 to 196, the domain is characterized as DPCK.
+At position 74 to 352, the domain is characterized as PPM-type phosphatase.
+At position 354 to 407, the domain is characterized as HAMP.
+At position 13 to 443, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 928 to 1235, the domain is characterized as PKS/mFAS DH.
+At position 2467 to 2546, the domain is characterized as Carrier.
+At position 317 to 407, the domain is characterized as Ras-associating.
+At position 456 to 566, the domain is characterized as PH.
+At position 291 to 376, the domain is characterized as Apple 4.
+At position 390 to 622, the domain is characterized as Peptidase S1.
+At position 12 to 198, the domain is characterized as RNase H type-2.
+At position 133 to 218, the domain is characterized as MEIS N-terminal.
+At position 794 to 867, the domain is characterized as Carrier 1.
+At position 1900 to 1976, the domain is characterized as Carrier 2.
+At position 2436 to 2512, the domain is characterized as Carrier 3.
+At position 54 to 282, the domain is characterized as Ferric oxidoreductase.
+At position 283 to 390, the domain is characterized as FAD-binding FR-type.
+At position 458 to 664, the domain is characterized as MCM.
+At position 23 to 119, the domain is characterized as Ig-like.
+At position 21 to 185, the domain is characterized as PPIase cyclophilin-type.
+At position 100 to 335, the domain is characterized as Radical SAM core.
+At position 192 to 389, the domain is characterized as B30.2/SPRY.
+At position 506 to 628, the domain is characterized as HD.
+At position 746 to 829, the domain is characterized as ACT 1.
+At position 859 to 933, the domain is characterized as ACT 2.
+At position 4 to 470, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 501 to 795, the domain is characterized as UvrD-like helicase C-terminal.
+At position 5 to 135, the domain is characterized as MPN.
+At position 135 to 250, the domain is characterized as Gnk2-homologous 2.
+At position 346 to 626, the domain is characterized as Protein kinase.
+At position 35 to 254, the domain is characterized as BPL/LPL catalytic.
+At position 376 to 676, the domain is characterized as Protein kinase.
+At position 1020 to 1219, the domain is characterized as MAGE.
+At position 128 to 198, the domain is characterized as BTB.
+At position 243 to 308, the domain is characterized as BACK.
+At position 3 to 125, the domain is characterized as N-terminal Ras-GEF.
+At position 152 to 383, the domain is characterized as Ras-GEF.
+At position 420 to 455, the domain is characterized as EF-hand 1.
+At position 458 to 484, the domain is characterized as EF-hand 2.
+At position 376 to 418, the domain is characterized as EGF-like.
+At position 5 to 192, the domain is characterized as YrdC-like.
+At position 2 to 137, the domain is characterized as TIR.
+At position 166 to 417, the domain is characterized as NB-ARC.
+At position 28 to 68, the domain is characterized as EGF-like 1; calcium-binding.
+At position 69 to 110, the domain is characterized as EGF-like 2; calcium-binding.
+At position 111 to 147, the domain is characterized as EGF-like 3; calcium-binding.
+At position 160 to 196, the domain is characterized as EGF-like 4.
+At position 200 to 235, the domain is characterized as EGF-like 5.
+At position 269 to 304, the domain is characterized as EGF-like 6.
+At position 306 to 346, the domain is characterized as EGF-like 7; calcium-binding.
+At position 347 to 385, the domain is characterized as EGF-like 8; calcium-binding.
+At position 386 to 426, the domain is characterized as EGF-like 9; calcium-binding.
+At position 822 to 934, the domain is characterized as CUB.
+At position 401 to 480, the domain is characterized as B5.
+At position 367 to 473, the domain is characterized as ERCC4.
+At position 11 to 370, the domain is characterized as Kinesin motor.
+At position 666 to 931, the domain is characterized as Protein kinase.
+At position 262 to 407, the domain is characterized as YDG.
+At position 30 to 136, the domain is characterized as Ig-like V-type.
+At position 1 to 125, the domain is characterized as RNase III.
+At position 432 to 705, the domain is characterized as Protein kinase.
+At position 58 to 330, the domain is characterized as Septin-type G.
+At position 230 to 395, the domain is characterized as Hflx-type G.
+At position 161 to 280, the domain is characterized as Response regulatory.
+At position 410 to 733, the domain is characterized as PDEase.
+At position 75 to 124, the domain is characterized as TSP type-1 1.
+At position 418 to 468, the domain is characterized as TSP type-1 2.
+At position 478 to 535, the domain is characterized as TSP type-1 3.
+At position 564 to 626, the domain is characterized as TSP type-1 4.
+At position 703 to 760, the domain is characterized as TSP type-1 5.
+At position 763 to 818, the domain is characterized as TSP type-1 6.
+At position 819 to 881, the domain is characterized as TSP type-1 7.
+At position 896 to 992, the domain is characterized as Ig-like C2-type 1.
+At position 1185 to 1279, the domain is characterized as Ig-like C2-type 2.
+At position 1296 to 1378, the domain is characterized as Ig-like C2-type 3.
+At position 1424 to 1482, the domain is characterized as TSP type-1 8.
+At position 1483 to 1545, the domain is characterized as TSP type-1 9.
+At position 1597 to 1644, the domain is characterized as TSP type-1 10.
+At position 1655 to 1691, the domain is characterized as PLAC.
+At position 1 to 133, the domain is characterized as DAC.
+At position 23 to 217, the domain is characterized as EngB-type G.
+At position 22 to 289, the domain is characterized as Protein kinase.
+At position 155 to 439, the domain is characterized as CP-type G.
+At position 277 to 476, the domain is characterized as Helicase ATP-binding.
+At position 1190 to 1336, the domain is characterized as Helicase C-terminal.
+At position 346 to 398, the domain is characterized as bHLH.
+At position 243 to 429, the domain is characterized as Glutamine amidotransferase type-1.
+At position 60 to 326, the domain is characterized as GH18.
+At position 4 to 260, the domain is characterized as ABC transporter 1.
+At position 324 to 518, the domain is characterized as ABC transporter 2.
+At position 22 to 158, the domain is characterized as Thioredoxin.
+At position 300 to 351, the domain is characterized as LRRCT.
+At position 104 to 492, the domain is characterized as Protein kinase.
+At position 332 to 425, the domain is characterized as Fibronectin type-III 1.
+At position 427 to 523, the domain is characterized as Fibronectin type-III 2.
+At position 524 to 620, the domain is characterized as Fibronectin type-III 3.
+At position 622 to 733, the domain is characterized as Fibronectin type-III 4.
+At position 6 to 350, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 101 to 341, the domain is characterized as FAD-binding FR-type.
+At position 584 to 665, the domain is characterized as PDZ.
+At position 54 to 106, the domain is characterized as bHLH.
+At position 27 to 134, the domain is characterized as Rhodanese 1.
+At position 164 to 283, the domain is characterized as Rhodanese 2.
+At position 97 to 298, the domain is characterized as Helicase ATP-binding.
+At position 619 to 785, the domain is characterized as Toprim.
+At position 636 to 712, the domain is characterized as Ubiquitin-like.
+At position 1709 to 1779, the domain is characterized as Bromo.
+At position 1565 to 1739, the domain is characterized as Helicase C-terminal 2.
+At position 1812 to 2175, the domain is characterized as SEC63 2.
+At position 28 to 406, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 333 to 641, the domain is characterized as Pterin-binding.
+At position 19 to 142, the domain is characterized as Rhodanese.
+At position 67 to 165, the domain is characterized as Peptidase A1.
+At position 10 to 272, the domain is characterized as Protein kinase.
+At position 8 to 74, the domain is characterized as HMA.
+At position 601 to 677, the domain is characterized as BRCT.
+At position 74 to 145, the domain is characterized as KRAB.
+At position 351 to 466, the domain is characterized as BRCT.
+At position 330 to 379, the domain is characterized as PH.
+At position 94 to 199, the domain is characterized as FAD-binding FR-type.
+At position 72 to 259, the domain is characterized as hSac2.
+At position 32 to 308, the domain is characterized as CN hydrolase.
+At position 322 to 372, the domain is characterized as bHLH.
+At position 310 to 346, the domain is characterized as CBM1.
+At position 200 to 260, the domain is characterized as KH.
+At position 326 to 419, the domain is characterized as HD.
+At position 1 to 199, the domain is characterized as ABC transporter.
+At position 34 to 510, the domain is characterized as Sema.
+At position 512 to 582, the domain is characterized as PSI.
+At position 589 to 649, the domain is characterized as Ig-like C2-type.
+At position 115 to 154, the domain is characterized as Pentapeptide repeat.
+At position 91 to 372, the domain is characterized as Protein kinase.
+At position 577 to 659, the domain is characterized as S1 motif.
+At position 19 to 186, the domain is characterized as FAD-binding PCMH-type.
+At position 241 to 402, the domain is characterized as Helicase C-terminal.
+At position 116 to 144, the domain is characterized as IQ 1.
+At position 145 to 167, the domain is characterized as IQ 2.
+At position 488 to 658, the domain is characterized as tr-type G.
+At position 23 to 289, the domain is characterized as Dynamin-type G.
+At position 513 to 621, the domain is characterized as PH.
+At position 121 to 172, the domain is characterized as bHLH.
+At position 298 to 446, the domain is characterized as SIS 1.
+At position 480 to 621, the domain is characterized as SIS 2.
+At position 205 to 364, the domain is characterized as SUN.
+At position 624 to 796, the domain is characterized as PCI.
+At position 2 to 122, the domain is characterized as TRM112.
+At position 431 to 772, the domain is characterized as Kinesin motor.
+At position 57 to 238, the domain is characterized as Macro.
+At position 690 to 783, the domain is characterized as FDX-ACB.
+At position 146 to 234, the domain is characterized as PilZ.
+At position 171 to 394, the domain is characterized as Radical SAM core.
+At position 164 to 447, the domain is characterized as Protein kinase.
+At position 4 to 126, the domain is characterized as RCK N-terminal.
+At position 135 to 219, the domain is characterized as RCK C-terminal.
+At position 66 to 300, the domain is characterized as GP-PDE.
+At position 809 to 1207, the domain is characterized as FH2.
+At position 74 to 362, the domain is characterized as ABC transmembrane type-1.
+At position 507 to 737, the domain is characterized as ABC transporter.
+At position 13 to 80, the domain is characterized as PAS.
+At position 146 to 366, the domain is characterized as Histidine kinase.
+At position 35 to 461, the domain is characterized as Sema.
+At position 824 to 913, the domain is characterized as IPT/TIG 1.
+At position 1 to 27, the domain is characterized as Jacalin-type lectin.
+At position 508 to 596, the domain is characterized as SPAZ.
+At position 24 to 141, the domain is characterized as C-type lectin.
+At position 142 to 177, the domain is characterized as EGF-like.
+At position 180 to 241, the domain is characterized as Sushi 1.
+At position 242 to 303, the domain is characterized as Sushi 2.
+At position 305 to 366, the domain is characterized as Sushi 3.
+At position 368 to 429, the domain is characterized as Sushi 4.
+At position 430 to 488, the domain is characterized as Sushi 5.
+At position 148 to 379, the domain is characterized as Radical SAM core.
+At position 348 to 684, the domain is characterized as F5/8 type A 2.
+At position 348 to 526, the domain is characterized as Plastocyanin-like 3.
+At position 536 to 684, the domain is characterized as Plastocyanin-like 4.
+At position 1578 to 1907, the domain is characterized as F5/8 type A 3.
+At position 1578 to 1751, the domain is characterized as Plastocyanin-like 5.
+At position 1761 to 1907, the domain is characterized as Plastocyanin-like 6.
+At position 1907 to 2061, the domain is characterized as F5/8 type C 1.
+At position 2066 to 2221, the domain is characterized as F5/8 type C 2.
+At position 94 to 191, the domain is characterized as BRICHOS.
+At position 391 to 430, the domain is characterized as STI1.
+At position 20 to 476, the domain is characterized as Sema.
+At position 478 to 527, the domain is characterized as PSI.
+At position 556 to 592, the domain is characterized as Ig-like.
+At position 1513 to 1577, the domain is characterized as SAM.
+At position 239 to 400, the domain is characterized as Helicase C-terminal.
+At position 682 to 711, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 1131 to 1295, the domain is characterized as PNPLA.
+At position 33 to 279, the domain is characterized as GB1/RHD3-type G.
+At position 413 to 477, the domain is characterized as SAM 1.
+At position 483 to 549, the domain is characterized as SAM 2.
+At position 561 to 704, the domain is characterized as TIR.
+At position 1 to 298, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 279 to 584, the domain is characterized as UvrD-like helicase C-terminal.
+At position 403 to 550, the domain is characterized as MATH.
+At position 28 to 227, the domain is characterized as GH16.
+At position 181 to 272, the domain is characterized as CS.
+At position 292 to 379, the domain is characterized as SGS.
+At position 190 to 282, the domain is characterized as RRM.
+At position 85 to 285, the domain is characterized as MAGE.
+At position 1 to 68, the domain is characterized as Oxytoxin-type inhibitor cystine knot (ICK).
+At position 38 to 157, the domain is characterized as Plastocyanin-like 1.
+At position 169 to 335, the domain is characterized as Plastocyanin-like 2.
+At position 197 to 292, the domain is characterized as PDZ.
+At position 98 to 266, the domain is characterized as Helicase ATP-binding.
+At position 452 to 627, the domain is characterized as Helicase C-terminal.
+At position 400 to 655, the domain is characterized as Protein kinase.
+At position 813 to 877, the domain is characterized as Myb-like.
+At position 28 to 185, the domain is characterized as Helicase ATP-binding.
+At position 111 to 171, the domain is characterized as bZIP.
+At position 21 to 176, the domain is characterized as C-CAP/cofactor C-like.
+At position 72 to 187, the domain is characterized as RGS.
+At position 21 to 112, the domain is characterized as UPAR/Ly6.
+At position 18 to 184, the domain is characterized as FAD-binding PCMH-type.
+At position 98 to 132, the domain is characterized as Tify.
+At position 38 to 112, the domain is characterized as Inhibitor I9.
+At position 123 to 404, the domain is characterized as Peptidase S8.
+At position 29 to 134, the domain is characterized as Phytocyanin.
+At position 301 to 584, the domain is characterized as Protein kinase.
+At position 259 to 761, the domain is characterized as Biotin carboxylation.
+At position 414 to 609, the domain is characterized as ATP-grasp.
+At position 888 to 962, the domain is characterized as Biotinyl-binding.
+At position 1695 to 2025, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 2029 to 2345, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 106 to 290, the domain is characterized as Tyr recombinase.
+At position 21 to 92, the domain is characterized as MBD 1.
+At position 106 to 171, the domain is characterized as MBD 2.
+At position 172 to 242, the domain is characterized as MBD 3.
+At position 13 to 70, the domain is characterized as Sushi.
+At position 85 to 327, the domain is characterized as Peptidase S1.
+At position 43 to 228, the domain is characterized as BPL/LPL catalytic.
+At position 60 to 124, the domain is characterized as SEP.
+At position 169 to 246, the domain is characterized as UBX.
+At position 47 to 116, the domain is characterized as Sm.
+At position 771 to 834, the domain is characterized as SAM.
+At position 60 to 267, the domain is characterized as MARVEL.
+At position 1 to 236, the domain is characterized as Deacetylase sirtuin-type.
+At position 162 to 357, the domain is characterized as TRUD.
+At position 11 to 158, the domain is characterized as UBC core.
+At position 75 to 347, the domain is characterized as CN hydrolase.
+At position 431 to 680, the domain is characterized as Protein kinase.
+At position 270 to 510, the domain is characterized as MHD.
+At position 14 to 111, the domain is characterized as Rieske.
+At position 30 to 197, the domain is characterized as Helicase ATP-binding.
+At position 536 to 630, the domain is characterized as Dicer dsRNA-binding fold.
+At position 889 to 1033, the domain is characterized as RNase III 1.
+At position 1075 to 1258, the domain is characterized as RNase III 2.
+At position 688 to 737, the domain is characterized as GRIP.
+At position 203 to 303, the domain is characterized as Fe2OG dioxygenase.
+At position 357 to 527, the domain is characterized as tr-type G.
+At position 994 to 1122, the domain is characterized as BRCT.
+At position 373 to 436, the domain is characterized as TRAM.
+At position 48 to 356, the domain is characterized as Cbl-PTB.
+At position 61 to 127, the domain is characterized as DRBM 1.
+At position 197 to 272, the domain is characterized as DRBM 2.
+At position 348 to 672, the domain is characterized as A to I editase.
+At position 71 to 151, the domain is characterized as Core-binding (CB).
+At position 174 to 367, the domain is characterized as Tyr recombinase.
+At position 11 to 284, the domain is characterized as tr-type G.
+At position 4 to 82, the domain is characterized as Core-binding (CB).
+At position 118 to 305, the domain is characterized as Tyr recombinase.
+At position 216 to 279, the domain is characterized as bZIP.
+At position 90 to 288, the domain is characterized as SMP-LTD.
+At position 7 to 190, the domain is characterized as Prephenate dehydratase.
+At position 204 to 283, the domain is characterized as ACT.
+At position 258 to 458, the domain is characterized as GATase cobBQ-type.
+At position 12 to 84, the domain is characterized as Myb-like.
+At position 359 to 434, the domain is characterized as G5 1.
+At position 435 to 516, the domain is characterized as G5 2.
+At position 499 to 644, the domain is characterized as JmjC.
+At position 80 to 408, the domain is characterized as PORR.
+At position 60 to 128, the domain is characterized as BTB.
+At position 127 to 188, the domain is characterized as PWWP.
+At position 11 to 44, the domain is characterized as WW 1.
+At position 52 to 86, the domain is characterized as WW 2.
+At position 39 to 317, the domain is characterized as tr-type G.
+At position 26 to 129, the domain is characterized as Ig-like C2-type 1.
+At position 276 to 394, the domain is characterized as Ig-like C2-type 3.
+At position 1 to 208, the domain is characterized as ABC transporter.
+At position 777 to 837, the domain is characterized as RAP.
+At position 1 to 147, the domain is characterized as Ferritin-like diiron.
+At position 559 to 827, the domain is characterized as MHD.
+At position 47 to 546, the domain is characterized as Sema.
+At position 891 to 979, the domain is characterized as IPT/TIG 1.
+At position 981 to 1066, the domain is characterized as IPT/TIG 2.
+At position 1069 to 1160, the domain is characterized as IPT/TIG 3.
+At position 162 to 395, the domain is characterized as NR LBD.
+At position 15 to 206, the domain is characterized as DH.
+At position 237 to 353, the domain is characterized as PH.
+At position 382 to 456, the domain is characterized as DEP 1.
+At position 483 to 558, the domain is characterized as DEP 2.
+At position 584 to 663, the domain is characterized as PDZ 1.
+At position 669 to 746, the domain is characterized as PDZ 2.
+At position 78 to 107, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 122 to 151, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 151 to 181, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 212 to 241, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 233 to 265, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 273 to 302, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 304 to 333, the domain is characterized as 4Fe-4S ferredoxin-type 8.
+At position 28 to 109, the domain is characterized as PAH 1.
+At position 123 to 193, the domain is characterized as PAH 2.
+At position 641 to 895, the domain is characterized as Protein kinase.
+At position 383 to 554, the domain is characterized as tr-type G.
+At position 30 to 256, the domain is characterized as ABC transmembrane type-2.
+At position 22 to 257, the domain is characterized as ABC transporter.
+At position 7 to 129, the domain is characterized as Arf-GAP.
+At position 157 to 197, the domain is characterized as UBA.
+At position 15 to 123, the domain is characterized as C2.
+At position 64 to 135, the domain is characterized as POTRA.
+At position 95 to 282, the domain is characterized as GH16.
+At position 412 to 526, the domain is characterized as N-terminal Ras-GEF.
+At position 530 to 615, the domain is characterized as PDZ.
+At position 749 to 835, the domain is characterized as Ras-associating.
+At position 860 to 1088, the domain is characterized as Ras-GEF.
+At position 111 to 168, the domain is characterized as HTH myb-type.
+At position 48 to 281, the domain is characterized as FAD-binding PCMH-type.
+At position 662 to 695, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 30 to 124, the domain is characterized as Fibronectin type-III 1.
+At position 125 to 225, the domain is characterized as Fibronectin type-III 2.
+At position 316 to 412, the domain is characterized as Fibronectin type-III 3.
+At position 413 to 505, the domain is characterized as Fibronectin type-III 4.
+At position 318 to 410, the domain is characterized as ARID.
+At position 275 to 410, the domain is characterized as Fido.
+At position 644 to 711, the domain is characterized as Chromo 1.
+At position 726 to 792, the domain is characterized as Chromo 2.
+At position 825 to 999, the domain is characterized as Helicase ATP-binding.
+At position 1139 to 1290, the domain is characterized as Helicase C-terminal.
+At position 204 to 328, the domain is characterized as OTU.
+At position 27 to 210, the domain is characterized as Plastocyanin-like 1.
+At position 218 to 365, the domain is characterized as Plastocyanin-like 2.
+At position 380 to 562, the domain is characterized as Plastocyanin-like 3.
+At position 572 to 719, the domain is characterized as Plastocyanin-like 4.
+At position 730 to 915, the domain is characterized as Plastocyanin-like 5.
+At position 924 to 1114, the domain is characterized as Plastocyanin-like 6.
+At position 369 to 626, the domain is characterized as Protein kinase.
+At position 150 to 236, the domain is characterized as Ig-like.
+At position 398 to 506, the domain is characterized as BEN.
+At position 85 to 148, the domain is characterized as S5 DRBM.
+At position 53 to 143, the domain is characterized as Cyclin N-terminal.
+At position 928 to 994, the domain is characterized as BTB.
+At position 164 to 447, the domain is characterized as ABC transmembrane type-1.
+At position 480 to 719, the domain is characterized as ABC transporter.
+At position 22 to 88, the domain is characterized as SH3.
+At position 213 to 247, the domain is characterized as WW.
+At position 322 to 435, the domain is characterized as PH.
+At position 542 to 749, the domain is characterized as Rho-GAP.
+At position 50 to 330, the domain is characterized as Rab-GAP TBC.
+At position 6 to 234, the domain is characterized as ABC transporter 1.
+At position 255 to 495, the domain is characterized as ABC transporter 2.
+At position 100 to 180, the domain is characterized as KH 1.
+At position 235 to 317, the domain is characterized as KH 2.
+At position 107 to 282, the domain is characterized as Prephenate dehydratase.
+At position 296 to 387, the domain is characterized as ACT.
+At position 321 to 438, the domain is characterized as P/Homo B.
+At position 213 to 462, the domain is characterized as GH16.
+At position 416 to 577, the domain is characterized as Miro 2.
+At position 147 to 399, the domain is characterized as Protein kinase.
+At position 25 to 107, the domain is characterized as UPAR/Ly6.
+At position 1416 to 1486, the domain is characterized as Bromo 1.
+At position 1539 to 1609, the domain is characterized as Bromo 2.
+At position 21 to 156, the domain is characterized as MPN.
+At position 1182 to 1305, the domain is characterized as MI.
+At position 150 to 293, the domain is characterized as Jacalin-type lectin 2.
+At position 55 to 287, the domain is characterized as SET.
+At position 65 to 351, the domain is characterized as Protein kinase.
+At position 4 to 67, the domain is characterized as PAS.
+At position 136 to 350, the domain is characterized as Histidine kinase.
+At position 16 to 165, the domain is characterized as Ferritin-like diiron.
+At position 519 to 730, the domain is characterized as Helicase ATP-binding.
+At position 995 to 1165, the domain is characterized as Helicase C-terminal.
+At position 199 to 512, the domain is characterized as Protein kinase.
+At position 599 to 680, the domain is characterized as BRCT.
+At position 3 to 152, the domain is characterized as N-acetyltransferase 1.
+At position 155 to 303, the domain is characterized as N-acetyltransferase 2.
+At position 375 to 517, the domain is characterized as Cadherin 4.
+At position 517 to 630, the domain is characterized as Cadherin 5.
+At position 35 to 318, the domain is characterized as Protein kinase.
+At position 34 to 257, the domain is characterized as Fibrinogen C-terminal.
+At position 454 to 683, the domain is characterized as AIG1-type G.
+At position 7 to 820, the domain is characterized as Myosin motor.
+At position 103 to 148, the domain is characterized as G-patch.
+At position 28 to 111, the domain is characterized as EthD.
+At position 335 to 409, the domain is characterized as HSA.
+At position 823 to 988, the domain is characterized as Helicase ATP-binding.
+At position 1375 to 1525, the domain is characterized as Helicase C-terminal.
+At position 727 to 785, the domain is characterized as SH3.
+At position 52 to 282, the domain is characterized as Radical SAM core.
+At position 118 to 236, the domain is characterized as Response regulatory.
+At position 222 to 287, the domain is characterized as Plastocyanin-like.
+At position 595 to 684, the domain is characterized as PB1.
+At position 106 to 234, the domain is characterized as SEA.
+At position 247 to 360, the domain is characterized as CUB 1.
+At position 365 to 481, the domain is characterized as CUB 2.
+At position 483 to 519, the domain is characterized as LDL-receptor class A 1.
+At position 517 to 554, the domain is characterized as LDL-receptor class A 2.
+At position 558 to 595, the domain is characterized as LDL-receptor class A 3.
+At position 606 to 840, the domain is characterized as Peptidase S1.
+At position 128 to 325, the domain is characterized as Histidine kinase.
+At position 618 to 757, the domain is characterized as VPS9.
+At position 787 to 878, the domain is characterized as Ras-associating.
+At position 60 to 310, the domain is characterized as Protein kinase.
+At position 109 to 163, the domain is characterized as bHLH.
+At position 199 to 275, the domain is characterized as KH type-2.
+At position 253 to 484, the domain is characterized as START.
+At position 123 to 223, the domain is characterized as PB1.
+At position 42 to 140, the domain is characterized as PH.
+At position 621 to 813, the domain is characterized as Rab-GAP TBC.
+At position 89 to 263, the domain is characterized as Helicase ATP-binding.
+At position 277 to 442, the domain is characterized as Helicase C-terminal.
+At position 277 to 336, the domain is characterized as SH3.
+At position 82 to 235, the domain is characterized as CP-type G.
+At position 33 to 204, the domain is characterized as NAC.
+At position 249 to 396, the domain is characterized as Helicase C-terminal.
+At position 457 to 520, the domain is characterized as bZIP.
+At position 34 to 276, the domain is characterized as Peptidase S1.
+At position 5 to 81, the domain is characterized as REM-1.
+At position 286 to 393, the domain is characterized as PH.
+At position 339 to 484, the domain is characterized as Thioredoxin 2.
+At position 6 to 160, the domain is characterized as PPIase cyclophilin-type.
+At position 57 to 236, the domain is characterized as ABC transmembrane type-1.
+At position 210 to 438, the domain is characterized as NR LBD.
+At position 797 to 979, the domain is characterized as Lon proteolytic.
+At position 694 to 769, the domain is characterized as Smr.
+At position 431 to 501, the domain is characterized as Bromo.
+At position 25 to 285, the domain is characterized as ABC transporter.
+At position 156 to 202, the domain is characterized as F-box.
+At position 1013 to 1198, the domain is characterized as Laminin G-like 4.
+At position 43 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 349 to 440, the domain is characterized as Ig-like C2-type 2.
+At position 546 to 638, the domain is characterized as Fibronectin type-III 2.
+At position 835 to 1114, the domain is characterized as Protein kinase.
+At position 80 to 173, the domain is characterized as Rieske.
+At position 34 to 295, the domain is characterized as Brix.
+At position 375 to 808, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1293 to 1607, the domain is characterized as PKS/mFAS DH.
+At position 1649 to 1726, the domain is characterized as Carrier.
+At position 52 to 155, the domain is characterized as THUMP.
+At position 103 to 175, the domain is characterized as PRC barrel.
+At position 139 to 172, the domain is characterized as EF-hand 2.
+At position 169 to 204, the domain is characterized as EF-hand 3.
+At position 205 to 233, the domain is characterized as EF-hand 4.
+At position 234 to 268, the domain is characterized as EF-hand 5.
+At position 44 to 149, the domain is characterized as RRM.
+At position 388 to 805, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1290 to 1592, the domain is characterized as PKS/mFAS DH.
+At position 1650 to 1724, the domain is characterized as Carrier.
+At position 62 to 139, the domain is characterized as KRAB.
+At position 45 to 112, the domain is characterized as GRAM.
+At position 199 to 650, the domain is characterized as Myotubularin phosphatase.
+At position 1 to 84, the domain is characterized as Reverse transcriptase.
+At position 361 to 452, the domain is characterized as Fibronectin type-III 1.
+At position 453 to 545, the domain is characterized as Fibronectin type-III 2.
+At position 622 to 881, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 913 to 1196, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 276 to 486, the domain is characterized as Ku.
+At position 607 to 641, the domain is characterized as SAP.
+At position 6 to 74, the domain is characterized as S1 motif.
+At position 259 to 503, the domain is characterized as PPM-type phosphatase.
+At position 310 to 404, the domain is characterized as PH.
+At position 427 to 547, the domain is characterized as Arf-GAP.
+At position 1091 to 1155, the domain is characterized as SH3.
+At position 18 to 212, the domain is characterized as ABC transmembrane type-1.
+At position 125 to 310, the domain is characterized as ATP-grasp.
+At position 23 to 313, the domain is characterized as GH18.
+At position 153 to 216, the domain is characterized as bZIP.
+At position 18 to 347, the domain is characterized as PTS EIIC type-2.
+At position 390 to 478, the domain is characterized as PTS EIIB type-2.
+At position 63 to 378, the domain is characterized as Peptidase A1.
+At position 4 to 69, the domain is characterized as CSD.
+At position 116 to 170, the domain is characterized as FHA.
+At position 218 to 479, the domain is characterized as Protein kinase.
+At position 320 to 398, the domain is characterized as PDZ.
+At position 52 to 92, the domain is characterized as UBA 1.
+At position 198 to 242, the domain is characterized as UBA 2.
+At position 379 to 710, the domain is characterized as SAM-dependent MTase DRM-type.
+At position 1 to 330, the domain is characterized as SMP-LTD.
+At position 97 to 357, the domain is characterized as Protein kinase.
+At position 386 to 538, the domain is characterized as PA14.
+At position 182 to 270, the domain is characterized as Rieske.
+At position 264 to 353, the domain is characterized as Fibronectin type-III 1.
+At position 354 to 444, the domain is characterized as Fibronectin type-III 2.
+At position 533 to 622, the domain is characterized as Fibronectin type-III 4.
+At position 623 to 706, the domain is characterized as Fibronectin type-III 5.
+At position 709 to 798, the domain is characterized as Fibronectin type-III 6.
+At position 799 to 882, the domain is characterized as Fibronectin type-III 7.
+At position 885 to 970, the domain is characterized as Fibronectin type-III 8.
+At position 973 to 1062, the domain is characterized as Fibronectin type-III 9.
+At position 1063 to 1144, the domain is characterized as Fibronectin type-III 10.
+At position 1149 to 1238, the domain is characterized as Fibronectin type-III 11.
+At position 1239 to 1325, the domain is characterized as Fibronectin type-III 12.
+At position 1323 to 1540, the domain is characterized as Fibrinogen C-terminal.
+At position 6 to 75, the domain is characterized as J.
+At position 219 to 379, the domain is characterized as TrmE-type G.
+At position 261 to 318, the domain is characterized as Kazal-like 3.
+At position 448 to 523, the domain is characterized as RRM 3.
+At position 176 to 219, the domain is characterized as CUE.
+At position 441 to 609, the domain is characterized as Helicase ATP-binding.
+At position 786 to 948, the domain is characterized as Helicase C-terminal.
+At position 73 to 152, the domain is characterized as KRAB.
+At position 79 to 314, the domain is characterized as Radical SAM core.
+At position 61 to 138, the domain is characterized as RRM.
+At position 508 to 695, the domain is characterized as Rab-GAP TBC.
+At position 879 to 914, the domain is characterized as EF-hand.
+At position 270 to 347, the domain is characterized as PUA.
+At position 65 to 166, the domain is characterized as Ig-like C2-type.
+At position 65 to 137, the domain is characterized as MBD.
+At position 29 to 452, the domain is characterized as GH18.
+At position 533 to 746, the domain is characterized as FtsK.
+At position 519 to 807, the domain is characterized as UvrD-like helicase C-terminal.
+At position 130 to 167, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 6 to 118, the domain is characterized as MTTase N-terminal.
+At position 229 to 278, the domain is characterized as bHLH.
+At position 52 to 114, the domain is characterized as t-SNARE coiled-coil homology.
+At position 139 to 214, the domain is characterized as Carrier.
+At position 1092 to 1633, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 555 to 656, the domain is characterized as tRNA-binding.
+At position 62 to 311, the domain is characterized as Radical SAM core.
+At position 178 to 370, the domain is characterized as Ras-GAP.
+At position 163 to 253, the domain is characterized as 5'-3' exonuclease.
+At position 25 to 66, the domain is characterized as JmjN.
+At position 201 to 367, the domain is characterized as JmjC.
+At position 347 to 411, the domain is characterized as S4 RNA-binding.
+At position 542 to 658, the domain is characterized as SMC hinge.
+At position 67 to 257, the domain is characterized as YrdC-like.
+At position 164 to 199, the domain is characterized as QLQ.
+At position 227 to 271, the domain is characterized as WRC.
+At position 502 to 607, the domain is characterized as CBM2.
+At position 21 to 278, the domain is characterized as Protein kinase.
+At position 47 to 98, the domain is characterized as bHLH.
+At position 432 to 478, the domain is characterized as EGF-like 2.
+At position 514 to 551, the domain is characterized as EGF-like 3.
+At position 3 to 259, the domain is characterized as DegV.
+At position 77 to 203, the domain is characterized as C-type lectin.
+At position 113 to 300, the domain is characterized as Tyr recombinase.
+At position 108 to 226, the domain is characterized as PPIase FKBP-type.
+At position 328 to 496, the domain is characterized as Helicase ATP-binding.
+At position 666 to 840, the domain is characterized as Helicase C-terminal.
+At position 23 to 164, the domain is characterized as Thioredoxin.
+At position 119 to 155, the domain is characterized as EGF-like 3; calcium-binding.
+At position 1 to 184, the domain is characterized as GMPS ATP-PPase.
+At position 74 to 166, the domain is characterized as Fibronectin type-III.
+At position 280 to 453, the domain is characterized as tr-type G.
+At position 203 to 290, the domain is characterized as Ig-like C2-type 3.
+At position 299 to 399, the domain is characterized as Ig-like C2-type 4.
+At position 402 to 502, the domain is characterized as Ig-like C2-type 5.
+At position 582 to 910, the domain is characterized as Protein kinase.
+At position 5 to 145, the domain is characterized as Clp R.
+At position 37 to 126, the domain is characterized as PPIase FKBP-type.
+At position 573 to 680, the domain is characterized as tRNA-binding.
+At position 74 to 384, the domain is characterized as Peptidase S8.
+At position 37 to 339, the domain is characterized as Protein kinase.
+At position 20 to 107, the domain is characterized as SANTA.
+At position 617 to 678, the domain is characterized as Myb-like.
+At position 951 to 1050, the domain is characterized as HECT.
+At position 8 to 50, the domain is characterized as CHCH.
+At position 66 to 216, the domain is characterized as HD.
+At position 182 to 342, the domain is characterized as Integrase catalytic.
+At position 44 to 191, the domain is characterized as FPL.
+At position 14 to 141, the domain is characterized as Arf-GAP.
+At position 193 to 234, the domain is characterized as UBA.
+At position 4 to 91, the domain is characterized as Glutamine amidotransferase type-1.
+At position 105 to 404, the domain is characterized as SAM-dependent MTase C5-type.
+At position 216 to 367, the domain is characterized as Exonuclease.
+At position 169 to 352, the domain is characterized as MIF4G.
+At position 457 to 573, the domain is characterized as MI.
+At position 344 to 425, the domain is characterized as OCT.
+At position 121 to 161, the domain is characterized as LRRCT.
+At position 330 to 401, the domain is characterized as RRM.
+At position 20 to 60, the domain is characterized as CHCH.
+At position 439 to 534, the domain is characterized as Fibronectin type-III 2.
+At position 635 to 896, the domain is characterized as Protein kinase.
+At position 930 to 994, the domain is characterized as SAM.
+At position 278 to 436, the domain is characterized as W2.
+At position 488 to 531, the domain is characterized as CAP-Gly 3.
+At position 588 to 946, the domain is characterized as USP.
+At position 37 to 104, the domain is characterized as Histone-fold.
+At position 96 to 166, the domain is characterized as PRC barrel.
+At position 196 to 374, the domain is characterized as Helicase ATP-binding.
+At position 385 to 546, the domain is characterized as Helicase C-terminal.
+At position 85 to 212, the domain is characterized as GST C-terminal.
+At position 23 to 122, the domain is characterized as PPIase FKBP-type.
+At position 308 to 398, the domain is characterized as SprT-like.
+At position 48 to 285, the domain is characterized as ABC transporter.
+At position 389 to 653, the domain is characterized as ABC transmembrane type-2.
+At position 64 to 243, the domain is characterized as Guanylate kinase-like.
+At position 571 to 673, the domain is characterized as tRNA-binding.
+At position 62 to 111, the domain is characterized as F-box.
+At position 220 to 380, the domain is characterized as TrmE-type G.
+At position 36 to 286, the domain is characterized as Protein kinase.
+At position 258 to 356, the domain is characterized as BEN.
+At position 159 to 360, the domain is characterized as OBG-type G.
+At position 1 to 103, the domain is characterized as OTU.
+At position 74 to 384, the domain is characterized as Peptidase A1.
+At position 444 to 608, the domain is characterized as KIND 2.
+At position 1246 to 1371, the domain is characterized as N-terminal Ras-GEF.
+At position 1468 to 1719, the domain is characterized as Ras-GEF.
+At position 1 to 17, the domain is characterized as Kringle 4.
+At position 41 to 120, the domain is characterized as Kringle 5.
+At position 114 to 341, the domain is characterized as Peptidase S1.
+At position 360 to 415, the domain is characterized as Kazal-like.
+At position 40 to 369, the domain is characterized as Protein kinase.
+At position 22 to 115, the domain is characterized as Ig-like C1-type.
+At position 50 to 146, the domain is characterized as GS beta-grasp.
+At position 158 to 499, the domain is characterized as GS catalytic.
+At position 451 to 584, the domain is characterized as DOD-type homing endonuclease.
+At position 28 to 181, the domain is characterized as Saposin B-type.
+At position 45 to 157, the domain is characterized as HotDog ACOT-type 1.
+At position 217 to 330, the domain is characterized as HotDog ACOT-type 2.
+At position 370 to 582, the domain is characterized as START.
+At position 9 to 280, the domain is characterized as Protein kinase.
+At position 609 to 667, the domain is characterized as KH.
+At position 678 to 746, the domain is characterized as S1 motif 1.
+At position 925 to 987, the domain is characterized as S1 motif 2.
+At position 35 to 220, the domain is characterized as ATLF-like.
+At position 321 to 621, the domain is characterized as GP-PDE.
+At position 174 to 294, the domain is characterized as Ferric oxidoreductase.
+At position 323 to 430, the domain is characterized as FAD-binding FR-type.
+At position 171 to 266, the domain is characterized as TAFH.
+At position 28 to 54, the domain is characterized as Antistasin-like.
+At position 538 to 650, the domain is characterized as SMC hinge.
+At position 767 to 788, the domain is characterized as IQ 1.
+At position 814 to 837, the domain is characterized as IQ 3.
+At position 838 to 861, the domain is characterized as IQ 4.
+At position 1524 to 1801, the domain is characterized as Dilute.
+At position 505 to 540, the domain is characterized as CBM1.
+At position 20 to 138, the domain is characterized as CUB 1.
+At position 139 to 182, the domain is characterized as EGF-like; calcium-binding.
+At position 185 to 297, the domain is characterized as CUB 2.
+At position 299 to 364, the domain is characterized as Sushi 1.
+At position 365 to 434, the domain is characterized as Sushi 2.
+At position 449 to 696, the domain is characterized as Peptidase S1.
+At position 20 to 267, the domain is characterized as Protein kinase.
+At position 67 to 105, the domain is characterized as ShKT 1.
+At position 171 to 205, the domain is characterized as ShKT 3.
+At position 208 to 243, the domain is characterized as ShKT 4.
+At position 606 to 667, the domain is characterized as SAM.
+At position 120 to 263, the domain is characterized as RNase H type-1.
+At position 83 to 191, the domain is characterized as PB1.
+At position 700 to 781, the domain is characterized as ACT 1.
+At position 15 to 334, the domain is characterized as ABC transporter.
+At position 77 to 194, the domain is characterized as THUMP.
+At position 136 to 221, the domain is characterized as PDZ.
+At position 1512 to 1625, the domain is characterized as MaoC-like.
+At position 180 to 262, the domain is characterized as Thyroglobulin type-1.
+At position 32 to 169, the domain is characterized as MPN.
+At position 1349 to 1903, the domain is characterized as FAT.
+At position 2077 to 2389, the domain is characterized as PI3K/PI4K catalytic.
+At position 95 to 329, the domain is characterized as Radical SAM core.
+At position 411 to 578, the domain is characterized as tr-type G.
+At position 274 to 381, the domain is characterized as Cadherin 2.
+At position 382 to 494, the domain is characterized as Cadherin 3.
+At position 495 to 600, the domain is characterized as Cadherin 4.
+At position 40 to 90, the domain is characterized as bZIP.
+At position 1 to 203, the domain is characterized as RNase H type-2.
+At position 10 to 204, the domain is characterized as Peptidase M12B.
+At position 212 to 298, the domain is characterized as Disintegrin.
+At position 116 to 163, the domain is characterized as F-box.
+At position 66 to 165, the domain is characterized as Fibronectin type-III 1.
+At position 173 to 269, the domain is characterized as Fibronectin type-III 2.
+At position 270 to 376, the domain is characterized as Fibronectin type-III 3.
+At position 476 to 741, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 764 to 1016, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 2 to 406, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 844 to 1111, the domain is characterized as PKS/mFAS DH.
+At position 2120 to 2200, the domain is characterized as Carrier.
+At position 126 to 295, the domain is characterized as Helicase ATP-binding.
+At position 356 to 527, the domain is characterized as Helicase C-terminal.
+At position 13 to 107, the domain is characterized as ACB.
+At position 89 to 291, the domain is characterized as ATP-grasp.
+At position 227 to 422, the domain is characterized as ABC transmembrane type-1.
+At position 344 to 379, the domain is characterized as EF-hand 2.
+At position 3 to 392, the domain is characterized as F-BAR.
+At position 425 to 622, the domain is characterized as Rho-GAP.
+At position 15 to 114, the domain is characterized as SH2.
+At position 883 to 1106, the domain is characterized as MIF4G.
+At position 1299 to 1423, the domain is characterized as MI.
+At position 85 to 209, the domain is characterized as MH1.
+At position 265 to 431, the domain is characterized as MH2.
+At position 192 to 404, the domain is characterized as SMP-LTD.
+At position 559 to 898, the domain is characterized as Protein kinase.
+At position 234 to 423, the domain is characterized as Helicase ATP-binding.
+At position 103 to 425, the domain is characterized as Kinesin motor.
+At position 6 to 330, the domain is characterized as Kinesin motor.
+At position 120 to 188, the domain is characterized as POTRA.
+At position 4 to 155, the domain is characterized as Thioredoxin.
+At position 166 to 225, the domain is characterized as CBS.
+At position 273 to 463, the domain is characterized as B30.2/SPRY.
+At position 1 to 197, the domain is characterized as Protein kinase.
+At position 1 to 20, the domain is characterized as Disintegrin.
+At position 335 to 504, the domain is characterized as tr-type G.
+At position 1 to 120, the domain is characterized as PIK helical.
+At position 658 to 939, the domain is characterized as PI3K/PI4K catalytic.
+At position 204 to 388, the domain is characterized as PCI.
+At position 46 to 85, the domain is characterized as Beta/gamma crystallin 'Greek key' 1.
+At position 86 to 130, the domain is characterized as Beta/gamma crystallin 'Greek key' 2.
+At position 136 to 177, the domain is characterized as Beta/gamma crystallin 'Greek key' 3.
+At position 178 to 220, the domain is characterized as Beta/gamma crystallin 'Greek key' 4.
+At position 592 to 669, the domain is characterized as Carrier 1.
+At position 1678 to 1757, the domain is characterized as Carrier 2.
+At position 669 to 882, the domain is characterized as FtsK.
+At position 341 to 570, the domain is characterized as Sigma-54 factor interaction.
+At position 6 to 85, the domain is characterized as ACT.
+At position 42 to 177, the domain is characterized as Nudix hydrolase.
+At position 598 to 678, the domain is characterized as BRCT.
+At position 18 to 263, the domain is characterized as tr-type G.
+At position 39 to 592, the domain is characterized as PLA2c.
+At position 294 to 369, the domain is characterized as RRM 2.
+At position 587 to 659, the domain is characterized as RRM 4.
+At position 730 to 811, the domain is characterized as RRM 5.
+At position 832 to 912, the domain is characterized as RRM 6.
+At position 61 to 110, the domain is characterized as WAP.
+At position 3 to 70, the domain is characterized as NAC-A/B.
+At position 2 to 41, the domain is characterized as EGF-like 1.
+At position 44 to 88, the domain is characterized as EGF-like 2.
+At position 91 to 247, the domain is characterized as F5/8 type C 1.
+At position 252 to 409, the domain is characterized as F5/8 type C 2.
+At position 1 to 264, the domain is characterized as Protein kinase.
+At position 800 to 852, the domain is characterized as GPS.
+At position 679 to 929, the domain is characterized as ABC transporter 1.
+At position 1012 to 1306, the domain is characterized as ABC transmembrane type-1 2.
+At position 1344 to 1578, the domain is characterized as ABC transporter 2.
+At position 25 to 148, the domain is characterized as ABC transmembrane type-1.
+At position 70 to 176, the domain is characterized as GRAM.
+At position 18 to 258, the domain is characterized as tr-type G.
+At position 122 to 140, the domain is characterized as IQ 2.
+At position 144 to 170, the domain is characterized as IQ 3.
+At position 283 to 383, the domain is characterized as PDZ.
+At position 122 to 272, the domain is characterized as C2.
+At position 302 to 563, the domain is characterized as Protein kinase.
+At position 564 to 643, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 106, the domain is characterized as MTTase N-terminal.
+At position 129 to 359, the domain is characterized as Radical SAM core.
+At position 362 to 420, the domain is characterized as TRAM.
+At position 24 to 129, the domain is characterized as HPt.
+At position 53 to 174, the domain is characterized as RGS 1.
+At position 177 to 294, the domain is characterized as RGS 2.
+At position 309 to 574, the domain is characterized as Protein kinase.
+At position 577 to 642, the domain is characterized as AGC-kinase C-terminal.
+At position 78 to 240, the domain is characterized as CP-type G.
+At position 335 to 482, the domain is characterized as Cupin type-1 2.
+At position 143 to 382, the domain is characterized as Radical SAM core.
+At position 27 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 141 to 248, the domain is characterized as Gnk2-homologous 2.
+At position 663 to 723, the domain is characterized as CBS 1.
+At position 1048 to 1105, the domain is characterized as CBS 2.
+At position 154 to 341, the domain is characterized as CheB-type methylesterase.
+At position 74 to 138, the domain is characterized as BTB.
+At position 173 to 274, the domain is characterized as BACK.
+At position 18 to 342, the domain is characterized as PTS EIIC type-2.
+At position 383 to 471, the domain is characterized as PTS EIIB type-2.
+At position 44 to 130, the domain is characterized as POTRA.
+At position 16 to 255, the domain is characterized as Peptidase S1.
+At position 606 to 627, the domain is characterized as R.
+At position 826 to 891, the domain is characterized as J.
+At position 42 to 212, the domain is characterized as Helicase ATP-binding.
+At position 222 to 382, the domain is characterized as Helicase C-terminal.
+At position 566 to 629, the domain is characterized as R3H.
+At position 702 to 749, the domain is characterized as G-patch.
+At position 867 to 933, the domain is characterized as SAM 1.
+At position 952 to 1016, the domain is characterized as SAM 2.
+At position 1040 to 1109, the domain is characterized as SAM 3.
+At position 375 to 538, the domain is characterized as Helicase ATP-binding.
+At position 557 to 719, the domain is characterized as Helicase C-terminal.
+At position 142 to 223, the domain is characterized as PRC barrel.
+At position 61 to 354, the domain is characterized as PPM-type phosphatase.
+At position 721 to 813, the domain is characterized as ELM2.
+At position 828 to 879, the domain is characterized as SANT.
+At position 43 to 330, the domain is characterized as ABC transmembrane type-1.
+At position 364 to 603, the domain is characterized as ABC transporter.
+At position 13 to 93, the domain is characterized as WWE 1.
+At position 94 to 170, the domain is characterized as WWE 2.
+At position 341 to 585, the domain is characterized as Clu.
+At position 207 to 426, the domain is characterized as RMT2.
+At position 96 to 153, the domain is characterized as VWFC.
+At position 278 to 315, the domain is characterized as LRRNT.
+At position 1 to 90, the domain is characterized as CARD.
+At position 1504 to 1585, the domain is characterized as PDZ 4.
+At position 1596 to 1664, the domain is characterized as SH3.
+At position 1724 to 1907, the domain is characterized as Guanylate kinase-like.
+At position 114 to 431, the domain is characterized as Kinesin motor.
+At position 125 to 484, the domain is characterized as PTS EIIC type-1.
+At position 338 to 406, the domain is characterized as HP.
+At position 745 to 821, the domain is characterized as Carrier 1.
+At position 1833 to 1909, the domain is characterized as Carrier 2.
+At position 163 to 263, the domain is characterized as Cytochrome c.
+At position 82 to 176, the domain is characterized as Fibronectin type-III.
+At position 304 to 380, the domain is characterized as B5.
+At position 209 to 435, the domain is characterized as tr-type G.
+At position 381 to 442, the domain is characterized as TRAM.
+At position 24 to 86, the domain is characterized as SH3 1.
+At position 123 to 185, the domain is characterized as SH3 2.
+At position 293 to 413, the domain is characterized as PX.
+At position 459 to 533, the domain is characterized as PB1.
+At position 723 to 814, the domain is characterized as HTH La-type RNA-binding.
+At position 20 to 97, the domain is characterized as Cytochrome b5 heme-binding.
+At position 18 to 161, the domain is characterized as Ephrin RBD.
+At position 1368 to 1499, the domain is characterized as BEACH-type PH.
+At position 1545 to 1839, the domain is characterized as BEACH.
+At position 196 to 482, the domain is characterized as ABC transmembrane type-1 1.
+At position 560 to 783, the domain is characterized as ABC transporter 1.
+At position 853 to 1166, the domain is characterized as ABC transmembrane type-1 2.
+At position 1210 to 1444, the domain is characterized as ABC transporter 2.
+At position 24 to 179, the domain is characterized as Reelin.
+At position 65 to 255, the domain is characterized as VWFA 1.
+At position 638 to 825, the domain is characterized as VWFA 2.
+At position 849 to 1035, the domain is characterized as VWFA 3.
+At position 134 to 184, the domain is characterized as bHLH.
+At position 238 to 324, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 26 to 272, the domain is characterized as AB hydrolase-1.
+At position 139 to 340, the domain is characterized as TLC.
+At position 319 to 400, the domain is characterized as ACT.
+At position 76 to 235, the domain is characterized as Rho-GAP.
+At position 95 to 167, the domain is characterized as KRAB.
+At position 96 to 129, the domain is characterized as EF-hand 2.
+At position 286 to 375, the domain is characterized as ABM.
+At position 86 to 207, the domain is characterized as sHSP.
+At position 8 to 232, the domain is characterized as Radical SAM core.
+At position 126 to 217, the domain is characterized as Ig-like C2-type 2.
+At position 474 to 747, the domain is characterized as Protein kinase.
+At position 234 to 266, the domain is characterized as LisH.
+At position 53 to 239, the domain is characterized as SEC7.
+At position 261 to 377, the domain is characterized as PH.
+At position 333 to 595, the domain is characterized as Protein kinase.
+At position 3 to 121, the domain is characterized as Chorismate mutase aroH-type.
+At position 5 to 269, the domain is characterized as YjeF C-terminal.
+At position 138 to 450, the domain is characterized as IF rod.
+At position 22 to 115, the domain is characterized as Ig-like C2-type 1.
+At position 180 to 260, the domain is characterized as Ig-like C2-type 2.
+At position 297 to 387, the domain is characterized as Ig-like C2-type 3.
+At position 585 to 862, the domain is characterized as Protein kinase.
+At position 354 to 455, the domain is characterized as BRCT.
+At position 5 to 126, the domain is characterized as Thioredoxin.
+At position 134 to 162, the domain is characterized as ITAM.
+At position 107 to 330, the domain is characterized as Radical SAM core.
+At position 40 to 219, the domain is characterized as GH11.
+At position 246 to 282, the domain is characterized as CBM1.
+At position 434 to 493, the domain is characterized as LIM zinc-binding 1.
+At position 494 to 554, the domain is characterized as LIM zinc-binding 2.
+At position 555 to 623, the domain is characterized as LIM zinc-binding 3.
+At position 1841 to 1990, the domain is characterized as bMERB.
+At position 546 to 583, the domain is characterized as Collagen-like 3.
+At position 682 to 737, the domain is characterized as Collagen-like 4.
+At position 868 to 924, the domain is characterized as Collagen-like 5.
+At position 967 to 1025, the domain is characterized as Collagen-like 6.
+At position 1026 to 1055, the domain is characterized as Collagen-like 7.
+At position 1056 to 1086, the domain is characterized as Collagen-like 8.
+At position 1114 to 1172, the domain is characterized as Collagen-like 9.
+At position 1393 to 1447, the domain is characterized as Collagen-like 10.
+At position 1448 to 1499, the domain is characterized as Collagen-like 11.
+At position 51 to 254, the domain is characterized as AH.
+At position 134 to 384, the domain is characterized as ABC transporter 1.
+At position 482 to 550, the domain is characterized as PASTA.
+At position 13 to 274, the domain is characterized as Pyruvate carboxyltransferase.
+At position 498 to 573, the domain is characterized as Carrier.
+At position 155 to 289, the domain is characterized as Fido.
+At position 108 to 221, the domain is characterized as Calponin-homology (CH).
+At position 447 to 467, the domain is characterized as IQ 1.
+At position 538 to 567, the domain is characterized as IQ 2.
+At position 568 to 597, the domain is characterized as IQ 3.
+At position 599 to 628, the domain is characterized as IQ 4.
+At position 629 to 658, the domain is characterized as IQ 5.
+At position 687 to 716, the domain is characterized as IQ 6.
+At position 717 to 746, the domain is characterized as IQ 7.
+At position 860 to 1071, the domain is characterized as Ras-GAP.
+At position 436 to 595, the domain is characterized as Helicase C-terminal.
+At position 11 to 135, the domain is characterized as PX.
+At position 241 to 430, the domain is characterized as GATase cobBQ-type.
+At position 120 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 217 to 307, the domain is characterized as Ig-like C2-type 3.
+At position 314 to 400, the domain is characterized as Ig-like C2-type 4.
+At position 406 to 517, the domain is characterized as Ig-like C2-type 5.
+At position 577 to 675, the domain is characterized as Fibronectin type-III 1.
+At position 721 to 815, the domain is characterized as Fibronectin type-III 2.
+At position 826 to 923, the domain is characterized as Fibronectin type-III 3.
+At position 80 to 199, the domain is characterized as PLAT.
+At position 1 to 99, the domain is characterized as BRCT 1.
+At position 129 to 220, the domain is characterized as BRCT 2.
+At position 322 to 418, the domain is characterized as BRCT 3.
+At position 319 to 835, the domain is characterized as USP.
+At position 628 to 669, the domain is characterized as UBA 1.
+At position 700 to 740, the domain is characterized as UBA 2.
+At position 245 to 294, the domain is characterized as bHLH.
+At position 10 to 83, the domain is characterized as GST N-terminal.
+At position 84 to 213, the domain is characterized as GST C-terminal.
+At position 44 to 160, the domain is characterized as sHSP.
+At position 293 to 371, the domain is characterized as PUA.
+At position 12 to 176, the domain is characterized as N-acetyltransferase.
+At position 416 to 578, the domain is characterized as YDG.
+At position 62 to 328, the domain is characterized as Septin-type G.
+At position 13 to 268, the domain is characterized as CN hydrolase.
+At position 682 to 785, the domain is characterized as SRCR.
+At position 217 to 468, the domain is characterized as Ku.
+At position 242 to 515, the domain is characterized as Protein kinase.
+At position 33 to 306, the domain is characterized as Alpha-carbonic anhydrase.
+At position 219 to 471, the domain is characterized as Ras-GEF.
+At position 24 to 142, the domain is characterized as Rhodanese 1.
+At position 172 to 284, the domain is characterized as Rhodanese 2.
+At position 185 to 331, the domain is characterized as PX.
+At position 8 to 146, the domain is characterized as KID.
+At position 25 to 101, the domain is characterized as Saposin B-type.
+At position 45 to 178, the domain is characterized as VHS.
+At position 223 to 310, the domain is characterized as GAT.
+At position 2 to 242, the domain is characterized as KaiC.
+At position 72 to 135, the domain is characterized as 4Fe-4S.
+At position 17 to 260, the domain is characterized as ABC transporter.
+At position 604 to 702, the domain is characterized as Fibronectin type-III 2.
+At position 727 to 818, the domain is characterized as Fibronectin type-III 3.
+At position 829 to 924, the domain is characterized as Fibronectin type-III 4.
+At position 995 to 1270, the domain is characterized as Protein kinase.
+At position 4 to 106, the domain is characterized as SSB.
+At position 356 to 398, the domain is characterized as Myb-like.
+At position 31 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 123 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 311 to 404, the domain is characterized as Ig-like C2-type 4.
+At position 2 to 238, the domain is characterized as ABC transporter 1.
+At position 282 to 531, the domain is characterized as ABC transporter 2.
+At position 79 to 343, the domain is characterized as Protein kinase.
+At position 4 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 401, the domain is characterized as GMPS ATP-PPase.
+At position 2 to 234, the domain is characterized as Glutamine amidotransferase type-2.
+At position 1 to 183, the domain is characterized as tr-type G.
+At position 7 to 64, the domain is characterized as SpoVT-AbrB 1.
+At position 334 to 406, the domain is characterized as MBD.
+At position 167 to 251, the domain is characterized as PPIase FKBP-type.
+At position 280 to 530, the domain is characterized as Methyl-accepting transducer.
+At position 1 to 281, the domain is characterized as ABC transmembrane type-1.
+At position 314 to 547, the domain is characterized as ABC transporter.
+At position 641 to 715, the domain is characterized as S1 motif.
+At position 24 to 100, the domain is characterized as SAMD1-like winged helix (WH).
+At position 474 to 542, the domain is characterized as SAM.
+At position 50 to 198, the domain is characterized as Flavodoxin-like.
+At position 316 to 559, the domain is characterized as Radical SAM core.
+At position 17 to 71, the domain is characterized as HTH cro/C1-type.
+At position 275 to 462, the domain is characterized as DH.
+At position 374 to 422, the domain is characterized as SOCS box.
+At position 10 to 82, the domain is characterized as J.
+At position 97 to 169, the domain is characterized as DPH-type MB.
+At position 69 to 135, the domain is characterized as TGS.
+At position 142 to 415, the domain is characterized as ABC transporter 1.
+At position 493 to 706, the domain is characterized as ABC transmembrane type-2 1.
+At position 824 to 1076, the domain is characterized as ABC transporter 2.
+At position 1149 to 1363, the domain is characterized as ABC transmembrane type-2 2.
+At position 101 to 210, the domain is characterized as Rab-GAP TBC.
+At position 130 to 206, the domain is characterized as Ubiquitin-like.
+At position 32 to 114, the domain is characterized as GOLD.
+At position 13 to 186, the domain is characterized as Era-type G.
+At position 217 to 299, the domain is characterized as KH type-2.
+At position 132 to 515, the domain is characterized as IF rod.
+At position 575 to 698, the domain is characterized as LTD.
+At position 26 to 39, the domain is characterized as CRIB.
+At position 606 to 676, the domain is characterized as Bromo.
+At position 1076 to 1159, the domain is characterized as PWWP.
+At position 48 to 101, the domain is characterized as bHLH.
+At position 296 to 366, the domain is characterized as PAS 2.
+At position 371 to 414, the domain is characterized as PAC.
+At position 23 to 250, the domain is characterized as Phosphagen kinase C-terminal.
+At position 36 to 130, the domain is characterized as Ig-like V-type.
+At position 147 to 210, the domain is characterized as Ig-like C2-type.
+At position 37 to 435, the domain is characterized as Glutamine amidotransferase type-2.
+At position 285 to 364, the domain is characterized as Ubiquitin-like.
+At position 448 to 507, the domain is characterized as HTH myb-type.
+At position 139 to 231, the domain is characterized as WSC 1.
+At position 242 to 337, the domain is characterized as WSC 2.
+At position 28 to 290, the domain is characterized as Brix.
+At position 11 to 247, the domain is characterized as ABC transporter 1.
+At position 260 to 501, the domain is characterized as ABC transporter 2.
+At position 64 to 393, the domain is characterized as PPM-type phosphatase.
+At position 239 to 416, the domain is characterized as TrmE-type G.
+At position 100 to 195, the domain is characterized as POU-specific atypical.
+At position 15 to 60, the domain is characterized as Gla.
+At position 90 to 128, the domain is characterized as EGF-like 1.
+At position 130 to 173, the domain is characterized as EGF-like 2; calcium-binding.
+At position 174 to 215, the domain is characterized as EGF-like 3; calcium-binding.
+At position 216 to 256, the domain is characterized as EGF-like 4; calcium-binding.
+At position 272 to 448, the domain is characterized as Laminin G-like 1.
+At position 457 to 639, the domain is characterized as Laminin G-like 2.
+At position 25 to 65, the domain is characterized as Saposin A-type.
+At position 65 to 147, the domain is characterized as Saposin B-type 1.
+At position 204 to 281, the domain is characterized as Saposin B-type 2.
+At position 295 to 370, the domain is characterized as Saposin B-type 3.
+At position 93 to 222, the domain is characterized as MTTase N-terminal.
+At position 246 to 501, the domain is characterized as Radical SAM core.
+At position 504 to 580, the domain is characterized as TRAM.
+At position 231 to 318, the domain is characterized as ACB.
+At position 21 to 57, the domain is characterized as EGF-like 1.
+At position 58 to 98, the domain is characterized as EGF-like 2.
+At position 101 to 138, the domain is characterized as EGF-like 3.
+At position 139 to 175, the domain is characterized as EGF-like 4.
+At position 177 to 215, the domain is characterized as EGF-like 5; calcium-binding.
+At position 489 to 524, the domain is characterized as EGF-like 13; calcium-binding.
+At position 526 to 562, the domain is characterized as EGF-like 14; calcium-binding.
+At position 564 to 599, the domain is characterized as EGF-like 15; calcium-binding.
+At position 601 to 637, the domain is characterized as EGF-like 16; calcium-binding.
+At position 639 to 674, the domain is characterized as EGF-like 17; calcium-binding.
+At position 676 to 712, the domain is characterized as EGF-like 18; calcium-binding.
+At position 714 to 749, the domain is characterized as EGF-like 19; calcium-binding.
+At position 751 to 787, the domain is characterized as EGF-like 20; calcium-binding.
+At position 789 to 825, the domain is characterized as EGF-like 21; calcium-binding.
+At position 827 to 865, the domain is characterized as EGF-like 22.
+At position 867 to 903, the domain is characterized as EGF-like 23; calcium-binding.
+At position 905 to 941, the domain is characterized as EGF-like 24; calcium-binding.
+At position 943 to 979, the domain is characterized as EGF-like 25; calcium-binding.
+At position 981 to 1017, the domain is characterized as EGF-like 26.
+At position 1019 to 1055, the domain is characterized as EGF-like 27; calcium-binding.
+At position 1057 to 1093, the domain is characterized as EGF-like 28.
+At position 1095 to 1141, the domain is characterized as EGF-like 29.
+At position 1143 to 1179, the domain is characterized as EGF-like 30; calcium-binding.
+At position 1181 to 1217, the domain is characterized as EGF-like 31; calcium-binding.
+At position 1219 to 1263, the domain is characterized as EGF-like 32; calcium-binding.
+At position 1265 to 1303, the domain is characterized as EGF-like 33.
+At position 1305 to 1344, the domain is characterized as EGF-like 34.
+At position 1346 to 1382, the domain is characterized as EGF-like 35.
+At position 1385 to 1423, the domain is characterized as EGF-like 36.
+At position 196 to 289, the domain is characterized as PPIase FKBP-type.
+At position 4 to 409, the domain is characterized as BRO1.
+At position 441 to 504, the domain is characterized as SOCS box.
+At position 306 to 364, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 373 to 564, the domain is characterized as E2.
+At position 351 to 498, the domain is characterized as PI-PLC X-box.
+At position 1 to 51, the domain is characterized as Chitin-binding type R&R.
+At position 13 to 69, the domain is characterized as HTH myb-type 1.
+At position 70 to 120, the domain is characterized as HTH myb-type 2.
+At position 126 to 260, the domain is characterized as Fatty acid hydroxylase.
+At position 148 to 409, the domain is characterized as Peptidase M66.
+At position 440 to 659, the domain is characterized as ABC transporter 1.
+At position 692 to 1019, the domain is characterized as ABC transporter 2.
+At position 820 to 869, the domain is characterized as Chromo.
+At position 1082 to 1154, the domain is characterized as BIG2.
+At position 239 to 408, the domain is characterized as PCI.
+At position 29 to 372, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 381 to 705, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 156 to 290, the domain is characterized as TIR.
+At position 286 to 328, the domain is characterized as CUE.
+At position 99 to 346, the domain is characterized as Radical SAM core.
+At position 21 to 59, the domain is characterized as CBM1.
+At position 31 to 107, the domain is characterized as RRM 1.
+At position 122 to 199, the domain is characterized as RRM 2.
+At position 228 to 420, the domain is characterized as SEC7.
+At position 548 to 677, the domain is characterized as PH.
+At position 547 to 588, the domain is characterized as UBA.
+At position 1117 to 1189, the domain is characterized as RRM.
+At position 366 to 404, the domain is characterized as UBA.
+At position 523 to 614, the domain is characterized as GED.
+At position 24 to 250, the domain is characterized as Radical SAM core.
+At position 333 to 430, the domain is characterized as ERCC4.
+At position 6 to 206, the domain is characterized as N-acetyltransferase.
+At position 29 to 150, the domain is characterized as Thioredoxin.
+At position 4 to 44, the domain is characterized as F-box.
+At position 127 to 176, the domain is characterized as WAP.
+At position 186 to 287, the domain is characterized as Fibronectin type-III 1.
+At position 292 to 400, the domain is characterized as Fibronectin type-III 2.
+At position 425 to 523, the domain is characterized as Fibronectin type-III 3.
+At position 550 to 658, the domain is characterized as Fibronectin type-III 4.
+At position 620 to 787, the domain is characterized as Integrase catalytic.
+At position 1376 to 1511, the domain is characterized as Reverse transcriptase Ty1/copia-type.
+At position 1645 to 1791, the domain is characterized as RNase H Ty1/copia-type.
+At position 255 to 470, the domain is characterized as ABC transporter 2.
+At position 322 to 432, the domain is characterized as PAZ.
+At position 636 to 899, the domain is characterized as Piwi.
+At position 12 to 701, the domain is characterized as Myosin motor.
+At position 704 to 726, the domain is characterized as IQ 1.
+At position 727 to 756, the domain is characterized as IQ 2.
+At position 855 to 1029, the domain is characterized as TH1.
+At position 19 to 138, the domain is characterized as MARVEL.
+At position 640 to 816, the domain is characterized as PCI.
+At position 450 to 513, the domain is characterized as bZIP.
+At position 390 to 822, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1307 to 1609, the domain is characterized as PKS/mFAS DH.
+At position 10 to 95, the domain is characterized as MtN3/slv 1.
+At position 228 to 373, the domain is characterized as Helicase C-terminal.
+At position 148 to 322, the domain is characterized as Helicase ATP-binding.
+At position 360 to 542, the domain is characterized as Helicase C-terminal.
+At position 616 to 922, the domain is characterized as SEC63.
+At position 27 to 124, the domain is characterized as Cadherin 1.
+At position 696 to 808, the domain is characterized as Cadherin 7.
+At position 810 to 928, the domain is characterized as Cadherin 8.
+At position 930 to 1058, the domain is characterized as Cadherin 9.
+At position 586 to 671, the domain is characterized as BRCT.
+At position 39 to 351, the domain is characterized as Protein kinase.
+At position 259 to 506, the domain is characterized as ABC transporter 2.
+At position 397 to 470, the domain is characterized as RRM 2.
+At position 489 to 563, the domain is characterized as RRM 3.
+At position 575 to 650, the domain is characterized as RRM 4.
+At position 26 to 119, the domain is characterized as Ig-like C2-type 1.
+At position 121 to 221, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 316, the domain is characterized as Ig-like C2-type 3.
+At position 320 to 419, the domain is characterized as Ig-like C2-type 4.
+At position 426 to 520, the domain is characterized as Ig-like C2-type 5.
+At position 343 to 403, the domain is characterized as SH3.
+At position 103 to 208, the domain is characterized as Rieske.
+At position 2098 to 2161, the domain is characterized as SAM.
+At position 38 to 220, the domain is characterized as BPL/LPL catalytic.
+At position 211 to 334, the domain is characterized as OTU.
+At position 71 to 242, the domain is characterized as FAD-binding PCMH-type.
+At position 389 to 783, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1270 to 1581, the domain is characterized as PKS/mFAS DH.
+At position 1671 to 1747, the domain is characterized as Carrier.
+At position 76 to 118, the domain is characterized as Collagen-like.
+At position 154 to 287, the domain is characterized as C1q.
+At position 89 to 391, the domain is characterized as Peptidase A1.
+At position 141 to 401, the domain is characterized as F-BAR.
+At position 13 to 72, the domain is characterized as CBS 1.
+At position 78 to 133, the domain is characterized as CBS 2.
+At position 159 to 192, the domain is characterized as ACP-type MB.
+At position 138 to 245, the domain is characterized as Gnk2-homologous 2.
+At position 321 to 600, the domain is characterized as Protein kinase.
+At position 451 to 524, the domain is characterized as S1 motif 6.
+At position 14 to 242, the domain is characterized as Phosphagen kinase C-terminal.
+At position 16 to 114, the domain is characterized as Rieske.
+At position 444 to 575, the domain is characterized as Thioredoxin.
+At position 870 to 957, the domain is characterized as FH1.
+At position 972 to 1388, the domain is characterized as FH2.
+At position 59 to 364, the domain is characterized as Peptidase A1.
+At position 594 to 663, the domain is characterized as CBS 1.
+At position 708 to 770, the domain is characterized as CBS 2.
+At position 726 to 1013, the domain is characterized as Protein kinase.
+At position 75 to 278, the domain is characterized as ABC transmembrane type-1.
+At position 61 to 114, the domain is characterized as bHLH.
+At position 132 to 190, the domain is characterized as PAS 1.
+At position 294 to 343, the domain is characterized as PAS 2.
+At position 397 to 504, the domain is characterized as ERV/ALR sulfhydryl oxidase.
+At position 30 to 144, the domain is characterized as SCP.
+At position 19 to 98, the domain is characterized as RRM.
+At position 73 to 134, the domain is characterized as CBS 1.
+At position 117 to 149, the domain is characterized as EF-hand 3.
+At position 1 to 120, the domain is characterized as HTH marR-type.
+At position 108 to 391, the domain is characterized as Protein kinase.
+At position 249 to 423, the domain is characterized as Helicase ATP-binding.
+At position 457 to 603, the domain is characterized as Helicase C-terminal.
+At position 75 to 250, the domain is characterized as FAD-binding PCMH-type.
+At position 2 to 191, the domain is characterized as Brix.
+At position 935 to 1003, the domain is characterized as Carrier 1.
+At position 1984 to 2059, the domain is characterized as Carrier 2.
+At position 2112 to 2372, the domain is characterized as Thioester reductase (TE).
+At position 194 to 291, the domain is characterized as ELM2.
+At position 296 to 348, the domain is characterized as SANT.
+At position 214 to 371, the domain is characterized as GAF.
+At position 390 to 709, the domain is characterized as PDEase.
+At position 56 to 122, the domain is characterized as TGS.
+At position 81 to 785, the domain is characterized as USP.
+At position 23 to 125, the domain is characterized as PH.
+At position 129 to 142, the domain is characterized as CRIB.
+At position 309 to 566, the domain is characterized as Protein kinase.
+At position 322 to 513, the domain is characterized as B30.2/SPRY.
+At position 340 to 407, the domain is characterized as ACT.
+At position 295 to 531, the domain is characterized as GT92.
+At position 38 to 165, the domain is characterized as PLAT.
+At position 168 to 877, the domain is characterized as Lipoxygenase.
+At position 285 to 491, the domain is characterized as MCM.
+At position 156 to 424, the domain is characterized as SF4 helicase; first part.
+At position 308 to 568, the domain is characterized as SF4 helicase; second part.
+At position 18 to 162, the domain is characterized as Nudix hydrolase.
+At position 26 to 205, the domain is characterized as Helicase ATP-binding.
+At position 370 to 535, the domain is characterized as Helicase C-terminal.
+At position 565 to 659, the domain is characterized as Dicer dsRNA-binding fold.
+At position 915 to 1055, the domain is characterized as RNase III 1.
+At position 1094 to 1277, the domain is characterized as RNase III 2.
+At position 47 to 231, the domain is characterized as Laminin G-like.
+At position 292 to 346, the domain is characterized as Collagen-like 1.
+At position 347 to 388, the domain is characterized as Collagen-like 2.
+At position 389 to 430, the domain is characterized as Collagen-like 3.
+At position 519 to 577, the domain is characterized as Collagen-like 4.
+At position 578 to 618, the domain is characterized as Collagen-like 5.
+At position 620 to 673, the domain is characterized as Collagen-like 6.
+At position 722 to 777, the domain is characterized as Collagen-like 7.
+At position 778 to 810, the domain is characterized as Collagen-like 8.
+At position 833 to 891, the domain is characterized as Collagen-like 9.
+At position 180 to 501, the domain is characterized as DOT1.
+At position 137 to 307, the domain is characterized as Helicase ATP-binding.
+At position 317 to 478, the domain is characterized as Helicase C-terminal.
+At position 51 to 86, the domain is characterized as Tify.
+At position 313 to 394, the domain is characterized as ACT.
+At position 25 to 119, the domain is characterized as PH 1.
+At position 233 to 330, the domain is characterized as PH 2.
+At position 71 to 278, the domain is characterized as TLC.
+At position 45 to 74, the domain is characterized as IQ 1.
+At position 101 to 130, the domain is characterized as IQ 2.
+At position 365 to 601, the domain is characterized as ABC transporter 1.
+At position 687 to 975, the domain is characterized as ABC transmembrane type-1 2.
+At position 1010 to 1246, the domain is characterized as ABC transporter 2.
+At position 493 to 751, the domain is characterized as ATP-grasp.
+At position 19 to 226, the domain is characterized as ABC transporter.
+At position 243 to 295, the domain is characterized as SOCS box.
+At position 163 to 308, the domain is characterized as PPC.
+At position 700 to 748, the domain is characterized as GRIP.
+At position 709 to 801, the domain is characterized as FDX-ACB.
+At position 8 to 195, the domain is characterized as RNase H type-2.
+At position 18 to 60, the domain is characterized as Chitin-binding type-1.
+At position 68 to 189, the domain is characterized as Barwin.
+At position 210 to 400, the domain is characterized as PCI.
+At position 132 to 389, the domain is characterized as SMP-LTD.
+At position 84 to 206, the domain is characterized as GST C-terminal.
+At position 66 to 142, the domain is characterized as S1 motif.
+At position 321 to 496, the domain is characterized as PCI.
+At position 27 to 80, the domain is characterized as Kazal-like.
+At position 18 to 279, the domain is characterized as Protein kinase.
+At position 239 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 91 to 158, the domain is characterized as GRAM.
+At position 367 to 538, the domain is characterized as VASt.
+At position 817 to 1076, the domain is characterized as Protein kinase.
+At position 1077 to 1142, the domain is characterized as AGC-kinase C-terminal.
+At position 151 to 240, the domain is characterized as Ig-like C2-type 1.
+At position 251 to 336, the domain is characterized as Ig-like C2-type 2.
+At position 22 to 378, the domain is characterized as IF rod.
+At position 224 to 363, the domain is characterized as DAGKc.
+At position 721 to 988, the domain is characterized as Protein kinase.
+At position 46 to 234, the domain is characterized as VWFA 1.
+At position 833 to 1014, the domain is characterized as VWFA 3.
+At position 71 to 84, the domain is characterized as CRIB.
+At position 45 to 148, the domain is characterized as KRAB.
+At position 4 to 74, the domain is characterized as KRAB 1.
+At position 203 to 274, the domain is characterized as KRAB 2.
+At position 82 to 323, the domain is characterized as ABC transporter 1.
+At position 393 to 610, the domain is characterized as ABC transporter 2.
+At position 249 to 448, the domain is characterized as GATase cobBQ-type.
+At position 270 to 469, the domain is characterized as Reticulon.
+At position 34 to 246, the domain is characterized as Fibrinogen C-terminal.
+At position 32 to 105, the domain is characterized as IGFBP N-terminal.
+At position 108 to 174, the domain is characterized as VWFC.
+At position 205 to 250, the domain is characterized as TSP type-1.
+At position 264 to 338, the domain is characterized as CTCK.
+At position 975 to 1034, the domain is characterized as SH3.
+At position 2267 to 2302, the domain is characterized as EF-hand 1.
+At position 2310 to 2345, the domain is characterized as EF-hand 2.
+At position 2347 to 2382, the domain is characterized as EF-hand 3.
+At position 240 to 330, the domain is characterized as Ig-like 3.
+At position 1266 to 1351, the domain is characterized as Ig-like 11.
+At position 1355 to 1442, the domain is characterized as Ig-like 12.
+At position 1536 to 1628, the domain is characterized as Ig-like 13.
+At position 557 to 623, the domain is characterized as KH.
+At position 20 to 180, the domain is characterized as N-acetyltransferase.
+At position 241 to 274, the domain is characterized as WW 1.
+At position 310 to 343, the domain is characterized as WW 2.
+At position 12 to 105, the domain is characterized as PH.
+At position 147 to 384, the domain is characterized as Radical SAM core.
+At position 387 to 453, the domain is characterized as TRAM.
+At position 402 to 496, the domain is characterized as Fibronectin type-III.
+At position 13 to 135, the domain is characterized as VOC.
+At position 134 to 233, the domain is characterized as PilZ.
+At position 22 to 194, the domain is characterized as FAD-binding PCMH-type.
+At position 385 to 633, the domain is characterized as Rab-GAP TBC.
+At position 149 to 320, the domain is characterized as Helicase ATP-binding.
+At position 347 to 492, the domain is characterized as Helicase C-terminal.
+At position 31 to 122, the domain is characterized as Fibronectin type-III.
+At position 480 to 715, the domain is characterized as ABC transporter 1.
+At position 1285 to 1518, the domain is characterized as ABC transporter 2.
+At position 59 to 157, the domain is characterized as Rieske.
+At position 42 to 169, the domain is characterized as TBDR plug.
+At position 174 to 746, the domain is characterized as TBDR beta-barrel.
+At position 340 to 436, the domain is characterized as Rhodanese.
+At position 14 to 330, the domain is characterized as Peptidase A1.
+At position 421 to 495, the domain is characterized as POU-specific.
+At position 30 to 100, the domain is characterized as KRAB.
+At position 1 to 309, the domain is characterized as Teneurin N-terminal.
+At position 514 to 545, the domain is characterized as EGF-like 1.
+At position 546 to 576, the domain is characterized as EGF-like 2.
+At position 578 to 610, the domain is characterized as EGF-like 3.
+At position 611 to 642, the domain is characterized as EGF-like 4.
+At position 644 to 677, the domain is characterized as EGF-like 5.
+At position 678 to 709, the domain is characterized as EGF-like 6.
+At position 710 to 739, the domain is characterized as EGF-like 7.
+At position 740 to 774, the domain is characterized as EGF-like 8.
+At position 175 to 263, the domain is characterized as Rieske.
+At position 7 to 130, the domain is characterized as MATH.
+At position 40 to 163, the domain is characterized as Ricin B-type lectin.
+At position 175 to 223, the domain is characterized as Fibronectin type-II.
+At position 240 to 357, the domain is characterized as C-type lectin 1.
+At position 524 to 645, the domain is characterized as C-type lectin 3.
+At position 675 to 799, the domain is characterized as C-type lectin 4.
+At position 821 to 940, the domain is characterized as C-type lectin 5.
+At position 967 to 1098, the domain is characterized as C-type lectin 6.
+At position 1123 to 1234, the domain is characterized as C-type lectin 7.
+At position 1259 to 1379, the domain is characterized as C-type lectin 8.
+At position 49 to 337, the domain is characterized as AB hydrolase-1.
+At position 145 to 426, the domain is characterized as Protein kinase.
+At position 354 to 523, the domain is characterized as tr-type G.
+At position 594 to 672, the domain is characterized as Carrier.
+At position 851 to 883, the domain is characterized as LisH.
+At position 335 to 369, the domain is characterized as EF-hand.
+At position 708 to 795, the domain is characterized as Fibronectin type-III.
+At position 196 to 279, the domain is characterized as Doublecortin 2.
+At position 409 to 666, the domain is characterized as Protein kinase.
+At position 23 to 57, the domain is characterized as CBM1.
+At position 793 to 859, the domain is characterized as HP.
+At position 201 to 379, the domain is characterized as tr-type G.
+At position 42 to 97, the domain is characterized as Ig-like C2-type 1.
+At position 137 to 197, the domain is characterized as Ig-like C2-type 2.
+At position 237 to 295, the domain is characterized as Ig-like C2-type 3.
+At position 20 to 168, the domain is characterized as PX.
+At position 31 to 150, the domain is characterized as Plastocyanin-like 1.
+At position 179 to 379, the domain is characterized as Plastocyanin-like 2.
+At position 469 to 588, the domain is characterized as Plastocyanin-like 3.
+At position 19 to 265, the domain is characterized as tr-type G.
+At position 1087 to 1204, the domain is characterized as SET.
+At position 1213 to 1229, the domain is characterized as Post-SET.
+At position 302 to 365, the domain is characterized as bZIP.
+At position 641 to 741, the domain is characterized as tRNA-binding.
+At position 44 to 103, the domain is characterized as Collagen-like.
+At position 133 to 483, the domain is characterized as PUM-HD.
+At position 58 to 316, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 79 to 147, the domain is characterized as DRBM.
+At position 470 to 638, the domain is characterized as Helicase ATP-binding.
+At position 680 to 853, the domain is characterized as Helicase C-terminal.
+At position 1880 to 1975, the domain is characterized as Peptidase C50.
+At position 167 to 358, the domain is characterized as CheB-type methylesterase.
+At position 95 to 430, the domain is characterized as Peptidase A1.
+At position 246 to 285, the domain is characterized as GRAM 1.
+At position 724 to 790, the domain is characterized as GRAM 2.
+At position 8 to 185, the domain is characterized as Clp R.
+At position 17 to 84, the domain is characterized as DDT.
+At position 37 to 312, the domain is characterized as Pyruvate carboxyltransferase.
+At position 92 to 229, the domain is characterized as PH.
+At position 12 to 332, the domain is characterized as SAM-dependent MTase PRMT-type 1.
+At position 337 to 647, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 70 to 244, the domain is characterized as FAD-binding PCMH-type.
+At position 8 to 255, the domain is characterized as PPM-type phosphatase.
+At position 163 to 319, the domain is characterized as Plastocyanin-like 2.
+At position 428 to 562, the domain is characterized as Plastocyanin-like 3.
+At position 280 to 340, the domain is characterized as LIM zinc-binding.
+At position 154 to 683, the domain is characterized as USP.
+At position 786 to 893, the domain is characterized as DUSP 2.
+At position 24 to 249, the domain is characterized as Radical SAM core.
+At position 54 to 145, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 89 to 456, the domain is characterized as Peptidase A1.
+At position 57 to 160, the domain is characterized as FAD-binding FR-type.
+At position 223 to 409, the domain is characterized as IRG-type G.
+At position 208 to 246, the domain is characterized as LRRCT.
+At position 519 to 548, the domain is characterized as IQ.
+At position 14 to 276, the domain is characterized as Pyruvate carboxyltransferase.
+At position 23 to 52, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 62 to 92, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 100 to 129, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 200 to 274, the domain is characterized as POU-specific.
+At position 12 to 53, the domain is characterized as JmjN.
+At position 170 to 324, the domain is characterized as JmjC.
+At position 55 to 137, the domain is characterized as Lipoyl-binding.
+At position 83 to 126, the domain is characterized as CUE.
+At position 94 to 160, the domain is characterized as Importin N-terminal.
+At position 99 to 432, the domain is characterized as Asparaginase/glutaminase.
+At position 132 to 729, the domain is characterized as PLA2c.
+At position 350 to 412, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 32 to 134, the domain is characterized as Phytocyanin.
+At position 3 to 165, the domain is characterized as DHFR.
+At position 80 to 144, the domain is characterized as SH3b.
+At position 201 to 244, the domain is characterized as LysM 2.
+At position 366 to 484, the domain is characterized as NlpC/P60.
+At position 1042 to 1205, the domain is characterized as JmjC.
+At position 92 to 208, the domain is characterized as RGS.
+At position 11 to 314, the domain is characterized as MACPF.
+At position 39 to 202, the domain is characterized as N-acetyltransferase.
+At position 402 to 836, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1693 to 1770, the domain is characterized as Carrier.
+At position 11 to 203, the domain is characterized as RNase H type-2.
+At position 568 to 635, the domain is characterized as BTB.
+At position 118 to 299, the domain is characterized as CP-type G.
+At position 633 to 772, the domain is characterized as C2.
+At position 184 to 256, the domain is characterized as RRM.
+At position 58 to 314, the domain is characterized as PPM-type phosphatase.
+At position 131 to 174, the domain is characterized as CUE.
+At position 35 to 727, the domain is characterized as Myosin motor.
+At position 785 to 974, the domain is characterized as TH1.
+At position 1127 to 1187, the domain is characterized as SH3.
+At position 765 to 851, the domain is characterized as SUEL-type lectin.
+At position 646 to 724, the domain is characterized as BRCT.
+At position 26 to 136, the domain is characterized as Thioredoxin.
+At position 449 to 499, the domain is characterized as DHHC.
+At position 26 to 262, the domain is characterized as ABC transporter 1.
+At position 272 to 511, the domain is characterized as ABC transporter 2.
+At position 131 to 166, the domain is characterized as EF-hand.
+At position 113 to 219, the domain is characterized as RAMA.
+At position 284 to 420, the domain is characterized as MPN.
+At position 289 to 570, the domain is characterized as UvrD-like helicase C-terminal.
+At position 360 to 552, the domain is characterized as PNPLA.
+At position 77 to 331, the domain is characterized as Protein kinase.
+At position 86 to 115, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 155 to 184, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 46 to 111, the domain is characterized as Ig-like C2-type 1.
+At position 143 to 209, the domain is characterized as Ig-like C2-type 2.
+At position 226 to 325, the domain is characterized as Ig-like C2-type 3.
+At position 330 to 416, the domain is characterized as Ig-like C2-type 4.
+At position 423 to 542, the domain is characterized as Ig-like C2-type 5.
+At position 549 to 656, the domain is characterized as Ig-like C2-type 6.
+At position 665 to 751, the domain is characterized as Ig-like C2-type 7.
+At position 832 to 1160, the domain is characterized as Protein kinase.
+At position 63 to 216, the domain is characterized as Fido.
+At position 489 to 659, the domain is characterized as tr-type G.
+At position 486 to 655, the domain is characterized as tr-type G.
+At position 149 to 369, the domain is characterized as PE-PPE.
+At position 371 to 522, the domain is characterized as CBM3.
+At position 505 to 593, the domain is characterized as PDZ.
+At position 989 to 1052, the domain is characterized as SAM.
+At position 151 to 250, the domain is characterized as Glutaredoxin.
+At position 3 to 115, the domain is characterized as CMP/dCMP-type deaminase.
+At position 190 to 245, the domain is characterized as LRRCT.
+At position 913 to 1249, the domain is characterized as AdoMet activation.
+At position 33 to 173, the domain is characterized as C-type lectin.
+At position 246 to 288, the domain is characterized as EGF-like.
+At position 583 to 786, the domain is characterized as Helicase ATP-binding.
+At position 995 to 1157, the domain is characterized as Helicase C-terminal.
+At position 803 to 856, the domain is characterized as bHLH.
+At position 46 to 126, the domain is characterized as Ig-like C2-type 1.
+At position 258 to 302, the domain is characterized as EGF-like 2.
+At position 304 to 342, the domain is characterized as EGF-like 3.
+At position 348 to 438, the domain is characterized as Ig-like C2-type 2.
+At position 444 to 538, the domain is characterized as Fibronectin type-III 1.
+At position 540 to 633, the domain is characterized as Fibronectin type-III 2.
+At position 634 to 729, the domain is characterized as Fibronectin type-III 3.
+At position 816 to 1095, the domain is characterized as Protein kinase.
+At position 25 to 140, the domain is characterized as MTTase N-terminal.
+At position 163 to 393, the domain is characterized as Radical SAM core.
+At position 396 to 466, the domain is characterized as TRAM.
+At position 290 to 352, the domain is characterized as Mop.
+At position 400 to 582, the domain is characterized as RHD.
+At position 218 to 377, the domain is characterized as TrmE-type G.
+At position 394 to 576, the domain is characterized as RHD.
+At position 169 to 208, the domain is characterized as UBA.
+At position 102 to 185, the domain is characterized as PRC barrel.
+At position 136 to 512, the domain is characterized as MACPF.
+At position 513 to 543, the domain is characterized as EGF-like.
+At position 101 to 146, the domain is characterized as F-box.
+At position 187 to 407, the domain is characterized as ABC transmembrane type-1.
+At position 439 to 738, the domain is characterized as Protein kinase.
+At position 242 to 485, the domain is characterized as ABC transporter.
+At position 562 to 810, the domain is characterized as ABC transmembrane type-2.
+At position 85 to 769, the domain is characterized as Peptidase M13.
+At position 210 to 271, the domain is characterized as Thyroglobulin type-1.
+At position 171 to 588, the domain is characterized as Protein kinase.
+At position 2 to 180, the domain is characterized as DHFR.
+At position 76 to 252, the domain is characterized as FAD-binding PCMH-type.
+At position 10 to 135, the domain is characterized as Response regulatory.
+At position 57 to 123, the domain is characterized as HMA 1.
+At position 142 to 208, the domain is characterized as HMA 2.
+At position 256 to 322, the domain is characterized as HMA 3.
+At position 355 to 421, the domain is characterized as HMA 4.
+At position 481 to 547, the domain is characterized as HMA 5.
+At position 557 to 623, the domain is characterized as HMA 6.
+At position 181 to 248, the domain is characterized as SH3 1.
+At position 311 to 404, the domain is characterized as Fibronectin type-III 1.
+At position 407 to 489, the domain is characterized as Fibronectin type-III 2.
+At position 503 to 604, the domain is characterized as Fibronectin type-III 3.
+At position 868 to 936, the domain is characterized as SH3 2.
+At position 972 to 1039, the domain is characterized as SH3 3.
+At position 597 to 728, the domain is characterized as B12-binding.
+At position 139 to 204, the domain is characterized as Tudor; degenerate.
+At position 44 to 336, the domain is characterized as NB-ARC.
+At position 71 to 122, the domain is characterized as bHLH.
+At position 108 to 177, the domain is characterized as S4 RNA-binding.
+At position 8 to 146, the domain is characterized as N-acetyltransferase 1.
+At position 727 to 1020, the domain is characterized as Protein kinase.
+At position 165 to 237, the domain is characterized as Bromo 1.
+At position 332 to 404, the domain is characterized as Bromo 2.
+At position 518 to 598, the domain is characterized as NET.
+At position 155 to 612, the domain is characterized as TBDR beta-barrel.
+At position 312 to 384, the domain is characterized as PDZ 1.
+At position 880 to 960, the domain is characterized as PDZ 2.
+At position 61 to 177, the domain is characterized as DOMON.
+At position 556 to 608, the domain is characterized as F-box.
+At position 4 to 317, the domain is characterized as SAM-dependent MTase C5-type.
+At position 137 to 209, the domain is characterized as Thioredoxin.
+At position 24 to 224, the domain is characterized as HORMA.
+At position 35 to 203, the domain is characterized as FAD-binding PCMH-type.
+At position 145 to 204, the domain is characterized as Collagen-like 1.
+At position 205 to 255, the domain is characterized as Collagen-like 2.
+At position 264 to 323, the domain is characterized as Collagen-like 3.
+At position 351 to 488, the domain is characterized as C1q.
+At position 4 to 86, the domain is characterized as Plastocyanin-like 1.
+At position 99 to 237, the domain is characterized as Plastocyanin-like 2.
+At position 290 to 389, the domain is characterized as PpiC 2.
+At position 1185 to 1419, the domain is characterized as Fibrillar collagen NC1.
+At position 102 to 503, the domain is characterized as Glutamine amidotransferase type-2.
+At position 147 to 334, the domain is characterized as B30.2/SPRY.
+At position 365 to 397, the domain is characterized as LisH.
+At position 403 to 460, the domain is characterized as CTLH.
+At position 399 to 459, the domain is characterized as COS.
+At position 474 to 567, the domain is characterized as Fibronectin type-III.
+At position 549 to 736, the domain is characterized as B30.2/SPRY.
+At position 20 to 154, the domain is characterized as sHSP.
+At position 17 to 86, the domain is characterized as HTH merR-type.
+At position 6 to 68, the domain is characterized as HTH iclR-type.
+At position 83 to 252, the domain is characterized as IclR-ED.
+At position 582 to 755, the domain is characterized as Helicase ATP-binding.
+At position 849 to 1026, the domain is characterized as Helicase C-terminal.
+At position 18 to 214, the domain is characterized as DPCK.
+At position 73 to 298, the domain is characterized as Radical SAM core.
+At position 157 to 200, the domain is characterized as LysM 3.
+At position 225 to 268, the domain is characterized as LysM 4.
+At position 296 to 414, the domain is characterized as NlpC/P60.
+At position 8 to 92, the domain is characterized as YcgL.
+At position 201 to 232, the domain is characterized as ShKT.
+At position 98 to 150, the domain is characterized as bHLH.
+At position 106 to 227, the domain is characterized as MPN.
+At position 10 to 168, the domain is characterized as UBC core.
+At position 265 to 337, the domain is characterized as MIT.
+At position 1 to 79, the domain is characterized as PDZ 1.
+At position 268 to 345, the domain is characterized as PDZ 2.
+At position 812 to 1203, the domain is characterized as FH2.
+At position 36 to 197, the domain is characterized as Helicase ATP-binding.
+At position 254 to 419, the domain is characterized as Helicase C-terminal.
+At position 152 to 219, the domain is characterized as KH.
+At position 145 to 244, the domain is characterized as Ig-like C2-type 2.
+At position 476 to 765, the domain is characterized as Protein kinase.
+At position 14 to 142, the domain is characterized as CID.
+At position 240 to 335, the domain is characterized as SH2.
+At position 942 to 1108, the domain is characterized as PNPLA.
+At position 386 to 482, the domain is characterized as PH 2.
+At position 11 to 126, the domain is characterized as sHSP.
+At position 545 to 644, the domain is characterized as SH2.
+At position 137 to 233, the domain is characterized as PpiC.
+At position 7 to 140, the domain is characterized as Nudix hydrolase.
+At position 12 to 158, the domain is characterized as Nudix hydrolase.
+At position 11 to 170, the domain is characterized as N-acetyltransferase.
+At position 97 to 141, the domain is characterized as WRC.
+At position 1941 to 2036, the domain is characterized as Peptidase C50.
+At position 362 to 509, the domain is characterized as Helicase C-terminal.
+At position 25 to 154, the domain is characterized as PH.
+At position 646 to 792, the domain is characterized as MOSC.
+At position 36 to 84, the domain is characterized as Cytochrome b5 heme-binding.
+At position 13 to 194, the domain is characterized as Exonuclease.
+At position 203 to 351, the domain is characterized as ExoI SH3-like.
+At position 355 to 471, the domain is characterized as ExoI C-terminal.
+At position 171 to 221, the domain is characterized as DHHC.
+At position 295 to 438, the domain is characterized as Jacalin-type lectin.
+At position 67 to 127, the domain is characterized as BACON.
+At position 772 to 824, the domain is characterized as LRRCT.
+At position 878 to 1022, the domain is characterized as TIR.
+At position 119 to 298, the domain is characterized as FAD-binding PCMH-type.
+At position 61 to 165, the domain is characterized as Calponin-homology (CH) 1.
+At position 180 to 285, the domain is characterized as Calponin-homology (CH) 2.
+At position 2418 to 2527, the domain is characterized as PH.
+At position 42 to 71, the domain is characterized as IQ 1.
+At position 98 to 127, the domain is characterized as IQ 2.
+At position 119 to 275, the domain is characterized as F5/8 type C.
+At position 143 to 312, the domain is characterized as PCI.
+At position 55 to 567, the domain is characterized as Alpha-carbonic anhydrase.
+At position 32 to 213, the domain is characterized as Helicase ATP-binding.
+At position 246 to 400, the domain is characterized as Helicase C-terminal.
+At position 613 to 850, the domain is characterized as ABC transporter.
+At position 20 to 107, the domain is characterized as Ig-like 1.
+At position 108 to 225, the domain is characterized as Ig-like 2.
+At position 256 to 345, the domain is characterized as Ig-like 3.
+At position 467 to 666, the domain is characterized as MAGE 1.
+At position 721 to 912, the domain is characterized as MAGE 2.
+At position 130 to 357, the domain is characterized as RMT2.
+At position 17 to 259, the domain is characterized as ABC transporter.
+At position 84 to 427, the domain is characterized as SAM-dependent MTase C5-type.
+At position 5 to 69, the domain is characterized as SH3.
+At position 19 to 131, the domain is characterized as Rieske.
+At position 1 to 67, the domain is characterized as Ig-like C2-type.
+At position 346 to 605, the domain is characterized as Protein kinase.
+At position 37 to 117, the domain is characterized as Inhibitor I9.
+At position 40 to 117, the domain is characterized as GIY-YIG.
+At position 227 to 262, the domain is characterized as UVR.
+At position 9 to 59, the domain is characterized as WAP.
+At position 1 to 82, the domain is characterized as CARD 1.
+At position 107 to 178, the domain is characterized as CARD 2.
+At position 266 to 402, the domain is characterized as NACHT.
+At position 2513 to 2633, the domain is characterized as BAH.
+At position 67 to 160, the domain is characterized as Ig-like 1.
+At position 159 to 254, the domain is characterized as Ig-like 2.
+At position 2 to 89, the domain is characterized as Ig-like C1-type.
+At position 195 to 824, the domain is characterized as USP.
+At position 73 to 226, the domain is characterized as Cytochrome c.
+At position 75 to 289, the domain is characterized as TLC.
+At position 13 to 293, the domain is characterized as Protein kinase.
+At position 305 to 474, the domain is characterized as JmjC.
+At position 335 to 580, the domain is characterized as Clu.
+At position 98 to 139, the domain is characterized as UBA.
+At position 668 to 973, the domain is characterized as Protein kinase.
+At position 974 to 1052, the domain is characterized as AGC-kinase C-terminal.
+At position 13 to 89, the domain is characterized as S4 RNA-binding.
+At position 222 to 295, the domain is characterized as SAM.
+At position 106 to 242, the domain is characterized as PPC.
+At position 107 to 153, the domain is characterized as F-box.
+At position 83 to 239, the domain is characterized as CBS 1.
+At position 363 to 438, the domain is characterized as CBS 4.
+At position 665 to 884, the domain is characterized as Ras-GEF.
+At position 42 to 114, the domain is characterized as SH3.
+At position 18 to 219, the domain is characterized as N-acetyltransferase.
+At position 1 to 200, the domain is characterized as ABC transporter.
+At position 14 to 136, the domain is characterized as EamA 1.
+At position 159 to 285, the domain is characterized as EamA 2.
+At position 1 to 202, the domain is characterized as START.
+At position 38 to 199, the domain is characterized as SIS.
+At position 4 to 140, the domain is characterized as Toprim.
+At position 234 to 333, the domain is characterized as Fe2OG dioxygenase.
+At position 49 to 107, the domain is characterized as CTLH.
+At position 1 to 119, the domain is characterized as Eph LBD.
+At position 240 to 350, the domain is characterized as Fibronectin type-III 1.
+At position 351 to 448, the domain is characterized as Fibronectin type-III 2.
+At position 537 to 800, the domain is characterized as Protein kinase.
+At position 829 to 893, the domain is characterized as SAM.
+At position 38 to 104, the domain is characterized as Myb-like.
+At position 213 to 350, the domain is characterized as TrmE-type G.
+At position 1713 to 1772, the domain is characterized as RAP.
+At position 29 to 137, the domain is characterized as Ig-like V-type.
+At position 146 to 245, the domain is characterized as Ig-like C1-type 1.
+At position 252 to 340, the domain is characterized as Ig-like C1-type 2.
+At position 334 to 609, the domain is characterized as Protein kinase.
+At position 452 to 630, the domain is characterized as Helicase C-terminal.
+At position 634 to 741, the domain is characterized as PH.
+At position 913 to 1128, the domain is characterized as Rho-GAP.
+At position 2 to 130, the domain is characterized as PINc.
+At position 443 to 507, the domain is characterized as J.
+At position 181 to 253, the domain is characterized as Bromo.
+At position 394 to 475, the domain is characterized as NET.
+At position 28 to 136, the domain is characterized as Gnk2-homologous 1.
+At position 1163 to 1226, the domain is characterized as SAM.
+At position 240 to 502, the domain is characterized as Protein kinase.
+At position 335 to 553, the domain is characterized as Histidine kinase.
+At position 267 to 286, the domain is characterized as UIM 1.
+At position 34 to 125, the domain is characterized as ARID.
+At position 1 to 90, the domain is characterized as FERM.
+At position 254 to 433, the domain is characterized as PCI.
+At position 166 to 243, the domain is characterized as RRM 1.
+At position 263 to 341, the domain is characterized as RRM 2.
+At position 59 to 196, the domain is characterized as Tyrosine-protein phosphatase.
+At position 5 to 67, the domain is characterized as LCN-type CS-alpha/beta.
+At position 17 to 92, the domain is characterized as S1-like.
+At position 1 to 114, the domain is characterized as Peptidase M12A.
+At position 33 to 96, the domain is characterized as PUB.
+At position 442 to 632, the domain is characterized as PAW.
+At position 403 to 479, the domain is characterized as BIG2.
+At position 645 to 876, the domain is characterized as NR LBD.
+At position 108 to 138, the domain is characterized as EF-hand 3.
+At position 14 to 217, the domain is characterized as ABC transporter.
+At position 25 to 109, the domain is characterized as IGFBP N-terminal.
+At position 94 to 153, the domain is characterized as Kazal-like.
+At position 361 to 463, the domain is characterized as PDZ.
+At position 47 to 306, the domain is characterized as Protein kinase.
+At position 520 to 786, the domain is characterized as PI3K/PI4K catalytic.
+At position 869 to 1004, the domain is characterized as GRAM.
+At position 1106 to 1607, the domain is characterized as Myotubularin phosphatase.
+At position 1766 to 1870, the domain is characterized as PH.
+At position 169 to 344, the domain is characterized as Helicase ATP-binding.
+At position 341 to 449, the domain is characterized as Rhodanese.
+At position 25 to 152, the domain is characterized as Bulb-type lectin.
+At position 288 to 326, the domain is characterized as EGF-like.
+At position 345 to 428, the domain is characterized as PAN.
+At position 500 to 783, the domain is characterized as Protein kinase.
+At position 546 to 755, the domain is characterized as Lon N-terminal.
+At position 51 to 125, the domain is characterized as EamA.
+At position 29 to 102, the domain is characterized as BTB.
+At position 207 to 450, the domain is characterized as NPH3.
+At position 1 to 247, the domain is characterized as Helicase ATP-binding.
+At position 421 to 602, the domain is characterized as Helicase C-terminal.
+At position 59 to 124, the domain is characterized as SCAN box.
+At position 82 to 194, the domain is characterized as Ferric oxidoreductase.
+At position 215 to 344, the domain is characterized as FAD-binding FR-type.
+At position 39 to 368, the domain is characterized as USP.
+At position 478 to 594, the domain is characterized as HD.
+At position 732 to 817, the domain is characterized as ACT 1.
+At position 16 to 155, the domain is characterized as N-acetyltransferase 1.
+At position 164 to 304, the domain is characterized as N-acetyltransferase 2.
+At position 103 to 381, the domain is characterized as Radical SAM core.
+At position 225 to 651, the domain is characterized as Peptidase S53.
+At position 386 to 535, the domain is characterized as MATH.
+At position 19 to 79, the domain is characterized as HTH myb-type.
+At position 237 to 516, the domain is characterized as Asparagine synthetase.
+At position 60 to 242, the domain is characterized as FAD-binding PCMH-type.
+At position 137 to 228, the domain is characterized as RRM.
+At position 140 to 234, the domain is characterized as BRICHOS.
+At position 167 to 288, the domain is characterized as Fe2OG dioxygenase.
+At position 36 to 127, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 169 to 199, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 25 to 242, the domain is characterized as ABC transporter.
+At position 47 to 219, the domain is characterized as MENTAL.
+At position 232 to 445, the domain is characterized as START.
+At position 286 to 538, the domain is characterized as Protein kinase 1.
+At position 589 to 1000, the domain is characterized as Protein kinase 2.
+At position 233 to 323, the domain is characterized as PA.
+At position 1721 to 1848, the domain is characterized as SMC hinge.
+At position 149 to 458, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 114 to 216, the domain is characterized as Fibronectin type-III 2.
+At position 146 to 457, the domain is characterized as IF rod.
+At position 351 to 619, the domain is characterized as Protein kinase.
+At position 10 to 242, the domain is characterized as Radical SAM core.
+At position 385 to 480, the domain is characterized as Rhodanese.
+At position 40 to 101, the domain is characterized as Sushi 1.
+At position 102 to 165, the domain is characterized as Sushi 2.
+At position 166 to 227, the domain is characterized as Sushi 3.
+At position 228 to 291, the domain is characterized as Sushi 4.
+At position 1 to 41, the domain is characterized as IF rod.
+At position 25 to 111, the domain is characterized as ATP-cone.
+At position 15 to 273, the domain is characterized as Protein kinase.
+At position 420 to 757, the domain is characterized as HECT.
+At position 2 to 131, the domain is characterized as TRM112.
+At position 259 to 443, the domain is characterized as GATase cobBQ-type.
+At position 1007 to 1112, the domain is characterized as Calponin-homology (CH).
+At position 412 to 464, the domain is characterized as SOCS box.
+At position 416 to 850, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1344 to 1654, the domain is characterized as PKS/mFAS DH.
+At position 1728 to 1805, the domain is characterized as Carrier.
+At position 65 to 184, the domain is characterized as FZ.
+At position 71 to 166, the domain is characterized as RAMA.
+At position 272 to 407, the domain is characterized as MPN.
+At position 48 to 203, the domain is characterized as FAS1.
+At position 274 to 338, the domain is characterized as SH3.
+At position 14 to 166, the domain is characterized as N-acetyltransferase 1.
+At position 168 to 317, the domain is characterized as N-acetyltransferase 2.
+At position 4 to 149, the domain is characterized as UBC core.
+At position 264 to 304, the domain is characterized as UBA.
+At position 626 to 686, the domain is characterized as Tudor.
+At position 39 to 342, the domain is characterized as PPM-type phosphatase.
+At position 26 to 78, the domain is characterized as bHLH.
+At position 66 to 150, the domain is characterized as Death.
+At position 214 to 274, the domain is characterized as HTH myb-type.
+At position 30 to 258, the domain is characterized as Laminin G-like.
+At position 330 to 365, the domain is characterized as EF-hand.
+At position 441 to 584, the domain is characterized as PI-PLC X-box.
+At position 638 to 753, the domain is characterized as PI-PLC Y-box.
+At position 750 to 879, the domain is characterized as C2.
+At position 25 to 349, the domain is characterized as Asparaginase/glutaminase.
+At position 149 to 299, the domain is characterized as PI-PLC X-box.
+At position 413 to 529, the domain is characterized as PI-PLC Y-box.
+At position 532 to 657, the domain is characterized as C2.
+At position 1 to 359, the domain is characterized as Rtt109-type HAT.
+At position 115 to 243, the domain is characterized as OmpA-like.
+At position 349 to 399, the domain is characterized as FBD.
+At position 1 to 126, the domain is characterized as C-type lysozyme.
+At position 18 to 411, the domain is characterized as GBD/FH3.
+At position 827 to 858, the domain is characterized as FH1.
+At position 883 to 1279, the domain is characterized as FH2.
+At position 1359 to 1391, the domain is characterized as DAD.
+At position 102 to 266, the domain is characterized as CRAL-TRIO.
+At position 453 to 650, the domain is characterized as FtsK.
+At position 844 to 916, the domain is characterized as AGC-kinase C-terminal.
+At position 1141 to 1229, the domain is characterized as PDZ.
+At position 134 to 173, the domain is characterized as STI1 1.
+At position 520 to 559, the domain is characterized as STI1 2.
+At position 65 to 181, the domain is characterized as BURP.
+At position 36 to 178, the domain is characterized as SIS.
+At position 203 to 263, the domain is characterized as CBS 1.
+At position 268 to 319, the domain is characterized as CBS 2.
+At position 6 to 229, the domain is characterized as ABC transporter.
+At position 93 to 272, the domain is characterized as ABC transmembrane type-1.
+At position 372 to 457, the domain is characterized as Death.
+At position 20 to 125, the domain is characterized as WAC.
+At position 443 to 503, the domain is characterized as DDT.
+At position 257 to 309, the domain is characterized as G-patch.
+At position 1 to 327, the domain is characterized as SAM-dependent MTase C5-type.
+At position 411 to 537, the domain is characterized as Plastocyanin-like 3.
+At position 58 to 128, the domain is characterized as SH3.
+At position 1117 to 1247, the domain is characterized as N-terminal Ras-GEF.
+At position 1305 to 1542, the domain is characterized as Ras-GEF.
+At position 142 to 185, the domain is characterized as UBA 1.
+At position 239 to 282, the domain is characterized as STI1.
+At position 261 to 519, the domain is characterized as KaiC 2.
+At position 226 to 294, the domain is characterized as Histone-fold.
+At position 388 to 493, the domain is characterized as EH.
+At position 287 to 320, the domain is characterized as WW 1.
+At position 319 to 352, the domain is characterized as WW 2.
+At position 439 to 472, the domain is characterized as WW 4.
+At position 530 to 864, the domain is characterized as HECT.
+At position 108 to 187, the domain is characterized as PDZ 1.
+At position 192 to 267, the domain is characterized as PDZ 2.
+At position 7 to 283, the domain is characterized as MIF4G.
+At position 228 to 415, the domain is characterized as B30.2/SPRY.
+At position 302 to 438, the domain is characterized as VWFA.
+At position 772 to 939, the domain is characterized as Helicase ATP-binding.
+At position 1226 to 1370, the domain is characterized as Helicase C-terminal.
+At position 1 to 79, the domain is characterized as Runt.
+At position 254 to 344, the domain is characterized as Ig-like C2-type.
+At position 611 to 946, the domain is characterized as Protein kinase.
+At position 159 to 306, the domain is characterized as Plastocyanin-like 2.
+At position 410 to 550, the domain is characterized as Plastocyanin-like 3.
+At position 1 to 197, the domain is characterized as N-acetyltransferase.
+At position 833 to 1016, the domain is characterized as DH.
+At position 1044 to 1146, the domain is characterized as PH.
+At position 261 to 535, the domain is characterized as Protein kinase.
+At position 760 to 923, the domain is characterized as JmjC.
+At position 226 to 344, the domain is characterized as Nop.
+At position 17 to 66, the domain is characterized as F-box.
+At position 195 to 272, the domain is characterized as Saposin B-type 2.
+At position 291 to 366, the domain is characterized as Saposin B-type 3.
+At position 36 to 123, the domain is characterized as Ig-like C2-type 1.
+At position 129 to 213, the domain is characterized as Ig-like C2-type 2.
+At position 235 to 315, the domain is characterized as Ig-like C2-type 3.
+At position 323 to 409, the domain is characterized as Ig-like C2-type 4.
+At position 474 to 571, the domain is characterized as Fibronectin type-III 1.
+At position 608 to 703, the domain is characterized as Fibronectin type-III 2.
+At position 712 to 812, the domain is characterized as Fibronectin type-III 3.
+At position 68 to 257, the domain is characterized as RNase H type-2.
+At position 275 to 358, the domain is characterized as RAMA.
+At position 214 to 331, the domain is characterized as CUB 1.
+At position 340 to 444, the domain is characterized as CUB 2.
+At position 451 to 488, the domain is characterized as LDL-receptor class A 1.
+At position 489 to 522, the domain is characterized as LDL-receptor class A 2.
+At position 523 to 561, the domain is characterized as LDL-receptor class A 3.
+At position 565 to 604, the domain is characterized as LDL-receptor class A 4.
+At position 420 to 508, the domain is characterized as Death.
+At position 1 to 120, the domain is characterized as Ig-like 1.
+At position 130 to 223, the domain is characterized as Ig-like 2.
+At position 232 to 329, the domain is characterized as Ig-like 3.
+At position 333 to 437, the domain is characterized as Ig-like 4.
+At position 443 to 542, the domain is characterized as Ig-like 5.
+At position 27 to 219, the domain is characterized as RNase H type-2.
+At position 42 to 110, the domain is characterized as KRAB.
+At position 126 to 241, the domain is characterized as C-type lectin.
+At position 1 to 36, the domain is characterized as MADS-box.
+At position 59 to 149, the domain is characterized as K-box.
+At position 1 to 46, the domain is characterized as ACB.
+At position 3 to 24, the domain is characterized as J.
+At position 413 to 501, the domain is characterized as Death.
+At position 546 to 659, the domain is characterized as Cryptic POLO box 1 (CPB1).
+At position 660 to 773, the domain is characterized as Cryptic POLO box 2 (CPB2).
+At position 840 to 918, the domain is characterized as POLO box.
+At position 671 to 779, the domain is characterized as RWD.
+At position 45 to 170, the domain is characterized as Nudix hydrolase.
+At position 41 to 162, the domain is characterized as FZ.
+At position 330 to 519, the domain is characterized as B30.2/SPRY.
+At position 65 to 259, the domain is characterized as Peptidase M12A.
+At position 263 to 432, the domain is characterized as MAM.
+At position 433 to 594, the domain is characterized as MATH.
+At position 671 to 711, the domain is characterized as EGF-like.
+At position 13 to 249, the domain is characterized as Protein kinase.
+At position 300 to 536, the domain is characterized as NR LBD.
+At position 58 to 128, the domain is characterized as Chitin-binding type R&R.
+At position 34 to 239, the domain is characterized as Helicase ATP-binding.
+At position 273 to 437, the domain is characterized as Helicase C-terminal.
+At position 59 to 143, the domain is characterized as RRM 1.
+At position 182 to 258, the domain is characterized as RRM 2.
+At position 358 to 432, the domain is characterized as RRM 3.
+At position 475 to 550, the domain is characterized as RRM 4.
+At position 197 to 275, the domain is characterized as RRM 2.
+At position 433 to 520, the domain is characterized as RRM 3; atypical.
+At position 179 to 489, the domain is characterized as Peptidase S8.
+At position 498 to 647, the domain is characterized as P/Homo B.
+At position 215 to 292, the domain is characterized as Kringle 2.
+At position 361 to 615, the domain is characterized as Peptidase S1.
+At position 183 to 334, the domain is characterized as Protein kinase.
+At position 417 to 751, the domain is characterized as HECT.
+At position 1 to 52, the domain is characterized as Pyrin.
+At position 282 to 484, the domain is characterized as VWFA.
+At position 37 to 130, the domain is characterized as CTCK.
+At position 511 to 622, the domain is characterized as SMC hinge.
+At position 207 to 286, the domain is characterized as Carrier.
+At position 66 to 208, the domain is characterized as SCP.
+At position 194 to 362, the domain is characterized as Helicase ATP-binding.
+At position 538 to 699, the domain is characterized as Helicase C-terminal.
+At position 4 to 142, the domain is characterized as SprT-like.
+At position 493 to 608, the domain is characterized as Toprim.
+At position 44 to 231, the domain is characterized as BPL/LPL catalytic.
+At position 4 to 42, the domain is characterized as SCP.
+At position 78 to 111, the domain is characterized as ShKT.
+At position 29 to 72, the domain is characterized as CHCH.
+At position 5 to 80, the domain is characterized as Carrier 1.
+At position 1076 to 1151, the domain is characterized as Carrier 2.
+At position 9 to 159, the domain is characterized as RWD.
+At position 57 to 116, the domain is characterized as TSP type-1 1.
+At position 120 to 192, the domain is characterized as TSP type-1 2.
+At position 194 to 247, the domain is characterized as TSP type-1 3.
+At position 360 to 416, the domain is characterized as TSP type-1 4.
+At position 423 to 510, the domain is characterized as TSP type-1 5.
+At position 512 to 574, the domain is characterized as TSP type-1 6.
+At position 634 to 695, the domain is characterized as TSP type-1 7.
+At position 696 to 769, the domain is characterized as TSP type-1 8.
+At position 771 to 831, the domain is characterized as TSP type-1 9.
+At position 832 to 904, the domain is characterized as TSP type-1 10.
+At position 906 to 959, the domain is characterized as TSP type-1 11.
+At position 960 to 1033, the domain is characterized as TSP type-1 12.
+At position 1035 to 1095, the domain is characterized as TSP type-1 13.
+At position 1096 to 1163, the domain is characterized as TSP type-1 14.
+At position 1166 to 1220, the domain is characterized as TSP type-1 15.
+At position 1221 to 1284, the domain is characterized as TSP type-1 16.
+At position 1286 to 1341, the domain is characterized as TSP type-1 17.
+At position 1342 to 1412, the domain is characterized as TSP type-1 18.
+At position 1414 to 1475, the domain is characterized as TSP type-1 19.
+At position 223 to 369, the domain is characterized as Exonuclease.
+At position 144 to 207, the domain is characterized as bZIP.
+At position 141 to 336, the domain is characterized as MAGE.
+At position 105 to 211, the domain is characterized as sHSP.
+At position 95 to 149, the domain is characterized as J.
+At position 90 to 165, the domain is characterized as S4 RNA-binding.
+At position 188 to 378, the domain is characterized as Glutamine amidotransferase type-1.
+At position 29 to 78, the domain is characterized as bHLH.
+At position 41 to 296, the domain is characterized as AB hydrolase-1.
+At position 26 to 285, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 160 to 347, the domain is characterized as CheB-type methylesterase.
+At position 10 to 172, the domain is characterized as Exonuclease.
+At position 14 to 196, the domain is characterized as HORMA.
+At position 153 to 243, the domain is characterized as BRCT.
+At position 250 to 489, the domain is characterized as START.
+At position 4 to 21, the domain is characterized as WH2 1.
+At position 102 to 166, the domain is characterized as J.
+At position 240 to 557, the domain is characterized as Protein kinase.
+At position 559 to 658, the domain is characterized as AGC-kinase C-terminal.
+At position 1182 to 1226, the domain is characterized as LEM.
+At position 257 to 509, the domain is characterized as Histidine kinase.
+At position 511 to 646, the domain is characterized as CheW-like.
+At position 323 to 583, the domain is characterized as NR LBD.
+At position 42 to 365, the domain is characterized as Alpha-carbonic anhydrase.
+At position 12 to 90, the domain is characterized as PAS.
+At position 287 to 484, the domain is characterized as ERCC4.
+At position 232 to 306, the domain is characterized as POU-specific.
+At position 117 to 148, the domain is characterized as EF-hand 4.
+At position 4 to 428, the domain is characterized as Helicase ATP-binding.
+At position 306 to 391, the domain is characterized as Fibronectin type-III 4.
+At position 393 to 470, the domain is characterized as Fibronectin type-III 5.
+At position 1427 to 1696, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 556 to 704, the domain is characterized as GST C-terminal.
+At position 1 to 87, the domain is characterized as PE.
+At position 58 to 209, the domain is characterized as Tyrosine-protein phosphatase.
+At position 435 to 452, the domain is characterized as WH2.
+At position 70 to 261, the domain is characterized as TR mART core.
+At position 625 to 737, the domain is characterized as FAD-binding FR-type.
+At position 158 to 362, the domain is characterized as CP-type G.
+At position 1 to 125, the domain is characterized as Barwin.
+At position 51 to 107, the domain is characterized as Sm.
+At position 35 to 222, the domain is characterized as BPL/LPL catalytic.
+At position 414 to 623, the domain is characterized as FtsK.
+At position 1757 to 2083, the domain is characterized as PIPK.
+At position 173 to 252, the domain is characterized as Ubiquitin-like.
+At position 310 to 369, the domain is characterized as HTH myb-type.
+At position 13 to 162, the domain is characterized as MPN.
+At position 38 to 241, the domain is characterized as Tyr recombinase.
+At position 205 to 288, the domain is characterized as Cytochrome c 2.
+At position 3 to 118, the domain is characterized as I-type lysozyme.
+At position 60 to 156, the domain is characterized as Rieske.
+At position 205 to 396, the domain is characterized as Peptidase M12B.
+At position 631 to 660, the domain is characterized as EGF-like.
+At position 421 to 601, the domain is characterized as Exonuclease.
+At position 30 to 197, the domain is characterized as PID.
+At position 627 to 721, the domain is characterized as Fe2OG dioxygenase.
+At position 148 to 239, the domain is characterized as TonB C-terminal.
+At position 651 to 892, the domain is characterized as ABC transporter.
+At position 961 to 1218, the domain is characterized as ABC transmembrane type-1 2.
+At position 408 to 486, the domain is characterized as Rhodanese.
+At position 18 to 196, the domain is characterized as Eph LBD.
+At position 318 to 426, the domain is characterized as Fibronectin type-III 1.
+At position 427 to 522, the domain is characterized as Fibronectin type-III 2.
+At position 609 to 872, the domain is characterized as Protein kinase.
+At position 901 to 965, the domain is characterized as SAM.
+At position 107 to 184, the domain is characterized as PRC barrel.
+At position 46 to 154, the domain is characterized as EamA.
+At position 26 to 153, the domain is characterized as Response regulatory.
+At position 96 to 469, the domain is characterized as GT44.
+At position 568 to 775, the domain is characterized as Peptidase C80.
+At position 66 to 215, the domain is characterized as Ferritin-like diiron.
+At position 186 to 528, the domain is characterized as SET.
+At position 410 to 458, the domain is characterized as G-patch.
+At position 212 to 533, the domain is characterized as USP.
+At position 121 to 247, the domain is characterized as G8.
+At position 320 to 436, the domain is characterized as C-type lectin.
+At position 17 to 205, the domain is characterized as ABC transmembrane type-1.
+At position 69 to 196, the domain is characterized as AB hydrolase-1.
+At position 35 to 322, the domain is characterized as GP-PDE.
+At position 23 to 64, the domain is characterized as Anaphylatoxin-like 1.
+At position 65 to 96, the domain is characterized as Anaphylatoxin-like 2.
+At position 97 to 129, the domain is characterized as Anaphylatoxin-like 3.
+At position 155 to 194, the domain is characterized as EGF-like 1.
+At position 195 to 280, the domain is characterized as EGF-like 2; calcium-binding.
+At position 281 to 344, the domain is characterized as EGF-like 3; calcium-binding.
+At position 343 to 389, the domain is characterized as EGF-like 4; calcium-binding.
+At position 390 to 429, the domain is characterized as EGF-like 5; calcium-binding.
+At position 430 to 473, the domain is characterized as EGF-like 6; calcium-binding.
+At position 474 to 514, the domain is characterized as EGF-like 7; calcium-binding.
+At position 515 to 559, the domain is characterized as EGF-like 8; calcium-binding.
+At position 560 to 610, the domain is characterized as EGF-like 9; calcium-binding.
+At position 33 to 695, the domain is characterized as PFL.
+At position 706 to 826, the domain is characterized as Glycine radical.
+At position 147 to 329, the domain is characterized as PID.
+At position 487 to 578, the domain is characterized as SH2.
+At position 477 to 574, the domain is characterized as PAZ.
+At position 747 to 1056, the domain is characterized as Piwi.
+At position 602 to 719, the domain is characterized as BAH.
+At position 758 to 1296, the domain is characterized as SAM-dependent MTase C5-type.
+At position 863 to 928, the domain is characterized as Chromo.
+At position 3 to 268, the domain is characterized as Pyruvate carboxyltransferase.
+At position 482 to 651, the domain is characterized as tr-type G.
+At position 74 to 210, the domain is characterized as RanBD1.
+At position 307 to 380, the domain is characterized as SPOR.
+At position 300 to 520, the domain is characterized as Rab-GAP TBC.
+At position 43 to 115, the domain is characterized as S4 RNA-binding.
+At position 36 to 117, the domain is characterized as IGFBP N-terminal.
+At position 34 to 152, the domain is characterized as sHSP.
+At position 29 to 139, the domain is characterized as Ig-like V-type 1.
+At position 145 to 238, the domain is characterized as Ig-like C2-type 1.
+At position 243 to 357, the domain is characterized as Ig-like V-type 2.
+At position 363 to 456, the domain is characterized as Ig-like C2-type 2.
+At position 62 to 97, the domain is characterized as Tify.
+At position 95 to 311, the domain is characterized as ABC transmembrane type-1.
+At position 11 to 63, the domain is characterized as bHLH 1.
+At position 162 to 219, the domain is characterized as bHLH 2.
+At position 614 to 713, the domain is characterized as tRNA-binding.
+At position 62 to 131, the domain is characterized as POTRA.
+At position 29 to 236, the domain is characterized as Obg.
+At position 237 to 414, the domain is characterized as OBG-type G.
+At position 294 to 377, the domain is characterized as Apple 4.
+At position 392 to 627, the domain is characterized as Peptidase S1.
+At position 111 to 296, the domain is characterized as ATP-grasp.
+At position 379 to 467, the domain is characterized as Death.
+At position 408 to 528, the domain is characterized as Ricin B-type lectin.
+At position 38 to 142, the domain is characterized as Gnk2-homologous 1.
+At position 151 to 261, the domain is characterized as Gnk2-homologous 2.
+At position 256 to 339, the domain is characterized as IPT/TIG.
+At position 30 to 328, the domain is characterized as F5/8 type A 1.
+At position 30 to 192, the domain is characterized as Plastocyanin-like 1.
+At position 202 to 328, the domain is characterized as Plastocyanin-like 2.
+At position 347 to 682, the domain is characterized as F5/8 type A 2.
+At position 347 to 524, the domain is characterized as Plastocyanin-like 3.
+At position 534 to 682, the domain is characterized as Plastocyanin-like 4.
+At position 1538 to 1866, the domain is characterized as F5/8 type A 3.
+At position 1538 to 1711, the domain is characterized as Plastocyanin-like 5.
+At position 1721 to 1866, the domain is characterized as Plastocyanin-like 6.
+At position 1866 to 2020, the domain is characterized as F5/8 type C 1.
+At position 2025 to 2180, the domain is characterized as F5/8 type C 2.
+At position 179 to 323, the domain is characterized as MOSC.
+At position 123 to 222, the domain is characterized as Ig-like C2-type 2.
+At position 312 to 394, the domain is characterized as Ig-like C2-type 4.
+At position 398 to 501, the domain is characterized as Ig-like C2-type 5.
+At position 40 to 96, the domain is characterized as Collagen-like.
+At position 97 to 314, the domain is characterized as Fibrinogen C-terminal.
+At position 9 to 473, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 474 to 782, the domain is characterized as UvrD-like helicase C-terminal.
+At position 15 to 65, the domain is characterized as bHLH.
+At position 88 to 160, the domain is characterized as PAS 1.
+At position 255 to 321, the domain is characterized as PAS 2.
+At position 31 to 273, the domain is characterized as ATP-grasp.
+At position 15 to 107, the domain is characterized as SH2 1.
+At position 168 to 259, the domain is characterized as SH2 2.
+At position 371 to 631, the domain is characterized as Protein kinase.
+At position 1 to 212, the domain is characterized as PPM-type phosphatase.
+At position 276 to 312, the domain is characterized as EGF-like 2.
+At position 314 to 353, the domain is characterized as EGF-like 3.
+At position 355 to 391, the domain is characterized as EGF-like 4.
+At position 393 to 429, the domain is characterized as EGF-like 5.
+At position 431 to 467, the domain is characterized as EGF-like 6.
+At position 381 to 447, the domain is characterized as TRAM.
+At position 75 to 256, the domain is characterized as tr-type G.
+At position 62 to 181, the domain is characterized as Response regulatory.
+At position 21 to 158, the domain is characterized as ADD.
+At position 58 to 316, the domain is characterized as Protein kinase.
+At position 5 to 271, the domain is characterized as Pyruvate carboxyltransferase.
+At position 282 to 652, the domain is characterized as GRAS.
+At position 388 to 445, the domain is characterized as TRAM.
+At position 239 to 269, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 285 to 320, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 606 to 634, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 635 to 664, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 629 to 721, the domain is characterized as Dicer dsRNA-binding fold.
+At position 894 to 1041, the domain is characterized as PAZ.
+At position 1276 to 1404, the domain is characterized as RNase III 1.
+At position 1667 to 1825, the domain is characterized as RNase III 2.
+At position 1853 to 1915, the domain is characterized as DRBM.
+At position 118 to 402, the domain is characterized as Protein kinase.
+At position 122 to 366, the domain is characterized as Radical SAM core.
+At position 2 to 166, the domain is characterized as PBS-linker.
+At position 198 to 248, the domain is characterized as CpcD-like.
+At position 117 to 160, the domain is characterized as RPE1 insert.
+At position 12 to 88, the domain is characterized as EthD.
+At position 165 to 417, the domain is characterized as SMP-LTD.
+At position 58 to 312, the domain is characterized as Chorismate mutase.
+At position 72 to 326, the domain is characterized as Protein kinase.
+At position 370 to 405, the domain is characterized as EF-hand 1.
+At position 442 to 477, the domain is characterized as EF-hand 3.
+At position 536 to 636, the domain is characterized as PH.
+At position 1175 to 1422, the domain is characterized as PPM-type phosphatase.
+At position 11 to 71, the domain is characterized as S5 DRBM.
+At position 961 to 1083, the domain is characterized as VRR-NUC.
+At position 358 to 631, the domain is characterized as Protein kinase.
+At position 107 to 154, the domain is characterized as LysM 1.
+At position 173 to 216, the domain is characterized as LysM 2.
+At position 305 to 409, the domain is characterized as HTH arsR-type.
+At position 9 to 230, the domain is characterized as ATP-grasp.
+At position 28 to 157, the domain is characterized as HTH marR-type.
+At position 54 to 97, the domain is characterized as CWF21.
+At position 111 to 197, the domain is characterized as PNT.
+At position 162 to 382, the domain is characterized as TRUD.
+At position 197 to 279, the domain is characterized as PPIase FKBP-type.
+At position 173 to 240, the domain is characterized as BTB 1.
+At position 338 to 414, the domain is characterized as BTB 2.
+At position 604 to 784, the domain is characterized as Lon proteolytic.
+At position 179 to 211, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 68 to 284, the domain is characterized as ABC transmembrane type-1.
+At position 24 to 89, the domain is characterized as HMA.
+At position 33 to 152, the domain is characterized as C-type lectin.
+At position 160 to 251, the domain is characterized as SUEL-type lectin.
+At position 255 to 346, the domain is characterized as PKD.
+At position 424 to 1125, the domain is characterized as REJ.
+At position 1280 to 1329, the domain is characterized as GPS.
+At position 1391 to 1508, the domain is characterized as PLAT.
+At position 37 to 128, the domain is characterized as Pyrin.
+At position 194 to 511, the domain is characterized as NACHT.
+At position 144 to 255, the domain is characterized as PINc.
+At position 267 to 328, the domain is characterized as TRAM.
+At position 721 to 814, the domain is characterized as BRCT 1.
+At position 867 to 965, the domain is characterized as BRCT 2.
+At position 158 to 725, the domain is characterized as TBDR beta-barrel.
+At position 87 to 166, the domain is characterized as PA.
+At position 284 to 326, the domain is characterized as CUE.
+At position 36 to 477, the domain is characterized as Hexokinase.
+At position 124 to 309, the domain is characterized as ATP-grasp.
+At position 168 to 246, the domain is characterized as Toprim.
+At position 59 to 232, the domain is characterized as Helicase ATP-binding.
+At position 256 to 411, the domain is characterized as Helicase C-terminal.
+At position 14 to 261, the domain is characterized as Pterin-binding.
+At position 81 to 335, the domain is characterized as Protein kinase.
+At position 154 to 301, the domain is characterized as Plastocyanin-like 2.
+At position 362 to 497, the domain is characterized as Plastocyanin-like 3.
+At position 422 to 583, the domain is characterized as Helicase C-terminal.
+At position 12 to 193, the domain is characterized as tr-type G.
+At position 23 to 139, the domain is characterized as CUB.
+At position 214 to 453, the domain is characterized as Peptidase S1.
+At position 130 to 186, the domain is characterized as v-SNARE coiled-coil homology.
+At position 277 to 362, the domain is characterized as PDZ 1.
+At position 871 to 943, the domain is characterized as PDZ 2.
+At position 120 to 152, the domain is characterized as EF-hand 4.
+At position 539 to 628, the domain is characterized as EH.
+At position 572 to 607, the domain is characterized as EF-hand.
+At position 19 to 166, the domain is characterized as Reelin.
+At position 109 to 199, the domain is characterized as K-box.
+At position 130 to 437, the domain is characterized as Protein kinase.
+At position 438 to 510, the domain is characterized as AGC-kinase C-terminal.
+At position 25 to 156, the domain is characterized as Nudix hydrolase.
+At position 363 to 598, the domain is characterized as NR LBD.
+At position 268 to 343, the domain is characterized as PUA.
+At position 21 to 168, the domain is characterized as UBC core.
+At position 172 to 214, the domain is characterized as UBA.
+At position 12 to 124, the domain is characterized as BTB.
+At position 380 to 796, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1283 to 1600, the domain is characterized as PKS/mFAS DH.
+At position 1654 to 1731, the domain is characterized as Carrier 1.
+At position 39 to 254, the domain is characterized as GB1/RHD3-type G.
+At position 98 to 193, the domain is characterized as BRICHOS.
+At position 334 to 615, the domain is characterized as Protein kinase.
+At position 699 to 983, the domain is characterized as Protein kinase.
+At position 45 to 114, the domain is characterized as EamA.
+At position 9 to 82, the domain is characterized as TFIIS N-terminal.
+At position 203 to 265, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 22 to 64, the domain is characterized as F-box.
+At position 146 to 332, the domain is characterized as Helicase ATP-binding.
+At position 388 to 459, the domain is characterized as TRAM.
+At position 2 to 100, the domain is characterized as PTS EIIA type-3.
+At position 425 to 462, the domain is characterized as EGF-like.
+At position 522 to 709, the domain is characterized as VWFA.
+At position 98 to 178, the domain is characterized as PRC barrel.
+At position 17 to 310, the domain is characterized as BAR.
+At position 101 to 413, the domain is characterized as IF rod.
+At position 199 to 257, the domain is characterized as TRAM.
+At position 38 to 622, the domain is characterized as Peptidase M2 1.
+At position 641 to 1220, the domain is characterized as Peptidase M2 2.
+At position 37 to 205, the domain is characterized as Helicase ATP-binding.
+At position 229 to 374, the domain is characterized as Helicase C-terminal.
+At position 535 to 615, the domain is characterized as HRDC.
+At position 312 to 372, the domain is characterized as Tudor 1.
+At position 541 to 600, the domain is characterized as Tudor 2.
+At position 762 to 821, the domain is characterized as Tudor 3.
+At position 990 to 1048, the domain is characterized as Tudor 4.
+At position 39 to 408, the domain is characterized as GH18.
+At position 50 to 446, the domain is characterized as Alpha-carbonic anhydrase.
+At position 200 to 389, the domain is characterized as Helicase ATP-binding.
+At position 400 to 560, the domain is characterized as Helicase C-terminal.
+At position 928 to 973, the domain is characterized as UBA.
+At position 56 to 354, the domain is characterized as ABC transmembrane type-1 1.
+At position 390 to 669, the domain is characterized as ABC transporter 1.
+At position 768 to 1055, the domain is characterized as ABC transmembrane type-1 2.
+At position 1122 to 1361, the domain is characterized as ABC transporter 2.
+At position 75 to 244, the domain is characterized as Helicase ATP-binding.
+At position 269 to 449, the domain is characterized as Helicase C-terminal.
+At position 38 to 73, the domain is characterized as QLQ.
+At position 108 to 152, the domain is characterized as WRC.
+At position 319 to 457, the domain is characterized as C-CAP/cofactor C-like.
+At position 45 to 282, the domain is characterized as HBM.
+At position 309 to 361, the domain is characterized as HAMP.
+At position 366 to 602, the domain is characterized as Methyl-accepting transducer.
+At position 10 to 177, the domain is characterized as TIR.
+At position 172 to 447, the domain is characterized as NB-ARC.
+At position 231 to 374, the domain is characterized as Helicase C-terminal.
+At position 157 to 199, the domain is characterized as CUE 1.
+At position 251 to 294, the domain is characterized as CUE 2.
+At position 509 to 677, the domain is characterized as Helicase ATP-binding.
+At position 858 to 1010, the domain is characterized as Helicase C-terminal.
+At position 559 to 610, the domain is characterized as GPS.
+At position 35 to 322, the domain is characterized as ABC transmembrane type-1 1.
+At position 357 to 593, the domain is characterized as ABC transporter 1.
+At position 683 to 970, the domain is characterized as ABC transmembrane type-1 2.
+At position 1005 to 1242, the domain is characterized as ABC transporter 2.
+At position 274 to 378, the domain is characterized as Cadherin 3.
+At position 379 to 483, the domain is characterized as Cadherin 4.
+At position 484 to 598, the domain is characterized as Cadherin 5.
+At position 601 to 713, the domain is characterized as Cadherin 6.
+At position 835 to 897, the domain is characterized as R3H.
+At position 475 to 546, the domain is characterized as PAS.
+At position 1 to 280, the domain is characterized as Transferrin-like 1.
+At position 290 to 621, the domain is characterized as Transferrin-like 2.
+At position 212 to 416, the domain is characterized as Helicase ATP-binding.
+At position 484 to 631, the domain is characterized as Helicase C-terminal.
+At position 1 to 264, the domain is characterized as CheR-type methyltransferase.
+At position 99 to 305, the domain is characterized as ABC transmembrane type-1.
+At position 312 to 390, the domain is characterized as UBX.
+At position 22 to 123, the domain is characterized as Fibronectin type-III 1.
+At position 126 to 228, the domain is characterized as Fibronectin type-III 2.
+At position 51 to 305, the domain is characterized as Protein kinase.
+At position 9 to 286, the domain is characterized as EndoU.
+At position 63 to 148, the domain is characterized as UPAR/Ly6.
+At position 59 to 188, the domain is characterized as C-type lectin.
+At position 268 to 546, the domain is characterized as Protein kinase.
+At position 70 to 100, the domain is characterized as KOW.
+At position 199 to 280, the domain is characterized as PDZ 2.
+At position 25 to 153, the domain is characterized as EamA 1.
+At position 195 to 319, the domain is characterized as EamA 2.
+At position 40 to 221, the domain is characterized as FAD-binding PCMH-type.
+At position 400 to 610, the domain is characterized as Rab-GAP TBC.
+At position 20 to 266, the domain is characterized as ABC transporter.
+At position 12 to 240, the domain is characterized as Sigma-54 factor interaction.
+At position 2 to 174, the domain is characterized as DHFR.
+At position 210 to 434, the domain is characterized as NR LBD.
+At position 67 to 116, the domain is characterized as FHA.
+At position 92 to 144, the domain is characterized as Chitin-binding type-2.
+At position 151 to 251, the domain is characterized as PH.
+At position 279 to 341, the domain is characterized as CBS 1.
+At position 364 to 426, the domain is characterized as CBS 2.
+At position 438 to 499, the domain is characterized as CBS 3.
+At position 517 to 574, the domain is characterized as CBS 4.
+At position 22 to 388, the domain is characterized as GH18.
+At position 417 to 466, the domain is characterized as Chitin-binding type-2.
+At position 274 to 437, the domain is characterized as Helicase C-terminal.
+At position 27 to 307, the domain is characterized as Protein kinase.
+At position 1 to 236, the domain is characterized as SMP-LTD.
+At position 30 to 105, the domain is characterized as IGFBP N-terminal.
+At position 91 to 149, the domain is characterized as Kazal-like.
+At position 151 to 255, the domain is characterized as Ig-like C2-type.
+At position 336 to 430, the domain is characterized as HD.
+At position 3 to 128, the domain is characterized as CMP/dCMP-type deaminase.
+At position 173 to 261, the domain is characterized as EH 1.
+At position 205 to 240, the domain is characterized as EF-hand 1.
+At position 453 to 542, the domain is characterized as EH 2.
+At position 486 to 521, the domain is characterized as EF-hand 2.
+At position 1449 to 1466, the domain is characterized as WH2.
+At position 540 to 575, the domain is characterized as EF-hand 1.
+At position 584 to 617, the domain is characterized as EF-hand 2.
+At position 886 to 1028, the domain is characterized as Peptidase S59.
+At position 67 to 178, the domain is characterized as PH.
+At position 231 to 244, the domain is characterized as CRIB.
+At position 680 to 935, the domain is characterized as Protein kinase.
+At position 182 to 329, the domain is characterized as Cupin type-1.
+At position 98 to 279, the domain is characterized as DH.
+At position 309 to 407, the domain is characterized as PH.
+At position 86 to 228, the domain is characterized as Tyrosine-protein phosphatase.
+At position 143 to 336, the domain is characterized as CheB-type methylesterase.
+At position 13 to 283, the domain is characterized as Protein kinase.
+At position 396 to 511, the domain is characterized as Guanylate cyclase.
+At position 925 to 999, the domain is characterized as TSP type-1 12.
+At position 1001 to 1126, the domain is characterized as TSP type-1 13.
+At position 1128 to 1182, the domain is characterized as TSP type-1 14.
+At position 1183 to 1246, the domain is characterized as TSP type-1 15.
+At position 1248 to 1303, the domain is characterized as TSP type-1 16.
+At position 1304 to 1369, the domain is characterized as TSP type-1 17.
+At position 1371 to 1432, the domain is characterized as TSP type-1 18.
+At position 28 to 102, the domain is characterized as PAH 1.
+At position 138 to 208, the domain is characterized as PAH 2.
+At position 243 to 319, the domain is characterized as PAH 3.
+At position 16 to 374, the domain is characterized as Kinesin motor.
+At position 622 to 711, the domain is characterized as BRCT.
+At position 8 to 166, the domain is characterized as PNPLA.
+At position 275 to 465, the domain is characterized as FtsK.
+At position 37 to 256, the domain is characterized as Peptidase C83.
+At position 147 to 175, the domain is characterized as IQ.
+At position 656 to 887, the domain is characterized as NR LBD.
+At position 34 to 145, the domain is characterized as CFEM.
+At position 62 to 374, the domain is characterized as Peptidase A1.
+At position 60 to 248, the domain is characterized as BPL/LPL catalytic.
+At position 497 to 690, the domain is characterized as DH.
+At position 707 to 865, the domain is characterized as PH.
+At position 892 to 1019, the domain is characterized as C2.
+At position 1053 to 1247, the domain is characterized as Rho-GAP.
+At position 16 to 161, the domain is characterized as Thioredoxin.
+At position 212 to 402, the domain is characterized as B30.2/SPRY.
+At position 12 to 71, the domain is characterized as CHORD 1.
+At position 159 to 218, the domain is characterized as CHORD 2.
+At position 218 to 570, the domain is characterized as TTL.
+At position 165 to 253, the domain is characterized as Ras-associating.
+At position 29 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 129 to 230, the domain is characterized as Fibronectin type-III 2.
+At position 55 to 247, the domain is characterized as tr-type G.
+At position 50 to 120, the domain is characterized as POTRA.
+At position 204 to 314, the domain is characterized as Ig-like C2-type 2.
+At position 315 to 371, the domain is characterized as Ig-like C2-type 3.
+At position 290 to 351, the domain is characterized as Mop.
+At position 537 to 599, the domain is characterized as R3H.
+At position 673 to 718, the domain is characterized as G-patch.
+At position 111 to 325, the domain is characterized as TLDc.
+At position 97 to 177, the domain is characterized as PDZ.
+At position 93 to 160, the domain is characterized as Histone-fold.
+At position 660 to 747, the domain is characterized as BRCT.
+At position 67 to 339, the domain is characterized as GH16.
+At position 21 to 290, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 286 to 536, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 251 to 294, the domain is characterized as STI1.
+At position 330 to 371, the domain is characterized as UBA 2.
+At position 2 to 83, the domain is characterized as MIT.
+At position 118 to 437, the domain is characterized as Calpain catalytic.
+At position 60 to 249, the domain is characterized as FAD-binding PCMH-type.
+At position 331 to 429, the domain is characterized as ERCC4.
+At position 20 to 278, the domain is characterized as Protein kinase.
+At position 198 to 320, the domain is characterized as N-terminal Ras-GEF.
+At position 353 to 597, the domain is characterized as Ras-GEF.
+At position 219 to 477, the domain is characterized as Protein kinase.
+At position 103 to 206, the domain is characterized as FAD-binding FR-type.
+At position 342 to 383, the domain is characterized as PAC.
+At position 125 to 296, the domain is characterized as JmjC.
+At position 37 to 91, the domain is characterized as TIL.
+At position 11 to 20, the domain is characterized as C-type lectin.
+At position 441 to 504, the domain is characterized as bZIP.
+At position 12 to 210, the domain is characterized as N-acetyltransferase.
+At position 130 to 315, the domain is characterized as tr-type G.
+At position 207 to 382, the domain is characterized as EngA-type G 2.
+At position 383 to 469, the domain is characterized as KH-like.
+At position 1 to 350, the domain is characterized as FH2.
+At position 3 to 143, the domain is characterized as HTH marR-type.
+At position 29 to 281, the domain is characterized as Protein kinase.
+At position 111 to 181, the domain is characterized as PAH 1.
+At position 252 to 322, the domain is characterized as PAH 2.
+At position 403 to 472, the domain is characterized as PAH 3.
+At position 8 to 162, the domain is characterized as N-acetyltransferase 1.
+At position 159 to 304, the domain is characterized as N-acetyltransferase 2.
+At position 88 to 130, the domain is characterized as SMB 2.
+At position 139 to 412, the domain is characterized as EndoU.
+At position 24 to 126, the domain is characterized as Rieske.
+At position 470 to 505, the domain is characterized as F-box.
+At position 55 to 222, the domain is characterized as Phosphatase tensin-type.
+At position 228 to 366, the domain is characterized as C2 tensin-type.
+At position 849 to 913, the domain is characterized as J.
+At position 173 to 445, the domain is characterized as ABC transporter 1.
+At position 523 to 735, the domain is characterized as ABC transmembrane type-2 1.
+At position 847 to 1099, the domain is characterized as ABC transporter 2.
+At position 1172 to 1386, the domain is characterized as ABC transmembrane type-2 2.
+At position 64 to 135, the domain is characterized as Chitin-binding type R&R.
+At position 126 to 376, the domain is characterized as Protein kinase.
+At position 199 to 326, the domain is characterized as DBB.
+At position 154 to 287, the domain is characterized as Thioredoxin 2.
+At position 108 to 275, the domain is characterized as Helicase ATP-binding.
+At position 506 to 669, the domain is characterized as Helicase C-terminal.
+At position 80 to 177, the domain is characterized as Toprim.
+At position 145 to 481, the domain is characterized as Protein kinase.
+At position 434 to 556, the domain is characterized as HD.
+At position 676 to 756, the domain is characterized as ACT 1.
+At position 784 to 861, the domain is characterized as ACT 2.
+At position 5 to 345, the domain is characterized as Kinesin motor.
+At position 11 to 61, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 21 to 99, the domain is characterized as MANSC.
+At position 341 to 427, the domain is characterized as PKD 1.
+At position 435 to 524, the domain is characterized as PKD 2.
+At position 530 to 620, the domain is characterized as PKD 3.
+At position 621 to 714, the domain is characterized as PKD 4.
+At position 720 to 811, the domain is characterized as PKD 5.
+At position 4 to 250, the domain is characterized as DHFR.
+At position 297 to 550, the domain is characterized as Glutamine amidotransferase type-1.
+At position 265 to 301, the domain is characterized as EGF-like 1.
+At position 304 to 341, the domain is characterized as EGF-like 2.
+At position 346 to 384, the domain is characterized as EGF-like 3.
+At position 386 to 423, the domain is characterized as EGF-like 4; calcium-binding.
+At position 425 to 461, the domain is characterized as EGF-like 5; calcium-binding.
+At position 462 to 498, the domain is characterized as EGF-like 6.
+At position 543 to 579, the domain is characterized as EGF-like 7.
+At position 609 to 644, the domain is characterized as EGF-like 8.
+At position 646 to 683, the domain is characterized as EGF-like 9; calcium-binding.
+At position 685 to 721, the domain is characterized as EGF-like 10; calcium-binding.
+At position 723 to 759, the domain is characterized as EGF-like 11; calcium-binding.
+At position 761 to 798, the domain is characterized as EGF-like 12; calcium-binding.
+At position 800 to 836, the domain is characterized as EGF-like 13; calcium-binding.
+At position 838 to 900, the domain is characterized as EGF-like 14.
+At position 902 to 938, the domain is characterized as EGF-like 15; calcium-binding.
+At position 940 to 976, the domain is characterized as EGF-like 16; calcium-binding.
+At position 978 to 1019, the domain is characterized as EGF-like 17.
+At position 1021 to 1203, the domain is characterized as Laminin G-like 1.
+At position 1205 to 1241, the domain is characterized as EGF-like 18.
+At position 1248 to 1483, the domain is characterized as Laminin G-like 2.
+At position 1479 to 1515, the domain is characterized as EGF-like 19.
+At position 1555 to 1757, the domain is characterized as Laminin G-like 3.
+At position 1758 to 1792, the domain is characterized as EGF-like 20.
+At position 1794 to 1830, the domain is characterized as EGF-like 21; calcium-binding.
+At position 1832 to 1868, the domain is characterized as EGF-like 22; calcium-binding.
+At position 1871 to 1909, the domain is characterized as EGF-like 23.
+At position 1912 to 1948, the domain is characterized as EGF-like 24.
+At position 1950 to 1987, the domain is characterized as EGF-like 25; calcium-binding.
+At position 1989 to 2027, the domain is characterized as EGF-like 26; calcium-binding.
+At position 2028 to 2068, the domain is characterized as EGF-like 27.
+At position 1900 to 1929, the domain is characterized as IQ.
+At position 302 to 578, the domain is characterized as Dynamin-type G.
+At position 37 to 148, the domain is characterized as AB hydrolase-1.
+At position 153 to 260, the domain is characterized as WGR.
+At position 250 to 370, the domain is characterized as PARP alpha-helical.
+At position 378 to 605, the domain is characterized as PARP catalytic.
+At position 3 to 211, the domain is characterized as DPCK.
+At position 28 to 124, the domain is characterized as Ig-like V-type 1.
+At position 335 to 647, the domain is characterized as Protein kinase.
+At position 648 to 730, the domain is characterized as AGC-kinase C-terminal.
+At position 303 to 356, the domain is characterized as HAMP 1.
+At position 423 to 476, the domain is characterized as HAMP 2.
+At position 495 to 731, the domain is characterized as Methyl-accepting transducer.
+At position 610 to 671, the domain is characterized as SH3.
+At position 683 to 819, the domain is characterized as PID.
+At position 1 to 47, the domain is characterized as EAL.
+At position 45 to 126, the domain is characterized as Kringle.
+At position 143 to 393, the domain is characterized as Peptidase S1.
+At position 26 to 216, the domain is characterized as GH16.
+At position 142 to 376, the domain is characterized as Radical SAM core.
+At position 12 to 125, the domain is characterized as Pru.
+At position 237 to 351, the domain is characterized as DEUBAD.
+At position 152 to 256, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 191, the domain is characterized as Guanylate kinase-like.
+At position 518 to 803, the domain is characterized as Protein kinase.
+At position 589 to 937, the domain is characterized as Protein kinase.
+At position 262 to 314, the domain is characterized as bHLH.
+At position 122 to 359, the domain is characterized as Histidine kinase.
+At position 694 to 779, the domain is characterized as SUEL-type lectin.
+At position 345 to 482, the domain is characterized as NYN.
+At position 1173 to 1248, the domain is characterized as HTH OST-type 4.
+At position 1409 to 1483, the domain is characterized as HTH OST-type 7.
+At position 1484 to 1558, the domain is characterized as HTH OST-type 8.
+At position 48 to 295, the domain is characterized as PPM-type phosphatase.
+At position 4 to 127, the domain is characterized as VOC.
+At position 29 to 166, the domain is characterized as Thioredoxin.
+At position 77 to 149, the domain is characterized as PUB.
+At position 271 to 326, the domain is characterized as Laminin EGF-like 1.
+At position 327 to 382, the domain is characterized as Laminin EGF-like 2.
+At position 383 to 429, the domain is characterized as Laminin EGF-like 3.
+At position 430 to 479, the domain is characterized as Laminin EGF-like 4.
+At position 480 to 489, the domain is characterized as Laminin EGF-like 5; first part.
+At position 499 to 672, the domain is characterized as Laminin IV type A.
+At position 673 to 706, the domain is characterized as Laminin EGF-like 5; second part.
+At position 707 to 754, the domain is characterized as Laminin EGF-like 6.
+At position 755 to 809, the domain is characterized as Laminin EGF-like 7.
+At position 810 to 865, the domain is characterized as Laminin EGF-like 8.
+At position 866 to 916, the domain is characterized as Laminin EGF-like 9.
+At position 917 to 964, the domain is characterized as Laminin EGF-like 10.
+At position 965 to 1013, the domain is characterized as Laminin EGF-like 11.
+At position 21 to 198, the domain is characterized as DHFR.
+At position 6 to 241, the domain is characterized as Glutamine amidotransferase type-1.
+At position 807 to 871, the domain is characterized as SAM.
+At position 70 to 224, the domain is characterized as Helicase ATP-binding.
+At position 363 to 524, the domain is characterized as Helicase C-terminal.
+At position 1 to 115, the domain is characterized as MGS-like.
+At position 487 to 698, the domain is characterized as Helicase C-terminal.
+At position 25 to 96, the domain is characterized as IGFBP N-terminal.
+At position 99 to 165, the domain is characterized as VWFC.
+At position 196 to 241, the domain is characterized as TSP type-1.
+At position 254 to 328, the domain is characterized as CTCK.
+At position 160 to 283, the domain is characterized as TFIIS central.
+At position 1 to 433, the domain is characterized as SMP-LTD.
+At position 54 to 111, the domain is characterized as FHA.
+At position 180 to 472, the domain is characterized as Protein kinase.
+At position 15 to 435, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 971 to 1254, the domain is characterized as PKS/mFAS DH.
+At position 2413 to 2505, the domain is characterized as Carrier.
+At position 45 to 330, the domain is characterized as Protein kinase.
+At position 149 to 291, the domain is characterized as Tyrosine-protein phosphatase.
+At position 32 to 128, the domain is characterized as Ig-like V-type.
+At position 135 to 238, the domain is characterized as Ig-like C2-type.
+At position 175 to 352, the domain is characterized as tr-type G.
+At position 1409 to 1450, the domain is characterized as Ig-like.
+At position 24 to 155, the domain is characterized as WIF.
+At position 343 to 606, the domain is characterized as Protein kinase.
+At position 313 to 348, the domain is characterized as DMA.
+At position 227 to 312, the domain is characterized as KH.
+At position 18 to 90, the domain is characterized as Chitin-binding type R&R.
+At position 774 to 938, the domain is characterized as Helicase C-terminal.
+At position 46 to 157, the domain is characterized as RGS.
+At position 105 to 337, the domain is characterized as Peptidase S1.
+At position 198 to 361, the domain is characterized as Hflx-type G.
+At position 61 to 207, the domain is characterized as Cupin type-1.
+At position 350 to 588, the domain is characterized as ABC transporter.
+At position 485 to 758, the domain is characterized as Protein kinase.
+At position 57 to 241, the domain is characterized as RNase H type-2.
+At position 590 to 635, the domain is characterized as AWS.
+At position 638 to 750, the domain is characterized as SET.
+At position 1100 to 1223, the domain is characterized as BAH.
+At position 51 to 123, the domain is characterized as Bromo 1.
+At position 326 to 398, the domain is characterized as Bromo 2.
+At position 562 to 644, the domain is characterized as NET.
+At position 1 to 41, the domain is characterized as UBA.
+At position 14 to 221, the domain is characterized as ABC transporter.
+At position 183 to 343, the domain is characterized as Helicase ATP-binding.
+At position 412 to 575, the domain is characterized as Helicase C-terminal.
+At position 30 to 192, the domain is characterized as Laminin G-like 1.
+At position 202 to 380, the domain is characterized as Laminin G-like 2.
+At position 320 to 494, the domain is characterized as PCI.
+At position 76 to 250, the domain is characterized as FAD-binding PCMH-type.
+At position 214 to 370, the domain is characterized as TrmE-type G.
+At position 42 to 333, the domain is characterized as FAE.
+At position 110 to 395, the domain is characterized as Protein kinase.
+At position 1 to 169, the domain is characterized as Miro 1.
+At position 305 to 340, the domain is characterized as EF-hand 2.
+At position 420 to 584, the domain is characterized as Miro 2.
+At position 29 to 211, the domain is characterized as CNNM transmembrane.
+At position 230 to 291, the domain is characterized as CBS 1.
+At position 295 to 359, the domain is characterized as CBS 2.
+At position 365 to 431, the domain is characterized as CBS 3.
+At position 100 to 514, the domain is characterized as Peptidase A1.
+At position 183 to 242, the domain is characterized as HTH myb-type.
+At position 15 to 83, the domain is characterized as J.
+At position 1 to 78, the domain is characterized as TFIIS N-terminal.
+At position 160 to 272, the domain is characterized as TFIIS central.
+At position 231 to 565, the domain is characterized as Protein kinase.
+At position 577 to 630, the domain is characterized as bHLH.
+At position 449 to 700, the domain is characterized as Protein kinase.
+At position 448 to 699, the domain is characterized as Protein kinase.
+At position 184 to 216, the domain is characterized as LRRCT.
+At position 181 to 282, the domain is characterized as PpiC 1.
+At position 292 to 390, the domain is characterized as PpiC 2.
+At position 603 to 686, the domain is characterized as BRCT.
+At position 30 to 143, the domain is characterized as LIM zinc-binding 2.
+At position 222 to 273, the domain is characterized as bHLH.
+At position 167 to 275, the domain is characterized as PET.
+At position 274 to 338, the domain is characterized as LIM zinc-binding 1.
+At position 339 to 399, the domain is characterized as LIM zinc-binding 2.
+At position 400 to 462, the domain is characterized as LIM zinc-binding 3.
+At position 362 to 531, the domain is characterized as tr-type G.
+At position 25 to 64, the domain is characterized as SMB.
+At position 282 to 430, the domain is characterized as AMOP.
+At position 442 to 636, the domain is characterized as VWFD.
+At position 720 to 777, the domain is characterized as Sushi.
+At position 94 to 384, the domain is characterized as Radical SAM core.
+At position 408 to 559, the domain is characterized as N-acetyltransferase.
+At position 45 to 87, the domain is characterized as GRAM.
+At position 140 to 211, the domain is characterized as UPAR/Ly6.
+At position 277 to 462, the domain is characterized as Rho-GAP.
+At position 18 to 316, the domain is characterized as Protein kinase.
+At position 691 to 927, the domain is characterized as DH.
+At position 323 to 418, the domain is characterized as SH2.
+At position 138 to 209, the domain is characterized as COMM.
+At position 97 to 264, the domain is characterized as Helicase ATP-binding.
+At position 275 to 451, the domain is characterized as Helicase C-terminal.
+At position 62 to 323, the domain is characterized as Dynamin-type G.
+At position 575 to 669, the domain is characterized as GED.
+At position 275 to 332, the domain is characterized as CBS 2.
+At position 356 to 415, the domain is characterized as CBS 3.
+At position 66 to 484, the domain is characterized as Protein kinase.
+At position 58 to 133, the domain is characterized as S1-like.
+At position 114 to 356, the domain is characterized as ABC transporter.
+At position 441 to 653, the domain is characterized as ABC transmembrane type-2.
+At position 32 to 307, the domain is characterized as Septin-type G.
+At position 1715 to 1750, the domain is characterized as EF-hand.
+At position 144 to 225, the domain is characterized as Ig-like C2-type 1.
+At position 232 to 319, the domain is characterized as Ig-like C2-type 2.
+At position 355 to 438, the domain is characterized as Ig-like C2-type 3.
+At position 441 to 533, the domain is characterized as Ig-like C2-type 4.
+At position 539 to 626, the domain is characterized as Ig-like C2-type 5.
+At position 631 to 730, the domain is characterized as Ig-like C2-type 6.
+At position 736 to 844, the domain is characterized as Fibronectin type-III 1.
+At position 849 to 961, the domain is characterized as Fibronectin type-III 2.
+At position 963 to 1057, the domain is characterized as Fibronectin type-III 3.
+At position 1064 to 1168, the domain is characterized as Fibronectin type-III 4.
+At position 4 to 396, the domain is characterized as SAM-dependent MTase C5-type.
+At position 98 to 152, the domain is characterized as MADS-box.
+At position 87 to 310, the domain is characterized as GB1/RHD3-type G.
+At position 74 to 227, the domain is characterized as Ferritin-like diiron.
+At position 91 to 763, the domain is characterized as Peptidase M13.
+At position 28 to 104, the domain is characterized as POTRA.
+At position 27 to 176, the domain is characterized as PI-PLC X-box.
+At position 379 to 545, the domain is characterized as N-acetyltransferase.
+At position 1615 to 1644, the domain is characterized as IQ.
+At position 4 to 147, the domain is characterized as BAH.
+At position 1 to 135, the domain is characterized as uDENN.
+At position 160 to 294, the domain is characterized as cDENN.
+At position 296 to 349, the domain is characterized as dDENN.
+At position 195 to 380, the domain is characterized as Glutamine amidotransferase type-1.
+At position 529 to 721, the domain is characterized as ATP-grasp 1.
+At position 1066 to 1257, the domain is characterized as ATP-grasp 2.
+At position 1322 to 1477, the domain is characterized as MGS-like.
+At position 427 to 616, the domain is characterized as SUN.
+At position 70 to 141, the domain is characterized as PUB.
+At position 558 to 609, the domain is characterized as UBA.
+At position 284 to 453, the domain is characterized as Guanylate kinase-like.
+At position 24 to 190, the domain is characterized as Reelin.
+At position 191 to 383, the domain is characterized as Spondin.
+At position 436 to 489, the domain is characterized as TSP type-1 1.
+At position 495 to 549, the domain is characterized as TSP type-1 2.
+At position 552 to 605, the domain is characterized as TSP type-1 3.
+At position 608 to 662, the domain is characterized as TSP type-1 4.
+At position 664 to 717, the domain is characterized as TSP type-1 5.
+At position 750 to 802, the domain is characterized as TSP type-1 6.
+At position 440 to 490, the domain is characterized as DHHC.
+At position 174 to 371, the domain is characterized as HD-GYP.
+At position 91 to 294, the domain is characterized as SMP-LTD.
+At position 366 to 449, the domain is characterized as PDZ.
+At position 23 to 66, the domain is characterized as Chitin-binding type-1 1.
+At position 125 to 167, the domain is characterized as Chitin-binding type-1 2.
+At position 517 to 560, the domain is characterized as KASH.
+At position 1067 to 1320, the domain is characterized as Glutamine amidotransferase type-1.
+At position 944 to 1263, the domain is characterized as PKS/mFAS DH.
+At position 2302 to 2379, the domain is characterized as Carrier.
+At position 23 to 61, the domain is characterized as Chitin-binding type-1.
+At position 69 to 158, the domain is characterized as Fibronectin type-III 1.
+At position 159 to 246, the domain is characterized as Fibronectin type-III 2.
+At position 247 to 336, the domain is characterized as Fibronectin type-III 3.
+At position 337 to 425, the domain is characterized as Fibronectin type-III 4.
+At position 429 to 518, the domain is characterized as Fibronectin type-III 5.
+At position 519 to 603, the domain is characterized as Fibronectin type-III 6.
+At position 671 to 930, the domain is characterized as Tyrosine-protein phosphatase.
+At position 6 to 365, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 84 to 273, the domain is characterized as B30.2/SPRY.
+At position 263 to 314, the domain is characterized as SOCS box.
+At position 24 to 125, the domain is characterized as SRCR 1.
+At position 138 to 239, the domain is characterized as SRCR 2.
+At position 244 to 346, the domain is characterized as SRCR 3.
+At position 497 to 768, the domain is characterized as Protein kinase.
+At position 92 to 131, the domain is characterized as DHHC.
+At position 364 to 402, the domain is characterized as UBA.
+At position 241 to 356, the domain is characterized as SET.
+At position 178 to 507, the domain is characterized as PDEase.
+At position 8 to 193, the domain is characterized as YEATS.
+At position 703 to 797, the domain is characterized as PH 1.
+At position 811 to 919, the domain is characterized as PH 2.
+At position 955 to 1110, the domain is characterized as MyTH4.
+At position 1121 to 1451, the domain is characterized as FERM.
+At position 1 to 47, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 98 to 180, the domain is characterized as Chromo 1.
+At position 190 to 249, the domain is characterized as Chromo 2.
+At position 285 to 471, the domain is characterized as Helicase ATP-binding.
+At position 599 to 760, the domain is characterized as Helicase C-terminal.
+At position 67 to 159, the domain is characterized as PPIase FKBP-type.
+At position 12 to 95, the domain is characterized as PB1.
+At position 253 to 522, the domain is characterized as Protein kinase.
+At position 524 to 595, the domain is characterized as AGC-kinase C-terminal.
+At position 90 to 185, the domain is characterized as POU-specific atypical.
+At position 296 to 732, the domain is characterized as FH2.
+At position 28 to 114, the domain is characterized as Sm.
+At position 60 to 366, the domain is characterized as Protein kinase.
+At position 89 to 344, the domain is characterized as GS catalytic.
+At position 18 to 166, the domain is characterized as MRH.
+At position 1 to 190, the domain is characterized as AMMECR1.
+At position 153 to 180, the domain is characterized as PLD phosphodiesterase.
+At position 264 to 309, the domain is characterized as F-box.
+At position 157 to 220, the domain is characterized as bZIP.
+At position 567 to 877, the domain is characterized as Protein kinase.
+At position 44 to 125, the domain is characterized as SCAN box.
+At position 420 to 599, the domain is characterized as Helicase C-terminal.
+At position 321 to 393, the domain is characterized as HSA.
+At position 683 to 848, the domain is characterized as Helicase ATP-binding.
+At position 1221 to 1371, the domain is characterized as Helicase C-terminal.
+At position 306 to 357, the domain is characterized as Collagen-like.
+At position 270 to 329, the domain is characterized as CBS 2.
+At position 371 to 406, the domain is characterized as EF-hand 2.
+At position 407 to 442, the domain is characterized as EF-hand 3.
+At position 443 to 476, the domain is characterized as EF-hand 4.
+At position 661 to 722, the domain is characterized as Dockerin.
+At position 484 to 569, the domain is characterized as Fibronectin type-III 1.
+At position 579 to 667, the domain is characterized as Fibronectin type-III 2.
+At position 677 to 765, the domain is characterized as Fibronectin type-III 3.
+At position 763 to 872, the domain is characterized as CBM2.
+At position 241 to 409, the domain is characterized as PCI.
+At position 47 to 146, the domain is characterized as Cytochrome b5 heme-binding.
+At position 7 to 95, the domain is characterized as ASCH.
+At position 23 to 120, the domain is characterized as Ig-like.
+At position 18 to 278, the domain is characterized as Peptidase A1.
+At position 130 to 224, the domain is characterized as Olduvai 1.
+At position 401 to 493, the domain is characterized as Olduvai 2.
+At position 494 to 582, the domain is characterized as Olduvai 3.
+At position 585 to 640, the domain is characterized as Olduvai 4.
+At position 641 to 732, the domain is characterized as Olduvai 5.
+At position 735 to 808, the domain is characterized as Olduvai 6.
+At position 809 to 869, the domain is characterized as Olduvai 7.
+At position 1 to 82, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 16 to 233, the domain is characterized as Glutamine amidotransferase type-1.
+At position 31 to 322, the domain is characterized as ABC transmembrane type-1.
+At position 354 to 590, the domain is characterized as ABC transporter.
+At position 49 to 114, the domain is characterized as J.
+At position 12 to 87, the domain is characterized as PDZ.
+At position 80 to 200, the domain is characterized as SCP.
+At position 1 to 161, the domain is characterized as Peptidase S1.
+At position 6 to 199, the domain is characterized as ABC transporter 1.
+At position 299 to 487, the domain is characterized as ABC transporter 2.
+At position 267 to 328, the domain is characterized as SH3 3.
+At position 315 to 634, the domain is characterized as Protein kinase.
+At position 635 to 714, the domain is characterized as AGC-kinase C-terminal.
+At position 61 to 170, the domain is characterized as sHSP.
+At position 61 to 171, the domain is characterized as THUMP.
+At position 50 to 113, the domain is characterized as bZIP.
+At position 89 to 420, the domain is characterized as USP.
+At position 459 to 553, the domain is characterized as DUSP 1.
+At position 568 to 691, the domain is characterized as DUSP 2.
+At position 710 to 841, the domain is characterized as DUSP 3.
+At position 946 to 1026, the domain is characterized as Ubiquitin-like.
+At position 705 to 1010, the domain is characterized as Protein kinase.
+At position 1011 to 1090, the domain is characterized as AGC-kinase C-terminal.
+At position 19 to 111, the domain is characterized as GS beta-grasp.
+At position 178 to 325, the domain is characterized as DAGKc.
+At position 163 to 724, the domain is characterized as RINT1/TIP20.
+At position 10 to 190, the domain is characterized as Ku.
+At position 141 to 373, the domain is characterized as Radical SAM core.
+At position 98 to 275, the domain is characterized as VWFA.
+At position 405 to 468, the domain is characterized as bZIP.
+At position 47 to 193, the domain is characterized as Protein kinase.
+At position 14 to 77, the domain is characterized as bZIP.
+At position 656 to 858, the domain is characterized as MRH.
+At position 1 to 137, the domain is characterized as N-acetyltransferase.
+At position 26 to 140, the domain is characterized as Bulb-type lectin 1.
+At position 143 to 260, the domain is characterized as Bulb-type lectin 2.
+At position 264 to 301, the domain is characterized as EGF-like.
+At position 317 to 399, the domain is characterized as Apple.
+At position 484 to 759, the domain is characterized as Protein kinase.
+At position 185 to 379, the domain is characterized as Glutamine amidotransferase type-1.
+At position 27 to 168, the domain is characterized as SIS.
+At position 290 to 334, the domain is characterized as CHCH.
+At position 715 to 849, the domain is characterized as BAH 1.
+At position 916 to 1033, the domain is characterized as BAH 2.
+At position 1078 to 1512, the domain is characterized as SAM-dependent MTase C5-type.
+At position 222 to 580, the domain is characterized as TTL.
+At position 394 to 554, the domain is characterized as Cupin type-1 2.
+At position 31 to 101, the domain is characterized as Bromo 1.
+At position 229 to 299, the domain is characterized as Bromo 2.
+At position 351 to 469, the domain is characterized as BAH.
+At position 58 to 176, the domain is characterized as OmpA-like.
+At position 194 to 459, the domain is characterized as NPH3.
+At position 346 to 554, the domain is characterized as MCM.
+At position 279 to 577, the domain is characterized as FERM.
+At position 378 to 474, the domain is characterized as PH.
+At position 180 to 264, the domain is characterized as RCK C-terminal 1.
+At position 265 to 349, the domain is characterized as RCK C-terminal 2.
+At position 12 to 695, the domain is characterized as Myosin motor.
+At position 698 to 727, the domain is characterized as IQ 1.
+At position 721 to 750, the domain is characterized as IQ 2.
+At position 849 to 1024, the domain is characterized as TH1.
+At position 495 to 617, the domain is characterized as HD.
+At position 734 to 813, the domain is characterized as ACT 1.
+At position 845 to 924, the domain is characterized as ACT 2.
+At position 59 to 363, the domain is characterized as AB hydrolase-1.
+At position 131 to 207, the domain is characterized as Ubiquitin-like.
+At position 338 to 367, the domain is characterized as IQ.
+At position 108 to 180, the domain is characterized as S4 RNA-binding.
+At position 148 to 248, the domain is characterized as Fibronectin type-III.
+At position 67 to 274, the domain is characterized as Radical SAM core.
+At position 85 to 283, the domain is characterized as Laminin G-like.
+At position 89 to 180, the domain is characterized as HIG1.
+At position 247 to 481, the domain is characterized as Helicase C-terminal.
+At position 310 to 345, the domain is characterized as EF-hand 2.
+At position 340 to 402, the domain is characterized as LIM zinc-binding 2.
+At position 923 to 989, the domain is characterized as BTB.
+At position 21 to 117, the domain is characterized as UPAR/Ly6.
+At position 388 to 448, the domain is characterized as LIM zinc-binding.
+At position 589 to 691, the domain is characterized as tRNA-binding.
+At position 172 to 368, the domain is characterized as CheB-type methylesterase.
+At position 15 to 480, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 497 to 791, the domain is characterized as UvrD-like helicase C-terminal.
+At position 125 to 415, the domain is characterized as ABC transmembrane type-1.
+At position 466 to 585, the domain is characterized as Ricin B-type lectin.
+At position 622 to 1048, the domain is characterized as Protein kinase.
+At position 759 to 837, the domain is characterized as DEP.
+At position 26 to 245, the domain is characterized as Radical SAM core.
+At position 761 to 1058, the domain is characterized as Protein kinase.
+At position 597 to 758, the domain is characterized as Helicase ATP-binding.
+At position 774 to 933, the domain is characterized as Helicase C-terminal.
+At position 3 to 250, the domain is characterized as Radical SAM core.
+At position 42 to 245, the domain is characterized as AIG1-type G.
+At position 1 to 62, the domain is characterized as Protein kinase.
+At position 494 to 636, the domain is characterized as PTS EIIA type-2.
+At position 505 to 714, the domain is characterized as Lon N-terminal.
+At position 12 to 82, the domain is characterized as S1 motif.
+At position 326 to 456, the domain is characterized as VWFA.
+At position 1 to 296, the domain is characterized as Protein kinase.
+At position 496 to 656, the domain is characterized as PID.
+At position 148 to 246, the domain is characterized as HTH araC/xylS-type.
+At position 22 to 114, the domain is characterized as Lipoyl-binding.
+At position 231 to 378, the domain is characterized as Helicase C-terminal.
+At position 393 to 447, the domain is characterized as FF 1.
+At position 460 to 514, the domain is characterized as FF 2.
+At position 527 to 587, the domain is characterized as FF 3.
+At position 607 to 667, the domain is characterized as FF 4.
+At position 672 to 727, the domain is characterized as FF 5.
+At position 742 to 799, the domain is characterized as FF 6.
+At position 378 to 579, the domain is characterized as MIF4G.
+At position 22 to 252, the domain is characterized as Radical SAM core.
+At position 58 to 185, the domain is characterized as TBDR plug.
+At position 193 to 993, the domain is characterized as TBDR beta-barrel.
+At position 177 to 373, the domain is characterized as Peptidase M12B.
+At position 379 to 466, the domain is characterized as Disintegrin.
+At position 620 to 652, the domain is characterized as EGF-like.
+At position 227 to 330, the domain is characterized as RCSD.
+At position 24 to 222, the domain is characterized as Pentraxin (PTX).
+At position 677 to 753, the domain is characterized as RRM.
+At position 11 to 277, the domain is characterized as Protein kinase.
+At position 379 to 445, the domain is characterized as PASTA 1.
+At position 446 to 511, the domain is characterized as PASTA 2.
+At position 512 to 580, the domain is characterized as PASTA 3.
+At position 581 to 649, the domain is characterized as PASTA 4.
+At position 225 to 275, the domain is characterized as BPTI/Kunitz inhibitor 3.
+At position 28 to 712, the domain is characterized as Myosin motor.
+At position 715 to 744, the domain is characterized as IQ 1.
+At position 738 to 767, the domain is characterized as IQ 2.
+At position 866 to 1040, the domain is characterized as TH1.
+At position 660 to 880, the domain is characterized as Histidine kinase.
+At position 14 to 119, the domain is characterized as Calponin-homology (CH).
+At position 472 to 799, the domain is characterized as Kinesin motor.
+At position 807 to 1083, the domain is characterized as Protein kinase.
+At position 255 to 331, the domain is characterized as Ig-like C2-type 3.
+At position 339 to 394, the domain is characterized as MIR 1.
+At position 407 to 463, the domain is characterized as MIR 2.
+At position 471 to 529, the domain is characterized as MIR 3.
+At position 495 to 655, the domain is characterized as PID.
+At position 73 to 117, the domain is characterized as CHCH.
+At position 139 to 223, the domain is characterized as Ig-like C2-type 1.
+At position 230 to 323, the domain is characterized as Ig-like C2-type 2.
+At position 109 to 387, the domain is characterized as SET.
+At position 289 to 436, the domain is characterized as SIS 1.
+At position 470 to 611, the domain is characterized as SIS 2.
+At position 30 to 56, the domain is characterized as Antistasin-like.
+At position 272 to 347, the domain is characterized as B5.
+At position 812 to 1006, the domain is characterized as TH1.
+At position 35 to 590, the domain is characterized as PLA2c.
+At position 2 to 158, the domain is characterized as Obg.
+At position 159 to 326, the domain is characterized as OBG-type G.
+At position 10 to 248, the domain is characterized as HORMA.
+At position 1 to 245, the domain is characterized as Pyruvate carboxyltransferase.
+At position 23 to 115, the domain is characterized as Fibronectin type-III 1.
+At position 117 to 211, the domain is characterized as Fibronectin type-III 2.
+At position 213 to 304, the domain is characterized as Fibronectin type-III 3.
+At position 305 to 403, the domain is characterized as Fibronectin type-III 4.
+At position 408 to 502, the domain is characterized as Fibronectin type-III 5.
+At position 95 to 273, the domain is characterized as PXA.
+At position 538 to 668, the domain is characterized as PX.
+At position 102 to 167, the domain is characterized as MaoC-like.
+At position 99 to 172, the domain is characterized as RRM.
+At position 488 to 554, the domain is characterized as HMA 6.
+At position 564 to 630, the domain is characterized as HMA 7.
+At position 2 to 76, the domain is characterized as REM-1 1.
+At position 106 to 183, the domain is characterized as REM-1 2.
+At position 189 to 311, the domain is characterized as C2.
+At position 770 to 1029, the domain is characterized as Protein kinase.
+At position 1030 to 1097, the domain is characterized as AGC-kinase C-terminal.
+At position 216 to 302, the domain is characterized as PDZ 1.
+At position 355 to 440, the domain is characterized as PDZ 2.
+At position 1112 to 1197, the domain is characterized as PDZ 3.
+At position 1234 to 1319, the domain is characterized as PDZ 4.
+At position 14 to 83, the domain is characterized as Ubiquitin-like.
+At position 77 to 113, the domain is characterized as EF-hand 3.
+At position 123 to 288, the domain is characterized as PX.
+At position 309 to 400, the domain is characterized as PKD 1.
+At position 408 to 497, the domain is characterized as PKD 2.
+At position 503 to 593, the domain is characterized as PKD 3.
+At position 599 to 687, the domain is characterized as PKD 4.
+At position 693 to 784, the domain is characterized as PKD 5.
+At position 7 to 124, the domain is characterized as DMAP1-binding.
+At position 52 to 116, the domain is characterized as SH3.
+At position 144 to 412, the domain is characterized as Protein kinase.
+At position 2 to 243, the domain is characterized as Deacetylase sirtuin-type.
+At position 140 to 336, the domain is characterized as B30.2/SPRY.
+At position 693 to 1029, the domain is characterized as Protein kinase; inactive.
+At position 271 to 452, the domain is characterized as Helicase ATP-binding.
+At position 487 to 641, the domain is characterized as Helicase C-terminal.
+At position 281 to 347, the domain is characterized as TGS.
+At position 173 to 265, the domain is characterized as Methyl-accepting transducer.
+At position 889 to 936, the domain is characterized as F-box.
+At position 12 to 61, the domain is characterized as Myosin N-terminal SH3-like.
+At position 67 to 737, the domain is characterized as Myosin motor.
+At position 763 to 792, the domain is characterized as IQ 1.
+At position 811 to 840, the domain is characterized as IQ 3.
+At position 859 to 888, the domain is characterized as IQ 5.
+At position 1164 to 1456, the domain is characterized as Dilute.
+At position 28 to 111, the domain is characterized as KRAB.
+At position 7 to 162, the domain is characterized as DHFR.
+At position 39 to 104, the domain is characterized as Inhibitor I9.
+At position 112 to 384, the domain is characterized as Peptidase S8.
+At position 12 to 410, the domain is characterized as Helicase ATP-binding.
+At position 1 to 214, the domain is characterized as Peptidase S1.
+At position 1 to 68, the domain is characterized as Rho RNA-BD.
+At position 428 to 592, the domain is characterized as Helicase ATP-binding.
+At position 617 to 790, the domain is characterized as Helicase C-terminal.
+At position 252 to 450, the domain is characterized as GATase cobBQ-type.
+At position 108 to 295, the domain is characterized as ATP-grasp.
+At position 1 to 335, the domain is characterized as Myosin motor.
+At position 355 to 384, the domain is characterized as IQ.
+At position 492 to 643, the domain is characterized as MyTH4.
+At position 1422 to 1483, the domain is characterized as SH3.
+At position 119 to 152, the domain is characterized as EF-hand 1.
+At position 149 to 184, the domain is characterized as EF-hand 2.
+At position 185 to 213, the domain is characterized as EF-hand 3.
+At position 214 to 248, the domain is characterized as EF-hand 4.
+At position 163 to 307, the domain is characterized as PI-PLC X-box.
+At position 386 to 502, the domain is characterized as PI-PLC Y-box.
+At position 502 to 627, the domain is characterized as C2.
+At position 186 to 288, the domain is characterized as PpiC 1.
+At position 345 to 624, the domain is characterized as ABC transporter 1.
+At position 644 to 972, the domain is characterized as ABC transporter 2.
+At position 29 to 102, the domain is characterized as TB.
+At position 93 to 116, the domain is characterized as Follistatin-like 1.
+At position 99 to 165, the domain is characterized as Kazal-like 1.
+At position 166 to 189, the domain is characterized as Follistatin-like 2.
+At position 185 to 240, the domain is characterized as Kazal-like 2.
+At position 243 to 267, the domain is characterized as Follistatin-like 3.
+At position 263 to 317, the domain is characterized as Kazal-like 3.
+At position 694 to 785, the domain is characterized as FDX-ACB.
+At position 36 to 260, the domain is characterized as Peptidase S1.
+At position 71 to 362, the domain is characterized as ABC transmembrane type-1.
+At position 194 to 557, the domain is characterized as Peptidase S53.
+At position 90 to 166, the domain is characterized as Lipoyl-binding 1.
+At position 217 to 293, the domain is characterized as Lipoyl-binding 2.
+At position 351 to 388, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 9 to 192, the domain is characterized as CNNM transmembrane.
+At position 211 to 275, the domain is characterized as CBS 1.
+At position 276 to 319, the domain is characterized as CBS 2.
+At position 326 to 386, the domain is characterized as CBS 3.
+At position 491 to 567, the domain is characterized as Ig-like C2-type 6.
+At position 572 to 651, the domain is characterized as Ig-like C2-type 7.
+At position 665 to 738, the domain is characterized as Ig-like C2-type 8.
+At position 745 to 828, the domain is characterized as Ig-like C2-type 9.
+At position 363 to 556, the domain is characterized as FtsK.
+At position 173 to 446, the domain is characterized as ABC transporter 1.
+At position 524 to 737, the domain is characterized as ABC transmembrane type-2 1.
+At position 896 to 1167, the domain is characterized as Tyrosine-protein phosphatase.
+At position 355 to 596, the domain is characterized as Peptidase S1.
+At position 51 to 251, the domain is characterized as Cupin type-1 1.
+At position 7 to 52, the domain is characterized as WRC.
+At position 601 to 881, the domain is characterized as JmjC.
+At position 100 to 250, the domain is characterized as Flavodoxin-like.
+At position 302 to 549, the domain is characterized as FAD-binding FR-type.
+At position 83 to 373, the domain is characterized as Radical SAM core.
+At position 397 to 548, the domain is characterized as N-acetyltransferase.
+At position 158 to 221, the domain is characterized as SANT.
+At position 26 to 155, the domain is characterized as N-terminal Ras-GEF.
+At position 353 to 582, the domain is characterized as Ras-GEF.
+At position 940 to 1006, the domain is characterized as GRAM.
+At position 121 to 203, the domain is characterized as RWP-RK.
+At position 134 to 218, the domain is characterized as PilZ.
+At position 8 to 81, the domain is characterized as Pyrin.
+At position 37 to 250, the domain is characterized as Cupin type-1 1.
+At position 391 to 537, the domain is characterized as Cupin type-1 2.
+At position 6 to 98, the domain is characterized as HTH La-type RNA-binding.
+At position 110 to 202, the domain is characterized as RRM.
+At position 226 to 348, the domain is characterized as xRRM.
+At position 221 to 445, the domain is characterized as Rab-GAP TBC.
+At position 22 to 247, the domain is characterized as Phosphagen kinase C-terminal.
+At position 242 to 314, the domain is characterized as RRM.
+At position 227 to 280, the domain is characterized as HAMP.
+At position 320 to 451, the domain is characterized as Guanylate cyclase.
+At position 389 to 488, the domain is characterized as Zinc-hook.
+At position 141 to 217, the domain is characterized as Laminin G-like.
+At position 487 to 542, the domain is characterized as Collagen-like 1.
+At position 552 to 611, the domain is characterized as Collagen-like 2.
+At position 660 to 719, the domain is characterized as Collagen-like 3.
+At position 741 to 797, the domain is characterized as Collagen-like 4.
+At position 798 to 857, the domain is characterized as Collagen-like 5.
+At position 858 to 887, the domain is characterized as Collagen-like 6.
+At position 888 to 947, the domain is characterized as Collagen-like 7.
+At position 948 to 1007, the domain is characterized as Collagen-like 8.
+At position 1011 to 1052, the domain is characterized as Collagen-like 9.
+At position 1053 to 1112, the domain is characterized as Collagen-like 10.
+At position 1116 to 1170, the domain is characterized as Collagen-like 11.
+At position 1172 to 1196, the domain is characterized as Collagen-like 12.
+At position 1201 to 1249, the domain is characterized as Collagen-like 13.
+At position 1252 to 1306, the domain is characterized as Collagen-like 14.
+At position 1309 to 1353, the domain is characterized as Collagen-like 15.
+At position 1354 to 1413, the domain is characterized as Collagen-like 16.
+At position 1420 to 1479, the domain is characterized as Collagen-like 17.
+At position 1515 to 1714, the domain is characterized as Fibrillar collagen NC1.
+At position 16 to 48, the domain is characterized as LDL-receptor class A.
+At position 1 to 196, the domain is characterized as Tyr recombinase.
+At position 398 to 458, the domain is characterized as TRAM.
+At position 149 to 208, the domain is characterized as CHORD 2.
+At position 215 to 304, the domain is characterized as CS.
+At position 202 to 414, the domain is characterized as CN hydrolase.
+At position 1082 to 1165, the domain is characterized as CARD.
+At position 265 to 348, the domain is characterized as ACT.
+At position 62 to 130, the domain is characterized as POTRA.
+At position 237 to 289, the domain is characterized as PAC.
+At position 324 to 547, the domain is characterized as Histidine kinase.
+At position 928 to 1048, the domain is characterized as Response regulatory.
+At position 221 to 489, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 30 to 271, the domain is characterized as Peptidase S1.
+At position 620 to 797, the domain is characterized as Reverse transcriptase.
+At position 893 to 1011, the domain is characterized as RNase H Ty3/gyspy-type.
+At position 1159 to 1324, the domain is characterized as Integrase catalytic.
+At position 55 to 297, the domain is characterized as Peptidase S6.
+At position 1039 to 1305, the domain is characterized as Autotransporter.
+At position 27 to 117, the domain is characterized as BRCT.
+At position 356 to 422, the domain is characterized as RhoBD.
+At position 1 to 107, the domain is characterized as PCI.
+At position 18 to 83, the domain is characterized as LCN-type CS-alpha/beta.
+At position 332 to 568, the domain is characterized as ABC transporter.
+At position 111 to 409, the domain is characterized as PPM-type phosphatase.
+At position 265 to 409, the domain is characterized as Flavodoxin-like.
+At position 28 to 109, the domain is characterized as EMI.
+At position 108 to 140, the domain is characterized as EGF-like 1.
+At position 142 to 182, the domain is characterized as EGF-like 2; calcium-binding.
+At position 6 to 272, the domain is characterized as F-BAR.
+At position 515 to 575, the domain is characterized as SH3 1.
+At position 584 to 642, the domain is characterized as SH3 2.
+At position 54 to 105, the domain is characterized as bHLH.
+At position 193 to 278, the domain is characterized as KH type-2.
+At position 24 to 124, the domain is characterized as Ig-like C2-type 1.
+At position 150 to 238, the domain is characterized as Ig-like C2-type 2.
+At position 466 to 755, the domain is characterized as Protein kinase.
+At position 585 to 866, the domain is characterized as Protein kinase.
+At position 116 to 411, the domain is characterized as Septin-type G.
+At position 73 to 277, the domain is characterized as SMP-LTD.
+At position 79 to 155, the domain is characterized as ZAD.
+At position 435 to 538, the domain is characterized as RWD.
+At position 221 to 258, the domain is characterized as EGF-like 6; incomplete.
+At position 1375 to 1412, the domain is characterized as EGF-like 35.
+At position 580 to 664, the domain is characterized as Ig-like C2-type.
+At position 394 to 562, the domain is characterized as Helicase ATP-binding.
+At position 627 to 781, the domain is characterized as Helicase C-terminal.
+At position 112 to 356, the domain is characterized as GS catalytic.
+At position 306 to 470, the domain is characterized as Hflx-type G.
+At position 1 to 249, the domain is characterized as Pyruvate carboxyltransferase.
+At position 584 to 685, the domain is characterized as tRNA-binding.
+At position 2 to 177, the domain is characterized as N-acetyltransferase.
+At position 24 to 128, the domain is characterized as Fibronectin type-III 1.
+At position 132 to 227, the domain is characterized as Fibronectin type-III 2.
+At position 236 to 322, the domain is characterized as Ig-like 1.
+At position 328 to 426, the domain is characterized as Fibronectin type-III 3.
+At position 531 to 631, the domain is characterized as Fibronectin type-III 4.
+At position 636 to 736, the domain is characterized as Fibronectin type-III 5.
+At position 737 to 846, the domain is characterized as Fibronectin type-III 6.
+At position 841 to 948, the domain is characterized as Ig-like 2.
+At position 955 to 1050, the domain is characterized as Fibronectin type-III 7.
+At position 1148 to 1234, the domain is characterized as Fibronectin type-III 8.
+At position 1236 to 1343, the domain is characterized as Fibronectin type-III 9.
+At position 1347 to 1438, the domain is characterized as Fibronectin type-III 10.
+At position 414 to 787, the domain is characterized as Protein kinase.
+At position 427 to 463, the domain is characterized as PAP-associated.
+At position 54 to 333, the domain is characterized as CN hydrolase.
+At position 92 to 337, the domain is characterized as AB hydrolase-1.
+At position 17 to 166, the domain is characterized as NAC.
+At position 27 to 220, the domain is characterized as RNase H type-2.
+At position 212 to 309, the domain is characterized as PH 1.
+At position 5 to 149, the domain is characterized as Flavodoxin-like.
+At position 196 to 442, the domain is characterized as FAD-binding FR-type.
+At position 77 to 230, the domain is characterized as Ferritin-like diiron.
+At position 69 to 263, the domain is characterized as RNase H type-2.
+At position 73 to 206, the domain is characterized as Thioredoxin.
+At position 21 to 239, the domain is characterized as Radical SAM core.
+At position 110 to 353, the domain is characterized as GS catalytic.
+At position 170 to 322, the domain is characterized as C-CAP/cofactor C-like.
+At position 281 to 381, the domain is characterized as PpiC 2.
+At position 112 to 166, the domain is characterized as BSD 1.
+At position 191 to 243, the domain is characterized as BSD 2.
+At position 17 to 219, the domain is characterized as YjeF N-terminal.
+At position 229 to 494, the domain is characterized as YjeF C-terminal.
+At position 44 to 119, the domain is characterized as Carrier.
+At position 1109 to 1129, the domain is characterized as WH2 1.
+At position 1149 to 1169, the domain is characterized as WH2 2.
+At position 1237 to 1257, the domain is characterized as WH2 3.
+At position 379 to 1031, the domain is characterized as Protein kinase.
+At position 134 to 167, the domain is characterized as WW 1.
+At position 175 to 208, the domain is characterized as WW 2.
+At position 83 to 118, the domain is characterized as KH.
+At position 453 to 592, the domain is characterized as SIS 2.
+At position 80 to 93, the domain is characterized as CRIB.
+At position 125 to 310, the domain is characterized as Rho-GAP.
+At position 26 to 150, the domain is characterized as MH1.
+At position 261 to 455, the domain is characterized as MH2.
+At position 5 to 117, the domain is characterized as HotDog ACOT-type 1.
+At position 179 to 294, the domain is characterized as HotDog ACOT-type 2.
+At position 340 to 549, the domain is characterized as START.
+At position 40 to 279, the domain is characterized as Laminin N-terminal.
+At position 280 to 335, the domain is characterized as Laminin EGF-like 1.
+At position 336 to 391, the domain is characterized as Laminin EGF-like 2.
+At position 392 to 438, the domain is characterized as Laminin EGF-like 3.
+At position 439 to 488, the domain is characterized as Laminin EGF-like 4.
+At position 489 to 498, the domain is characterized as Laminin EGF-like 5; first part.
+At position 508 to 684, the domain is characterized as Laminin IV type A.
+At position 685 to 718, the domain is characterized as Laminin EGF-like 5; second part.
+At position 719 to 766, the domain is characterized as Laminin EGF-like 6.
+At position 767 to 821, the domain is characterized as Laminin EGF-like 7.
+At position 822 to 877, the domain is characterized as Laminin EGF-like 8.
+At position 878 to 927, the domain is characterized as Laminin EGF-like 9.
+At position 928 to 975, the domain is characterized as Laminin EGF-like 10.
+At position 976 to 1024, the domain is characterized as Laminin EGF-like 11.
+At position 17 to 163, the domain is characterized as PPIase cyclophilin-type.
+At position 23 to 176, the domain is characterized as Saposin B-type.
+At position 27 to 132, the domain is characterized as Phytocyanin.
+At position 165 to 346, the domain is characterized as VWFA 1.
+At position 940 to 1259, the domain is characterized as PKS/mFAS DH.
+At position 9 to 240, the domain is characterized as ABC transporter.
+At position 377 to 443, the domain is characterized as PASTA 1.
+At position 444 to 512, the domain is characterized as PASTA 2.
+At position 513 to 577, the domain is characterized as PASTA 3.
+At position 6 to 87, the domain is characterized as GST N-terminal.
+At position 95 to 214, the domain is characterized as GST C-terminal.
+At position 233 to 273, the domain is characterized as EGF-like 1.
+At position 274 to 391, the domain is characterized as SEA.
+At position 385 to 425, the domain is characterized as EGF-like 2.
+At position 425 to 467, the domain is characterized as EGF-like 3.
+At position 6 to 91, the domain is characterized as RAMA.
+At position 37 to 167, the domain is characterized as N-terminal Ras-GEF.
+At position 1197 to 1438, the domain is characterized as Ras-GEF.
+At position 92 to 182, the domain is characterized as PDZ.
+At position 5 to 59, the domain is characterized as Myb-like 1.
+At position 60 to 110, the domain is characterized as Myb-like 2.
+At position 111 to 162, the domain is characterized as Myb-like 3.
+At position 1 to 105, the domain is characterized as NTR.
+At position 82 to 503, the domain is characterized as Peptidase A1.
+At position 312 to 417, the domain is characterized as Saposin B-type.
+At position 357 to 409, the domain is characterized as SAM.
+At position 173 to 278, the domain is characterized as Fe2OG dioxygenase.
+At position 279 to 354, the domain is characterized as B5.
+At position 13 to 75, the domain is characterized as HTH iclR-type.
+At position 88 to 259, the domain is characterized as IclR-ED.
+At position 125 to 501, the domain is characterized as Myotubularin phosphatase.
+At position 303 to 631, the domain is characterized as Protein kinase.
+At position 632 to 716, the domain is characterized as AGC-kinase C-terminal.
+At position 151 to 208, the domain is characterized as Chitin-binding type-2 3.
+At position 224 to 283, the domain is characterized as Chitin-binding type-2 4.
+At position 285 to 356, the domain is characterized as Chitin-binding type-2 5.
+At position 187 to 263, the domain is characterized as UBX.
+At position 284 to 358, the domain is characterized as PUA.
+At position 187 to 250, the domain is characterized as R3H.
+At position 163 to 352, the domain is characterized as CheB-type methylesterase.
+At position 270 to 468, the domain is characterized as 3'-5' exonuclease.
+At position 57 to 176, the domain is characterized as Expansin-like EG45.
+At position 189 to 273, the domain is characterized as Expansin-like CBD.
+At position 112 to 178, the domain is characterized as DRBM.
+At position 258 to 579, the domain is characterized as A to I editase.
+At position 1 to 178, the domain is characterized as N-acetyltransferase.
+At position 85 to 134, the domain is characterized as bHLH.
+At position 815 to 869, the domain is characterized as FHA.
+At position 196 to 281, the domain is characterized as Rieske.
+At position 498 to 621, the domain is characterized as HD.
+At position 739 to 820, the domain is characterized as ACT 1.
+At position 849 to 925, the domain is characterized as ACT 2.
+At position 315 to 466, the domain is characterized as PI-PLC X-box.
+At position 589 to 705, the domain is characterized as PI-PLC Y-box.
+At position 706 to 834, the domain is characterized as C2.
+At position 70 to 324, the domain is characterized as AB hydrolase-1.
+At position 683 to 1053, the domain is characterized as DZF.
+At position 403 to 477, the domain is characterized as B5.
+At position 706 to 798, the domain is characterized as FDX-ACB.
+At position 27 to 301, the domain is characterized as Septin-type G.
+At position 18 to 328, the domain is characterized as Protein kinase.
+At position 158 to 264, the domain is characterized as Cadherin 1.
+At position 489 to 597, the domain is characterized as Cadherin 4.
+At position 607 to 688, the domain is characterized as Cadherin 5.
+At position 559 to 592, the domain is characterized as EF-hand 4.
+At position 521 to 589, the domain is characterized as J.
+At position 39 to 322, the domain is characterized as Protein kinase.
+At position 270 to 347, the domain is characterized as B5.
+At position 473 to 807, the domain is characterized as Kinesin motor.
+At position 663 to 708, the domain is characterized as VWFC 1.
+At position 828 to 902, the domain is characterized as VWFC 2.
+At position 1281 to 1385, the domain is characterized as Fibronectin type-III 1.
+At position 1407 to 1506, the domain is characterized as Fibronectin type-III 2.
+At position 1512 to 1608, the domain is characterized as Fibronectin type-III 3.
+At position 235 to 363, the domain is characterized as PARP alpha-helical.
+At position 362 to 566, the domain is characterized as PARP catalytic.
+At position 600 to 728, the domain is characterized as VIT.
+At position 869 to 1039, the domain is characterized as VWFA.
+At position 1443 to 1541, the domain is characterized as FH1.
+At position 1081 to 1263, the domain is characterized as Ferric oxidoreductase.
+At position 1264 to 1370, the domain is characterized as FAD-binding FR-type.
+At position 244 to 424, the domain is characterized as PBS-linker 1.
+At position 496 to 678, the domain is characterized as PBS-linker 2.
+At position 695 to 876, the domain is characterized as PBS-linker 3.
+At position 122 to 171, the domain is characterized as DHHC.
+At position 45 to 157, the domain is characterized as Expansin-like EG45.
+At position 98 to 236, the domain is characterized as PX.
+At position 453 to 543, the domain is characterized as CARD.
+At position 339 to 374, the domain is characterized as EF-hand 1.
+At position 378 to 408, the domain is characterized as EF-hand 2.
+At position 600 to 635, the domain is characterized as EF-hand 2.
+At position 387 to 505, the domain is characterized as PH.
+At position 374 to 426, the domain is characterized as FBD.
+At position 210 to 326, the domain is characterized as PAZ.
+At position 500 to 799, the domain is characterized as Piwi.
+At position 107 to 282, the domain is characterized as Tyr recombinase.
+At position 211 to 446, the domain is characterized as PABS.
+At position 25 to 82, the domain is characterized as 4Fe-4S Wbl-type.
+At position 4 to 187, the domain is characterized as DOC.
+At position 168 to 258, the domain is characterized as 5'-3' exonuclease.
+At position 9 to 129, the domain is characterized as C-type lectin.
+At position 305 to 421, the domain is characterized as C2.
+At position 459 to 550, the domain is characterized as RRM 1.
+At position 567 to 649, the domain is characterized as RRM 2.
+At position 8 to 80, the domain is characterized as Myb-like.
+At position 105 to 156, the domain is characterized as bHLH.
+At position 144 to 261, the domain is characterized as C2 1.
+At position 275 to 396, the domain is characterized as C2 2.
+At position 593 to 1077, the domain is characterized as Protein kinase.
+At position 1 to 43, the domain is characterized as LIM zinc-binding 1.
+At position 52 to 106, the domain is characterized as LIM zinc-binding 2.
+At position 21 to 162, the domain is characterized as Tyrosine-protein phosphatase.
+At position 244 to 482, the domain is characterized as CN hydrolase.
+At position 437 to 487, the domain is characterized as Bromo.
+At position 528 to 579, the domain is characterized as PWWP.
+At position 49 to 167, the domain is characterized as SEA.
+At position 158 to 213, the domain is characterized as BRX.
+At position 167 to 219, the domain is characterized as BSD.
+At position 9 to 474, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 491 to 785, the domain is characterized as UvrD-like helicase C-terminal.
+At position 160 to 401, the domain is characterized as NR LBD.
+At position 499 to 705, the domain is characterized as MCM.
+At position 517 to 815, the domain is characterized as UvrD-like helicase C-terminal.
+At position 941 to 979, the domain is characterized as EGF-like 1.
+At position 981 to 1019, the domain is characterized as EGF-like 2; calcium-binding.
+At position 385 to 599, the domain is characterized as Histidine kinase.
+At position 63 to 162, the domain is characterized as PINc.
+At position 731 to 991, the domain is characterized as Tyrosine-protein phosphatase.
+At position 199 to 223, the domain is characterized as HhH.
+At position 106 to 175, the domain is characterized as PDZ.
+At position 603 to 683, the domain is characterized as PB1.
+At position 49 to 118, the domain is characterized as BON 1.
+At position 127 to 194, the domain is characterized as BON 2.
+At position 767 to 877, the domain is characterized as Peptidase S74.
+At position 135 to 374, the domain is characterized as Radical SAM core.
+At position 117 to 206, the domain is characterized as EH 1.
+At position 1405 to 1422, the domain is characterized as WH2.
+At position 184 to 370, the domain is characterized as Peptidase M12B.
+At position 482 to 537, the domain is characterized as TSP type-1 1.
+At position 833 to 899, the domain is characterized as TSP type-1 2.
+At position 900 to 952, the domain is characterized as TSP type-1 3.
+At position 3 to 471, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 509 to 808, the domain is characterized as UvrD-like helicase C-terminal.
+At position 176 to 273, the domain is characterized as Rhodanese.
+At position 273 to 439, the domain is characterized as VWFA.
+At position 32 to 78, the domain is characterized as LysM.
+At position 313 to 379, the domain is characterized as Thyroglobulin type-1.
+At position 1 to 100, the domain is characterized as KRAB.
+At position 18 to 173, the domain is characterized as Nudix hydrolase.
+At position 337 to 511, the domain is characterized as Helicase ATP-binding.
+At position 538 to 690, the domain is characterized as Helicase C-terminal.
+At position 1051 to 1108, the domain is characterized as SH3.
+At position 129 to 164, the domain is characterized as EF-hand 1.
+At position 183 to 200, the domain is characterized as EF-hand 2.
+At position 206 to 241, the domain is characterized as EF-hand 3.
+At position 243 to 275, the domain is characterized as EF-hand 4.
+At position 1389 to 1451, the domain is characterized as PWWP.
+At position 187 to 268, the domain is characterized as RRM Nup35-type.
+At position 214 to 353, the domain is characterized as C2.
+At position 33 to 170, the domain is characterized as Thioredoxin.
+At position 144 to 194, the domain is characterized as DHHC.
+At position 69 to 140, the domain is characterized as RRM 1.
+At position 142 to 220, the domain is characterized as RRM 2.
+At position 231 to 309, the domain is characterized as RRM 3.
+At position 71 to 408, the domain is characterized as G-alpha.
+At position 218 to 292, the domain is characterized as U-box.
+At position 486 to 574, the domain is characterized as Fibronectin type-III.
+At position 398 to 450, the domain is characterized as SOCS box.
+At position 109 to 146, the domain is characterized as Peripheral subunit-binding (PSBD).
+At position 697 to 1073, the domain is characterized as DZF.
+At position 479 to 639, the domain is characterized as Helicase C-terminal.
+At position 48 to 249, the domain is characterized as Helicase ATP-binding.
+At position 286 to 444, the domain is characterized as Helicase C-terminal.
+At position 6 to 263, the domain is characterized as Septin-type G.
+At position 28 to 240, the domain is characterized as Brix.
+At position 158 to 330, the domain is characterized as VWFA 1.
+At position 355 to 444, the domain is characterized as Fibronectin type-III 2.
+At position 445 to 536, the domain is characterized as Fibronectin type-III 3.
+At position 537 to 627, the domain is characterized as Fibronectin type-III 4.
+At position 628 to 716, the domain is characterized as Fibronectin type-III 5.
+At position 744 to 833, the domain is characterized as Fibronectin type-III 6.
+At position 835 to 925, the domain is characterized as Fibronectin type-III 7.
+At position 926 to 1017, the domain is characterized as Fibronectin type-III 8.
+At position 1042 to 1215, the domain is characterized as VWFA 2.
+At position 1239 to 1434, the domain is characterized as Laminin G-like.
+At position 1468 to 1520, the domain is characterized as Collagen-like 1.
+At position 1524 to 1579, the domain is characterized as Collagen-like 2.
+At position 1580 to 1618, the domain is characterized as Collagen-like 3.
+At position 1664 to 1715, the domain is characterized as Collagen-like 4.
+At position 116 to 1008, the domain is characterized as Vitellogenin.
+At position 1770 to 1979, the domain is characterized as VWFD.
+At position 31 to 279, the domain is characterized as ABC transporter.
+At position 364 to 610, the domain is characterized as ABC transmembrane type-2.
+At position 54 to 123, the domain is characterized as POTRA.
+At position 660 to 781, the domain is characterized as STAS.
+At position 759 to 884, the domain is characterized as BAH 1.
+At position 977 to 1105, the domain is characterized as BAH 2.
+At position 1144 to 1603, the domain is characterized as SAM-dependent MTase C5-type.
+At position 85 to 195, the domain is characterized as Rieske.
+At position 36 to 221, the domain is characterized as BPL/LPL catalytic.
+At position 203 to 487, the domain is characterized as GT92.
+At position 70 to 124, the domain is characterized as CBS 2.
+At position 467 to 513, the domain is characterized as G-patch.
+At position 10 to 80, the domain is characterized as BTB.
+At position 24 to 90, the domain is characterized as Ig-like C2-type 1.
+At position 107 to 474, the domain is characterized as PTS EIIC type-1.
+At position 274 to 436, the domain is characterized as Helicase C-terminal.
+At position 76 to 280, the domain is characterized as N-acetyltransferase.
+At position 3 to 334, the domain is characterized as Kinesin motor.
+At position 13 to 328, the domain is characterized as Hcy-binding.
+At position 32 to 62, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 245 to 275, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 293 to 322, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 582 to 611, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 612 to 641, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 4 to 118, the domain is characterized as CENP-V/GFA.
+At position 207 to 400, the domain is characterized as Peptidase M12B.
+At position 635 to 663, the domain is characterized as EGF-like.
+At position 669 to 925, the domain is characterized as Protein kinase.
+At position 53 to 172, the domain is characterized as VOC.
+At position 39 to 464, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 933 to 1206, the domain is characterized as PKS/mFAS DH.
+At position 1706 to 1781, the domain is characterized as Carrier.
+At position 22 to 271, the domain is characterized as AB hydrolase-1.
+At position 286 to 357, the domain is characterized as PDZ 1.
+At position 419 to 466, the domain is characterized as PDZ 2.
+At position 593 to 652, the domain is characterized as KH.
+At position 664 to 733, the domain is characterized as S1 motif.
+At position 291 to 371, the domain is characterized as YcgL.
+At position 27 to 80, the domain is characterized as F-box.
+At position 385 to 436, the domain is characterized as FBD.
+At position 552 to 848, the domain is characterized as NB-ARC.
+At position 1284 to 1348, the domain is characterized as HMA.
+At position 260 to 332, the domain is characterized as bHLH.
+At position 2 to 199, the domain is characterized as MIF4G.
+At position 298 to 539, the domain is characterized as Glutamine amidotransferase type-1.
+At position 351 to 431, the domain is characterized as PAN.
+At position 22 to 112, the domain is characterized as Core-binding (CB).
+At position 136 to 325, the domain is characterized as Tyr recombinase.
+At position 13 to 93, the domain is characterized as PDZ 1.
+At position 4 to 84, the domain is characterized as ACT.
+At position 147 to 244, the domain is characterized as Glutaredoxin.
+At position 547 to 686, the domain is characterized as SIS 2.
+At position 9 to 98, the domain is characterized as ACB.
+At position 3 to 32, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 145 to 320, the domain is characterized as Helicase ATP-binding.
+At position 348 to 495, the domain is characterized as Helicase C-terminal.
+At position 77 to 176, the domain is characterized as N-acetyltransferase 1.
+At position 156 to 263, the domain is characterized as Cadherin 1.
+At position 264 to 376, the domain is characterized as Cadherin 2.
+At position 377 to 487, the domain is characterized as Cadherin 3.
+At position 488 to 593, the domain is characterized as Cadherin 4.
+At position 594 to 704, the domain is characterized as Cadherin 5.
+At position 35 to 220, the domain is characterized as Rab-GAP TBC.
+At position 281 to 462, the domain is characterized as VWFA.
+At position 419 to 510, the domain is characterized as Fibronectin type-III.
+At position 508 to 720, the domain is characterized as B30.2/SPRY.
+At position 22 to 147, the domain is characterized as Bulb-type lectin.
+At position 283 to 321, the domain is characterized as EGF-like.
+At position 341 to 424, the domain is characterized as PAN.
+At position 523 to 808, the domain is characterized as Protein kinase.
+At position 82 to 246, the domain is characterized as CP-type G.
+At position 121 to 215, the domain is characterized as Ig-like C2-type 2.
+At position 40 to 337, the domain is characterized as Deacetylase sirtuin-type.
+At position 38 to 92, the domain is characterized as HTH myb-type.
+At position 504 to 627, the domain is characterized as STAS.
+At position 36 to 234, the domain is characterized as tr-type G.
+At position 30 to 89, the domain is characterized as Clip.
+At position 107 to 359, the domain is characterized as Peptidase S1.
+At position 230 to 317, the domain is characterized as PDZ 1.
+At position 325 to 412, the domain is characterized as PDZ 2.
+At position 474 to 555, the domain is characterized as PDZ 3.
+At position 683 to 858, the domain is characterized as Guanylate kinase-like.
+At position 120 to 219, the domain is characterized as Ig-like 2.
+At position 228 to 324, the domain is characterized as Ig-like 3.
+At position 65 to 99, the domain is characterized as Orange.
+At position 150 to 232, the domain is characterized as Ig-like C2-type.
+At position 311 to 507, the domain is characterized as B30.2/SPRY.
+At position 41 to 126, the domain is characterized as ELM2.
+At position 127 to 178, the domain is characterized as SANT 1.
+At position 830 to 1060, the domain is characterized as Peptidase S1 3.
+At position 354 to 639, the domain is characterized as Protein kinase.
+At position 635 to 776, the domain is characterized as TIR.
+At position 593 to 669, the domain is characterized as Carrier 1.
+At position 2090 to 2164, the domain is characterized as Carrier 2.
+At position 152 to 409, the domain is characterized as PPM-type phosphatase.
+At position 654 to 740, the domain is characterized as BRCT.
+At position 76 to 617, the domain is characterized as PLA2c.
+At position 198 to 362, the domain is characterized as UBC core.
+At position 268 to 442, the domain is characterized as Helicase ATP-binding.
+At position 695 to 848, the domain is characterized as Helicase C-terminal.
+At position 7 to 198, the domain is characterized as RNase H type-2.
+At position 347 to 625, the domain is characterized as Protein kinase.
+At position 206 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 106 to 315, the domain is characterized as GS catalytic.
+At position 632 to 713, the domain is characterized as PH.
+At position 891 to 1147, the domain is characterized as Protein kinase.
+At position 57 to 132, the domain is characterized as KRAB.
+At position 35 to 208, the domain is characterized as FAD-binding PCMH-type.
+At position 166 to 352, the domain is characterized as CheB-type methylesterase.
+At position 56 to 130, the domain is characterized as RBD.
+At position 340 to 600, the domain is characterized as Protein kinase.
+At position 19 to 134, the domain is characterized as Response regulatory.
+At position 231 to 409, the domain is characterized as GAF.
+At position 623 to 694, the domain is characterized as PAS 1.
+At position 757 to 828, the domain is characterized as PAS 2.
+At position 905 to 1125, the domain is characterized as Histidine kinase.
+At position 26 to 108, the domain is characterized as Ig-like C2-type 1.
+At position 113 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 215 to 294, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 396, the domain is characterized as Ig-like C2-type 4.
+At position 402 to 491, the domain is characterized as Ig-like C2-type 5.
+At position 496 to 585, the domain is characterized as Ig-like C2-type 6.
+At position 592 to 688, the domain is characterized as Fibronectin type-III 1.
+At position 693 to 789, the domain is characterized as Fibronectin type-III 2.
+At position 794 to 893, the domain is characterized as Fibronectin type-III 3.
+At position 897 to 991, the domain is characterized as Fibronectin type-III 4.
+At position 995 to 1094, the domain is characterized as Fibronectin type-III 5.
+At position 1099 to 1197, the domain is characterized as Fibronectin type-III 6.
+At position 1202 to 1299, the domain is characterized as Fibronectin type-III 7.
+At position 1303 to 1397, the domain is characterized as Fibronectin type-III 8.
+At position 1402 to 1499, the domain is characterized as Fibronectin type-III 9.
+At position 1504 to 1621, the domain is characterized as Fibronectin type-III 10.
+At position 1626 to 1722, the domain is characterized as Fibronectin type-III 11.
+At position 1726 to 1821, the domain is characterized as Fibronectin type-III 12.
+At position 1824 to 1923, the domain is characterized as Fibronectin type-III 13.
+At position 101 to 259, the domain is characterized as Cupin type-1 1.
+At position 302 to 475, the domain is characterized as Cupin type-1 2.
+At position 816 to 881, the domain is characterized as HTH luxR-type.
+At position 604 to 705, the domain is characterized as tRNA-binding.
+At position 195 to 236, the domain is characterized as CHCH.
+At position 240 to 317, the domain is characterized as RRM 1.
+At position 340 to 417, the domain is characterized as RRM 2.
+At position 506 to 590, the domain is characterized as RRM 3.
+At position 2 to 237, the domain is characterized as CN hydrolase.
+At position 95 to 188, the domain is characterized as Rieske.
+At position 68 to 470, the domain is characterized as Protein kinase.
+At position 233 to 309, the domain is characterized as RRM 1.
+At position 325 to 399, the domain is characterized as RRM 2.
+At position 415 to 488, the domain is characterized as RRM 3.
+At position 503 to 578, the domain is characterized as RRM 4.
+At position 14 to 249, the domain is characterized as ABC transporter.
+At position 45 to 326, the domain is characterized as ABC transmembrane type-1.
+At position 357 to 592, the domain is characterized as ABC transporter.
+At position 100 to 268, the domain is characterized as CRAL-TRIO.
+At position 33 to 167, the domain is characterized as MATH.
+At position 203 to 270, the domain is characterized as BTB.
+At position 569 to 904, the domain is characterized as HECT.
+At position 182 to 356, the domain is characterized as EngA-type G 2.
+At position 357 to 442, the domain is characterized as KH-like.
+At position 16 to 264, the domain is characterized as ABC transporter.
+At position 342 to 593, the domain is characterized as dDENN.
+At position 41 to 75, the domain is characterized as LRRNT.
+At position 443 to 494, the domain is characterized as LRRCT.
+At position 498 to 597, the domain is characterized as Ig-like C2-type 1.
+At position 602 to 691, the domain is characterized as Ig-like C2-type 2.
+At position 696 to 785, the domain is characterized as Ig-like C2-type 3.
+At position 41 to 113, the domain is characterized as TRAM.
+At position 155 to 343, the domain is characterized as CheB-type methylesterase.
+At position 33 to 234, the domain is characterized as PNPLA.
+At position 110 to 193, the domain is characterized as RRM.
+At position 31 to 139, the domain is characterized as Ig-like V-type.
+At position 8 to 71, the domain is characterized as Myosin N-terminal SH3-like.
+At position 75 to 791, the domain is characterized as Myosin motor.
+At position 9 to 248, the domain is characterized as ABC transporter.
+At position 237 to 310, the domain is characterized as RRM.
+At position 7 to 72, the domain is characterized as MIT.
+At position 87 to 482, the domain is characterized as FH2.
+At position 168 to 344, the domain is characterized as TNase-like.
+At position 119 to 216, the domain is characterized as PA.
+At position 373 to 438, the domain is characterized as S4 RNA-binding.
+At position 41 to 320, the domain is characterized as Protein kinase.
+At position 157 to 211, the domain is characterized as PQ-loop 2.
+At position 175 to 289, the domain is characterized as SPR.
+At position 113 to 298, the domain is characterized as ATP-grasp.
+At position 138 to 320, the domain is characterized as Helicase ATP-binding.
+At position 349 to 491, the domain is characterized as Helicase C-terminal.
+At position 290 to 582, the domain is characterized as Glutamine amidotransferase type-1.
+At position 429 to 473, the domain is characterized as RPE1 insert.
+At position 824 to 1010, the domain is characterized as SEC7.
+At position 47 to 111, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 163 to 280, the domain is characterized as Thioredoxin.
+At position 430 to 654, the domain is characterized as Helicase C-terminal.
+At position 86 to 785, the domain is characterized as Myosin motor.
+At position 129 to 158, the domain is characterized as IQ.
+At position 30 to 140, the domain is characterized as sHSP.
+At position 2028 to 2046, the domain is characterized as WH2.
+At position 288 to 933, the domain is characterized as USP.
+At position 221 to 454, the domain is characterized as Grh/CP2 DB.
+At position 5 to 383, the domain is characterized as SAM-dependent MTase C5-type.
+At position 53 to 242, the domain is characterized as Brix.
+At position 398 to 603, the domain is characterized as Helicase ATP-binding.
+At position 614 to 777, the domain is characterized as Helicase C-terminal.
+At position 435 to 641, the domain is characterized as MCM.
+At position 4 to 303, the domain is characterized as Protein kinase.
+At position 177 to 289, the domain is characterized as SPR.
+At position 8 to 204, the domain is characterized as AMMECR1.
+At position 44 to 117, the domain is characterized as BTB.
+At position 153 to 253, the domain is characterized as BACK.
+At position 2 to 180, the domain is characterized as DPCK.
+At position 29 to 134, the domain is characterized as Glutaredoxin.
+At position 69 to 155, the domain is characterized as PNT.
+At position 186 to 253, the domain is characterized as KH 1.
+At position 276 to 345, the domain is characterized as KH 2.
+At position 457 to 521, the domain is characterized as KH 3.
+At position 654 to 737, the domain is characterized as G5 1.
+At position 783 to 865, the domain is characterized as G5 2.
+At position 911 to 993, the domain is characterized as G5 3.
+At position 1039 to 1121, the domain is characterized as G5 4.
+At position 1167 to 1250, the domain is characterized as G5 5.
+At position 15 to 207, the domain is characterized as DPCK.
+At position 1131 to 1238, the domain is characterized as SH2.
+At position 1266 to 1399, the domain is characterized as PTB.
+At position 252 to 433, the domain is characterized as GAF.
+At position 652 to 723, the domain is characterized as PAS 1.
+At position 786 to 857, the domain is characterized as PAS 2.
+At position 934 to 1153, the domain is characterized as Histidine kinase.
+At position 624 to 673, the domain is characterized as KA1.
+At position 262 to 332, the domain is characterized as RRM.
+At position 164 to 314, the domain is characterized as GAF 1.
+At position 346 to 503, the domain is characterized as GAF 2.
+At position 536 to 860, the domain is characterized as PDEase.
+At position 91 to 277, the domain is characterized as ATP-grasp.
+At position 234 to 466, the domain is characterized as Peptidase S1.
+At position 214 to 410, the domain is characterized as Peptidase M12B.
+At position 256 to 420, the domain is characterized as TrmE-type G.
+At position 144 to 309, the domain is characterized as Helicase ATP-binding.
+At position 439 to 590, the domain is characterized as Helicase C-terminal.
+At position 797 to 848, the domain is characterized as SANT 1.
+At position 899 to 963, the domain is characterized as SANT 2.
+At position 776 to 875, the domain is characterized as HECT.
+At position 5 to 99, the domain is characterized as FAD-binding FR-type.
+At position 78 to 107, the domain is characterized as IQ.
+At position 237 to 480, the domain is characterized as NR LBD.
+At position 131 to 562, the domain is characterized as Urease.
+At position 40 to 170, the domain is characterized as Cyclin N-terminal.
+At position 13 to 95, the domain is characterized as GIY-YIG.
+At position 235 to 357, the domain is characterized as SEA 1.
+At position 575 to 688, the domain is characterized as SEA 2.
+At position 76 to 460, the domain is characterized as Kinesin motor.
+At position 134 to 393, the domain is characterized as Rho-GAP.
+At position 12 to 171, the domain is characterized as Ku.
+At position 28 to 90, the domain is characterized as t-SNARE coiled-coil homology.
+At position 5 to 307, the domain is characterized as FERM.
+At position 33 to 130, the domain is characterized as Stress-response A/B barrel.
+At position 207 to 276, the domain is characterized as PWWP.
+At position 885 to 1002, the domain is characterized as SET.
+At position 1011 to 1027, the domain is characterized as Post-SET.
+At position 96 to 180, the domain is characterized as KH-like.
+At position 598 to 750, the domain is characterized as RNase NYN.
+At position 24 to 53, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 108 to 137, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 147 to 176, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 187 to 216, the domain is characterized as 4Fe-4S ferredoxin-type 5.
+At position 235 to 264, the domain is characterized as 4Fe-4S ferredoxin-type 6.
+At position 267 to 296, the domain is characterized as 4Fe-4S ferredoxin-type 7.
+At position 102 to 174, the domain is characterized as S4 RNA-binding.
+At position 158 to 399, the domain is characterized as Radical SAM core.
+At position 177 to 280, the domain is characterized as SH2.
+At position 37 to 233, the domain is characterized as ABC transmembrane type-1.
+At position 27 to 163, the domain is characterized as CMP/dCMP-type deaminase.
+At position 59 to 128, the domain is characterized as POTRA.
+At position 15 to 404, the domain is characterized as Protein kinase.
+At position 350 to 629, the domain is characterized as Autotransporter.
+At position 236 to 290, the domain is characterized as bHLH.
+At position 424 to 647, the domain is characterized as TRUD.
+At position 4 to 235, the domain is characterized as ABC transporter 1.
+At position 261 to 489, the domain is characterized as ABC transporter 2.
+At position 586 to 759, the domain is characterized as RNase III 1.
+At position 811 to 935, the domain is characterized as RNase III 2.
+At position 962 to 1037, the domain is characterized as DRBM.
+At position 13 to 220, the domain is characterized as tr-type G.
+At position 72 to 237, the domain is characterized as Bms1-type G.
+At position 442 to 744, the domain is characterized as Protein kinase.
+At position 404 to 512, the domain is characterized as Fe2OG dioxygenase.
+At position 19 to 117, the domain is characterized as SSB.
+At position 236 to 373, the domain is characterized as GAF 1.
+At position 408 to 547, the domain is characterized as GAF 2.
+At position 577 to 901, the domain is characterized as PDEase.
+At position 804 to 1098, the domain is characterized as Protein kinase.
+At position 117 to 349, the domain is characterized as Radical SAM core.
+At position 160 to 382, the domain is characterized as Histidine kinase.
+At position 8 to 230, the domain is characterized as Radical SAM core.
+At position 908 to 1106, the domain is characterized as MAGE.
+At position 7 to 86, the domain is characterized as Carrier.
+At position 92 to 145, the domain is characterized as bHLH.
+At position 163 to 235, the domain is characterized as PAS 1.
+At position 342 to 412, the domain is characterized as PAS 2.
+At position 417 to 460, the domain is characterized as PAC.
+At position 69 to 185, the domain is characterized as PX.
+At position 1 to 219, the domain is characterized as BRO1.
+At position 1055 to 1315, the domain is characterized as Tyrosine-protein phosphatase.
+At position 237 to 288, the domain is characterized as GRAM 1.
+At position 719 to 785, the domain is characterized as GRAM 2.
+At position 2 to 52, the domain is characterized as BPTI/Kunitz inhibitor.
+At position 434 to 560, the domain is characterized as C2 B9-type.
+At position 128 to 424, the domain is characterized as Protein kinase.
+At position 445 to 524, the domain is characterized as AGC-kinase C-terminal.
+At position 254 to 411, the domain is characterized as Helicase C-terminal.
+At position 79 to 356, the domain is characterized as Protein kinase.
+At position 270 to 343, the domain is characterized as RRM 1.
+At position 355 to 428, the domain is characterized as RRM 2.
+At position 951 to 1005, the domain is characterized as GPS.
+At position 55 to 164, the domain is characterized as Cadherin 1.
+At position 165 to 277, the domain is characterized as Cadherin 2.
+At position 278 to 398, the domain is characterized as Cadherin 3.
+At position 397 to 504, the domain is characterized as Cadherin 4.
+At position 35 to 240, the domain is characterized as YjeF N-terminal.
+At position 202 to 350, the domain is characterized as ExoI SH3-like.
+At position 356 to 471, the domain is characterized as ExoI C-terminal.
+At position 63 to 244, the domain is characterized as FAD-binding PCMH-type.
+At position 253 to 390, the domain is characterized as MPN.
+At position 88 to 218, the domain is characterized as GST C-terminal.
+At position 70 to 162, the domain is characterized as Rieske.
+At position 43 to 177, the domain is characterized as MATH.
+At position 222 to 295, the domain is characterized as BTB.
+At position 555 to 617, the domain is characterized as KH.
+At position 627 to 698, the domain is characterized as S1 motif.
+At position 24 to 128, the domain is characterized as Phytocyanin.
+At position 26 to 286, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 530 to 726, the domain is characterized as Glutamine amidotransferase type-1.
+At position 33 to 469, the domain is characterized as Protein kinase.
+At position 10 to 91, the domain is characterized as RRM 1.
+At position 163 to 240, the domain is characterized as RRM 2.
+At position 365 to 406, the domain is characterized as UBA.
+At position 430 to 531, the domain is characterized as RWD.
+At position 614 to 782, the domain is characterized as Helicase ATP-binding.
+At position 845 to 1020, the domain is characterized as Helicase C-terminal.
+At position 104 to 262, the domain is characterized as Cupin type-1 1.
+At position 311 to 493, the domain is characterized as Cupin type-1 2.
+At position 126 to 325, the domain is characterized as Peptidase M12A.
+At position 327 to 439, the domain is characterized as CUB 1.
+At position 440 to 551, the domain is characterized as CUB 2.
+At position 552 to 593, the domain is characterized as EGF-like 1; calcium-binding.
+At position 596 to 707, the domain is characterized as CUB 3.
+At position 708 to 748, the domain is characterized as EGF-like 2; calcium-binding.
+At position 752 to 864, the domain is characterized as CUB 4.
+At position 865 to 981, the domain is characterized as CUB 5.
+At position 2 to 137, the domain is characterized as HTH rrf2-type.
+At position 2 to 262, the domain is characterized as Pyruvate carboxyltransferase.
+At position 492 to 567, the domain is characterized as Biotinyl-binding.
+At position 204 to 453, the domain is characterized as NR LBD.
+At position 799 to 906, the domain is characterized as Calponin-homology (CH).
+At position 294 to 345, the domain is characterized as TSP type-1.
+At position 212 to 462, the domain is characterized as NR LBD.
+At position 70 to 155, the domain is characterized as PA.
+At position 609 to 944, the domain is characterized as HECT.
+At position 74 to 212, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 1.
+At position 235 to 358, the domain is characterized as N-acetylmuramoyl-L-alanine amidase 2.
+At position 70 to 324, the domain is characterized as Protein kinase.
+At position 325 to 380, the domain is characterized as AGC-kinase C-terminal.
+At position 76 to 144, the domain is characterized as DRBM.
+At position 467 to 635, the domain is characterized as Helicase ATP-binding.
+At position 677 to 850, the domain is characterized as Helicase C-terminal.
+At position 8 to 63, the domain is characterized as Kazal-like.
+At position 62 to 97, the domain is characterized as EF-hand.
+At position 68 to 135, the domain is characterized as CSD.
+At position 47 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 11 to 165, the domain is characterized as N-acetyltransferase.
+At position 259 to 333, the domain is characterized as POU-specific.
+At position 107 to 369, the domain is characterized as Protein kinase.
+At position 366 to 426, the domain is characterized as SH3.
+At position 29 to 71, the domain is characterized as CHCH.
+At position 88 to 123, the domain is characterized as EF-hand 1.
+At position 212 to 247, the domain is characterized as EF-hand 4.
+At position 225 to 398, the domain is characterized as EngA-type G 2.
+At position 399 to 483, the domain is characterized as KH-like.
+At position 993 to 1127, the domain is characterized as C1q.
+At position 99 to 137, the domain is characterized as LRRCT.
+At position 187 to 292, the domain is characterized as Fe2OG dioxygenase.
+At position 9 to 51, the domain is characterized as CHCH.
+At position 416 to 521, the domain is characterized as SEA.
+At position 358 to 415, the domain is characterized as S4 RNA-binding.
+At position 134 to 168, the domain is characterized as EF-hand 3.
+At position 43 to 74, the domain is characterized as EF-hand 2.
+At position 52 to 138, the domain is characterized as KRAB.
+At position 100 to 304, the domain is characterized as ATP-grasp.
+At position 8 to 83, the domain is characterized as Peptidase M12B.
+At position 495 to 678, the domain is characterized as Helicase ATP-binding 1.
+At position 717 to 923, the domain is characterized as Helicase C-terminal 1.
+At position 987 to 1296, the domain is characterized as SEC63 1.
+At position 1345 to 1520, the domain is characterized as Helicase ATP-binding 2.
+At position 1553 to 1760, the domain is characterized as Helicase C-terminal 2.
+At position 1821 to 2184, the domain is characterized as SEC63 2.
+At position 203 to 397, the domain is characterized as Peptidase M12B.
+At position 406 to 490, the domain is characterized as Disintegrin.
+At position 631 to 665, the domain is characterized as EGF-like.
+At position 40 to 252, the domain is characterized as GH16.
+At position 716 to 786, the domain is characterized as PAS 1.
+At position 789 to 841, the domain is characterized as PAC 1.
+At position 848 to 920, the domain is characterized as PAS 2.
+At position 929 to 982, the domain is characterized as PAC 2.
+At position 1000 to 1223, the domain is characterized as Histidine kinase.
+At position 1507 to 1629, the domain is characterized as Response regulatory.
+At position 4 to 176, the domain is characterized as Flavodoxin-like.
+At position 253 to 467, the domain is characterized as FAD-binding FR-type.
+At position 568 to 661, the domain is characterized as EH.
+At position 117 to 370, the domain is characterized as ABC transporter 1.
+At position 475 to 700, the domain is characterized as ABC transmembrane type-2 1.
+At position 805 to 1049, the domain is characterized as ABC transporter 2.
+At position 1141 to 1366, the domain is characterized as ABC transmembrane type-2 2.
+At position 1248 to 1508, the domain is characterized as Tyrosine-protein phosphatase.
+At position 26 to 203, the domain is characterized as DHFR.
+At position 42 to 93, the domain is characterized as SANT.
+At position 482 to 516, the domain is characterized as EF-hand 4.
+At position 353 to 461, the domain is characterized as PH.
+At position 714 to 1007, the domain is characterized as Protein kinase.
+At position 752 to 811, the domain is characterized as CBS 2.
+At position 359 to 416, the domain is characterized as SH3.
+At position 75 to 359, the domain is characterized as Protein kinase.
+At position 54 to 238, the domain is characterized as tr-type G.
+At position 514 to 589, the domain is characterized as Cytochrome b5 heme-binding.
+At position 615 to 726, the domain is characterized as FAD-binding FR-type.
+At position 13 to 266, the domain is characterized as BAR.
+At position 251 to 448, the domain is characterized as Rho-GAP.
+At position 1 to 143, the domain is characterized as PPPDE.
+At position 591 to 867, the domain is characterized as Autotransporter.
+At position 172 to 408, the domain is characterized as Radical SAM core.
+At position 411 to 487, the domain is characterized as TRAM.
+At position 228 to 404, the domain is characterized as Phosphatase tensin-type.
+At position 411 to 540, the domain is characterized as C2 tensin-type.
+At position 31 to 309, the domain is characterized as Dynamin-type G.
+At position 305 to 448, the domain is characterized as JmjC.
+At position 530 to 742, the domain is characterized as STAS.
+At position 155 to 229, the domain is characterized as RRM 2.
+At position 2 to 103, the domain is characterized as Phytocyanin.
+At position 314 to 406, the domain is characterized as BRCT.
+At position 15 to 336, the domain is characterized as YjeF C-terminal.
+At position 346 to 583, the domain is characterized as TLDc.
+At position 37 to 201, the domain is characterized as Helicase ATP-binding.
+At position 235 to 431, the domain is characterized as Helicase C-terminal.
+At position 141 to 219, the domain is characterized as KRAB.
+At position 18 to 153, the domain is characterized as MPN.
+At position 37 to 111, the domain is characterized as H15.
+At position 184 to 248, the domain is characterized as bZIP.
+At position 29 to 199, the domain is characterized as FAD-binding PCMH-type.
+At position 118 to 339, the domain is characterized as Radical SAM core.
+At position 64 to 148, the domain is characterized as Core-binding (CB).
+At position 175 to 384, the domain is characterized as Tyr recombinase.
+At position 216 to 243, the domain is characterized as PLD phosphodiesterase 1.
+At position 253 to 402, the domain is characterized as Helicase ATP-binding.
+At position 457 to 600, the domain is characterized as Helicase C-terminal.
+At position 17 to 130, the domain is characterized as Toprim.
+At position 8 to 203, the domain is characterized as Laminin G-like 1.
+At position 210 to 369, the domain is characterized as Laminin G-like 2.
+At position 371 to 413, the domain is characterized as EGF-like 1.
+At position 621 to 788, the domain is characterized as Laminin G-like 3.
+At position 789 to 825, the domain is characterized as EGF-like 2.
+At position 10 to 204, the domain is characterized as Glutamine amidotransferase type-1.
+At position 205 to 396, the domain is characterized as GMPS ATP-PPase.
+At position 22 to 441, the domain is characterized as Trm1 methyltransferase.
+At position 578 to 661, the domain is characterized as BRCT.
+At position 25 to 181, the domain is characterized as PPIase cyclophilin-type.
+At position 53 to 163, the domain is characterized as sHSP.
+At position 304 to 482, the domain is characterized as Helicase ATP-binding.
+At position 519 to 669, the domain is characterized as Helicase C-terminal.
+At position 294 to 374, the domain is characterized as TFIIS N-terminal.
+At position 5 to 103, the domain is characterized as PINc.
+At position 182 to 292, the domain is characterized as Ig-like.
+At position 58 to 129, the domain is characterized as H15.
+At position 197 to 541, the domain is characterized as SEC63 1.
+At position 11 to 90, the domain is characterized as PDZ 1.
+At position 150 to 230, the domain is characterized as PDZ 2.
+At position 28 to 220, the domain is characterized as RNase H type-2.
+At position 88 to 399, the domain is characterized as Protein kinase.
+At position 35 to 65, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 97 to 129, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 130 to 159, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 164 to 195, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 18 to 345, the domain is characterized as YjeF C-terminal.
+At position 201 to 273, the domain is characterized as U-box.
+At position 337 to 377, the domain is characterized as UBA.
+At position 1 to 276, the domain is characterized as CheR-type methyltransferase.
+At position 32 to 157, the domain is characterized as Bulb-type lectin.
+At position 294 to 330, the domain is characterized as EGF-like; atypical.
+At position 349 to 435, the domain is characterized as PAN.
+At position 524 to 810, the domain is characterized as Protein kinase.
+At position 104 to 478, the domain is characterized as USP.
+At position 146 to 502, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 116 to 271, the domain is characterized as CP-type G.
+At position 69 to 173, the domain is characterized as FAD-binding FR-type.
+At position 4 to 448, the domain is characterized as Biotin carboxylation.
+At position 123 to 320, the domain is characterized as ATP-grasp.
+At position 21 to 181, the domain is characterized as PPIase cyclophilin-type.
+At position 441 to 507, the domain is characterized as FHA.
+At position 668 to 915, the domain is characterized as Dilute.
+At position 1014 to 1100, the domain is characterized as PDZ.
+At position 247 to 376, the domain is characterized as PH.
+At position 27 to 284, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 2 to 144, the domain is characterized as Thioredoxin.
+At position 788 to 1037, the domain is characterized as ABC transporter 2.
+At position 51 to 148, the domain is characterized as Rieske.
+At position 37 to 157, the domain is characterized as Bulb-type lectin.
+At position 299 to 349, the domain is characterized as EGF-like; atypical.
+At position 357 to 446, the domain is characterized as PAN.
+At position 531 to 803, the domain is characterized as Protein kinase.
+At position 1 to 147, the domain is characterized as TLDc.
+At position 508 to 607, the domain is characterized as Zinc-hook.
+At position 3 to 94, the domain is characterized as Chorismate mutase.
+At position 103 to 366, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 26 to 68, the domain is characterized as EGF-like 1.
+At position 69 to 108, the domain is characterized as EGF-like 1; calcium-binding.
+At position 121 to 159, the domain is characterized as EGF-like 2; calcium-binding.
+At position 165 to 203, the domain is characterized as EGF-like 3; calcium-binding.
+At position 214 to 253, the domain is characterized as EGF-like 4; calcium-binding.
+At position 486 to 536, the domain is characterized as GPS.
+At position 270 to 362, the domain is characterized as BRCT.
+At position 610 to 643, the domain is characterized as WW 1.
+At position 767 to 800, the domain is characterized as WW 2.
+At position 840 to 873, the domain is characterized as WW 3.
+At position 892 to 925, the domain is characterized as WW 4.
+At position 984 to 1318, the domain is characterized as HECT.
+At position 180 to 280, the domain is characterized as Fe2OG dioxygenase.
+At position 8 to 304, the domain is characterized as tr-type G.
+At position 11 to 46, the domain is characterized as QLQ.
+At position 87 to 131, the domain is characterized as WRC.
+At position 59 to 212, the domain is characterized as CP-type G.
+At position 48 to 305, the domain is characterized as GB1/RHD3-type G.
+At position 852 to 881, the domain is characterized as IQ 1.
+At position 875 to 904, the domain is characterized as IQ 2.
+At position 20 to 120, the domain is characterized as DUSP.
+At position 279 to 848, the domain is characterized as USP.
+At position 374 to 583, the domain is characterized as Helicase ATP-binding.
+At position 594 to 757, the domain is characterized as Helicase C-terminal.
+At position 42 to 185, the domain is characterized as Cupin type-1 1.
+At position 247 to 403, the domain is characterized as Cupin type-1 2.
+At position 95 to 159, the domain is characterized as KH 1.
+At position 180 to 246, the domain is characterized as KH 2.
+At position 270 to 334, the domain is characterized as KH 3.
+At position 371 to 438, the domain is characterized as KH 4.
+At position 65 to 128, the domain is characterized as S5 DRBM.
+At position 61 to 335, the domain is characterized as Protein kinase.
+At position 125 to 215, the domain is characterized as Fibronectin type-III 1.
+At position 223 to 323, the domain is characterized as Fibronectin type-III 2.
+At position 328 to 418, the domain is characterized as Fibronectin type-III 3.
+At position 422 to 516, the domain is characterized as Fibronectin type-III 4.
+At position 518 to 612, the domain is characterized as Fibronectin type-III 5.
+At position 146 to 503, the domain is characterized as PDEase.
+At position 307 to 727, the domain is characterized as Peptidase S8.
+At position 1075 to 1358, the domain is characterized as ABC transmembrane type-1.
+At position 1576 to 1813, the domain is characterized as ABC transporter.
+At position 1003 to 1085, the domain is characterized as PDZ 7.
+At position 1195 to 1258, the domain is characterized as bZIP.
+At position 683 to 860, the domain is characterized as Helicase ATP-binding.
+At position 917 to 1066, the domain is characterized as Helicase C-terminal.
+At position 24 to 132, the domain is characterized as HIT.
+At position 23 to 290, the domain is characterized as tr-type G.
+At position 4 to 124, the domain is characterized as PTS EIIA type-4.
+At position 42 to 100, the domain is characterized as S4 RNA-binding.
+At position 7 to 199, the domain is characterized as ThyX.
+At position 74 to 109, the domain is characterized as QLQ.
+At position 140 to 184, the domain is characterized as WRC.
+At position 25 to 308, the domain is characterized as ABC transmembrane type-1.
+At position 179 to 478, the domain is characterized as Protein kinase.
+At position 361 to 640, the domain is characterized as Protein kinase.
+At position 19 to 147, the domain is characterized as EamA 1.
+At position 191 to 320, the domain is characterized as EamA 2.
+At position 79 to 316, the domain is characterized as PE-PPE.
+At position 810 to 1236, the domain is characterized as Protein kinase.
+At position 1237 to 1347, the domain is characterized as AGC-kinase C-terminal.
+At position 65 to 187, the domain is characterized as sHSP.
+At position 22 to 462, the domain is characterized as GBD/FH3.
+At position 580 to 970, the domain is characterized as FH2.
+At position 1000 to 1037, the domain is characterized as DAD.
+At position 3 to 195, the domain is characterized as Glutamine amidotransferase type-1.
+At position 268 to 488, the domain is characterized as TLDc.
+At position 24 to 180, the domain is characterized as F5/8 type C 1.
+At position 195 to 351, the domain is characterized as F5/8 type C 2.
+At position 519 to 766, the domain is characterized as Protein kinase.
+At position 1 to 97, the domain is characterized as SUEL-type lectin 1.
+At position 104 to 195, the domain is characterized as SUEL-type lectin 2.
+At position 387 to 556, the domain is characterized as tr-type G.
+At position 255 to 372, the domain is characterized as Chitin-binding type-2.
+At position 331 to 366, the domain is characterized as EF-hand.
+At position 111 to 181, the domain is characterized as PAS 1.
+At position 275 to 342, the domain is characterized as PAS 2.
+At position 348 to 386, the domain is characterized as PAC.
+At position 2 to 133, the domain is characterized as C2 1.
+At position 212 to 339, the domain is characterized as C2 2.
+At position 382 to 581, the domain is characterized as VWFA.
+At position 17 to 131, the domain is characterized as Response regulatory.
+At position 65 to 290, the domain is characterized as Radical SAM core.
+At position 590 to 693, the domain is characterized as tRNA-binding.
+At position 6 to 107, the domain is characterized as LOB.
+At position 141 to 228, the domain is characterized as 3'-5' exonuclease.
+At position 434 to 496, the domain is characterized as t-SNARE coiled-coil homology 1.
+At position 588 to 650, the domain is characterized as t-SNARE coiled-coil homology 2.
+At position 306 to 338, the domain is characterized as LRRCT.
+At position 61 to 105, the domain is characterized as Gla.
+At position 106 to 142, the domain is characterized as EGF-like 1; calcium-binding.
+At position 147 to 188, the domain is characterized as EGF-like 2.
+At position 213 to 452, the domain is characterized as Peptidase S1.
+At position 15 to 104, the domain is characterized as RRM.
+At position 223 to 461, the domain is characterized as NR LBD.
+At position 162 to 214, the domain is characterized as KH.
+At position 224 to 425, the domain is characterized as Pentraxin (PTX).
+At position 2 to 98, the domain is characterized as CRM.
+At position 46 to 357, the domain is characterized as AB hydrolase-1.
+At position 19 to 121, the domain is characterized as CUB.
+At position 13 to 369, the domain is characterized as FMN hydroxy acid dehydrogenase.
+At position 42 to 101, the domain is characterized as Sushi 1.
+At position 102 to 163, the domain is characterized as Sushi 2.
+At position 164 to 234, the domain is characterized as Sushi 3.
+At position 236 to 295, the domain is characterized as Sushi 4.
+At position 295 to 355, the domain is characterized as Sushi 5.
+At position 356 to 418, the domain is characterized as Sushi 6.
+At position 419 to 489, the domain is characterized as Sushi 7.
+At position 491 to 551, the domain is characterized as Sushi 8.
+At position 552 to 613, the domain is characterized as Sushi 9.
+At position 614 to 684, the domain is characterized as Sushi 10.
+At position 686 to 745, the domain is characterized as Sushi 11.
+At position 745 to 805, the domain is characterized as Sushi 12.
+At position 806 to 868, the domain is characterized as Sushi 13.
+At position 869 to 939, the domain is characterized as Sushi 14.
+At position 941 to 1001, the domain is characterized as Sushi 15.
+At position 1002 to 1063, the domain is characterized as Sushi 16.
+At position 1064 to 1134, the domain is characterized as Sushi 17.
+At position 1136 to 1195, the domain is characterized as Sushi 18.
+At position 1195 to 1255, the domain is characterized as Sushi 19.
+At position 1256 to 1318, the domain is characterized as Sushi 20.
+At position 1319 to 1389, the domain is characterized as Sushi 21.
+At position 1394 to 1454, the domain is characterized as Sushi 22.
+At position 1455 to 1516, the domain is characterized as Sushi 23.
+At position 1517 to 1587, the domain is characterized as Sushi 24.
+At position 1589 to 1648, the domain is characterized as Sushi 25.
+At position 1648 to 1708, the domain is characterized as Sushi 26.
+At position 1709 to 1771, the domain is characterized as Sushi 27.
+At position 1772 to 1842, the domain is characterized as Sushi 28.
+At position 1846 to 1906, the domain is characterized as Sushi 29.
+At position 1907 to 1967, the domain is characterized as Sushi 30.
+At position 186 to 292, the domain is characterized as HTH APSES-type.
+At position 37 to 132, the domain is characterized as Ig-like C2-type.
+At position 188 to 232, the domain is characterized as EGF-like.
+At position 134 to 340, the domain is characterized as ATP-grasp.
+At position 835 to 1007, the domain is characterized as Helicase ATP-binding.
+At position 1410 to 1570, the domain is characterized as Helicase C-terminal.
+At position 130 to 158, the domain is characterized as KOW.
+At position 8 to 693, the domain is characterized as Myosin motor.
+At position 694 to 722, the domain is characterized as IQ 1.
+At position 716 to 745, the domain is characterized as IQ 2.
+At position 810 to 1004, the domain is characterized as TH1.
+At position 151 to 372, the domain is characterized as TRUD.
+At position 162 to 239, the domain is characterized as RRM.
+At position 50 to 292, the domain is characterized as GB1/RHD3-type G.
+At position 411 to 533, the domain is characterized as RCK N-terminal.
+At position 221 to 622, the domain is characterized as PPM-type phosphatase.
+At position 20 to 105, the domain is characterized as GS beta-grasp.
+At position 112 to 447, the domain is characterized as GS catalytic.
+At position 319 to 493, the domain is characterized as PCI.
+At position 135 to 364, the domain is characterized as Sigma-54 factor interaction.
+At position 58 to 284, the domain is characterized as Glutamine amidotransferase type-2.
+At position 41 to 184, the domain is characterized as PH.
+At position 342 to 402, the domain is characterized as SH3.
+At position 410 to 503, the domain is characterized as SH2.
+At position 526 to 779, the domain is characterized as Protein kinase.
+At position 5 to 84, the domain is characterized as TFIIS N-terminal.
+At position 148 to 263, the domain is characterized as TFIIS central.
+At position 27 to 297, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 24 to 281, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 637 to 771, the domain is characterized as C2.
+At position 601 to 775, the domain is characterized as PCI.
+At position 182 to 363, the domain is characterized as CRAL-TRIO.
+At position 5 to 354, the domain is characterized as Trm1 methyltransferase.
+At position 156 to 215, the domain is characterized as CHORD 2.
+At position 226 to 315, the domain is characterized as CS.
+At position 264 to 379, the domain is characterized as PAZ.
+At position 546 to 853, the domain is characterized as Piwi.
+At position 615 to 1006, the domain is characterized as FH2.
+At position 1038 to 1077, the domain is characterized as DAD.
+At position 21 to 128, the domain is characterized as Calponin-homology (CH).
+At position 985 to 1051, the domain is characterized as LIM zinc-binding.
+At position 49 to 307, the domain is characterized as Glutamine amidotransferase type-1.
+At position 190 to 226, the domain is characterized as DFDF.
+At position 281 to 485, the domain is characterized as YjeF N-terminal.
+At position 104 to 172, the domain is characterized as POTRA.
+At position 19 to 78, the domain is characterized as LCN-type CS-alpha/beta.
+At position 10 to 177, the domain is characterized as N-acetyltransferase.
+At position 235 to 295, the domain is characterized as HTH myb-type.
+At position 9 to 64, the domain is characterized as CBS 1.
+At position 67 to 126, the domain is characterized as CBS 2.
+At position 2 to 67, the domain is characterized as TGS.
+At position 62 to 179, the domain is characterized as C2 1.
+At position 218 to 354, the domain is characterized as C2 2.
+At position 996 to 1124, the domain is characterized as C2 3.
+At position 1159 to 1283, the domain is characterized as C2 4.
+At position 1408 to 1527, the domain is characterized as C2 5.
+At position 1645 to 1793, the domain is characterized as C2 6.
+At position 316 to 472, the domain is characterized as Helicase ATP-binding.
+At position 582 to 752, the domain is characterized as Helicase C-terminal.
+At position 239 to 641, the domain is characterized as PPM-type phosphatase.
+At position 135 to 205, the domain is characterized as S1 motif.
+At position 307 to 373, the domain is characterized as KH.
+At position 226 to 366, the domain is characterized as MPN.
+At position 1 to 84, the domain is characterized as HPr.
+At position 75 to 780, the domain is characterized as Myosin motor.
+At position 783 to 805, the domain is characterized as IQ 1.
+At position 806 to 830, the domain is characterized as IQ 2.
+At position 831 to 854, the domain is characterized as IQ 3.
+At position 855 to 878, the domain is characterized as IQ 4.
+At position 879 to 901, the domain is characterized as IQ 5.
+At position 902 to 931, the domain is characterized as IQ 6.
+At position 1143 to 1357, the domain is characterized as Dilute.
+At position 1125 to 1291, the domain is characterized as SEC7.
+At position 1332 to 1445, the domain is characterized as PH.
+At position 32 to 137, the domain is characterized as CBM2.
+At position 237 to 305, the domain is characterized as PUA.
+At position 48 to 165, the domain is characterized as PX.
+At position 116 to 167, the domain is characterized as SANT.
+At position 372 to 470, the domain is characterized as SWIRM.
+At position 577 to 709, the domain is characterized as MPN.
+At position 73 to 229, the domain is characterized as TIR.
+At position 1 to 133, the domain is characterized as ADF-H.
+At position 171 to 314, the domain is characterized as PPC.
+At position 181 to 339, the domain is characterized as MOSC.
+At position 46 to 102, the domain is characterized as 4Fe-4S Mo/W bis-MGD-type.
+At position 103 to 396, the domain is characterized as FAE.
+At position 35 to 337, the domain is characterized as ABC transmembrane type-1.
+At position 367 to 561, the domain is characterized as ABC transporter.
+At position 1 to 143, the domain is characterized as PPIase cyclophilin-type.
+At position 40 to 202, the domain is characterized as PCI.
+At position 17 to 356, the domain is characterized as tr-type G.
+At position 101 to 173, the domain is characterized as PRC barrel.
+At position 3 to 238, the domain is characterized as CN hydrolase.
+At position 799 to 1081, the domain is characterized as Protein kinase.
+At position 80 to 194, the domain is characterized as Plastocyanin-like 1.
+At position 205 to 358, the domain is characterized as Plastocyanin-like 2.
+At position 427 to 554, the domain is characterized as Plastocyanin-like 3.
+At position 245 to 287, the domain is characterized as EGF-like.
+At position 504 to 702, the domain is characterized as B30.2/SPRY.
+At position 366 to 568, the domain is characterized as DhaL.
+At position 138 to 379, the domain is characterized as Radical SAM core.
+At position 382 to 448, the domain is characterized as TRAM.
+At position 83 to 181, the domain is characterized as FAS1 1.
+At position 254 to 352, the domain is characterized as FAS1 2.
+At position 26 to 352, the domain is characterized as Transferrin-like 1.
+At position 52 to 263, the domain is characterized as PCI.
+At position 672 to 906, the domain is characterized as NR LBD.
+At position 19 to 186, the domain is characterized as SprT-like.
+At position 93 to 430, the domain is characterized as Kinesin motor.
+At position 10 to 86, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 464 to 620, the domain is characterized as Helicase C-terminal.
+At position 13 to 189, the domain is characterized as PITH.
+At position 66 to 199, the domain is characterized as TNase-like.
+At position 7 to 115, the domain is characterized as Calponin-homology (CH).
+At position 228 to 441, the domain is characterized as Helicase ATP-binding.
+At position 481 to 649, the domain is characterized as Helicase C-terminal.
+At position 153 to 401, the domain is characterized as Radical SAM core.
+At position 404 to 483, the domain is characterized as TRAM.
+At position 69 to 127, the domain is characterized as CBS 1.
+At position 135 to 200, the domain is characterized as CBS 2.
+At position 263 to 319, the domain is characterized as CBS 3.
+At position 328 to 385, the domain is characterized as CBS 4.
+At position 572 to 649, the domain is characterized as PB1.
+At position 23 to 260, the domain is characterized as Radical SAM core.
+At position 20 to 103, the domain is characterized as GIY-YIG.
+At position 59 to 729, the domain is characterized as Myosin motor.
+At position 1148 to 1463, the domain is characterized as Dilute.
+At position 45 to 180, the domain is characterized as Guanylate cyclase.
+At position 936 to 1255, the domain is characterized as PKS/mFAS DH.
+At position 2283 to 2360, the domain is characterized as Carrier.
+At position 35 to 411, the domain is characterized as PPM-type phosphatase.
+At position 1 to 123, the domain is characterized as ApaG.
+At position 232 to 458, the domain is characterized as CN hydrolase.
+At position 53 to 274, the domain is characterized as Velvet.
+At position 185 to 407, the domain is characterized as Fibrinogen C-terminal.
+At position 416 to 491, the domain is characterized as ACT 1.
+At position 497 to 574, the domain is characterized as ACT 2.
+At position 748 to 827, the domain is characterized as Carrier.
+At position 14 to 140, the domain is characterized as EamA.
+At position 213 to 299, the domain is characterized as PDZ 1.
+At position 352 to 437, the domain is characterized as PDZ 2.
+At position 1105 to 1190, the domain is characterized as PDZ 3.
+At position 1226 to 1309, the domain is characterized as PDZ 4.
+At position 259 to 320, the domain is characterized as SH3.
+At position 98 to 341, the domain is characterized as ABC transporter 1.
+At position 767 to 1013, the domain is characterized as ABC transporter 2.
+At position 45 to 90, the domain is characterized as LysM.
+At position 629 to 703, the domain is characterized as S1 motif.
+At position 76 to 247, the domain is characterized as VWFA.
+At position 592 to 621, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 331 to 529, the domain is characterized as Protein kinase.
+At position 52 to 240, the domain is characterized as RNase H type-2.
+At position 755 to 880, the domain is characterized as BAH 1.
+At position 972 to 1100, the domain is characterized as BAH 2.
+At position 1139 to 1599, the domain is characterized as SAM-dependent MTase C5-type.
+At position 117 to 294, the domain is characterized as Prephenate dehydratase.
+At position 308 to 399, the domain is characterized as ACT.
+At position 32 to 120, the domain is characterized as Ig-like C2-type 1.
+At position 216 to 330, the domain is characterized as Ig-like C2-type 3.
+At position 335 to 426, the domain is characterized as Ig-like C2-type 4.
+At position 433 to 553, the domain is characterized as Ig-like C2-type 5.
+At position 556 to 667, the domain is characterized as Ig-like C2-type 6.
+At position 676 to 762, the domain is characterized as Ig-like C2-type 7.
+At position 843 to 1173, the domain is characterized as Protein kinase.
+At position 4 to 140, the domain is characterized as MPN.
+At position 292 to 419, the domain is characterized as Ricin B-type lectin 1.
+At position 422 to 546, the domain is characterized as Ricin B-type lectin 2.
+At position 91 to 150, the domain is characterized as S4 RNA-binding.
+At position 104 to 227, the domain is characterized as MPN.
+At position 40 to 89, the domain is characterized as bHLH.
+At position 21 to 189, the domain is characterized as FAD-binding PCMH-type.
+At position 139 to 187, the domain is characterized as WAP.
+At position 614 to 682, the domain is characterized as HP.
+At position 869 to 1013, the domain is characterized as TIR.
+At position 14 to 209, the domain is characterized as HORMA.
+At position 1 to 67, the domain is characterized as Plastocyanin-like 1.
+At position 79 to 238, the domain is characterized as Plastocyanin-like 2.
+At position 354 to 488, the domain is characterized as Plastocyanin-like 3.
+At position 153 to 190, the domain is characterized as LDL-receptor class A.
+At position 203 to 436, the domain is characterized as Peptidase S1 1.
+At position 504 to 736, the domain is characterized as Peptidase S1 2.
+At position 827 to 1058, the domain is characterized as Peptidase S1 3.
+At position 49 to 470, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 973 to 1277, the domain is characterized as PKS/mFAS DH.
+At position 2452 to 2529, the domain is characterized as Carrier.
+At position 41 to 72, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 140 to 172, the domain is characterized as 4Fe-4S ferredoxin-type 4.
+At position 17 to 61, the domain is characterized as Histone-fold.
+At position 159 to 310, the domain is characterized as Plastocyanin-like 2.
+At position 419 to 554, the domain is characterized as Plastocyanin-like 3.
+At position 9 to 128, the domain is characterized as MATH.
+At position 47 to 279, the domain is characterized as FAD-binding PCMH-type.
+At position 655 to 687, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 262 to 443, the domain is characterized as Helicase ATP-binding.
+At position 480 to 659, the domain is characterized as Helicase C-terminal.
+At position 452 to 524, the domain is characterized as ACT.
+At position 2 to 172, the domain is characterized as PRELI/MSF1.
+At position 1271 to 1289, the domain is characterized as WH2.
+At position 58 to 574, the domain is characterized as Protein kinase.
+At position 174 to 278, the domain is characterized as Fe2OG dioxygenase.
+At position 91 to 341, the domain is characterized as ABC transporter 1.
+At position 786 to 1029, the domain is characterized as ABC transporter 2.
+At position 72 to 299, the domain is characterized as Radical SAM core.
+At position 502 to 746, the domain is characterized as PNPLA.
+At position 30 to 245, the domain is characterized as GH16.
+At position 191 to 450, the domain is characterized as MHD.
+At position 179 to 244, the domain is characterized as HTH luxR-type.
+At position 243 to 479, the domain is characterized as Helicase C-terminal.
+At position 416 to 451, the domain is characterized as UVR.
+At position 51 to 108, the domain is characterized as TRAM.
+At position 9 to 102, the domain is characterized as RRM 1.
+At position 114 to 192, the domain is characterized as RRM 2.
+At position 222 to 294, the domain is characterized as RRM 3.
+At position 260 to 427, the domain is characterized as GATase cobBQ-type.
+At position 68 to 215, the domain is characterized as SCP.
+At position 117 to 233, the domain is characterized as C2 1.
+At position 245 to 360, the domain is characterized as C2 2.
+At position 26 to 106, the domain is characterized as UPAR/Ly6.
+At position 282 to 448, the domain is characterized as Helicase ATP-binding.
+At position 545 to 699, the domain is characterized as Helicase C-terminal.
+At position 426 to 569, the domain is characterized as FH1.
+At position 621 to 1009, the domain is characterized as FH2.
+At position 1037 to 1052, the domain is characterized as WH2.
+At position 79 to 194, the domain is characterized as MTTase N-terminal.
+At position 218 to 475, the domain is characterized as Radical SAM core.
+At position 478 to 543, the domain is characterized as TRAM.
+At position 464 to 499, the domain is characterized as EF-hand.
+At position 162 to 240, the domain is characterized as RRM 2.
+At position 341 to 413, the domain is characterized as RRM 3.
+At position 7 to 133, the domain is characterized as VOC.
+At position 972 to 1007, the domain is characterized as EF-hand 2.
+At position 154 to 198, the domain is characterized as CHCH.
+At position 147 to 275, the domain is characterized as VOC 2.
+At position 1 to 42, the domain is characterized as SH2.
+At position 66 to 321, the domain is characterized as Protein kinase.
+At position 236 to 405, the domain is characterized as tr-type G.
+At position 611 to 737, the domain is characterized as C2.
+At position 255 to 308, the domain is characterized as Laminin EGF-like 1.
+At position 311 to 371, the domain is characterized as Laminin EGF-like 2.
+At position 374 to 421, the domain is characterized as Laminin EGF-like 3.
+At position 18 to 351, the domain is characterized as Protein kinase.
+At position 154 to 234, the domain is characterized as Ubiquitin-like.
+At position 256 to 336, the domain is characterized as BAG.
+At position 196 to 259, the domain is characterized as bZIP.
+At position 34 to 108, the domain is characterized as H15.
+At position 107 to 370, the domain is characterized as Protein kinase.
+At position 402 to 516, the domain is characterized as Plastocyanin-like 3.
+At position 64 to 135, the domain is characterized as KRAB.
+At position 3 to 174, the domain is characterized as 3'-5' exonuclease.
+At position 213 to 294, the domain is characterized as HRDC.
+At position 207 to 307, the domain is characterized as Fe2OG dioxygenase.
+At position 29 to 81, the domain is characterized as BPTI/Kunitz inhibitor 1.
+At position 83 to 141, the domain is characterized as BPTI/Kunitz inhibitor 2.
+At position 33 to 228, the domain is characterized as GH11.
+At position 251 to 371, the domain is characterized as CBM6 1.
+At position 388 to 508, the domain is characterized as CBM6 2.
+At position 58 to 146, the domain is characterized as BRCT 1.
+At position 266 to 347, the domain is characterized as BRCT 2.
+At position 104 to 389, the domain is characterized as ABC transmembrane type-1 1.
+At position 457 to 678, the domain is characterized as ABC transporter 1.
+At position 765 to 1046, the domain is characterized as ABC transmembrane type-1 2.
+At position 1083 to 1316, the domain is characterized as ABC transporter 2.
+At position 15 to 236, the domain is characterized as Radical SAM core.
+At position 8 to 93, the domain is characterized as Core-binding (CB).
+At position 114 to 318, the domain is characterized as Tyr recombinase.
+At position 1 to 98, the domain is characterized as PTS EIIB type-2.
+At position 123 to 456, the domain is characterized as PTS EIIC type-2.
+At position 504 to 649, the domain is characterized as PTS EIIA type-2.
+At position 109 to 141, the domain is characterized as EF-hand 3.
+At position 66 to 284, the domain is characterized as Radical SAM core.
+At position 336 to 421, the domain is characterized as OCT.
+At position 384 to 439, the domain is characterized as DEK-C.
+At position 24 to 367, the domain is characterized as GH18.
+At position 94 to 163, the domain is characterized as PRC barrel.
+At position 166 to 360, the domain is characterized as CheB-type methylesterase.
+At position 185 to 217, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 224 to 375, the domain is characterized as TrmE-type G.
+At position 93 to 177, the domain is characterized as Saposin B-type.
+At position 88 to 218, the domain is characterized as PLAT.
+At position 225 to 924, the domain is characterized as Lipoxygenase.
+At position 3 to 397, the domain is characterized as BRO1.
+At position 25 to 86, the domain is characterized as Chitin-binding type R&R.
+At position 241 to 371, the domain is characterized as Nudix hydrolase.
+At position 99 to 773, the domain is characterized as Myosin motor.
+At position 123 to 302, the domain is characterized as SMP-LTD.
+At position 301 to 421, the domain is characterized as C2 1.
+At position 446 to 592, the domain is characterized as C2 2.
+At position 741 to 863, the domain is characterized as C2 3.
+At position 39 to 168, the domain is characterized as Guanylate cyclase.
+At position 811 to 904, the domain is characterized as Fibronectin type-III 6.
+At position 97 to 266, the domain is characterized as CRAL-TRIO.
+At position 34 to 108, the domain is characterized as KRAB.
+At position 14 to 74, the domain is characterized as Sushi 1.
+At position 75 to 136, the domain is characterized as Sushi 2.
+At position 137 to 201, the domain is characterized as Sushi 3.
+At position 202 to 260, the domain is characterized as Sushi 4.
+At position 261 to 326, the domain is characterized as Sushi 5.
+At position 327 to 388, the domain is characterized as Sushi 6.
+At position 389 to 445, the domain is characterized as Sushi 7.
+At position 446 to 503, the domain is characterized as Sushi 8.
+At position 220 to 264, the domain is characterized as bZIP.
+At position 285 to 499, the domain is characterized as DOG1.
+At position 1 to 46, the domain is characterized as PDZ 1.
+At position 90 to 178, the domain is characterized as PDZ 2.
+At position 312 to 460, the domain is characterized as Helicase C-terminal.
+At position 316 to 565, the domain is characterized as Clu.
+At position 13 to 688, the domain is characterized as Myosin motor.
+At position 691 to 720, the domain is characterized as IQ.
+At position 1155 to 1313, the domain is characterized as MyTH4 1.
+At position 1318 to 1620, the domain is characterized as FERM 1.
+At position 1618 to 1678, the domain is characterized as SH3.
+At position 1894 to 2051, the domain is characterized as MyTH4 2.
+At position 2060 to 2357, the domain is characterized as FERM 2.
+At position 757 to 845, the domain is characterized as Death.
+At position 162 to 533, the domain is characterized as GRAS.
+At position 87 to 224, the domain is characterized as Plastocyanin-like 1.
+At position 494 to 621, the domain is characterized as Plastocyanin-like 2.
+At position 292 to 358, the domain is characterized as Mop.
+At position 1170 to 1292, the domain is characterized as N-terminal Ras-GEF.
+At position 1339 to 1564, the domain is characterized as Ras-GEF.
+At position 21 to 141, the domain is characterized as Ig-like V-type.
+At position 152 to 239, the domain is characterized as Ig-like C2-type 1.
+At position 242 to 339, the domain is characterized as Ig-like C2-type 2.
+At position 182 to 245, the domain is characterized as R3H.
+At position 308 to 400, the domain is characterized as PH.
+At position 424 to 546, the domain is characterized as Arf-GAP.
+At position 896 to 958, the domain is characterized as SH3.
+At position 1 to 74, the domain is characterized as Peptidase M12B.
+At position 83 to 164, the domain is characterized as Disintegrin.
+At position 165 to 205, the domain is characterized as TSP type-1.
+At position 18 to 82, the domain is characterized as HMA.
+At position 9 to 43, the domain is characterized as WW.
+At position 57 to 170, the domain is characterized as PpiC.
+At position 2 to 45, the domain is characterized as CHCH.
+At position 46 to 82, the domain is characterized as LDL-receptor class A 1.
+At position 85 to 123, the domain is characterized as LDL-receptor class A 2.
+At position 126 to 164, the domain is characterized as LDL-receptor class A 3.
+At position 166 to 202, the domain is characterized as LDL-receptor class A 4.
+At position 205 to 246, the domain is characterized as LDL-receptor class A 5.
+At position 258 to 295, the domain is characterized as LDL-receptor class A 6.
+At position 298 to 334, the domain is characterized as LDL-receptor class A 7.
+At position 336 to 375, the domain is characterized as EGF-like 1.
+At position 376 to 415, the domain is characterized as EGF-like 2; calcium-binding.
+At position 45 to 129, the domain is characterized as GST N-terminal.
+At position 177 to 344, the domain is characterized as GST C-terminal.
+At position 63 to 483, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 961 to 1244, the domain is characterized as PKS/mFAS DH.
+At position 2447 to 2525, the domain is characterized as Carrier.
+At position 1266 to 1338, the domain is characterized as MIB/HERC2.
+At position 2151 to 2610, the domain is characterized as HECT.
+At position 219 to 377, the domain is characterized as TrmE-type G.
+At position 8 to 155, the domain is characterized as N-acetyltransferase 1.
+At position 160 to 308, the domain is characterized as N-acetyltransferase 2.
+At position 970 to 1029, the domain is characterized as SH3.
+At position 2265 to 2300, the domain is characterized as EF-hand 1.
+At position 2308 to 2343, the domain is characterized as EF-hand 2.
+At position 9 to 150, the domain is characterized as N-acetyltransferase.
+At position 88 to 276, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 197, the domain is characterized as IF rod.
+At position 7 to 171, the domain is characterized as TIR.
+At position 185 to 413, the domain is characterized as NB-ARC.
+At position 434 to 486, the domain is characterized as BRX 1.
+At position 538 to 594, the domain is characterized as BRX 2.
+At position 719 to 772, the domain is characterized as BRX 3.
+At position 171 to 251, the domain is characterized as Expansin-like CBD.
+At position 29 to 196, the domain is characterized as UBC core.
+At position 64 to 98, the domain is characterized as Collagen-like.
+At position 90 to 446, the domain is characterized as IF rod.
+At position 504 to 618, the domain is characterized as LTD.
+At position 1 to 336, the domain is characterized as Trm1 methyltransferase.
+At position 29 to 262, the domain is characterized as Reverse transcriptase.
+At position 73 to 232, the domain is characterized as CP-type G.
+At position 444 to 508, the domain is characterized as R3H.
+At position 510 to 576, the domain is characterized as SUZ.
+At position 104 to 395, the domain is characterized as Protein kinase.
+At position 9 to 192, the domain is characterized as Miro 1.
+At position 441 to 604, the domain is characterized as Miro 2.
+At position 234 to 274, the domain is characterized as P-type.
+At position 279 to 553, the domain is characterized as ZP.
+At position 143 to 188, the domain is characterized as Pre-SET.
+At position 191 to 323, the domain is characterized as SET.
+At position 334 to 350, the domain is characterized as Post-SET.
+At position 268 to 600, the domain is characterized as USP.
+At position 69 to 140, the domain is characterized as KRAB.
+At position 140 to 175, the domain is characterized as EF-hand 4.
+At position 197 to 349, the domain is characterized as GST C-terminal.
+At position 158 to 481, the domain is characterized as NACHT.
+At position 665 to 692, the domain is characterized as LRRNT.
+At position 904 to 968, the domain is characterized as LRRCT.
+At position 1702 to 1850, the domain is characterized as MyTH4 2.
+At position 1856 to 2159, the domain is characterized as FERM 2.
+At position 10 to 63, the domain is characterized as HTH merR-type.
+At position 338 to 1053, the domain is characterized as Myosin motor.
+At position 1055 to 1084, the domain is characterized as IQ 1.
+At position 1082 to 1111, the domain is characterized as IQ 2.
+At position 1346 to 1375, the domain is characterized as IQ 3.
+At position 262 to 339, the domain is characterized as PUA.
+At position 250 to 300, the domain is characterized as DHHC.
+At position 5 to 144, the domain is characterized as Flavodoxin-like.
+At position 36 to 112, the domain is characterized as Inhibitor I9.
+At position 124 to 395, the domain is characterized as Peptidase S8.
+At position 31 to 226, the domain is characterized as Velvet.
+At position 67 to 231, the domain is characterized as Laminin G-like.
+At position 275 to 334, the domain is characterized as VWFC 1.
+At position 400 to 442, the domain is characterized as EGF-like 1.
+At position 443 to 484, the domain is characterized as EGF-like 2; calcium-binding.
+At position 485 to 525, the domain is characterized as EGF-like 3; calcium-binding.
+At position 526 to 556, the domain is characterized as EGF-like 4.
+At position 558 to 604, the domain is characterized as EGF-like 5; calcium-binding.
+At position 605 to 640, the domain is characterized as EGF-like 6; calcium-binding.
+At position 701 to 759, the domain is characterized as VWFC 2.
+At position 13 to 436, the domain is characterized as GRAS.
+At position 460 to 563, the domain is characterized as Pre-SET.
+At position 566 to 696, the domain is characterized as SET.
+At position 707 to 723, the domain is characterized as Post-SET.
+At position 418 to 481, the domain is characterized as bZIP.
+At position 241 to 351, the domain is characterized as Glutaredoxin.
+At position 85 to 260, the domain is characterized as Helicase ATP-binding.
+At position 272 to 433, the domain is characterized as Helicase C-terminal.
+At position 50 to 289, the domain is characterized as Ras-GEF.
+At position 459 to 571, the domain is characterized as PH.
+At position 355 to 565, the domain is characterized as PPM-type phosphatase.
+At position 27 to 128, the domain is characterized as SRCR 1.
+At position 141 to 241, the domain is characterized as SRCR 2.
+At position 246 to 348, the domain is characterized as SRCR 3.
+At position 20 to 52, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 53 to 83, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 272 to 331, the domain is characterized as SH3.
+At position 13 to 137, the domain is characterized as EamA 1.
+At position 164 to 394, the domain is characterized as AIG1-type G.
+At position 6 to 235, the domain is characterized as Radical SAM core.
+At position 19 to 298, the domain is characterized as Septin-type G.
+At position 37 to 107, the domain is characterized as PAH 1.
+At position 153 to 238, the domain is characterized as PAH 2.
+At position 292 to 369, the domain is characterized as PAH 3.
+At position 116 to 332, the domain is characterized as ATP-grasp.
+At position 9 to 173, the domain is characterized as NAC.
+At position 38 to 102, the domain is characterized as SH3.
+At position 124 to 401, the domain is characterized as Protein kinase.
+At position 117 to 136, the domain is characterized as HhH.
+At position 343 to 449, the domain is characterized as Calponin-homology (CH).
+At position 391 to 821, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1309 to 1621, the domain is characterized as PKS/mFAS DH.
+At position 1698 to 1775, the domain is characterized as Carrier.
+At position 95 to 209, the domain is characterized as NlpC/P60.
+At position 156 to 209, the domain is characterized as SANT.
+At position 166 to 346, the domain is characterized as Protein kinase.
+At position 7 to 236, the domain is characterized as ABC transporter.
+At position 535 to 610, the domain is characterized as Carrier.
+At position 70 to 205, the domain is characterized as N-acetyltransferase.
+At position 411 to 507, the domain is characterized as Fibronectin type-III.
+At position 273 to 341, the domain is characterized as Collagen-like.
+At position 350 to 450, the domain is characterized as SRCR.
+At position 926 to 1213, the domain is characterized as CNH.
+At position 34 to 713, the domain is characterized as Myosin motor.
+At position 769 to 959, the domain is characterized as TH1.
+At position 1103 to 1165, the domain is characterized as SH3.
+At position 658 to 725, the domain is characterized as S1 motif.
+At position 127 to 297, the domain is characterized as tr-type G.
+At position 13 to 91, the domain is characterized as Ubiquitin-like.
+At position 1354 to 1498, the domain is characterized as Nudix hydrolase.
+At position 171 to 262, the domain is characterized as PPIase FKBP-type.
+At position 25 to 99, the domain is characterized as Importin N-terminal.
+At position 135 to 366, the domain is characterized as tr-type G.
+At position 391 to 557, the domain is characterized as N-acetyltransferase.
+At position 1193 to 1317, the domain is characterized as C2 1.
+At position 1627 to 1770, the domain is characterized as MHD1.
+At position 1876 to 2018, the domain is characterized as MHD2.
+At position 2032 to 2159, the domain is characterized as C2 2.
+At position 3 to 410, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 7 to 163, the domain is characterized as Thioredoxin.
+At position 18 to 161, the domain is characterized as Clp R.
+At position 460 to 495, the domain is characterized as UVR.
+At position 33 to 180, the domain is characterized as CBM-cenC 1.
+At position 189 to 538, the domain is characterized as GH10.
+At position 565 to 714, the domain is characterized as CBM-cenC 2.
+At position 728 to 796, the domain is characterized as Dockerin.
+At position 453 to 527, the domain is characterized as ACT.
+At position 948 to 1084, the domain is characterized as MGS-like.
+At position 52 to 217, the domain is characterized as FAD-binding PCMH-type.
+At position 111 to 251, the domain is characterized as PA14.
+At position 284 to 320, the domain is characterized as CBM1.
+At position 52 to 362, the domain is characterized as AB hydrolase-1.
+At position 250 to 306, the domain is characterized as bHLH.
+At position 43 to 222, the domain is characterized as FAD-binding PCMH-type.
+At position 24 to 210, the domain is characterized as GH11.
+At position 33 to 160, the domain is characterized as ALOG.
+At position 7 to 62, the domain is characterized as Myosin N-terminal SH3-like.
+At position 73 to 766, the domain is characterized as Myosin motor.
+At position 793 to 813, the domain is characterized as IQ 1.
+At position 818 to 838, the domain is characterized as IQ 2.
+At position 840 to 865, the domain is characterized as IQ 3.
+At position 866 to 886, the domain is characterized as IQ 4.
+At position 888 to 917, the domain is characterized as IQ 5.
+At position 1163 to 1431, the domain is characterized as Dilute.
+At position 7 to 53, the domain is characterized as SpoVT-AbrB 1.
+At position 488 to 761, the domain is characterized as Protein kinase.
+At position 1 to 40, the domain is characterized as Cadherin 1.
+At position 41 to 146, the domain is characterized as Cadherin 2.
+At position 147 to 248, the domain is characterized as Cadherin 3.
+At position 253 to 371, the domain is characterized as Cadherin 4.
+At position 453 to 511, the domain is characterized as EGF-like 1; calcium-binding.
+At position 513 to 549, the domain is characterized as EGF-like 2; calcium-binding.
+At position 553 to 591, the domain is characterized as EGF-like 3; calcium-binding.
+At position 592 to 796, the domain is characterized as Laminin G-like 1.
+At position 799 to 835, the domain is characterized as EGF-like 4; calcium-binding.
+At position 839 to 1016, the domain is characterized as Laminin G-like 2.
+At position 1018 to 1053, the domain is characterized as EGF-like 5; calcium-binding.
+At position 1054 to 1092, the domain is characterized as EGF-like 6; calcium-binding.
+At position 1108 to 1147, the domain is characterized as EGF-like 7; calcium-binding.
+At position 1149 to 1196, the domain is characterized as Laminin EGF-like.
+At position 1541 to 1593, the domain is characterized as GPS.
+At position 513 to 871, the domain is characterized as PUM-HD.
+At position 20 to 310, the domain is characterized as ABC transmembrane type-1.
+At position 130 to 238, the domain is characterized as CUB.
+At position 237 to 274, the domain is characterized as EGF-like.
+At position 280 to 346, the domain is characterized as Sushi 1.
+At position 393 to 446, the domain is characterized as Sushi 2.
+At position 447 to 722, the domain is characterized as Peptidase S1.
+At position 9 to 44, the domain is characterized as WW.
+At position 68 to 243, the domain is characterized as NodB homology.
+At position 338 to 565, the domain is characterized as PRORP.
+At position 131 to 421, the domain is characterized as ABC transmembrane type-1.
+At position 1 to 284, the domain is characterized as PTS EIIC type-1; first part.
+At position 479 to 630, the domain is characterized as PTS EIIC type-1; second part.
+At position 661 to 743, the domain is characterized as PTS EIIB type-1.
+At position 794 to 907, the domain is characterized as PTS EIIA type-1.
+At position 81 to 116, the domain is characterized as EF-hand 1.
+At position 135 to 152, the domain is characterized as EF-hand 2.
+At position 158 to 193, the domain is characterized as EF-hand 3.
+At position 195 to 226, the domain is characterized as EF-hand 4.
+At position 1084 to 1266, the domain is characterized as Ferric oxidoreductase.
+At position 1267 to 1373, the domain is characterized as FAD-binding FR-type.
+At position 59 to 241, the domain is characterized as FAD-binding PCMH-type.
+At position 32 to 95, the domain is characterized as HMA 1.
+At position 133 to 204, the domain is characterized as HMA 2.
+At position 167 to 301, the domain is characterized as ZU5 1.
+At position 302 to 483, the domain is characterized as ZU5 2.
+At position 679 to 764, the domain is characterized as Death.
+At position 74 to 313, the domain is characterized as GB1/RHD3-type G.
+At position 304 to 895, the domain is characterized as USP.
+At position 172 to 260, the domain is characterized as GAT.
+At position 36 to 265, the domain is characterized as Radical SAM core.
+At position 2 to 101, the domain is characterized as Thioredoxin.
+At position 53 to 150, the domain is characterized as SRCR.
+At position 825 to 883, the domain is characterized as TSP type-1 2.
+At position 884 to 945, the domain is characterized as TSP type-1 3.
+At position 947 to 1001, the domain is characterized as TSP type-1 4.
+At position 1003 to 1058, the domain is characterized as TSP type-1 5.
+At position 1065 to 1103, the domain is characterized as PLAC.
+At position 21 to 139, the domain is characterized as CBM6.
+At position 163 to 457, the domain is characterized as GH26.
+At position 489 to 525, the domain is characterized as CBM10 1.
+At position 532 to 569, the domain is characterized as CBM10 2.
+At position 59 to 117, the domain is characterized as Tudor 1.
+At position 289 to 347, the domain is characterized as Tudor 2.
+At position 531 to 589, the domain is characterized as Tudor 3.
+At position 799 to 856, the domain is characterized as Tudor 4.
+At position 1011 to 1070, the domain is characterized as Tudor 5.
+At position 1342 to 1401, the domain is characterized as Tudor 6.
+At position 1574 to 1633, the domain is characterized as Tudor 7.
+At position 1780 to 1838, the domain is characterized as Tudor 8.
+At position 246 to 571, the domain is characterized as Protein kinase.
+At position 477 to 689, the domain is characterized as BURP.
+At position 129 to 167, the domain is characterized as LRRCT.
+At position 179 to 257, the domain is characterized as RRM.
+At position 29 to 112, the domain is characterized as Kringle.
+At position 114 to 208, the domain is characterized as WSC.
+At position 212 to 319, the domain is characterized as CUB.
+At position 27 to 90, the domain is characterized as HMA.
+At position 87 to 151, the domain is characterized as SLH.
+At position 46 to 91, the domain is characterized as F-box.
+At position 22 to 213, the domain is characterized as GH16.
+At position 35 to 64, the domain is characterized as LRRNT.
+At position 362 to 416, the domain is characterized as LRRCT.
+At position 404 to 508, the domain is characterized as Ig-like C2-type.
+At position 41 to 233, the domain is characterized as Lon N-terminal.
+At position 627 to 811, the domain is characterized as Lon proteolytic.
+At position 53 to 155, the domain is characterized as Plastocyanin-like.
+At position 183 to 278, the domain is characterized as RRM 1.
+At position 285 to 362, the domain is characterized as RRM 2.
+At position 760 to 843, the domain is characterized as Smr.
+At position 458 to 649, the domain is characterized as FtsK.
+At position 365 to 424, the domain is characterized as DDT.
+At position 59 to 91, the domain is characterized as LisH.
+At position 3 to 322, the domain is characterized as Asparaginase/glutaminase.
+At position 19 to 153, the domain is characterized as MPN.
+At position 1410 to 1824, the domain is characterized as DOCKER.
+At position 117 to 238, the domain is characterized as OmpA-like.
+At position 14 to 335, the domain is characterized as DOT1.
+At position 12 to 149, the domain is characterized as B12-binding.
+At position 177 to 278, the domain is characterized as PpiC 1.
+At position 287 to 386, the domain is characterized as PpiC 2.
+At position 542 to 702, the domain is characterized as GGDEF.
+At position 25 to 181, the domain is characterized as N-acetyltransferase.
+At position 99 to 118, the domain is characterized as UIM 1.
+At position 127 to 148, the domain is characterized as UIM 2; degenerate.
+At position 160 to 220, the domain is characterized as LIM zinc-binding.
+At position 3 to 119, the domain is characterized as PH.
+At position 61 to 247, the domain is characterized as Reticulon.
+At position 27 to 131, the domain is characterized as Expansin-like EG45; incomplete.
+At position 251 to 356, the domain is characterized as RRM 1.
+At position 373 to 444, the domain is characterized as RRM 2.
+At position 56 to 330, the domain is characterized as Dynamin-type G.
+At position 670 to 761, the domain is characterized as GED.
+At position 461 to 853, the domain is characterized as G-alpha.
+At position 12 to 161, the domain is characterized as UEV.
+At position 322 to 385, the domain is characterized as SB.
+At position 60 to 362, the domain is characterized as PPM-type phosphatase.
+At position 133 to 215, the domain is characterized as RCK C-terminal.
+At position 285 to 344, the domain is characterized as SH3 1.
+At position 347 to 402, the domain is characterized as SH3 2.
+At position 424 to 586, the domain is characterized as YDG.
+At position 58 to 190, the domain is characterized as Cupin type-1.
+At position 470 to 641, the domain is characterized as tr-type G.
+At position 292 to 431, the domain is characterized as SIS 1.
+At position 501 to 608, the domain is characterized as CBM20.
+At position 144 to 301, the domain is characterized as DAC.
+At position 80 to 183, the domain is characterized as USP.
+At position 20 to 201, the domain is characterized as Helicase ATP-binding.
+At position 371 to 542, the domain is characterized as Helicase C-terminal.
+At position 571 to 667, the domain is characterized as Dicer dsRNA-binding fold.
+At position 845 to 1003, the domain is characterized as PAZ.
+At position 1381 to 1589, the domain is characterized as RNase III 1.
+At position 1643 to 1805, the domain is characterized as RNase III 2.
+At position 1833 to 1896, the domain is characterized as DRBM.
+At position 46 to 137, the domain is characterized as UPAR/Ly6.
+At position 538 to 715, the domain is characterized as W2.
+At position 155 to 256, the domain is characterized as HTH LytTR-type.
+At position 33 to 184, the domain is characterized as SIS.
+At position 196 to 395, the domain is characterized as Peptidase M12B.
+At position 611 to 643, the domain is characterized as EGF-like.
+At position 162 to 233, the domain is characterized as POTRA.
+At position 191 to 387, the domain is characterized as Peptidase M12B.
+At position 15 to 65, the domain is characterized as F-box.
+At position 361 to 413, the domain is characterized as FBD.
+At position 10 to 89, the domain is characterized as GST N-terminal.
+At position 73 to 213, the domain is characterized as GST C-terminal.
+At position 202 to 377, the domain is characterized as Helicase ATP-binding.
+At position 405 to 552, the domain is characterized as Helicase C-terminal.
+At position 69 to 366, the domain is characterized as Protein kinase.
+At position 971 to 1253, the domain is characterized as ABC transmembrane type-1 2.
+At position 1290 to 1524, the domain is characterized as ABC transporter 2.
+At position 26 to 205, the domain is characterized as Eph LBD.
+At position 442 to 536, the domain is characterized as Fibronectin type-III 2.
+At position 4 to 148, the domain is characterized as Jacalin-type lectin 1.
+At position 163 to 308, the domain is characterized as Jacalin-type lectin 2.
+At position 20 to 168, the domain is characterized as uDENN FLCN/SMCR8-type.
+At position 282 to 425, the domain is characterized as cDENN FLCN/SMCR8-type.
+At position 434 to 488, the domain is characterized as dDENN FLCN/SMCR8-type.
+At position 2305 to 2351, the domain is characterized as G-patch.
+At position 2371 to 2426, the domain is characterized as DRBM.
+At position 394 to 500, the domain is characterized as Calponin-homology (CH) 3.
+At position 515 to 623, the domain is characterized as Calponin-homology (CH) 4.
+At position 140 to 389, the domain is characterized as SMP-LTD.
+At position 32 to 89, the domain is characterized as VWFC.
+At position 4 to 128, the domain is characterized as TIR.
+At position 54 to 255, the domain is characterized as ABC transmembrane type-1.
+At position 48 to 215, the domain is characterized as FAD-binding PCMH-type.
+At position 295 to 583, the domain is characterized as Protein kinase.
+At position 67 to 132, the domain is characterized as Kazal-like 1.
+At position 133 to 197, the domain is characterized as Kazal-like 2.
+At position 198 to 263, the domain is characterized as Kazal-like 3.
+At position 264 to 329, the domain is characterized as Kazal-like 4.
+At position 330 to 394, the domain is characterized as Kazal-like 5.
+At position 395 to 460, the domain is characterized as Kazal-like 6.
+At position 461 to 517, the domain is characterized as Kazal-like 7.
+At position 42 to 140, the domain is characterized as Plastocyanin-like 1.
+At position 26 to 213, the domain is characterized as BPL/LPL catalytic.
+At position 119 to 291, the domain is characterized as Helicase ATP-binding.
+At position 111 to 181, the domain is characterized as BTB.
+At position 272 to 429, the domain is characterized as JmjC.
+At position 1 to 120, the domain is characterized as C2 1.
+At position 128 to 251, the domain is characterized as C2 2.
+At position 290 to 507, the domain is characterized as VWFA.
+At position 624 to 825, the domain is characterized as ATP-grasp.
+At position 141 to 440, the domain is characterized as NB-ARC.
+At position 142 to 275, the domain is characterized as TIR.
+At position 704 to 733, the domain is characterized as IQ 1.
+At position 728 to 748, the domain is characterized as IQ 2.
+At position 779 to 808, the domain is characterized as IQ 4.
+At position 4 to 168, the domain is characterized as 3'-5' exonuclease.
+At position 207 to 286, the domain is characterized as HRDC.
+At position 542 to 830, the domain is characterized as Protein kinase.
+At position 888 to 1018, the domain is characterized as Guanylate cyclase.
+At position 104 to 199, the domain is characterized as TAFH.
+At position 45 to 97, the domain is characterized as PISA.
+At position 1516 to 1795, the domain is characterized as Autotransporter.
+At position 56 to 215, the domain is characterized as PPIase cyclophilin-type.
+At position 89 to 279, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 445 to 700, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 22 to 172, the domain is characterized as Reelin.
+At position 111 to 149, the domain is characterized as EGF-like 1.
+At position 157 to 194, the domain is characterized as EGF-like 2.
+At position 196 to 232, the domain is characterized as EGF-like 3.
+At position 233 to 272, the domain is characterized as EGF-like 4.
+At position 357 to 495, the domain is characterized as FAS1 1.
+At position 507 to 642, the domain is characterized as FAS1 2.
+At position 729 to 769, the domain is characterized as EGF-like 5.
+At position 819 to 859, the domain is characterized as EGF-like 6.
+At position 862 to 904, the domain is characterized as EGF-like 7.
+At position 905 to 947, the domain is characterized as EGF-like 8.
+At position 948 to 987, the domain is characterized as EGF-like 9.
+At position 989 to 1119, the domain is characterized as FAS1 3.
+At position 1129 to 1254, the domain is characterized as FAS1 4.
+At position 1328 to 1393, the domain is characterized as Laminin EGF-like 1.
+At position 1417 to 1455, the domain is characterized as EGF-like 10.
+At position 1456 to 1497, the domain is characterized as EGF-like 11.
+At position 1498 to 1540, the domain is characterized as EGF-like 12.
+At position 1541 to 1583, the domain is characterized as EGF-like 13.
+At position 1583 to 1709, the domain is characterized as FAS1 5.
+At position 1725 to 1865, the domain is characterized as FAS1 6.
+At position 2208 to 2301, the domain is characterized as Link.
+At position 39 to 179, the domain is characterized as MATH.
+At position 205 to 536, the domain is characterized as USP.
+At position 53 to 462, the domain is characterized as GBD/FH3.
+At position 491 to 647, the domain is characterized as FH1.
+At position 648 to 1045, the domain is characterized as FH2.
+At position 1085 to 1166, the domain is characterized as DAD.
+At position 201 to 644, the domain is characterized as Myotubularin phosphatase.
+At position 23 to 71, the domain is characterized as WAP.
+At position 1 to 103, the domain is characterized as FAD-binding FR-type.
+At position 232 to 318, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 97 to 136, the domain is characterized as PDZ.
+At position 353 to 484, the domain is characterized as Plus3.
+At position 9 to 386, the domain is characterized as TTL.
+At position 58 to 111, the domain is characterized as bHLH.
+At position 152 to 222, the domain is characterized as PAS 1.
+At position 324 to 394, the domain is characterized as PAS 2.
+At position 342 to 619, the domain is characterized as Protein kinase.
+At position 21 to 105, the domain is characterized as Saposin B-type.
+At position 626 to 751, the domain is characterized as DBINO.
+At position 854 to 1026, the domain is characterized as Helicase ATP-binding.
+At position 1433 to 1591, the domain is characterized as Helicase C-terminal.
+At position 1 to 225, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 226 to 476, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 149 to 418, the domain is characterized as Collagen-like.
+At position 423 to 518, the domain is characterized as SRCR.
+At position 25 to 207, the domain is characterized as Plastocyanin-like 1.
+At position 379 to 561, the domain is characterized as Plastocyanin-like 3.
+At position 571 to 719, the domain is characterized as Plastocyanin-like 4.
+At position 731 to 907, the domain is characterized as Plastocyanin-like 5.
+At position 915 to 1092, the domain is characterized as Plastocyanin-like 6.
+At position 139 to 453, the domain is characterized as IF rod.
+At position 33 to 221, the domain is characterized as FAD-binding PCMH-type.
+At position 41 to 115, the domain is characterized as H15.
+At position 1 to 68, the domain is characterized as HTH merR-type.
+At position 19 to 80, the domain is characterized as HTH iclR-type.
+At position 95 to 266, the domain is characterized as IclR-ED.
+At position 182 to 382, the domain is characterized as Helicase ATP-binding.
+At position 416 to 614, the domain is characterized as Helicase C-terminal.
+At position 179 to 311, the domain is characterized as DOD-type homing endonuclease 1.
+At position 780 to 927, the domain is characterized as DOD-type homing endonuclease 2.
+At position 1348 to 1508, the domain is characterized as DOD-type homing endonuclease 3.
+At position 112 to 149, the domain is characterized as LRRNT.
+At position 69 to 175, the domain is characterized as Expansin-like EG45.
+At position 346 to 447, the domain is characterized as BRCT.
+At position 31 to 141, the domain is characterized as MTTase N-terminal.
+At position 158 to 397, the domain is characterized as Radical SAM core.
+At position 400 to 466, the domain is characterized as TRAM.
+At position 5 to 55, the domain is characterized as Kazal-like.
+At position 307 to 476, the domain is characterized as VWFA.
+At position 18 to 74, the domain is characterized as Kazal-like.
+At position 307 to 567, the domain is characterized as NR LBD.
+At position 209 to 284, the domain is characterized as SPOR.
+At position 66 to 213, the domain is characterized as Thioredoxin.
+At position 733 to 796, the domain is characterized as R3H.
+At position 40 to 315, the domain is characterized as Protein kinase.
+At position 765 to 993, the domain is characterized as MIF4G.
+At position 1429 to 1599, the domain is characterized as W2.
+At position 294 to 526, the domain is characterized as Glutamine amidotransferase type-1.
+At position 85 to 352, the domain is characterized as Calpain catalytic.
+At position 520 to 545, the domain is characterized as KOW.
+At position 157 to 274, the domain is characterized as C2.
+At position 172 to 364, the domain is characterized as Glutamine amidotransferase type-1.
+At position 65 to 429, the domain is characterized as PRONE.
+At position 135 to 394, the domain is characterized as Tyrosine-protein phosphatase 1.
+At position 426 to 689, the domain is characterized as Tyrosine-protein phosphatase 2.
+At position 688 to 787, the domain is characterized as BRCT 1.
+At position 845 to 945, the domain is characterized as BRCT 2.
+At position 2 to 164, the domain is characterized as Thioredoxin.
+At position 55 to 102, the domain is characterized as TSP type-1 1.
+At position 109 to 155, the domain is characterized as TSP type-1 2.
+At position 47 to 359, the domain is characterized as AB hydrolase-1.
+At position 101 to 221, the domain is characterized as PX.
+At position 92 to 352, the domain is characterized as Lon N-terminal.
+At position 773 to 960, the domain is characterized as Lon proteolytic.
+At position 34 to 257, the domain is characterized as Radical SAM core.
+At position 110 to 198, the domain is characterized as Cytochrome c 1.
+At position 132 to 398, the domain is characterized as NR LBD.
+At position 645 to 758, the domain is characterized as Calponin-homology (CH).
+At position 11 to 147, the domain is characterized as VIT.
+At position 354 to 525, the domain is characterized as VWFA.
+At position 1317 to 1527, the domain is characterized as MIF4G.
+At position 1760 to 1882, the domain is characterized as MI.
+At position 306 to 536, the domain is characterized as Glutamine amidotransferase type-1.
+At position 400 to 474, the domain is characterized as DEP.
+At position 242 to 340, the domain is characterized as Fibronectin type-III.
+At position 212 to 276, the domain is characterized as SH3b 1.
+At position 278 to 342, the domain is characterized as SH3b 2.
+At position 138 to 225, the domain is characterized as PPIase FKBP-type.
+At position 85 to 289, the domain is characterized as ABC transmembrane type-1.
+At position 310 to 586, the domain is characterized as ABC transporter 1.
+At position 343 to 417, the domain is characterized as ACT-like.
+At position 21 to 180, the domain is characterized as N-acetyltransferase.
+At position 6 to 56, the domain is characterized as Tudor-knot.
+At position 166 to 336, the domain is characterized as MRG.
+At position 116 to 244, the domain is characterized as Thioredoxin.
+At position 166 to 273, the domain is characterized as TBDR plug.
+At position 278 to 809, the domain is characterized as TBDR beta-barrel.
+At position 110 to 140, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 263 to 322, the domain is characterized as SH3 2.
+At position 173 to 611, the domain is characterized as PPM-type phosphatase.
+At position 332 to 385, the domain is characterized as bHLH.
+At position 73 to 171, the domain is characterized as PA.
+At position 131 to 204, the domain is characterized as SUI1.
+At position 344 to 514, the domain is characterized as tr-type G.
+At position 207 to 282, the domain is characterized as EMI.
+At position 1041 to 1077, the domain is characterized as EGF-like.
+At position 1096 to 1228, the domain is characterized as C1q.
+At position 79 to 169, the domain is characterized as Fibronectin type-III.
+At position 167 to 256, the domain is characterized as BRCT.
+At position 359 to 594, the domain is characterized as NR LBD.
+At position 1 to 483, the domain is characterized as SMP-LTD.
+At position 286 to 405, the domain is characterized as sHSP.
+At position 115 to 402, the domain is characterized as IF rod.
+At position 141 to 318, the domain is characterized as Helicase ATP-binding.
+At position 342 to 492, the domain is characterized as Helicase C-terminal.
+At position 98 to 423, the domain is characterized as Protein kinase.
+At position 25 to 193, the domain is characterized as FAD-binding PCMH-type.
+At position 174 to 316, the domain is characterized as PPC.
+At position 280 to 561, the domain is characterized as ABC transmembrane type-1 1.
+At position 594 to 818, the domain is characterized as ABC transporter 1.
+At position 1010 to 1308, the domain is characterized as ABC transmembrane type-1 2.
+At position 17 to 120, the domain is characterized as AB hydrolase-1.
+At position 478 to 513, the domain is characterized as EF-hand 4.
+At position 47 to 161, the domain is characterized as FAD-binding FR-type.
+At position 208 to 270, the domain is characterized as PQ-loop 2.
+At position 1399 to 1944, the domain is characterized as FAT.
+At position 2049 to 2352, the domain is characterized as PI3K/PI4K catalytic.
+At position 2336 to 2368, the domain is characterized as FATC.
+At position 163 to 237, the domain is characterized as PUA.
+At position 5 to 293, the domain is characterized as Prephenate/arogenate dehydrogenase.
+At position 8 to 51, the domain is characterized as CUE 1.
+At position 55 to 98, the domain is characterized as CUE 2.
+At position 347 to 443, the domain is characterized as Smr.
+At position 335 to 395, the domain is characterized as S4 RNA-binding.
+At position 32 to 353, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 289 to 399, the domain is characterized as BEN.
+At position 35 to 327, the domain is characterized as Protein kinase.
+At position 235 to 429, the domain is characterized as Peptidase M12B.
+At position 438 to 522, the domain is characterized as Disintegrin.
+At position 663 to 697, the domain is characterized as EGF-like.
+At position 173 to 218, the domain is characterized as LysM.
+At position 324 to 599, the domain is characterized as Protein kinase.
+At position 1132 to 1265, the domain is characterized as DOD-type homing endonuclease 2.
+At position 138 to 392, the domain is characterized as NR LBD.
+At position 69 to 309, the domain is characterized as Lon N-terminal.
+At position 308 to 416, the domain is characterized as CULT.
+At position 10 to 280, the domain is characterized as tr-type G.
+At position 57 to 245, the domain is characterized as RNase H type-2.
+At position 191 to 360, the domain is characterized as tr-type G.
+At position 413 to 519, the domain is characterized as Fe2OG dioxygenase.
+At position 100 to 255, the domain is characterized as N-acetyltransferase.
+At position 344 to 414, the domain is characterized as Bromo.
+At position 6 to 226, the domain is characterized as BAR.
+At position 17 to 194, the domain is characterized as DHFR.
+At position 40 to 168, the domain is characterized as N-acetylmuramoyl-L-alanine amidase.
+At position 2 to 118, the domain is characterized as Pru.
+At position 177 to 286, the domain is characterized as DEUBAD.
+At position 109 to 428, the domain is characterized as Deacetylase sirtuin-type.
+At position 389 to 560, the domain is characterized as tr-type G.
+At position 209 to 259, the domain is characterized as DHHC.
+At position 23 to 119, the domain is characterized as SH2.
+At position 131 to 386, the domain is characterized as Protein kinase.
+At position 95 to 165, the domain is characterized as Bromo.
+At position 363 to 520, the domain is characterized as CRAL-TRIO.
+At position 528 to 719, the domain is characterized as Rho-GAP.
+At position 339 to 628, the domain is characterized as Protein kinase.
+At position 27 to 115, the domain is characterized as SUEL-type lectin 1.
+At position 123 to 213, the domain is characterized as SUEL-type lectin 2.
+At position 218 to 308, the domain is characterized as SUEL-type lectin 3.
+At position 576 to 638, the domain is characterized as KH.
+At position 648 to 715, the domain is characterized as S1 motif.
+At position 292 to 578, the domain is characterized as ABC transmembrane type-1 1.
+At position 639 to 871, the domain is characterized as ABC transporter 1.
+At position 980 to 1265, the domain is characterized as ABC transmembrane type-1 2.
+At position 1302 to 1553, the domain is characterized as ABC transporter 2.
+At position 657 to 845, the domain is characterized as Rho-GAP.
+At position 29 to 359, the domain is characterized as G-alpha.
+At position 1485 to 1726, the domain is characterized as VLIG-type G.
+At position 15 to 210, the domain is characterized as AMMECR1.
+At position 202 to 254, the domain is characterized as VWFC.
+At position 39 to 295, the domain is characterized as Fe/B12 periplasmic-binding.
+At position 222 to 489, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 1 to 17, the domain is characterized as Ubiquitin-like.
+At position 34 to 68, the domain is characterized as SAP.
+At position 162 to 314, the domain is characterized as PINIT.
+At position 301 to 471, the domain is characterized as Helicase ATP-binding.
+At position 656 to 818, the domain is characterized as Helicase C-terminal.
+At position 401 to 817, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1243 to 1552, the domain is characterized as PKS/mFAS DH.
+At position 1597 to 1671, the domain is characterized as Carrier.
+At position 219 to 296, the domain is characterized as TFIIS N-terminal.
+At position 242 to 317, the domain is characterized as Ig-like C2-type 2.
+At position 20 to 151, the domain is characterized as CMP/dCMP-type deaminase 1.
+At position 181 to 293, the domain is characterized as CMP/dCMP-type deaminase 2.
+At position 18 to 248, the domain is characterized as Radical SAM core.
+At position 1901 to 1930, the domain is characterized as IQ.
+At position 185 to 394, the domain is characterized as Galectin.
+At position 115 to 233, the domain is characterized as SET.
+At position 93 to 169, the domain is characterized as PRC barrel.
+At position 52 to 335, the domain is characterized as Protein kinase.
+At position 387 to 448, the domain is characterized as PAP-associated.
+At position 50 to 99, the domain is characterized as bHLH.
+At position 10 to 60, the domain is characterized as HTH cro/C1-type.
+At position 232 to 374, the domain is characterized as VLRF1.
+At position 34 to 118, the domain is characterized as Doublecortin 1.
+At position 118 to 196, the domain is characterized as PRC barrel.
+At position 258 to 588, the domain is characterized as Kinesin motor.
+At position 75 to 214, the domain is characterized as Nudix hydrolase.
+At position 416 to 567, the domain is characterized as Thioredoxin.
+At position 290 to 368, the domain is characterized as PDZ 1.
+At position 758 to 843, the domain is characterized as PDZ 2.
+At position 193 to 382, the domain is characterized as VWFA.
+At position 45 to 122, the domain is characterized as NB-ARC.
+At position 3 to 89, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 94 to 192, the domain is characterized as FAD-binding FR-type.
+At position 860 to 1159, the domain is characterized as ABC transmembrane type-1 2.
+At position 88 to 200, the domain is characterized as Rieske.
+At position 124 to 303, the domain is characterized as FAD-binding PCMH-type.
+At position 75 to 159, the domain is characterized as KH-like.
+At position 659 to 811, the domain is characterized as RNase NYN.
+At position 48 to 163, the domain is characterized as Plastocyanin-like.
+At position 165 to 344, the domain is characterized as Helicase ATP-binding.
+At position 377 to 521, the domain is characterized as Helicase C-terminal.
+At position 448 to 612, the domain is characterized as YDG.
+At position 7 to 191, the domain is characterized as YrdC-like.
+At position 3 to 209, the domain is characterized as ABC transporter.
+At position 38 to 120, the domain is characterized as IGFBP N-terminal.
+At position 209 to 291, the domain is characterized as Thyroglobulin type-1.
+At position 97 to 350, the domain is characterized as Tyrosine-protein phosphatase.
+At position 586 to 650, the domain is characterized as CBS 1.
+At position 682 to 742, the domain is characterized as CBS 2.
+At position 147 to 460, the domain is characterized as Protein kinase.
+At position 326 to 368, the domain is characterized as CCT.
+At position 39 to 368, the domain is characterized as Protein kinase.
+At position 19 to 171, the domain is characterized as NAC.
+At position 307 to 620, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 43 to 155, the domain is characterized as THUMP.
+At position 1052 to 1251, the domain is characterized as MAGE.
+At position 72 to 252, the domain is characterized as B30.2/SPRY.
+At position 161 to 235, the domain is characterized as POU-specific.
+At position 249 to 437, the domain is characterized as GATase cobBQ-type.
+At position 118 to 230, the domain is characterized as C-type lectin.
+At position 159 to 203, the domain is characterized as bZIP.
+At position 236 to 455, the domain is characterized as DOG1.
+At position 47 to 261, the domain is characterized as Radical SAM core.
+At position 4 to 92, the domain is characterized as Acylphosphatase-like.
+At position 120 to 349, the domain is characterized as Sigma-54 factor interaction.
+At position 37 to 277, the domain is characterized as Peptidase S1.
+At position 15 to 151, the domain is characterized as N-acetyltransferase.
+At position 285 to 566, the domain is characterized as ABC transmembrane type-1 1.
+At position 603 to 825, the domain is characterized as ABC transporter 1.
+At position 886 to 1170, the domain is characterized as ABC transmembrane type-1 2.
+At position 1207 to 1441, the domain is characterized as ABC transporter 2.
+At position 12 to 240, the domain is characterized as ABC transporter.
+At position 70 to 116, the domain is characterized as G-patch.
+At position 58 to 211, the domain is characterized as NAC.
+At position 284 to 425, the domain is characterized as SIS 1.
+At position 7 to 62, the domain is characterized as HTH deoR-type.
+At position 118 to 292, the domain is characterized as FCP1 homology.
+At position 337 to 429, the domain is characterized as BRCT.
+At position 3 to 307, the domain is characterized as DegV.
+At position 515 to 566, the domain is characterized as Sushi 9.
+At position 567 to 625, the domain is characterized as Sushi 10.
+At position 628 to 686, the domain is characterized as Sushi 11.
+At position 689 to 746, the domain is characterized as Sushi 12.
+At position 751 to 805, the domain is characterized as Sushi 13.
+At position 868 to 928, the domain is characterized as Sushi 15.
+At position 929 to 986, the domain is characterized as Sushi 16.
+At position 987 to 1045, the domain is characterized as Sushi 17.
+At position 1046 to 1104, the domain is characterized as Sushi 18.
+At position 1107 to 1165, the domain is characterized as Sushi 19.
+At position 1170 to 1230, the domain is characterized as Sushi 20.
+At position 20 to 109, the domain is characterized as RRM 1.
+At position 117 to 197, the domain is characterized as RRM 2.
+At position 255 to 333, the domain is characterized as RRM 3.
+At position 544 to 584, the domain is characterized as UBA.
+At position 461 to 600, the domain is characterized as SIS 2.
+At position 53 to 292, the domain is characterized as Radical SAM core.
+At position 23 to 85, the domain is characterized as S4 RNA-binding.
+At position 113 to 280, the domain is characterized as SSD.
+At position 712 to 1001, the domain is characterized as Protein kinase.
+At position 74 to 305, the domain is characterized as Radical SAM core.
+At position 75 to 179, the domain is characterized as Longin.
+At position 195 to 255, the domain is characterized as v-SNARE coiled-coil homology.
+At position 51 to 121, the domain is characterized as Rho RNA-BD.
+At position 1011 to 1057, the domain is characterized as G-patch.
+At position 266 to 513, the domain is characterized as ABC transporter 2.
+At position 316 to 718, the domain is characterized as PIPK.
+At position 1895 to 1924, the domain is characterized as IQ.
+At position 281 to 564, the domain is characterized as UvrD-like helicase C-terminal.
+At position 106 to 225, the domain is characterized as GST C-terminal.
+At position 376 to 449, the domain is characterized as TRAM.
+At position 39 to 550, the domain is characterized as USP.
+At position 155 to 247, the domain is characterized as 3'-5' exonuclease.
+At position 82 to 150, the domain is characterized as DRBM 2.
+At position 1 to 334, the domain is characterized as SPX.
+At position 50 to 147, the domain is characterized as HD.
+At position 64 to 379, the domain is characterized as tr-type G.
+At position 626 to 754, the domain is characterized as G8.
+At position 140 to 668, the domain is characterized as USP.
+At position 306 to 476, the domain is characterized as VWFA.
+At position 330 to 376, the domain is characterized as F-box.
+At position 134 to 413, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 414 to 676, the domain is characterized as UvrD-like helicase C-terminal.
+At position 159 to 286, the domain is characterized as Fatty acid hydroxylase.
+At position 82 to 377, the domain is characterized as AB hydrolase-1.
+At position 48 to 219, the domain is characterized as FAD-binding PCMH-type.
+At position 655 to 754, the domain is characterized as BRCT 1.
+At position 800 to 906, the domain is characterized as BRCT 2.
+At position 295 to 358, the domain is characterized as Mop.
+At position 238 to 472, the domain is characterized as NR LBD.
+At position 30 to 147, the domain is characterized as PX.
+At position 233 to 487, the domain is characterized as Helicase ATP-binding.
+At position 527 to 689, the domain is characterized as Helicase C-terminal.
+At position 54 to 240, the domain is characterized as BPL/LPL catalytic.
+At position 10 to 93, the domain is characterized as GIY-YIG.
+At position 42 to 81, the domain is characterized as VM.
+At position 687 to 722, the domain is characterized as EF-hand 1.
+At position 768 to 786, the domain is characterized as EF-hand 2.
+At position 134 to 396, the domain is characterized as ABC transporter 1.
+At position 838 to 1081, the domain is characterized as ABC transporter 2.
+At position 205 to 261, the domain is characterized as GYF.
+At position 1 to 92, the domain is characterized as Thioredoxin.
+At position 229 to 338, the domain is characterized as DEUBAD.
+At position 33 to 266, the domain is characterized as ABC transporter.
+At position 674 to 843, the domain is characterized as Helicase C-terminal.
+At position 39 to 179, the domain is characterized as PADR1 zinc-binding.
+At position 182 to 274, the domain is characterized as BRCT.
+At position 1606 to 1708, the domain is characterized as MaoC-like.
+At position 19 to 98, the domain is characterized as G protein gamma.
+At position 34 to 230, the domain is characterized as tr-type G.
+At position 178 to 239, the domain is characterized as Pre-SET.
+At position 242 to 365, the domain is characterized as SET.
+At position 395 to 411, the domain is characterized as Post-SET.
+At position 59 to 228, the domain is characterized as TLDc.
+At position 23 to 158, the domain is characterized as GAF.
+At position 200 to 428, the domain is characterized as Sigma-54 factor interaction.
+At position 9 to 76, the domain is characterized as LIM zinc-binding.
+At position 36 to 102, the domain is characterized as Importin N-terminal.
+At position 248 to 518, the domain is characterized as Protein kinase.
+At position 14 to 97, the domain is characterized as GST N-terminal.
+At position 102 to 222, the domain is characterized as GST C-terminal.
+At position 1 to 43, the domain is characterized as Bromo.
+At position 213 to 383, the domain is characterized as GAF.
+At position 598 to 669, the domain is characterized as PAS 1.
+At position 672 to 728, the domain is characterized as PAC.
+At position 880 to 1100, the domain is characterized as Histidine kinase.
+At position 12 to 177, the domain is characterized as Exonuclease.
+At position 114 to 200, the domain is characterized as Ig-like C2-type 2.
+At position 252 to 366, the domain is characterized as Ig-like C2-type 3.
+At position 369 to 464, the domain is characterized as Ig-like C2-type 4.
+At position 694 to 1035, the domain is characterized as Protein kinase; inactive.
+At position 390 to 461, the domain is characterized as TRAM.
+At position 228 to 492, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 378 to 575, the domain is characterized as VWFA.
+At position 133 to 372, the domain is characterized as Radical SAM core.
+At position 622 to 681, the domain is characterized as KH.
+At position 693 to 762, the domain is characterized as S1 motif.
+At position 90 to 178, the domain is characterized as ACB.
+At position 105 to 156, the domain is characterized as F-box.
+At position 14 to 100, the domain is characterized as ABM.
+At position 44 to 129, the domain is characterized as Cytochrome b5 heme-binding.
+At position 49 to 352, the domain is characterized as Gamma-glutamyl hydrolase.
+At position 218 to 306, the domain is characterized as Ras-associating.
+At position 313 to 360, the domain is characterized as SARAH.
+At position 26 to 123, the domain is characterized as HPt.
+At position 566 to 838, the domain is characterized as Protein kinase.
+At position 76 to 194, the domain is characterized as MTTase N-terminal.
+At position 217 to 450, the domain is characterized as Radical SAM core.
+At position 450 to 509, the domain is characterized as SH3.
+At position 300 to 411, the domain is characterized as Cyclin N-terminal.
+At position 53 to 256, the domain is characterized as Brix.
+At position 60 to 95, the domain is characterized as EF-hand.
+At position 23 to 112, the domain is characterized as Ig-like 1.
+At position 113 to 231, the domain is characterized as Ig-like 2.
+At position 289 to 561, the domain is characterized as Protein kinase.
+At position 13 to 313, the domain is characterized as Protein kinase.
+At position 115 to 288, the domain is characterized as Helicase ATP-binding.
+At position 317 to 462, the domain is characterized as Helicase C-terminal.
+At position 140 to 231, the domain is characterized as PA.
+At position 19 to 167, the domain is characterized as MRH.
+At position 31 to 283, the domain is characterized as GH16.
+At position 624 to 699, the domain is characterized as Carrier 1.
+At position 1282 to 1358, the domain is characterized as Carrier 2.
+At position 16 to 119, the domain is characterized as LOB.
+At position 1720 to 1847, the domain is characterized as SMC hinge.
+At position 393 to 650, the domain is characterized as Protein kinase.
+At position 665 to 780, the domain is characterized as GAE.
+At position 123 to 487, the domain is characterized as PTS EIIC type-1.
+At position 224 to 353, the domain is characterized as Plastocyanin-like.
+At position 447 to 622, the domain is characterized as Helicase ATP-binding.
+At position 648 to 795, the domain is characterized as Helicase C-terminal.
+At position 983 to 1063, the domain is characterized as HRDC.
+At position 183 to 459, the domain is characterized as ABC transporter 1.
+At position 518 to 734, the domain is characterized as ABC transporter 2.
+At position 486 to 607, the domain is characterized as C2 3.
+At position 9 to 284, the domain is characterized as CN hydrolase.
+At position 139 to 373, the domain is characterized as ABC transporter.
+At position 34 to 205, the domain is characterized as NAC.
+At position 71 to 188, the domain is characterized as SSB.
+At position 87 to 180, the domain is characterized as K-box.
+At position 124 to 191, the domain is characterized as GRAM.
+At position 194 to 430, the domain is characterized as NR LBD.
+At position 45 to 105, the domain is characterized as PAS 1.
+At position 166 to 239, the domain is characterized as PAS 2.
+At position 241 to 292, the domain is characterized as PAC.
+At position 307 to 530, the domain is characterized as Histidine kinase.
+At position 563 to 680, the domain is characterized as Response regulatory.
+At position 44 to 169, the domain is characterized as Calponin-homology (CH).
+At position 39 to 74, the domain is characterized as Tify 1.
+At position 125 to 160, the domain is characterized as Tify 2.
+At position 82 to 235, the domain is characterized as Ferritin-like diiron.
+At position 212 to 378, the domain is characterized as Helicase ATP-binding.
+At position 472 to 640, the domain is characterized as Helicase C-terminal.
+At position 207 to 419, the domain is characterized as SMP-LTD.
+At position 39 to 208, the domain is characterized as FAD-binding PCMH-type.
+At position 109 to 295, the domain is characterized as Rho-GAP.
+At position 330 to 425, the domain is characterized as SH2 1.
+At position 202 to 261, the domain is characterized as OVATE.
+At position 815 to 880, the domain is characterized as HTH luxR-type.
+At position 537 to 626, the domain is characterized as Fibronectin type-III 4.
+At position 627 to 715, the domain is characterized as Fibronectin type-III 5.
+At position 737 to 829, the domain is characterized as Fibronectin type-III 6.
+At position 831 to 921, the domain is characterized as Fibronectin type-III 7.
+At position 922 to 1010, the domain is characterized as Fibronectin type-III 8.
+At position 1032 to 1205, the domain is characterized as VWFA 2.
+At position 1229 to 1424, the domain is characterized as Laminin G-like.
+At position 1462 to 1510, the domain is characterized as Collagen-like 1.
+At position 1514 to 1570, the domain is characterized as Collagen-like 2.
+At position 1571 to 1609, the domain is characterized as Collagen-like 3.
+At position 1653 to 1705, the domain is characterized as Collagen-like 4.
+At position 72 to 325, the domain is characterized as Protein kinase.
+At position 88 to 399, the domain is characterized as IF rod.
+At position 150 to 295, the domain is characterized as Jacalin-type lectin 2.
+At position 307 to 461, the domain is characterized as Jacalin-type lectin 3.
+At position 84 to 166, the domain is characterized as Sm.
+At position 222 to 529, the domain is characterized as Protein kinase.
+At position 31 to 122, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 164 to 194, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 246 to 336, the domain is characterized as Rieske.
+At position 564 to 764, the domain is characterized as FtsK.
+At position 44 to 284, the domain is characterized as GB1/RHD3-type G.
+At position 146 to 206, the domain is characterized as BTB.
+At position 121 to 320, the domain is characterized as Peptidase M12A.
+At position 322 to 434, the domain is characterized as CUB 1.
+At position 435 to 546, the domain is characterized as CUB 2.
+At position 547 to 588, the domain is characterized as EGF-like 1; calcium-binding.
+At position 591 to 703, the domain is characterized as CUB 3.
+At position 704 to 743, the domain is characterized as EGF-like 2; calcium-binding.
+At position 747 to 859, the domain is characterized as CUB 4.
+At position 860 to 976, the domain is characterized as CUB 5.
+At position 21 to 118, the domain is characterized as Yippee.
+At position 497 to 665, the domain is characterized as N-acetyltransferase.
+At position 25 to 245, the domain is characterized as Peptidase S1.
+At position 3 to 344, the domain is characterized as SAM-dependent MTase C5-type.
+At position 219 to 353, the domain is characterized as PADR1 zinc-binding.
+At position 385 to 461, the domain is characterized as BRCT.
+At position 77 to 360, the domain is characterized as PPM-type phosphatase.
+At position 141 to 176, the domain is characterized as EF-hand 4.
+At position 1533 to 1756, the domain is characterized as Collagen IV NC1.
+At position 366 to 698, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 226 to 251, the domain is characterized as EF-hand 6.
+At position 458 to 675, the domain is characterized as tr-type G.
+At position 41 to 116, the domain is characterized as RRM 1.
+At position 117 to 195, the domain is characterized as RRM 2.
+At position 210 to 289, the domain is characterized as RRM 3.
+At position 16 to 134, the domain is characterized as Response regulatory.
+At position 205 to 400, the domain is characterized as CheB-type methylesterase.
+At position 33 to 149, the domain is characterized as Ig-like V-type.
+At position 234 to 286, the domain is characterized as HAMP.
+At position 301 to 518, the domain is characterized as Histidine kinase.
+At position 550 to 579, the domain is characterized as IQ.
+At position 381 to 459, the domain is characterized as RRM.
+At position 184 to 356, the domain is characterized as Helicase ATP-binding.
+At position 385 to 534, the domain is characterized as Helicase C-terminal.
+At position 41 to 345, the domain is characterized as GH18.
+At position 249 to 480, the domain is characterized as NR LBD.
+At position 314 to 507, the domain is characterized as VWFA.
+At position 9 to 123, the domain is characterized as NTF2.
+At position 5 to 154, the domain is characterized as RNase H type-1.
+At position 122 to 369, the domain is characterized as PPM-type phosphatase.
+At position 576 to 654, the domain is characterized as BRCT.
+At position 839 to 921, the domain is characterized as BRCT.
+At position 47 to 618, the domain is characterized as Lipoxygenase.
+At position 340 to 400, the domain is characterized as SH3.
+At position 233 to 588, the domain is characterized as Protein kinase.
+At position 33 to 286, the domain is characterized as ABC transporter.
+At position 24 to 130, the domain is characterized as Fibronectin type-III 1.
+At position 131 to 227, the domain is characterized as Fibronectin type-III 2.
+At position 105 to 170, the domain is characterized as CBS 1.
+At position 5 to 106, the domain is characterized as BMC circularly permuted 1.
+At position 108 to 213, the domain is characterized as BMC circularly permuted 2.
+At position 1009 to 1036, the domain is characterized as PLD phosphodiesterase 1.
+At position 1460 to 1487, the domain is characterized as PLD phosphodiesterase 2.
+At position 171 to 204, the domain is characterized as WW 1.
+At position 230 to 263, the domain is characterized as WW 2.
+At position 28 to 185, the domain is characterized as PPIase cyclophilin-type.
+At position 111 to 203, the domain is characterized as RRM.
+At position 227 to 349, the domain is characterized as xRRM.
+At position 369 to 528, the domain is characterized as PA14.
+At position 190 to 276, the domain is characterized as RCK C-terminal 1.
+At position 277 to 361, the domain is characterized as RCK C-terminal 2.
+At position 21 to 128, the domain is characterized as Thioredoxin 1.
+At position 335 to 465, the domain is characterized as Thioredoxin 2.
+At position 450 to 647, the domain is characterized as FtsK.
+At position 25 to 244, the domain is characterized as MurNAc-LAA.
+At position 292 to 335, the domain is characterized as LysM 1.
+At position 385 to 429, the domain is characterized as LysM 2.
+At position 145 to 180, the domain is characterized as EF-hand 2.
+At position 251 to 286, the domain is characterized as EF-hand 3.
+At position 287 to 322, the domain is characterized as EF-hand 4.
+At position 352 to 387, the domain is characterized as EF-hand 5.
+At position 482 to 517, the domain is characterized as EF-hand 6.
+At position 589 to 624, the domain is characterized as EF-hand 7.
+At position 695 to 730, the domain is characterized as EF-hand 8.
+At position 731 to 766, the domain is characterized as EF-hand 9.
+At position 812 to 847, the domain is characterized as EF-hand 10.
+At position 917 to 952, the domain is characterized as EF-hand 11.
+At position 136 to 178, the domain is characterized as EGF-like 1.
+At position 290 to 331, the domain is characterized as EGF-like 2; calcium-binding.
+At position 155 to 467, the domain is characterized as Protein kinase.
+At position 36 to 376, the domain is characterized as G-alpha.
+At position 496 to 585, the domain is characterized as PDZ 3.
+At position 154 to 178, the domain is characterized as KOW.
+At position 3 to 79, the domain is characterized as REM-1.
+At position 285 to 392, the domain is characterized as PH.
+At position 76 to 108, the domain is characterized as EF-hand 2.
+At position 184 to 344, the domain is characterized as Tyrosine-protein phosphatase.
+At position 105 to 185, the domain is characterized as KH 1.
+At position 244 to 458, the domain is characterized as Histidine kinase.
+At position 177 to 354, the domain is characterized as VWFA.
+At position 121 to 212, the domain is characterized as Rhodanese.
+At position 487 to 604, the domain is characterized as Cadherin 5.
+At position 33 to 293, the domain is characterized as AB hydrolase-1.
+At position 147 to 527, the domain is characterized as SAC.
+At position 508 to 542, the domain is characterized as WW.
+At position 609 to 697, the domain is characterized as PKD.
+At position 219 to 256, the domain is characterized as EGF-like 1.
+At position 283 to 480, the domain is characterized as Laminin G-like 2.
+At position 487 to 679, the domain is characterized as Laminin G-like 3.
+At position 683 to 720, the domain is characterized as EGF-like 2.
+At position 725 to 898, the domain is characterized as Laminin G-like 4.
+At position 912 to 1087, the domain is characterized as Laminin G-like 5.
+At position 1090 to 1127, the domain is characterized as EGF-like 3.
+At position 1133 to 1331, the domain is characterized as Laminin G-like 6.
+At position 295 to 413, the domain is characterized as Nop.
+At position 169 to 368, the domain is characterized as Helicase ATP-binding.
+At position 395 to 600, the domain is characterized as Helicase C-terminal.
+At position 261 to 387, the domain is characterized as Ricin B-type lectin 1.
+At position 390 to 518, the domain is characterized as Ricin B-type lectin 2.
+At position 45 to 331, the domain is characterized as GH10.
+At position 1 to 46, the domain is characterized as SoHo.
+At position 249 to 418, the domain is characterized as PCI.
+At position 273 to 287, the domain is characterized as SAP 2.
+At position 7 to 74, the domain is characterized as EF-hand.
+At position 122 to 239, the domain is characterized as Calponin-homology (CH) 1.
+At position 267 to 370, the domain is characterized as Calponin-homology (CH) 2.
+At position 339 to 573, the domain is characterized as ABC transporter.
+At position 147 to 326, the domain is characterized as ABC transmembrane type-1 1.
+At position 465 to 644, the domain is characterized as ABC transmembrane type-1 2.
+At position 395 to 484, the domain is characterized as CBM2.
+At position 154 to 189, the domain is characterized as EF-hand 3.
+At position 25 to 296, the domain is characterized as Protein kinase.
+At position 266 to 332, the domain is characterized as Ig-like C2-type.
+At position 37 to 110, the domain is characterized as Inhibitor I9.
+At position 123 to 394, the domain is characterized as Peptidase S8.
+At position 280 to 696, the domain is characterized as Peptidase S8.
+At position 1059 to 1341, the domain is characterized as ABC transmembrane type-1.
+At position 1374 to 1610, the domain is characterized as ABC transporter.
+At position 16 to 89, the domain is characterized as S4 RNA-binding.
+At position 286 to 567, the domain is characterized as ABC transmembrane type-1 1.
+At position 601 to 824, the domain is characterized as ABC transporter 1.
+At position 900 to 1182, the domain is characterized as ABC transmembrane type-1 2.
+At position 1219 to 1453, the domain is characterized as ABC transporter 2.
+At position 347 to 585, the domain is characterized as ABC transporter.
+At position 55 to 90, the domain is characterized as EGF-like 1.
+At position 92 to 131, the domain is characterized as EGF-like 2; calcium-binding.
+At position 135 to 171, the domain is characterized as EGF-like 3.
+At position 172 to 210, the domain is characterized as EGF-like 4; calcium-binding.
+At position 217 to 257, the domain is characterized as EGF-like 5; calcium-binding.
+At position 397 to 543, the domain is characterized as MAM.
+At position 87 to 250, the domain is characterized as Helicase ATP-binding.
+At position 274 to 444, the domain is characterized as Helicase C-terminal.
+At position 53 to 159, the domain is characterized as B30.2/SPRY.
+At position 21 to 172, the domain is characterized as NAC.
+At position 49 to 397, the domain is characterized as Peptidase S8.
+At position 136 to 374, the domain is characterized as Radical SAM core.
+At position 23 to 77, the domain is characterized as F-box.
+At position 90 to 762, the domain is characterized as Peptidase M13.
+At position 50 to 279, the domain is characterized as Peptidase S1.
+At position 594 to 643, the domain is characterized as KA1.
+At position 65 to 117, the domain is characterized as F-box.
+At position 79 to 134, the domain is characterized as HTH myb-type 2.
+At position 486 to 533, the domain is characterized as PSI.
+At position 784 to 839, the domain is characterized as TSP type-1 4.
+At position 841 to 896, the domain is characterized as TSP type-1 5.
+At position 897 to 944, the domain is characterized as TSP type-1 6.
+At position 24 to 254, the domain is characterized as AB hydrolase-1.
+At position 686 to 772, the domain is characterized as PDZ 5.
+At position 1068 to 1160, the domain is characterized as PDZ 6.
+At position 1239 to 1322, the domain is characterized as PDZ 7.
+At position 1437 to 1520, the domain is characterized as PDZ 8.
+At position 1533 to 1615, the domain is characterized as PDZ 9.
+At position 1676 to 1762, the domain is characterized as PDZ 10.
+At position 276 to 463, the domain is characterized as Ku.
+At position 584 to 618, the domain is characterized as SAP.
+At position 119 to 182, the domain is characterized as Sushi 2.
+At position 84 to 115, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 949 to 981, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 983 to 1013, the domain is characterized as 4Fe-4S ferredoxin-type 3.
+At position 28 to 77, the domain is characterized as bHLH.
+At position 88 to 187, the domain is characterized as K-box.
+At position 394 to 490, the domain is characterized as SWIRM.
+At position 1 to 336, the domain is characterized as Velvet.
+At position 12 to 157, the domain is characterized as Jacalin-type lectin.
+At position 1 to 125, the domain is characterized as Thioredoxin.
+At position 144 to 240, the domain is characterized as Glutaredoxin.
+At position 8 to 77, the domain is characterized as Sm.
+At position 281 to 355, the domain is characterized as POU-specific.
+At position 135 to 335, the domain is characterized as Peptidase M12A.
+At position 330 to 370, the domain is characterized as EGF-like.
+At position 380 to 494, the domain is characterized as CUB.
+At position 133 to 241, the domain is characterized as sHSP.
+At position 215 to 305, the domain is characterized as Death.
+At position 541 to 840, the domain is characterized as Peptidase M60.
+At position 6 to 91, the domain is characterized as Phosphagen kinase N-terminal.
+At position 347 to 439, the domain is characterized as SH2.
+At position 32 to 211, the domain is characterized as VWFA.
+At position 212 to 302, the domain is characterized as Fibronectin type-III 1.
+At position 305 to 395, the domain is characterized as Fibronectin type-III 2.
+At position 1624 to 1696, the domain is characterized as PAH 1.
+At position 1706 to 1777, the domain is characterized as PAH 2.
+At position 2148 to 2201, the domain is characterized as Myb-like.
+At position 16 to 188, the domain is characterized as Era-type G.
+At position 17 to 168, the domain is characterized as Resolvase/invertase-type recombinase catalytic.
+At position 333 to 575, the domain is characterized as Glutamine amidotransferase type-1.
+At position 1 to 168, the domain is characterized as uDENN.
+At position 194 to 341, the domain is characterized as cDENN.
+At position 343 to 434, the domain is characterized as dDENN.
+At position 560 to 659, the domain is characterized as Peptidase S74.
+At position 163 to 390, the domain is characterized as Radical SAM core.
+At position 117 to 153, the domain is characterized as Orange.
+At position 18 to 137, the domain is characterized as MTTase N-terminal.
+At position 399 to 470, the domain is characterized as TRAM.
+At position 53 to 168, the domain is characterized as OmpA-like.
+At position 220 to 309, the domain is characterized as Ig-like C1-type.
+At position 172 to 383, the domain is characterized as NR LBD.
+At position 90 to 155, the domain is characterized as PRC barrel.
+At position 13 to 160, the domain is characterized as MPN.
+At position 134 to 355, the domain is characterized as Radical SAM core.
+At position 36 to 96, the domain is characterized as Chitin-binding type R&R.
+At position 45 to 261, the domain is characterized as Tyrosine-protein phosphatase.
+At position 1014 to 1287, the domain is characterized as Autotransporter.
+At position 154 to 254, the domain is characterized as BACK.
+At position 180 to 305, the domain is characterized as Fatty acid hydroxylase.
+At position 106 to 286, the domain is characterized as ATP-grasp.
+At position 7 to 171, the domain is characterized as N-acetyltransferase.
+At position 34 to 193, the domain is characterized as SIS.
+At position 51 to 307, the domain is characterized as GH18.
+At position 367 to 544, the domain is characterized as Helicase C-terminal.
+At position 563 to 657, the domain is characterized as Dicer dsRNA-binding fold.
+At position 916 to 1056, the domain is characterized as RNase III 1.
+At position 1090 to 1274, the domain is characterized as RNase III 2.
+At position 802 to 989, the domain is characterized as Macro 1.
+At position 1014 to 1202, the domain is characterized as Macro 2.
+At position 1227 to 1398, the domain is characterized as Macro 3.
+At position 1539 to 1617, the domain is characterized as WWE.
+At position 1621 to 1817, the domain is characterized as PARP catalytic.
+At position 7 to 71, the domain is characterized as LCN-type CS-alpha/beta.
+At position 295 to 545, the domain is characterized as B30.2/SPRY.
+At position 13 to 47, the domain is characterized as SAP.
+At position 345 to 423, the domain is characterized as RRM.
+At position 102 to 338, the domain is characterized as Radical SAM core.
+At position 312 to 341, the domain is characterized as IQ.
+At position 648 to 841, the domain is characterized as SEC7.
+At position 854 to 987, the domain is characterized as PH.
+At position 322 to 359, the domain is characterized as EGF-like 1.
+At position 394 to 431, the domain is characterized as EGF-like 2.
+At position 789 to 876, the domain is characterized as WWE.
+At position 1919 to 2026, the domain is characterized as HECT.
+At position 199 to 389, the domain is characterized as DH.
+At position 443 to 546, the domain is characterized as PH.
+At position 596 to 740, the domain is characterized as N-terminal Ras-GEF.
+At position 779 to 1018, the domain is characterized as Ras-GEF.
+At position 98 to 327, the domain is characterized as Radical SAM core.
+At position 94 to 221, the domain is characterized as C-type lysozyme.
+At position 58 to 276, the domain is characterized as Radical SAM core.
+At position 537 to 665, the domain is characterized as SET.
+At position 671 to 687, the domain is characterized as Post-SET.
+At position 185 to 328, the domain is characterized as FCP1 homology.
+At position 358 to 426, the domain is characterized as S4 RNA-binding.
+At position 1052 to 1201, the domain is characterized as Exonuclease.
+At position 244 to 546, the domain is characterized as Protein kinase.
+At position 24 to 277, the domain is characterized as AB hydrolase-1.
+At position 269 to 431, the domain is characterized as PCI.
+At position 549 to 607, the domain is characterized as LIM zinc-binding 1.
+At position 608 to 667, the domain is characterized as LIM zinc-binding 2.
+At position 668 to 727, the domain is characterized as LIM zinc-binding 3.
+At position 22 to 119, the domain is characterized as Ig-like.
+At position 137 to 211, the domain is characterized as PRC barrel.
+At position 277 to 398, the domain is characterized as C2 2.
+At position 437 to 562, the domain is characterized as C2 3.
+At position 605 to 727, the domain is characterized as C2 4.
+At position 951 to 1079, the domain is characterized as C-type lectin 6.
+At position 1101 to 1212, the domain is characterized as C-type lectin 7.
+At position 1240 to 1355, the domain is characterized as C-type lectin 8.
+At position 198 to 263, the domain is characterized as KH 1.
+At position 279 to 346, the domain is characterized as KH 2.
+At position 407 to 472, the domain is characterized as KH 3.
+At position 489 to 555, the domain is characterized as KH 4.
+At position 54 to 171, the domain is characterized as RGS.
+At position 10 to 139, the domain is characterized as RNase III.
+At position 165 to 234, the domain is characterized as DRBM.
+At position 165 to 252, the domain is characterized as PPIase FKBP-type.
+At position 25 to 148, the domain is characterized as EamA 1.
+At position 191 to 304, the domain is characterized as EamA 2.
+At position 120 to 216, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 299, the domain is characterized as Ig-like C2-type 3.
+At position 308 to 387, the domain is characterized as Ig-like C2-type 4.
+At position 392 to 488, the domain is characterized as Ig-like C2-type 5.
+At position 128 to 303, the domain is characterized as Helicase ATP-binding.
+At position 318 to 478, the domain is characterized as Helicase C-terminal.
+At position 31 to 119, the domain is characterized as Toprim.
+At position 151 to 426, the domain is characterized as Dynamin-type G.
+At position 307 to 477, the domain is characterized as VWFA.
+At position 206 to 329, the domain is characterized as NlpC/P60.
+At position 345 to 457, the domain is characterized as STAS.
+At position 1 to 76, the domain is characterized as TGS.
+At position 92 to 162, the domain is characterized as S4 RNA-binding.
+At position 123 to 432, the domain is characterized as NB-ARC.
+At position 380 to 812, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1327 to 1643, the domain is characterized as PKS/mFAS DH.
+At position 1712 to 1791, the domain is characterized as Carrier 1.
+At position 1839 to 1915, the domain is characterized as Carrier 2.
+At position 175 to 263, the domain is characterized as EH 1.
+At position 207 to 242, the domain is characterized as EF-hand 1.
+At position 466 to 555, the domain is characterized as EH 2.
+At position 499 to 534, the domain is characterized as EF-hand 2.
+At position 1436 to 1453, the domain is characterized as WH2.
+At position 371 to 411, the domain is characterized as UBA 2.
+At position 356 to 468, the domain is characterized as PLAT.
+At position 86 to 325, the domain is characterized as ABC transporter 1.
+At position 396 to 613, the domain is characterized as ABC transporter 2.
+At position 806 to 875, the domain is characterized as ACT 2.
+At position 62 to 200, the domain is characterized as HD.
+At position 508 to 674, the domain is characterized as W2.
+At position 27 to 105, the domain is characterized as Kringle.
+At position 1030 to 1089, the domain is characterized as SAM.
+At position 1112 to 1317, the domain is characterized as PARP catalytic.
+At position 1 to 64, the domain is characterized as GST N-terminal.
+At position 70 to 199, the domain is characterized as GST C-terminal.
+At position 420 to 609, the domain is characterized as VWFA.
+At position 1 to 137, the domain is characterized as ADF-H 1.
+At position 173 to 304, the domain is characterized as ADF-H 2.
+At position 111 to 175, the domain is characterized as J.
+At position 34 to 154, the domain is characterized as C-type lectin.
+At position 138 to 188, the domain is characterized as DHHC.
+At position 16 to 78, the domain is characterized as PWWP.
+At position 160 to 212, the domain is characterized as KH.
+At position 675 to 828, the domain is characterized as CRAL-TRIO.
+At position 21 to 137, the domain is characterized as BAH.
+At position 348 to 420, the domain is characterized as PAS.
+At position 23 to 122, the domain is characterized as CBM39.
+At position 128 to 482, the domain is characterized as GH16.
+At position 23 to 150, the domain is characterized as Calponin-homology (CH).
+At position 191 to 263, the domain is characterized as GAR.
+At position 1216 to 1314, the domain is characterized as PH 1.
+At position 1396 to 1501, the domain is characterized as PH 2.
+At position 1551 to 1699, the domain is characterized as MyTH4.
+At position 1704 to 2048, the domain is characterized as FERM.
+At position 6 to 238, the domain is characterized as PABS.
+At position 12 to 172, the domain is characterized as N-acetyltransferase.
+At position 41 to 130, the domain is characterized as ACB.
+At position 21 to 106, the domain is characterized as Ig-like C2-type 1.
+At position 117 to 198, the domain is characterized as Ig-like C2-type 2.
+At position 202 to 297, the domain is characterized as Fibronectin type-III 1.
+At position 299 to 403, the domain is characterized as Fibronectin type-III 2.
+At position 1 to 153, the domain is characterized as Brix.
+At position 2 to 287, the domain is characterized as Glutamine amidotransferase type-2.
+At position 359 to 498, the domain is characterized as SIS 1.
+At position 530 to 671, the domain is characterized as SIS 2.
+At position 19 to 140, the domain is characterized as PX.
+At position 170 to 229, the domain is characterized as SH3.
+At position 237 to 329, the domain is characterized as PB1.
+At position 1 to 163, the domain is characterized as uDENN.
+At position 186 to 318, the domain is characterized as cDENN.
+At position 320 to 424, the domain is characterized as dDENN.
+At position 31 to 110, the domain is characterized as Sm.
+At position 21 to 158, the domain is characterized as SprT-like.
+At position 360 to 548, the domain is characterized as Rab-GAP TBC.
+At position 141 to 188, the domain is characterized as F-box.
+At position 361 to 437, the domain is characterized as RRM.
+At position 21 to 168, the domain is characterized as Thioredoxin 1.
+At position 170 to 300, the domain is characterized as Thioredoxin 2.
+At position 36 to 138, the domain is characterized as Ig-like C2-type.
+At position 63 to 169, the domain is characterized as Thioredoxin.
+At position 471 to 530, the domain is characterized as SH3.
+At position 571 to 665, the domain is characterized as PDZ.
+At position 1668 to 1731, the domain is characterized as SAM.
+At position 111 to 181, the domain is characterized as PAS.
+At position 4 to 239, the domain is characterized as Radical SAM core.
+At position 117 to 192, the domain is characterized as PRC barrel.
+At position 77 to 329, the domain is characterized as Protein kinase.
+At position 199 to 436, the domain is characterized as FAD-binding FR-type.
+At position 29 to 164, the domain is characterized as N-terminal Ras-GEF.
+At position 1073 to 1314, the domain is characterized as Ras-GEF.
+At position 347 to 404, the domain is characterized as KASH.
+At position 1 to 103, the domain is characterized as ULD.
+At position 79 to 272, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 31 to 197, the domain is characterized as 3'-5' exonuclease.
+At position 239 to 318, the domain is characterized as HRDC.
+At position 195 to 388, the domain is characterized as GMPS ATP-PPase.
+At position 1 to 88, the domain is characterized as CRAL-TRIO.
+At position 495 to 675, the domain is characterized as DH.
+At position 687 to 809, the domain is characterized as PH.
+At position 8 to 77, the domain is characterized as H15.
+At position 45 to 471, the domain is characterized as Sema.
+At position 473 to 526, the domain is characterized as PSI 1.
+At position 620 to 682, the domain is characterized as PSI 2.
+At position 787 to 833, the domain is characterized as PSI 3.
+At position 835 to 925, the domain is characterized as IPT/TIG 1.
+At position 927 to 1012, the domain is characterized as IPT/TIG 2.
+At position 1015 to 1145, the domain is characterized as IPT/TIG 3.
+At position 1159 to 1244, the domain is characterized as IPT/TIG 4.
+At position 41 to 54, the domain is characterized as CRIB.
+At position 376 to 627, the domain is characterized as Protein kinase.
+At position 164 to 327, the domain is characterized as Integrase catalytic.
+At position 1 to 101, the domain is characterized as Thioredoxin.
+At position 291 to 384, the domain is characterized as Spaetzle.
+At position 45 to 628, the domain is characterized as Peptidase M2 1.
+At position 647 to 1226, the domain is characterized as Peptidase M2 2.
+At position 264 to 488, the domain is characterized as NR LBD.
+At position 57 to 119, the domain is characterized as KH.
+At position 120 to 346, the domain is characterized as Radical SAM core.
+At position 121 to 162, the domain is characterized as LRRCT.
+At position 35 to 113, the domain is characterized as IGFBP N-terminal.
+At position 379 to 471, the domain is characterized as PDZ.
+At position 453 to 728, the domain is characterized as Protein kinase.
+At position 170 to 273, the domain is characterized as BACK.
+At position 7 to 280, the domain is characterized as tr-type G.
+At position 282 to 440, the domain is characterized as SSD.
+At position 69 to 129, the domain is characterized as Chitin-binding type R&R.
+At position 6 to 311, the domain is characterized as PKS/mFAS DH.
+At position 30 to 90, the domain is characterized as Ubiquitin-like.
+At position 31 to 224, the domain is characterized as GH16.
+At position 168 to 241, the domain is characterized as RRM 1.
+At position 253 to 326, the domain is characterized as RRM 2.
+At position 191 to 364, the domain is characterized as uDENN.
+At position 3 to 166, the domain is characterized as FeoB-type G.
+At position 44 to 218, the domain is characterized as EngB-type G.
+At position 44 to 120, the domain is characterized as EMI.
+At position 840 to 892, the domain is characterized as Collagen-like.
+At position 901 to 1052, the domain is characterized as C1q.
+At position 154 to 200, the domain is characterized as G-patch.
+At position 226 to 253, the domain is characterized as KOW 1.
+At position 428 to 455, the domain is characterized as KOW 2.
+At position 167 to 364, the domain is characterized as CheB-type methylesterase.
+At position 909 to 982, the domain is characterized as U-box.
+At position 99 to 240, the domain is characterized as Clp R.
+At position 518 to 553, the domain is characterized as UVR.
+At position 1103 to 1174, the domain is characterized as S1 motif.
+At position 131 to 253, the domain is characterized as MPN.
+At position 55 to 139, the domain is characterized as ELM2.
+At position 140 to 191, the domain is characterized as SANT.
+At position 26 to 110, the domain is characterized as Inhibitor I9.
+At position 116 to 606, the domain is characterized as Peptidase S8.
+At position 4 to 458, the domain is characterized as BRO1.
+At position 119 to 271, the domain is characterized as Exonuclease.
+At position 310 to 388, the domain is characterized as RRM 1.
+At position 418 to 509, the domain is characterized as RRM 2.
+At position 625 to 766, the domain is characterized as PA14.
+At position 297 to 319, the domain is characterized as RRM.
+At position 181 to 223, the domain is characterized as CAP-Gly.
+At position 1 to 139, the domain is characterized as DAGKc.
+At position 153 to 409, the domain is characterized as ABC transporter 1.
+At position 885 to 1128, the domain is characterized as ABC transporter 2.
+At position 111 to 394, the domain is characterized as ABC transmembrane type-1 1.
+At position 470 to 690, the domain is characterized as ABC transporter 1.
+At position 763 to 1061, the domain is characterized as ABC transmembrane type-1 2.
+At position 1116 to 1350, the domain is characterized as ABC transporter 2.
+At position 439 to 474, the domain is characterized as EF-hand 2.
+At position 475 to 510, the domain is characterized as EF-hand 3.
+At position 237 to 412, the domain is characterized as Helicase ATP-binding.
+At position 423 to 613, the domain is characterized as Helicase C-terminal.
+At position 10 to 94, the domain is characterized as YcgL.
+At position 1 to 82, the domain is characterized as Ig-like.
+At position 92 to 212, the domain is characterized as MTTase N-terminal.
+At position 237 to 491, the domain is characterized as Radical SAM core.
+At position 494 to 569, the domain is characterized as TRAM.
+At position 253 to 350, the domain is characterized as Link 2.
+At position 496 to 591, the domain is characterized as Link 3.
+At position 597 to 693, the domain is characterized as Link 4.
+At position 2081 to 2117, the domain is characterized as EGF-like; calcium-binding.
+At position 2130 to 2245, the domain is characterized as C-type lectin.
+At position 2248 to 2308, the domain is characterized as Sushi.
+At position 365 to 793, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1265 to 1573, the domain is characterized as PKS/mFAS DH.
+At position 1626 to 1704, the domain is characterized as Carrier.
+At position 54 to 179, the domain is characterized as MATH.
+At position 199 to 524, the domain is characterized as USP.
+At position 19 to 113, the domain is characterized as EthD.
+At position 113 to 170, the domain is characterized as J.
+At position 343 to 734, the domain is characterized as TTL.
+At position 424 to 557, the domain is characterized as SHD.
+At position 565 to 872, the domain is characterized as MHD.
+At position 229 to 396, the domain is characterized as tr-type G.
+At position 291 to 487, the domain is characterized as PX.
+At position 496 to 664, the domain is characterized as PH.
+At position 791 to 818, the domain is characterized as PLD phosphodiesterase 1.
+At position 1091 to 1118, the domain is characterized as PLD phosphodiesterase 2.
+At position 45 to 231, the domain is characterized as FAD-binding PCMH-type.
+At position 1 to 238, the domain is characterized as NR LBD.
+At position 172 to 273, the domain is characterized as PpiC 1.
+At position 283 to 381, the domain is characterized as PpiC 2.
+At position 651 to 928, the domain is characterized as Protein kinase.
+At position 378 to 469, the domain is characterized as SH2.
+At position 403 to 820, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1302 to 1612, the domain is characterized as PKS/mFAS DH.
+At position 156 to 379, the domain is characterized as Radical SAM core.
+At position 74 to 247, the domain is characterized as MDFI.
+At position 286 to 423, the domain is characterized as SIS 1.
+At position 452 to 589, the domain is characterized as SIS 2.
+At position 143 to 218, the domain is characterized as Carrier.
+At position 1097 to 1634, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1879 to 2138, the domain is characterized as Protein kinase.
+At position 40 to 86, the domain is characterized as Gla.
+At position 86 to 122, the domain is characterized as EGF-like; calcium-binding.
+At position 852 to 1105, the domain is characterized as ABC transporter 2.
+At position 109 to 277, the domain is characterized as CP-type G.
+At position 22 to 185, the domain is characterized as TIR.
+At position 201 to 440, the domain is characterized as NB-ARC.
+At position 404 to 506, the domain is characterized as Zinc-hook.
+At position 58 to 209, the domain is characterized as Cupin type-1.
+At position 276 to 382, the domain is characterized as B5.
+At position 68 to 203, the domain is characterized as HD.
+At position 12 to 90, the domain is characterized as Cytochrome c 1.
+At position 99 to 191, the domain is characterized as Cytochrome c 2.
+At position 27 to 128, the domain is characterized as Thioredoxin.
+At position 372 to 469, the domain is characterized as FDX-ACB.
+At position 96 to 190, the domain is characterized as SH2.
+At position 13 to 309, the domain is characterized as Protein kinase.
+At position 242 to 427, the domain is characterized as FAD-binding PCMH-type.
+At position 217 to 307, the domain is characterized as PKD.
+At position 21 to 122, the domain is characterized as Ig-like V-type.
+At position 10 to 71, the domain is characterized as HTH tetR-type.
+At position 518 to 708, the domain is characterized as FtsK.
+At position 28 to 139, the domain is characterized as STAS.
+At position 53 to 93, the domain is characterized as Fibronectin type-I 1.
+At position 98 to 141, the domain is characterized as Fibronectin type-I 2.
+At position 142 to 185, the domain is characterized as Fibronectin type-I 3.
+At position 187 to 231, the domain is characterized as Fibronectin type-I 4.
+At position 232 to 276, the domain is characterized as Fibronectin type-I 5.
+At position 307 to 346, the domain is characterized as Fibronectin type-I 6.
+At position 469 to 512, the domain is characterized as Fibronectin type-I 7.
+At position 611 to 703, the domain is characterized as Fibronectin type-III 1.
+At position 720 to 808, the domain is characterized as Fibronectin type-III 2.
+At position 811 to 904, the domain is characterized as Fibronectin type-III 3.
+At position 2195 to 2299, the domain is characterized as Fibronectin type-III 17.
+At position 2299 to 2343, the domain is characterized as Fibronectin type-I 10.
+At position 2344 to 2386, the domain is characterized as Fibronectin type-I 11.
+At position 2388 to 2431, the domain is characterized as Fibronectin type-I 12.
+At position 408 to 578, the domain is characterized as tr-type G.
+At position 101 to 296, the domain is characterized as Peptidase M12A.
+At position 347 to 381, the domain is characterized as ShKT.
+At position 262 to 480, the domain is characterized as Integrase catalytic.
+At position 134 to 297, the domain is characterized as Exonuclease.
+At position 247 to 280, the domain is characterized as WW 1.
+At position 397 to 430, the domain is characterized as WW 3.
+At position 486 to 820, the domain is characterized as HECT.
+At position 164 to 203, the domain is characterized as UBA.
+At position 132 to 199, the domain is characterized as KH 1.
+At position 284 to 348, the domain is characterized as KH 2.
+At position 34 to 210, the domain is characterized as Helicase ATP-binding.
+At position 244 to 390, the domain is characterized as Helicase C-terminal.
+At position 552 to 605, the domain is characterized as bHLH.
+At position 82 to 240, the domain is characterized as CP-type G.
+At position 751 to 912, the domain is characterized as SUN.
+At position 59 to 342, the domain is characterized as Protein kinase.
+At position 363 to 434, the domain is characterized as RRM.
+At position 73 to 249, the domain is characterized as Helicase ATP-binding.
+At position 263 to 433, the domain is characterized as Helicase C-terminal.
+At position 99 to 343, the domain is characterized as Radical SAM core.
+At position 841 to 966, the domain is characterized as RGS.
+At position 5 to 61, the domain is characterized as DPH-type MB.
+At position 82 to 352, the domain is characterized as Protein kinase.
+At position 28 to 290, the domain is characterized as Alpha-carbonic anhydrase.
+At position 144 to 230, the domain is characterized as PKD.
+At position 84 to 187, the domain is characterized as C-type lectin.
+At position 56 to 168, the domain is characterized as OmpA-like.
+At position 1 to 152, the domain is characterized as GRAD2.
+At position 153 to 657, the domain is characterized as GRAD1.
+At position 60 to 154, the domain is characterized as SH2.
+At position 189 to 260, the domain is characterized as Olduvai 2.
+At position 261 to 352, the domain is characterized as Olduvai 3.
+At position 355 to 410, the domain is characterized as Olduvai 4.
+At position 411 to 503, the domain is characterized as Olduvai 5.
+At position 504 to 596, the domain is characterized as Olduvai 6.
+At position 599 to 671, the domain is characterized as Olduvai 7.
+At position 674 to 729, the domain is characterized as Olduvai 8.
+At position 730 to 822, the domain is characterized as Olduvai 9.
+At position 823 to 921, the domain is characterized as Olduvai 10.
+At position 460 to 773, the domain is characterized as Protein kinase.
+At position 151 to 174, the domain is characterized as PAS 2; truncated.
+At position 141 to 275, the domain is characterized as TIR.
+At position 87 to 367, the domain is characterized as Protein kinase.
+At position 27 to 273, the domain is characterized as Deacetylase sirtuin-type.
+At position 230 to 376, the domain is characterized as Helicase C-terminal.
+At position 426 to 510, the domain is characterized as PDZ 2.
+At position 605 to 683, the domain is characterized as PDZ 3.
+At position 778 to 860, the domain is characterized as PDZ 4.
+At position 920 to 1010, the domain is characterized as PDZ 5.
+At position 1147 to 1229, the domain is characterized as PDZ 6.
+At position 270 to 333, the domain is characterized as bZIP.
+At position 17 to 165, the domain is characterized as Thioredoxin.
+At position 292 to 512, the domain is characterized as Helicase ATP-binding.
+At position 728 to 896, the domain is characterized as Helicase C-terminal.
+At position 408 to 485, the domain is characterized as RRM.
+At position 190 to 309, the domain is characterized as C2.
+At position 824 to 1083, the domain is characterized as Protein kinase.
+At position 1084 to 1151, the domain is characterized as AGC-kinase C-terminal.
+At position 1 to 17, the domain is characterized as Lipoyl-binding 1.
+At position 18 to 28, the domain is characterized as Lipoyl-binding 2.
+At position 281 to 355, the domain is characterized as PUA.
+At position 157 to 240, the domain is characterized as RRM.
+At position 28 to 449, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1009 to 1306, the domain is characterized as PKS/mFAS DH.
+At position 2522 to 2600, the domain is characterized as Carrier.
+At position 385 to 636, the domain is characterized as SF4 helicase.
+At position 217 to 365, the domain is characterized as Plastocyanin-like 2.
+At position 378 to 560, the domain is characterized as Plastocyanin-like 3.
+At position 730 to 906, the domain is characterized as Plastocyanin-like 5.
+At position 914 to 1092, the domain is characterized as Plastocyanin-like 6.
+At position 33 to 124, the domain is characterized as GOLD.
+At position 25 to 143, the domain is characterized as MTTase N-terminal.
+At position 114 to 458, the domain is characterized as G-alpha.
+At position 704 to 972, the domain is characterized as PPM-type phosphatase.
+At position 209 to 357, the domain is characterized as Plastocyanin-like 2.
+At position 370 to 718, the domain is characterized as F5/8 type A 2.
+At position 370 to 560, the domain is characterized as Plastocyanin-like 3.
+At position 730 to 1061, the domain is characterized as F5/8 type A 3.
+At position 730 to 900, the domain is characterized as Plastocyanin-like 5.
+At position 908 to 1061, the domain is characterized as Plastocyanin-like 6.
+At position 472 to 489, the domain is characterized as WH2 1.
+At position 499 to 516, the domain is characterized as WH2 2.
+At position 13 to 129, the domain is characterized as Arf-GAP.
+At position 1647 to 1721, the domain is characterized as Carrier 1.
+At position 1768 to 1845, the domain is characterized as Carrier 2.
+At position 75 to 192, the domain is characterized as HD.
+At position 138 to 348, the domain is characterized as JmjC.
+At position 113 to 392, the domain is characterized as GS catalytic.
+At position 149 to 302, the domain is characterized as YDG.
+At position 381 to 443, the domain is characterized as Pre-SET.
+At position 446 to 594, the domain is characterized as SET.
+At position 608 to 624, the domain is characterized as Post-SET.
+At position 30 to 262, the domain is characterized as Peptidase S1.
+At position 127 to 168, the domain is characterized as PAC.
+At position 211 to 257, the domain is characterized as F-box.
+At position 250 to 654, the domain is characterized as USP.
+At position 311 to 364, the domain is characterized as LRRCT.
+At position 576 to 675, the domain is characterized as Fibronectin type-III.
+At position 120 to 263, the domain is characterized as Thioredoxin.
+At position 98 to 313, the domain is characterized as RNase H type-2.
+At position 495 to 721, the domain is characterized as Peptidase S1.
+At position 46 to 298, the domain is characterized as CN hydrolase.
+At position 22 to 107, the domain is characterized as Saposin B-type.
+At position 22 to 281, the domain is characterized as OBG-type G.
+At position 302 to 385, the domain is characterized as TGS.
+At position 12 to 157, the domain is characterized as N-acetyltransferase 1.
+At position 66 to 108, the domain is characterized as KRAB.
+At position 169 to 412, the domain is characterized as Fibrinogen C-terminal.
+At position 1129 to 1246, the domain is characterized as SET.
+At position 1255 to 1271, the domain is characterized as Post-SET.
+At position 11 to 64, the domain is characterized as ClpX-type ZB.
+At position 63 to 201, the domain is characterized as Thioredoxin.
+At position 3 to 42, the domain is characterized as UBA.
+At position 882 to 1171, the domain is characterized as Protein kinase.
+At position 1172 to 1277, the domain is characterized as AGC-kinase C-terminal.
+At position 578 to 641, the domain is characterized as bZIP.
+At position 461 to 632, the domain is characterized as tr-type G.
+At position 194 to 293, the domain is characterized as Glutaredoxin.
+At position 94 to 289, the domain is characterized as VWFA.
+At position 97 to 352, the domain is characterized as Dynamin-type G.
+At position 146 to 260, the domain is characterized as Gnk2-homologous 2.
+At position 163 to 338, the domain is characterized as Helicase ATP-binding.
+At position 370 to 515, the domain is characterized as Helicase C-terminal.
+At position 275 to 335, the domain is characterized as CBS 1.
+At position 357 to 415, the domain is characterized as CBS 2.
+At position 430 to 492, the domain is characterized as CBS 3.
+At position 504 to 562, the domain is characterized as CBS 4.
+At position 30 to 142, the domain is characterized as Ig-like V-type.
+At position 295 to 488, the domain is characterized as B30.2/SPRY.
+At position 428 to 699, the domain is characterized as Protein kinase.
+At position 360 to 614, the domain is characterized as Peptidase S1.
+At position 217 to 371, the domain is characterized as TrmE-type G.
+At position 577 to 713, the domain is characterized as C2 1.
+At position 207 to 290, the domain is characterized as RRM 1.
+At position 327 to 405, the domain is characterized as RRM 2.
+At position 446 to 532, the domain is characterized as RRM 3.
+At position 112 to 406, the domain is characterized as Protein kinase.
+At position 407 to 508, the domain is characterized as AGC-kinase C-terminal.
+At position 517 to 567, the domain is characterized as PSI 1.
+At position 663 to 710, the domain is characterized as PSI 2.
+At position 811 to 864, the domain is characterized as PSI 3.
+At position 866 to 960, the domain is characterized as IPT/TIG 1.
+At position 962 to 1046, the domain is characterized as IPT/TIG 2.
+At position 1049 to 1148, the domain is characterized as IPT/TIG 3.
+At position 1151 to 1246, the domain is characterized as IPT/TIG 4.
+At position 270 to 452, the domain is characterized as VWFA.
+At position 466 to 559, the domain is characterized as Cache.
+At position 31 to 186, the domain is characterized as SIS.
+At position 1 to 323, the domain is characterized as UvrD-like helicase ATP-binding.
+At position 349 to 607, the domain is characterized as UvrD-like helicase C-terminal.
+At position 7 to 277, the domain is characterized as Helicase ATP-binding.
+At position 118 to 216, the domain is characterized as PB1.
+At position 6 to 153, the domain is characterized as RNase H type-1.
+At position 8 to 181, the domain is characterized as PCI.
+At position 28 to 127, the domain is characterized as Ig-like V-type.
+At position 128 to 206, the domain is characterized as Ig-like C2-type 1.
+At position 207 to 316, the domain is characterized as Ig-like C2-type 2.
+At position 317 to 374, the domain is characterized as Ig-like C2-type 3.
+At position 160 to 492, the domain is characterized as WAPL.
+At position 1343 to 1601, the domain is characterized as Protein kinase.
+At position 142 to 210, the domain is characterized as KH.
+At position 236 to 430, the domain is characterized as MH2.
+At position 12 to 156, the domain is characterized as N-acetyltransferase 1.
+At position 169 to 330, the domain is characterized as N-acetyltransferase 2.
+At position 19 to 99, the domain is characterized as IGFBP N-terminal.
+At position 166 to 248, the domain is characterized as Thyroglobulin type-1.
+At position 9 to 84, the domain is characterized as Sm.
+At position 25 to 121, the domain is characterized as EthD.
+At position 72 to 425, the domain is characterized as Protein kinase.
+At position 657 to 844, the domain is characterized as Rab-GAP TBC.
+At position 40 to 155, the domain is characterized as Response regulatory.
+At position 143 to 230, the domain is characterized as N-acetyltransferase.
+At position 204 to 444, the domain is characterized as FAD-binding FR-type.
+At position 23 to 258, the domain is characterized as ABC transporter 1.
+At position 269 to 515, the domain is characterized as ABC transporter 2.
+At position 6 to 151, the domain is characterized as SprT-like.
+At position 495 to 567, the domain is characterized as Bromo 2.
+At position 942 to 1024, the domain is characterized as NET.
+At position 108 to 281, the domain is characterized as tr-type G.
+At position 3 to 135, the domain is characterized as ADF-H.
+At position 167 to 379, the domain is characterized as Helicase ATP-binding.
+At position 406 to 573, the domain is characterized as Helicase C-terminal.
+At position 66 to 274, the domain is characterized as ABC transmembrane type-1.
+At position 109 to 165, the domain is characterized as S4 RNA-binding.
+At position 141 to 300, the domain is characterized as JmjC.
+At position 1592 to 1822, the domain is characterized as Alpha-type protein kinase.
+At position 40 to 171, the domain is characterized as Nudix hydrolase.
+At position 56 to 178, the domain is characterized as PX.
+At position 166 to 229, the domain is characterized as bZIP.
+At position 233 to 450, the domain is characterized as DOG1.
+At position 17 to 290, the domain is characterized as Protein kinase.
+At position 568 to 654, the domain is characterized as Death.
+At position 305 to 363, the domain is characterized as CBS 1.
+At position 367 to 423, the domain is characterized as CBS 2.
+At position 335 to 387, the domain is characterized as bHLH.
+At position 1 to 55, the domain is characterized as Sushi 1.
+At position 56 to 119, the domain is characterized as Sushi 2.
+At position 120 to 181, the domain is characterized as Sushi 3.
+At position 182 to 244, the domain is characterized as Sushi 4.
+At position 64 to 482, the domain is characterized as USP.
+At position 534 to 625, the domain is characterized as SH2.
+At position 47 to 342, the domain is characterized as RHD.
+At position 201 to 327, the domain is characterized as FZ 1.
+At position 336 to 372, the domain is characterized as LDL-receptor class A 1.
+At position 373 to 408, the domain is characterized as LDL-receptor class A 2.
+At position 409 to 445, the domain is characterized as LDL-receptor class A 3.
+At position 446 to 483, the domain is characterized as LDL-receptor class A 4.
+At position 518 to 641, the domain is characterized as FZ 2.
+At position 647 to 682, the domain is characterized as LDL-receptor class A 5.
+At position 683 to 721, the domain is characterized as LDL-receptor class A 6.
+At position 722 to 757, the domain is characterized as LDL-receptor class A 7.
+At position 758 to 853, the domain is characterized as SRCR.
+At position 869 to 1102, the domain is characterized as Peptidase S1.
+At position 64 to 185, the domain is characterized as CRC.
+At position 183 to 369, the domain is characterized as Glutamine amidotransferase type-1.
+At position 51 to 119, the domain is characterized as KH type-2.
+At position 51 to 357, the domain is characterized as ABC transmembrane type-1 1.
+At position 392 to 628, the domain is characterized as ABC transporter 1.
+At position 711 to 1000, the domain is characterized as ABC transmembrane type-1 2.
+At position 1035 to 1273, the domain is characterized as ABC transporter 2.
+At position 287 to 411, the domain is characterized as Ferric oxidoreductase.
+At position 412 to 546, the domain is characterized as FAD-binding FR-type.
+At position 44 to 136, the domain is characterized as Inhibitor I9.
+At position 148 to 454, the domain is characterized as Peptidase S8.
+At position 290 to 560, the domain is characterized as Radical SAM core.
+At position 149 to 184, the domain is characterized as QLQ.
+At position 243 to 287, the domain is characterized as WRC.
+At position 225 to 619, the domain is characterized as GRAS.
+At position 441 to 558, the domain is characterized as C2.
+At position 580 to 686, the domain is characterized as PH.
+At position 975 to 1106, the domain is characterized as MHD1.
+At position 130 to 409, the domain is characterized as Peptidase S8.
+At position 88 to 243, the domain is characterized as RNase NYN.
+At position 287 to 378, the domain is characterized as PDZ 1.
+At position 401 to 491, the domain is characterized as PDZ 2.
+At position 70 to 185, the domain is characterized as Expansin-like EG45.
+At position 195 to 275, the domain is characterized as Expansin-like CBD.
+At position 13 to 131, the domain is characterized as Arf-GAP.
+At position 345 to 545, the domain is characterized as Reticulon.
+At position 27 to 174, the domain is characterized as FAS1 1.
+At position 187 to 326, the domain is characterized as FAS1 2.
+At position 21 to 352, the domain is characterized as SET.
+At position 911 to 976, the domain is characterized as HP.
+At position 119 to 437, the domain is characterized as Kinesin motor.
+At position 5 to 69, the domain is characterized as PQ-loop 1.
+At position 138 to 194, the domain is characterized as PQ-loop 2.
+At position 21 to 231, the domain is characterized as Ch-type lysozyme.
+At position 130 to 557, the domain is characterized as Urease.
+At position 15 to 336, the domain is characterized as Deacetylase sirtuin-type.
+At position 131 to 329, the domain is characterized as VWFA.
+At position 979 to 1084, the domain is characterized as Calx-beta.
+At position 1129 to 1218, the domain is characterized as Fibronectin type-III 1.
+At position 1222 to 1321, the domain is characterized as Fibronectin type-III 2.
+At position 1530 to 1625, the domain is characterized as Fibronectin type-III 3.
+At position 1643 to 1739, the domain is characterized as Fibronectin type-III 4.
+At position 150 to 253, the domain is characterized as Ig-like V-type 2.
+At position 254 to 355, the domain is characterized as Ig-like C2-type 1.
+At position 355 to 441, the domain is characterized as Ig-like C2-type 2.
+At position 448 to 538, the domain is characterized as Ig-like C2-type 3.
+At position 225 to 499, the domain is characterized as Protein kinase.
+At position 1483 to 1659, the domain is characterized as PIK helical.
+At position 1734 to 2012, the domain is characterized as PI3K/PI4K catalytic.
+At position 23 to 305, the domain is characterized as GH18.
+At position 111 to 271, the domain is characterized as PA14.
+At position 26 to 142, the domain is characterized as MTTase N-terminal.
+At position 398 to 464, the domain is characterized as TRAM.
+At position 15 to 146, the domain is characterized as MPN.
+At position 93 to 163, the domain is characterized as CSD.
+At position 550 to 651, the domain is characterized as tRNA-binding.
+At position 55 to 215, the domain is characterized as SIS.
+At position 145 to 313, the domain is characterized as Helicase ATP-binding.
+At position 405 to 557, the domain is characterized as Helicase C-terminal.
+At position 770 to 884, the domain is characterized as VRR-NUC.
+At position 273 to 326, the domain is characterized as HAMP.
+At position 345 to 581, the domain is characterized as Methyl-accepting transducer.
+At position 164 to 262, the domain is characterized as RRM 1.
+At position 270 to 348, the domain is characterized as RRM 2.
+At position 3 to 289, the domain is characterized as Clp R.
+At position 603 to 638, the domain is characterized as UVR.
+At position 2 to 308, the domain is characterized as SAM-dependent MTase C5-type.
+At position 31 to 226, the domain is characterized as BPL/LPL catalytic.
+At position 19 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 5 to 411, the domain is characterized as PTS EIIC type-3.
+At position 174 to 344, the domain is characterized as tr-type G.
+At position 15 to 101, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 257 to 442, the domain is characterized as FAD-binding PCMH-type.
+At position 635 to 706, the domain is characterized as S1 motif.
+At position 187 to 457, the domain is characterized as F-BAR.
+At position 668 to 883, the domain is characterized as Rho-GAP.
+At position 760 to 826, the domain is characterized as HP.
+At position 517 to 796, the domain is characterized as ASD2.
+At position 359 to 394, the domain is characterized as UVR.
+At position 353 to 520, the domain is characterized as tr-type G.
+At position 86 to 315, the domain is characterized as Radical SAM core.
+At position 33 to 389, the domain is characterized as IF rod.
+At position 431 to 547, the domain is characterized as LTD.
+At position 102 to 266, the domain is characterized as JmjC.
+At position 115 to 443, the domain is characterized as Protein kinase.
+At position 281 to 379, the domain is characterized as SWIRM.
+At position 36 to 100, the domain is characterized as J.
+At position 131 to 233, the domain is characterized as Thioredoxin 1.
+At position 455 to 554, the domain is characterized as Thioredoxin 2.
+At position 558 to 668, the domain is characterized as Thioredoxin 3.
+At position 672 to 780, the domain is characterized as Thioredoxin 4.
+At position 12 to 221, the domain is characterized as YjeF N-terminal.
+At position 369 to 483, the domain is characterized as Response regulatory.
+At position 415 to 604, the domain is characterized as DH.
+At position 646 to 759, the domain is characterized as PH.
+At position 1 to 180, the domain is characterized as YrdC-like.
+At position 256 to 441, the domain is characterized as GATase cobBQ-type.
+At position 300 to 370, the domain is characterized as PAS 1.
+At position 374 to 426, the domain is characterized as PAC 1.
+At position 501 to 552, the domain is characterized as PAC 2.
+At position 553 to 623, the domain is characterized as PAS 2.
+At position 626 to 680, the domain is characterized as PAC 3.
+At position 712 to 845, the domain is characterized as GGDEF.
+At position 855 to 1104, the domain is characterized as EAL.
+At position 47 to 116, the domain is characterized as MaoC-like.
+At position 3 to 195, the domain is characterized as PTS EIIB type-5.
+At position 104 to 318, the domain is characterized as ATP-grasp.
+At position 52 to 303, the domain is characterized as Protein kinase.
+At position 93 to 194, the domain is characterized as Thioredoxin.
+At position 62 to 147, the domain is characterized as LITAF.
+At position 28 to 143, the domain is characterized as MTTase N-terminal.
+At position 166 to 396, the domain is characterized as Radical SAM core.
+At position 45 to 187, the domain is characterized as Tyrosine-protein phosphatase.
+At position 146 to 235, the domain is characterized as RRM.
+At position 41 to 424, the domain is characterized as USP.
+At position 274 to 361, the domain is characterized as Plastocyanin-like.
+At position 209 to 294, the domain is characterized as Ig-like C2-type 3.
+At position 400 to 484, the domain is characterized as Ig-like C2-type 5.
+At position 594 to 690, the domain is characterized as Fibronectin type-III 2.
+At position 647 to 709, the domain is characterized as MucBP 3.
+At position 41 to 146, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 363 to 437, the domain is characterized as RRM 3.
+At position 480 to 555, the domain is characterized as RRM 4.
+At position 368 to 646, the domain is characterized as Radical SAM core.
+At position 52 to 272, the domain is characterized as Cupin type-1 1.
+At position 333 to 482, the domain is characterized as Cupin type-1 2.
+At position 1 to 302, the domain is characterized as Protein kinase 1.
+At position 1342 to 1592, the domain is characterized as Protein kinase 2.
+At position 230 to 421, the domain is characterized as Helicase C-terminal.
+At position 5 to 78, the domain is characterized as Histone-fold.
+At position 99 to 303, the domain is characterized as ATP-grasp.
+At position 1 to 319, the domain is characterized as Asparaginase/glutaminase.
+At position 6 to 53, the domain is characterized as SpoVT-AbrB 1.
+At position 52 to 228, the domain is characterized as GH11.
+At position 133 to 340, the domain is characterized as ATP-grasp.
+At position 552 to 752, the domain is characterized as FtsK.
+At position 435 to 590, the domain is characterized as Exonuclease.
+At position 1 to 128, the domain is characterized as Fido.
+At position 1 to 44, the domain is characterized as Gla.
+At position 197 to 460, the domain is characterized as Protein kinase.
+At position 102 to 388, the domain is characterized as tr-type G.
+At position 20 to 273, the domain is characterized as Protein kinase.
+At position 411 to 458, the domain is characterized as SARAH.
+At position 41 to 150, the domain is characterized as WH1.
+At position 240 to 253, the domain is characterized as CRIB.
+At position 448 to 465, the domain is characterized as WH2.
+At position 135 to 263, the domain is characterized as C2 2.
+At position 306 to 505, the domain is characterized as VWFA.
+At position 1 to 35, the domain is characterized as Peptidase S1.
+At position 280 to 554, the domain is characterized as Letm1 RBD.
+At position 770 to 805, the domain is characterized as EF-hand 2.
+At position 481 to 651, the domain is characterized as Miro 2.
+At position 74 to 264, the domain is characterized as ABC transmembrane type-1.
+At position 418 to 477, the domain is characterized as LIM zinc-binding 1.
+At position 477 to 536, the domain is characterized as LIM zinc-binding 2.
+At position 536 to 596, the domain is characterized as LIM zinc-binding 3.
+At position 45 to 227, the domain is characterized as PCI.
+At position 151 to 186, the domain is characterized as EF-hand 1.
+At position 282 to 317, the domain is characterized as EF-hand 3.
+At position 319 to 354, the domain is characterized as EF-hand 4.
+At position 286 to 816, the domain is characterized as USP.
+At position 73 to 151, the domain is characterized as RRM 1.
+At position 153 to 235, the domain is characterized as RRM 2.
+At position 248 to 320, the domain is characterized as RRM 3.
+At position 128 to 215, the domain is characterized as Ig-like V-type 2.
+At position 124 to 203, the domain is characterized as RRM.
+At position 391 to 541, the domain is characterized as NTF2.
+At position 570 to 625, the domain is characterized as TAP-C.
+At position 3 to 100, the domain is characterized as PB1.
+At position 388 to 433, the domain is characterized as UBA.
+At position 503 to 648, the domain is characterized as Helicase C-terminal.
+At position 954 to 1120, the domain is characterized as PNPLA.
+At position 1 to 142, the domain is characterized as YEATS.
+At position 34 to 102, the domain is characterized as Importin N-terminal.
+At position 342 to 574, the domain is characterized as TLDc.
+At position 2 to 69, the domain is characterized as Sm.
+At position 84 to 190, the domain is characterized as AD.
+At position 92 to 310, the domain is characterized as Radical SAM core.
+At position 117 to 601, the domain is characterized as Peptidase S8.
+At position 365 to 460, the domain is characterized as PA.
+At position 371 to 646, the domain is characterized as Protein kinase.
+At position 285 to 357, the domain is characterized as RRM 1.
+At position 359 to 445, the domain is characterized as RRM 2.
+At position 55 to 225, the domain is characterized as PPIase cyclophilin-type.
+At position 285 to 315, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 337 to 367, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 5 to 309, the domain is characterized as YEATS.
+At position 53 to 141, the domain is characterized as Ig-like V-type.
+At position 12 to 248, the domain is characterized as PABS.
+At position 218 to 379, the domain is characterized as TrmE-type G.
+At position 199 to 284, the domain is characterized as KH type-2.
+At position 3 to 183, the domain is characterized as Glutamine amidotransferase type-1.
+At position 597 to 679, the domain is characterized as BRCT.
+At position 29 to 191, the domain is characterized as FAD-binding PCMH-type.
+At position 99 to 250, the domain is characterized as Exonuclease.
+At position 23 to 288, the domain is characterized as Protein kinase.
+At position 132 to 234, the domain is characterized as Ig-like C2-type 2.
+At position 216 to 417, the domain is characterized as Helicase ATP-binding.
+At position 444 to 595, the domain is characterized as Helicase C-terminal.
+At position 58 to 150, the domain is characterized as J.
+At position 256 to 438, the domain is characterized as GATase cobBQ-type.
+At position 115 to 293, the domain is characterized as FAD-binding PCMH-type.
+At position 67 to 214, the domain is characterized as Thioredoxin.
+At position 57 to 148, the domain is characterized as HTH La-type RNA-binding.
+At position 154 to 236, the domain is characterized as RRM.
+At position 1677 to 1740, the domain is characterized as SAM.
+At position 1461 to 1754, the domain is characterized as Autotransporter.
+At position 90 to 394, the domain is characterized as Peptidase A1.
+At position 67 to 144, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 187 to 211, the domain is characterized as HhH.
+At position 298 to 487, the domain is characterized as Protein kinase.
+At position 180 to 202, the domain is characterized as LDL-receptor class A.
+At position 199 to 301, the domain is characterized as SRCR.
+At position 302 to 535, the domain is characterized as Peptidase S1.
+At position 268 to 310, the domain is characterized as CCT.
+At position 42 to 98, the domain is characterized as Myb-like.
+At position 5 to 205, the domain is characterized as ABC transporter.
+At position 41 to 156, the domain is characterized as sHSP.
+At position 73 to 212, the domain is characterized as Flavodoxin-like.
+At position 247 to 480, the domain is characterized as FAD-binding FR-type.
+At position 107 to 276, the domain is characterized as Helicase ATP-binding.
+At position 304 to 455, the domain is characterized as Helicase C-terminal.
+At position 90 to 278, the domain is characterized as Rab-GAP TBC.
+At position 210 to 281, the domain is characterized as PAS.
+At position 335 to 527, the domain is characterized as Histidine kinase.
+At position 1 to 62, the domain is characterized as F-box.
+At position 1031 to 1175, the domain is characterized as RUN.
+At position 1447 to 1506, the domain is characterized as SH3.
+At position 32 to 284, the domain is characterized as SET.
+At position 54 to 540, the domain is characterized as Hexokinase.
+At position 190 to 482, the domain is characterized as SF4 helicase.
+At position 70 to 92, the domain is characterized as Follistatin-like.
+At position 88 to 150, the domain is characterized as Kazal-like.
+At position 260 to 295, the domain is characterized as EF-hand.
+At position 48 to 198, the domain is characterized as Helicase ATP-binding.
+At position 275 to 467, the domain is characterized as Helicase C-terminal.
+At position 202 to 570, the domain is characterized as GRAS.
+At position 1 to 21, the domain is characterized as CSD.
+At position 27 to 68, the domain is characterized as LDL-receptor class A 1.
+At position 71 to 235, the domain is characterized as MAM 1.
+At position 234 to 402, the domain is characterized as MAM 2.
+At position 399 to 437, the domain is characterized as LDL-receptor class A 2.
+At position 443 to 603, the domain is characterized as MAM 3.
+At position 618 to 782, the domain is characterized as MAM 4.
+At position 788 to 826, the domain is characterized as LDL-receptor class A 3.
+At position 829 to 990, the domain is characterized as MAM 5.
+At position 1015 to 1052, the domain is characterized as LDL-receptor class A 4.
+At position 1054 to 1222, the domain is characterized as MAM 6.
+At position 1229 to 1267, the domain is characterized as LDL-receptor class A 5.
+At position 1271 to 1431, the domain is characterized as MAM 7.
+At position 1448 to 1484, the domain is characterized as LDL-receptor class A 6.
+At position 1485 to 1642, the domain is characterized as MAM 8.
+At position 1649 to 1686, the domain is characterized as LDL-receptor class A 7.
+At position 1693 to 1858, the domain is characterized as MAM 9.
+At position 1868 to 1905, the domain is characterized as LDL-receptor class A 8.
+At position 1912 to 1948, the domain is characterized as LDL-receptor class A 9.
+At position 1951 to 1989, the domain is characterized as LDL-receptor class A 10.
+At position 1990 to 2023, the domain is characterized as EGF-like.
+At position 1 to 123, the domain is characterized as Clp R.
+At position 62 to 167, the domain is characterized as TBDR plug.
+At position 180 to 181, the domain is characterized as TBDR beta-barrel.
+At position 68 to 322, the domain is characterized as ABC transporter.
+At position 411 to 617, the domain is characterized as ABC transmembrane type-2.
+At position 360 to 590, the domain is characterized as TLDc.
+At position 2 to 146, the domain is characterized as MGS-like.
+At position 3 to 114, the domain is characterized as MTTase N-terminal.
+At position 138 to 367, the domain is characterized as Radical SAM core.
+At position 41 to 131, the domain is characterized as 2Fe-2S ferredoxin-type.
+At position 735 to 908, the domain is characterized as Mic1.
+At position 3 to 174, the domain is characterized as MurNAc-LAA.
+At position 184 to 346, the domain is characterized as PCI.
+At position 591 to 738, the domain is characterized as MOSC.
+At position 137 to 520, the domain is characterized as GRAS.
+At position 16 to 270, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 238 to 309, the domain is characterized as RST.
+At position 333 to 446, the domain is characterized as PAZ.
+At position 620 to 941, the domain is characterized as Piwi.
+At position 675 to 851, the domain is characterized as PCI.
+At position 4 to 228, the domain is characterized as ABC transporter.
+At position 375 to 446, the domain is characterized as TRAM.
+At position 471 to 753, the domain is characterized as Protein kinase.
+At position 9 to 707, the domain is characterized as Myosin motor.
+At position 710 to 739, the domain is characterized as IQ.
+At position 824 to 1017, the domain is characterized as TH1.
+At position 576 to 635, the domain is characterized as KH.
+At position 647 to 719, the domain is characterized as S1 motif.
+At position 190 to 480, the domain is characterized as GT23.
+At position 489 to 550, the domain is characterized as SH3.
+At position 120 to 232, the domain is characterized as TBDR plug.
+At position 238 to 1001, the domain is characterized as TBDR beta-barrel.
+At position 131 to 466, the domain is characterized as Peptidase A1.
+At position 69 to 127, the domain is characterized as SCAN box.
+At position 41 to 71, the domain is characterized as EF-hand 2.
+At position 109 to 143, the domain is characterized as EF-hand 4.
+At position 35 to 99, the domain is characterized as CSD.
+At position 18 to 111, the domain is characterized as PH.
+At position 94 to 225, the domain is characterized as GST C-terminal.
+At position 367 to 534, the domain is characterized as tr-type G.
+At position 991 to 1059, the domain is characterized as R3H.
+At position 104 to 436, the domain is characterized as Kinesin motor.
+At position 15 to 110, the domain is characterized as sHSP.
+At position 582 to 670, the domain is characterized as Ig-like.
+At position 25 to 202, the domain is characterized as EngB-type G.
+At position 260 to 444, the domain is characterized as Laminin G-like 2.
+At position 451 to 643, the domain is characterized as Laminin G-like 3.
+At position 647 to 684, the domain is characterized as EGF-like 2.
+At position 689 to 861, the domain is characterized as Laminin G-like 4.
+At position 875 to 1050, the domain is characterized as Laminin G-like 5.
+At position 1053 to 1090, the domain is characterized as EGF-like 3.
+At position 1094 to 1294, the domain is characterized as Laminin G-like 6.
+At position 125 to 324, the domain is characterized as MAGE.
+At position 313 to 605, the domain is characterized as Protein kinase.
+At position 84 to 283, the domain is characterized as Peptidase M12A.
+At position 285 to 397, the domain is characterized as CUB 1.
+At position 398 to 509, the domain is characterized as CUB 2.
+At position 510 to 551, the domain is characterized as EGF-like; calcium-binding.
+At position 554 to 666, the domain is characterized as CUB 3.
+At position 687 to 748, the domain is characterized as TSP type-1 2.
+At position 750 to 804, the domain is characterized as TSP type-1 3.
+At position 805 to 871, the domain is characterized as TSP type-1 4.
+At position 872 to 931, the domain is characterized as TSP type-1 5.
+At position 932 to 988, the domain is characterized as TSP type-1 6.
+At position 991 to 1028, the domain is characterized as PLAC.
+At position 190 to 284, the domain is characterized as PpiC.
+At position 544 to 576, the domain is characterized as EGF-like 1.
+At position 733 to 817, the domain is characterized as BRCT.
+At position 10 to 206, the domain is characterized as AB hydrolase-1.
+At position 1 to 254, the domain is characterized as IF rod.
+At position 134 to 529, the domain is characterized as GRAS.
+At position 248 to 577, the domain is characterized as PDEase.
+At position 187 to 269, the domain is characterized as RCK C-terminal 1.
+At position 271 to 352, the domain is characterized as RCK C-terminal 2.
+At position 31 to 125, the domain is characterized as PpiC.
+At position 330 to 609, the domain is characterized as ABC transporter 1.
+At position 1 to 453, the domain is characterized as ADPK.
+At position 50 to 293, the domain is characterized as ABC transporter.
+At position 382 to 594, the domain is characterized as ABC transmembrane type-2.
+At position 91 to 183, the domain is characterized as K-box.
+At position 121 to 156, the domain is characterized as EF-hand 1.
+At position 187 to 222, the domain is characterized as EF-hand 2.
+At position 96 to 179, the domain is characterized as PDZ.
+At position 2323 to 2369, the domain is characterized as G-patch.
+At position 2389 to 2444, the domain is characterized as DRBM.
+At position 29 to 86, the domain is characterized as HTH lysR-type.
+At position 33 to 63, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 199 to 396, the domain is characterized as Helicase ATP-binding.
+At position 70 to 423, the domain is characterized as IF rod.
+At position 456 to 572, the domain is characterized as LTD.
+At position 157 to 522, the domain is characterized as GRAS.
+At position 417 to 477, the domain is characterized as SH3.
+At position 3 to 398, the domain is characterized as BRO1.
+At position 23 to 320, the domain is characterized as Deacetylase sirtuin-type.
+At position 267 to 342, the domain is characterized as PUA.
+At position 284 to 321, the domain is characterized as LIM zinc-binding 1.
+At position 344 to 403, the domain is characterized as LIM zinc-binding 2.
+At position 404 to 472, the domain is characterized as LIM zinc-binding 3.
+At position 37 to 129, the domain is characterized as HTH La-type RNA-binding.
+At position 141 to 228, the domain is characterized as RRM.
+At position 249 to 368, the domain is characterized as xRRM.
+At position 116 to 377, the domain is characterized as Protein kinase.
+At position 380 to 445, the domain is characterized as SH3.
+At position 357 to 408, the domain is characterized as FBD.
+At position 32 to 108, the domain is characterized as U-box.
+At position 40 to 76, the domain is characterized as Collagen-like.
+At position 82 to 212, the domain is characterized as C1q.
+At position 57 to 134, the domain is characterized as Inhibitor I9.
+At position 148 to 419, the domain is characterized as Peptidase S8.
+At position 272 to 479, the domain is characterized as SMP-LTD.
+At position 470 to 596, the domain is characterized as C2 1.
+At position 646 to 763, the domain is characterized as C2 2.
+At position 783 to 897, the domain is characterized as C2 3.
+At position 1119 to 1234, the domain is characterized as C2 4.
+At position 1396 to 1514, the domain is characterized as C2 5.
+At position 126 to 232, the domain is characterized as Calponin-homology (CH) 1.
+At position 341 to 449, the domain is characterized as Calponin-homology (CH) 2.
+At position 511 to 619, the domain is characterized as Calponin-homology (CH) 3.
+At position 632 to 846, the domain is characterized as DH.
+At position 876 to 1026, the domain is characterized as PH.
+At position 26 to 99, the domain is characterized as IGFBP N-terminal.
+At position 145 to 220, the domain is characterized as Thyroglobulin type-1.
+At position 821 to 876, the domain is characterized as CBS 2.
+At position 352 to 416, the domain is characterized as S4 RNA-binding.
+At position 674 to 980, the domain is characterized as Protein kinase.
+At position 983 to 1115, the domain is characterized as KEN.
+At position 147 to 220, the domain is characterized as HTH crp-type.
+At position 27 to 172, the domain is characterized as Thioredoxin.
+At position 38 to 233, the domain is characterized as Lon N-terminal.
+At position 619 to 800, the domain is characterized as Lon proteolytic.
+At position 3 to 54, the domain is characterized as HTH psq-type.
+At position 66 to 137, the domain is characterized as HTH CENPB-type.
+At position 170 to 372, the domain is characterized as DDE-1.
+At position 30 to 226, the domain is characterized as BPL/LPL catalytic.
+At position 25 to 193, the domain is characterized as Plastocyanin-like 1.
+At position 194 to 363, the domain is characterized as Plastocyanin-like 2.
+At position 30 to 262, the domain is characterized as Protein kinase.
+At position 542 to 870, the domain is characterized as HECT.
+At position 81 to 187, the domain is characterized as Rieske.
+At position 45 to 108, the domain is characterized as bZIP.
+At position 90 to 119, the domain is characterized as 4Fe-4S ferredoxin-type 1.
+At position 129 to 158, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 36 to 160, the domain is characterized as Response regulatory.
+At position 325 to 522, the domain is characterized as HD-GYP.
+At position 56 to 196, the domain is characterized as Nudix hydrolase.
+At position 92 to 167, the domain is characterized as PA.
+At position 11 to 248, the domain is characterized as SET.
+At position 104 to 219, the domain is characterized as sHSP.
+At position 57 to 148, the domain is characterized as Pyrin.
+At position 280 to 602, the domain is characterized as NACHT.
+At position 5 to 398, the domain is characterized as BRO1.
+At position 309 to 589, the domain is characterized as ABC transporter 1.
+At position 41 to 219, the domain is characterized as EngB-type G.
+At position 81 to 276, the domain is characterized as SAM-dependent MTase TRM10-type.
+At position 85 to 296, the domain is characterized as ABC transmembrane type-1.
+At position 91 to 307, the domain is characterized as RNase H type-2.
+At position 90 to 344, the domain is characterized as Protein kinase.
+At position 345 to 398, the domain is characterized as AGC-kinase C-terminal.
+At position 24 to 333, the domain is characterized as mRNA cap 0 methyltransferase.
+At position 164 to 484, the domain is characterized as Protein kinase.
+At position 72 to 195, the domain is characterized as SCP.
+At position 162 to 242, the domain is characterized as PPIase FKBP-type.
+At position 17 to 116, the domain is characterized as BRCT.
+At position 127 to 171, the domain is characterized as SMB 2.
+At position 275 to 383, the domain is characterized as PET.
+At position 382 to 446, the domain is characterized as LIM zinc-binding 1.
+At position 447 to 507, the domain is characterized as LIM zinc-binding 2.
+At position 508 to 570, the domain is characterized as LIM zinc-binding 3.
+At position 16 to 212, the domain is characterized as ABC transporter.
+At position 107 to 152, the domain is characterized as EGF-like 2.
+At position 178 to 224, the domain is characterized as EGF-like 3.
+At position 252 to 293, the domain is characterized as EGF-like 4.
+At position 13 to 135, the domain is characterized as EamA.
+At position 384 to 637, the domain is characterized as MIF4G.
+At position 193 to 370, the domain is characterized as MurNAc-LAA.
+At position 2 to 141, the domain is characterized as Flavodoxin-like.
+At position 302 to 383, the domain is characterized as PDZ.
+At position 160 to 464, the domain is characterized as Velvet.
+At position 37 to 110, the domain is characterized as S4 RNA-binding.
+At position 170 to 244, the domain is characterized as POU-specific.
+At position 1585 to 1679, the domain is characterized as BRCT 1.
+At position 1698 to 1797, the domain is characterized as BRCT 2.
+At position 163 to 226, the domain is characterized as R3H.
+At position 227 to 298, the domain is characterized as SUZ.
+At position 207 to 436, the domain is characterized as Sigma-54 factor interaction.
+At position 8 to 205, the domain is characterized as tr-type G.
+At position 1 to 340, the domain is characterized as Alpha-carbonic anhydrase.
+At position 28 to 67, the domain is characterized as EGF-like.
+At position 70 to 104, the domain is characterized as RIIa.
+At position 110 to 180, the domain is characterized as MBD.
+At position 84 to 130, the domain is characterized as Collagen-like 2.
+At position 34 to 126, the domain is characterized as Ig-like V-type 1.
+At position 131 to 240, the domain is characterized as Ig-like V-type 2.
+At position 251 to 333, the domain is characterized as Ig-like C2-type 1.
+At position 338 to 414, the domain is characterized as Ig-like C2-type 2.
+At position 421 to 501, the domain is characterized as Ig-like C2-type 3.
+At position 81 to 160, the domain is characterized as GIY-YIG.
+At position 302 to 614, the domain is characterized as Protein kinase.
+At position 222 to 460, the domain is characterized as PPM-type phosphatase.
+At position 581 to 616, the domain is characterized as EF-hand 1.
+At position 332 to 395, the domain is characterized as S4 RNA-binding.
+At position 81 to 278, the domain is characterized as SMP-LTD.
+At position 115 to 226, the domain is characterized as SET.
+At position 453 to 502, the domain is characterized as bHLH.
+At position 25 to 88, the domain is characterized as Kazal-like 1.
+At position 89 to 153, the domain is characterized as Kazal-like 2.
+At position 26 to 140, the domain is characterized as HD.
+At position 125 to 174, the domain is characterized as bHLH.
+At position 104 to 144, the domain is characterized as SMB 1.
+At position 145 to 189, the domain is characterized as SMB 2.
+At position 290 to 477, the domain is characterized as B30.2/SPRY.
+At position 28 to 102, the domain is characterized as Ricin B-type lectin 1.
+At position 115 to 245, the domain is characterized as Ricin B-type lectin 2.
+At position 261 to 293, the domain is characterized as Ricin B-type lectin 3.
+At position 223 to 342, the domain is characterized as C2 1.
+At position 344 to 471, the domain is characterized as C2 2.
+At position 79 to 404, the domain is characterized as Kinesin motor.
+At position 528 to 805, the domain is characterized as Protein kinase.
+At position 30 to 219, the domain is characterized as EngB-type G.
+At position 389 to 476, the domain is characterized as Disintegrin.
+At position 615 to 648, the domain is characterized as EGF-like.
+At position 20 to 109, the domain is characterized as PI3K-ABD.
+At position 188 to 279, the domain is characterized as PI3K-RBD.
+At position 323 to 490, the domain is characterized as C2 PI3K-type.
+At position 518 to 695, the domain is characterized as PIK helical.
+At position 766 to 1047, the domain is characterized as PI3K/PI4K catalytic.
+At position 67 to 251, the domain is characterized as BPL/LPL catalytic.
+At position 307 to 465, the domain is characterized as FCP1 homology.
+At position 1 to 45, the domain is characterized as LysM 1.
+At position 47 to 316, the domain is characterized as CoA carboxyltransferase N-terminal.
+At position 550 to 700, the domain is characterized as CBM3.
+At position 12 to 267, the domain is characterized as DOG1.
+At position 51 to 333, the domain is characterized as GH18.
+At position 508 to 768, the domain is characterized as Protein kinase.
+At position 771 to 899, the domain is characterized as KEN.
+At position 120 to 185, the domain is characterized as HTH luxR-type.
+At position 1 to 70, the domain is characterized as TGS.
+At position 225 to 241, the domain is characterized as UIM.
+At position 162 to 427, the domain is characterized as Protein kinase.
+At position 10 to 246, the domain is characterized as ABC transporter.
+At position 704 to 1130, the domain is characterized as CBP/p300-type HAT.
+At position 748 to 783, the domain is characterized as EF-hand.
+At position 236 to 362, the domain is characterized as Sox C-terminal.
+At position 86 to 317, the domain is characterized as CHASE.
+At position 396 to 526, the domain is characterized as Guanylate cyclase.
+At position 192 to 302, the domain is characterized as Ig-like C1-type.
+At position 100 to 178, the domain is characterized as RRM.
+At position 814 to 1003, the domain is characterized as JmjC.
+At position 419 to 652, the domain is characterized as UmuC.
+At position 7 to 230, the domain is characterized as DOG1.
+At position 59 to 120, the domain is characterized as KH 1.
+At position 155 to 216, the domain is characterized as KH 2.
+At position 192 to 289, the domain is characterized as HTH araC/xylS-type.
+At position 94 to 283, the domain is characterized as Brix.
+At position 353 to 677, the domain is characterized as SAM-dependent MTase PRMT-type 2.
+At position 45 to 111, the domain is characterized as EamA.
+At position 2 to 381, the domain is characterized as SPX.
+At position 638 to 828, the domain is characterized as EXS.
+At position 546 to 596, the domain is characterized as DHHC.
+At position 63 to 220, the domain is characterized as CP-type G.
+At position 68 to 333, the domain is characterized as AB hydrolase-1.
+At position 453 to 607, the domain is characterized as PPIase cyclophilin-type.
+At position 61 to 179, the domain is characterized as PH.
+At position 184 to 197, the domain is characterized as CRIB.
+At position 546 to 825, the domain is characterized as Protein kinase.
+At position 30 to 213, the domain is characterized as FAD-binding PCMH-type.
+At position 108 to 273, the domain is characterized as NIDO.
+At position 484 to 524, the domain is characterized as EGF-like 1.
+At position 528 to 758, the domain is characterized as Nidogen G2 beta-barrel.
+At position 759 to 800, the domain is characterized as EGF-like 2.
+At position 801 to 843, the domain is characterized as EGF-like 3; calcium-binding.
+At position 848 to 891, the domain is characterized as EGF-like 4.
+At position 892 to 930, the domain is characterized as EGF-like 5; calcium-binding.
+At position 937 to 1005, the domain is characterized as Thyroglobulin type-1 1.
+At position 1016 to 1084, the domain is characterized as Thyroglobulin type-1 2.
+At position 33 to 453, the domain is characterized as Helicase ATP-binding.
+At position 63 to 252, the domain is characterized as B30.2/SPRY.
+At position 512 to 715, the domain is characterized as Helicase C-terminal.
+At position 25 to 118, the domain is characterized as WSC.
+At position 7 to 158, the domain is characterized as Tyrosine-protein phosphatase.
+At position 279 to 363, the domain is characterized as PDZ.
+At position 1 to 162, the domain is characterized as ABC transmembrane type-1.
+At position 60 to 176, the domain is characterized as DOMON.
+At position 443 to 606, the domain is characterized as Helicase C-terminal.
+At position 33 to 276, the domain is characterized as Protein kinase.
+At position 192 to 423, the domain is characterized as GB1/RHD3-type G.
+At position 59 to 173, the domain is characterized as Expansin-like EG45.
+At position 188 to 281, the domain is characterized as Expansin-like CBD.
+At position 134 to 147, the domain is characterized as CRIB.
+At position 78 to 162, the domain is characterized as LITAF.
+At position 224 to 356, the domain is characterized as Nudix hydrolase.
+At position 204 to 278, the domain is characterized as POU-specific.
+At position 53 to 82, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 348 to 563, the domain is characterized as ABC transporter 2.
+At position 104 to 349, the domain is characterized as Radical SAM core.
+At position 143 to 257, the domain is characterized as C-type lectin.
+At position 14 to 245, the domain is characterized as ABC transporter.
+At position 34 to 116, the domain is characterized as Lipoyl-binding.
+At position 14 to 115, the domain is characterized as CUB.
+At position 1 to 115, the domain is characterized as IF rod.
+At position 207 to 264, the domain is characterized as CBS 1.
+At position 98 to 204, the domain is characterized as sHSP.
+At position 30 to 112, the domain is characterized as RRM 1.
+At position 115 to 194, the domain is characterized as RRM 2.
+At position 12 to 77, the domain is characterized as BRCT 1.
+At position 119 to 196, the domain is characterized as BRCT 2.
+At position 299 to 420, the domain is characterized as C2 1.
+At position 431 to 565, the domain is characterized as C2 2.
+At position 164 to 474, the domain is characterized as Velvet.
+At position 83 to 144, the domain is characterized as SH3.
+At position 150 to 247, the domain is characterized as SH2.
+At position 269 to 522, the domain is characterized as Protein kinase.
+At position 247 to 322, the domain is characterized as PUA.
+At position 786 to 1074, the domain is characterized as Protein kinase.
+At position 272 to 355, the domain is characterized as RRM 1.
+At position 392 to 470, the domain is characterized as RRM 2.
+At position 2 to 200, the domain is characterized as Glutamine amidotransferase type-1.
+At position 294 to 401, the domain is characterized as Rhodanese.
+At position 34 to 184, the domain is characterized as N-acetyltransferase.
+At position 130 to 190, the domain is characterized as OVATE.
+At position 32 to 182, the domain is characterized as Ricin B-type lectin.
+At position 958 to 1091, the domain is characterized as C-type lectin 5.
+At position 1110 to 1222, the domain is characterized as C-type lectin 6.
+At position 1251 to 1374, the domain is characterized as C-type lectin 7.
+At position 1401 to 1513, the domain is characterized as C-type lectin 8.
+At position 1542 to 1661, the domain is characterized as C-type lectin 9.
+At position 103 to 183, the domain is characterized as PRC barrel.
+At position 5 to 141, the domain is characterized as Photolyase/cryptochrome alpha/beta.
+At position 233 to 328, the domain is characterized as Fibronectin type-III.
+At position 1832 to 1981, the domain is characterized as bMERB.
+At position 444 to 503, the domain is characterized as Collagen-like 1.
+At position 510 to 569, the domain is characterized as Collagen-like 2.
+At position 611 to 710, the domain is characterized as C-type lectin.
+At position 259 to 434, the domain is characterized as Helicase ATP-binding.
+At position 17 to 183, the domain is characterized as EngB-type G.
+At position 8 to 239, the domain is characterized as Phosphagen kinase C-terminal.
+At position 182 to 366, the domain is characterized as Helicase ATP-binding.
+At position 377 to 542, the domain is characterized as Helicase C-terminal.
+At position 775 to 1045, the domain is characterized as Protein kinase.
+At position 852 to 980, the domain is characterized as RGS 1.
+At position 1021 to 1145, the domain is characterized as RGS 2.
+At position 317 to 550, the domain is characterized as ABC transporter 2.
+At position 357 to 436, the domain is characterized as Fibronectin type-III 1.
+At position 516 to 606, the domain is characterized as Fibronectin type-III 2.
+At position 608 to 720, the domain is characterized as Fibronectin type-III 3.
+At position 249 to 445, the domain is characterized as GATase cobBQ-type.
+At position 456 to 558, the domain is characterized as Collagen-like 1.
+At position 559 to 601, the domain is characterized as Collagen-like 2.
+At position 253 to 413, the domain is characterized as EF-1-gamma C-terminal.
+At position 88 to 288, the domain is characterized as MAGE 1.
+At position 311 to 502, the domain is characterized as MAGE 2.
+At position 208 to 309, the domain is characterized as Fe2OG dioxygenase.
+At position 179 to 208, the domain is characterized as 4Fe-4S ferredoxin-type.
+At position 78 to 131, the domain is characterized as bHLH.
+At position 149 to 221, the domain is characterized as PAS 1.
+At position 340 to 406, the domain is characterized as PAS 2.
+At position 413 to 456, the domain is characterized as PAC.
+At position 177 to 258, the domain is characterized as Expansin-like CBD.
+At position 41 to 351, the domain is characterized as AB hydrolase-1.
+At position 379 to 446, the domain is characterized as TRAM.
+At position 166 to 441, the domain is characterized as Lon N-terminal.
+At position 13 to 93, the domain is characterized as GIY-YIG.
+At position 123 to 217, the domain is characterized as PPIase FKBP-type.
+At position 266 to 464, the domain is characterized as GATase cobBQ-type.
+At position 33 to 151, the domain is characterized as MTTase N-terminal.
+At position 174 to 404, the domain is characterized as Radical SAM core.
+At position 407 to 470, the domain is characterized as TRAM.
+At position 8 to 318, the domain is characterized as Kinesin motor.
+At position 33 to 419, the domain is characterized as Helicase ATP-binding.
+At position 236 to 290, the domain is characterized as SOCS box.
+At position 265 to 434, the domain is characterized as tr-type G.
+At position 1 to 89, the domain is characterized as Glutaredoxin.
+At position 18 to 105, the domain is characterized as LBH.
+At position 203 to 309, the domain is characterized as RRM.
+At position 533 to 737, the domain is characterized as Fibrinogen C-terminal.
+At position 90 to 344, the domain is characterized as F-BAR.
+At position 533 to 716, the domain is characterized as Rho-GAP.
+At position 484 to 653, the domain is characterized as tr-type G.
+At position 108 to 469, the domain is characterized as GS catalytic.
+At position 97 to 171, the domain is characterized as Cytochrome b5 heme-binding.
+At position 304 to 336, the domain is characterized as NAF.
+At position 9 to 125, the domain is characterized as C-type lectin.
+At position 14 to 147, the domain is characterized as Nudix hydrolase.
+At position 56 to 203, the domain is characterized as Cupin type-1.
+At position 69 to 761, the domain is characterized as Myosin motor.
+At position 769 to 798, the domain is characterized as IQ 1.
+At position 792 to 821, the domain is characterized as IQ 2.
+At position 817 to 848, the domain is characterized as IQ 3.
+At position 840 to 869, the domain is characterized as IQ 4.
+At position 865 to 896, the domain is characterized as IQ 5.
+At position 888 to 917, the domain is characterized as IQ 6.
+At position 1526 to 1803, the domain is characterized as Dilute.
+At position 6 to 357, the domain is characterized as Asparaginase/glutaminase.
+At position 69 to 129, the domain is characterized as FHA.
+At position 174 to 441, the domain is characterized as Protein kinase.
+At position 156 to 238, the domain is characterized as Ig-like V-type 2.
+At position 269 to 375, the domain is characterized as Ig-like C2-type.
+At position 182 to 571, the domain is characterized as FH2.
+At position 131 to 206, the domain is characterized as Ig-like C2-type.
+At position 107 to 298, the domain is characterized as CP-type G.
+At position 489 to 539, the domain is characterized as SANT.
+At position 594 to 693, the domain is characterized as CXC.
+At position 707 to 822, the domain is characterized as SET.
+At position 190 to 344, the domain is characterized as Helicase ATP-binding.
+At position 398 to 544, the domain is characterized as Helicase C-terminal.
+At position 63 to 180, the domain is characterized as NR LBD.
+At position 15 to 339, the domain is characterized as SAM-dependent MTase PRMT-type.
+At position 29 to 161, the domain is characterized as Ephrin RBD.
+At position 32 to 484, the domain is characterized as Biotin carboxylation.
+At position 154 to 351, the domain is characterized as ATP-grasp.
+At position 570 to 838, the domain is characterized as Pyruvate carboxyltransferase.
+At position 1108 to 1183, the domain is characterized as Biotinyl-binding.
+At position 406 to 663, the domain is characterized as Protein kinase.
+At position 138 to 392, the domain is characterized as ABC transporter 1.
+At position 497 to 724, the domain is characterized as ABC transmembrane type-2 1.
+At position 1177 to 1399, the domain is characterized as ABC transmembrane type-2 2.
+At position 420 to 449, the domain is characterized as 4Fe-4S ferredoxin-type 2.
+At position 85 to 145, the domain is characterized as S4 RNA-binding.
+At position 39 to 61, the domain is characterized as Collagen-like 1.
+At position 67 to 97, the domain is characterized as Collagen-like 2.
+At position 126 to 237, the domain is characterized as C-type lectin.
+At position 24 to 72, the domain is characterized as UPAR/Ly6.
+At position 21 to 655, the domain is characterized as Vitellogenin.
+At position 2 to 125, the domain is characterized as HTH rrf2-type.
+At position 49 to 119, the domain is characterized as H15.
+At position 135 to 207, the domain is characterized as PAS 1.
+At position 293 to 359, the domain is characterized as PAS 2.
+At position 365 to 408, the domain is characterized as PAC.
+At position 151 to 203, the domain is characterized as HAMP.
+At position 211 to 398, the domain is characterized as Histidine kinase.
+At position 432 to 454, the domain is characterized as Follistatin-like.
+At position 450 to 511, the domain is characterized as Kazal-like.
+At position 622 to 657, the domain is characterized as EF-hand.
+At position 30 to 125, the domain is characterized as HPt.
+At position 102 to 227, the domain is characterized as OTU.
+At position 197 to 286, the domain is characterized as EH 1.
+At position 230 to 265, the domain is characterized as EF-hand 1.
+At position 463 to 552, the domain is characterized as EH 2.
+At position 496 to 531, the domain is characterized as EF-hand 2.
+At position 1429 to 1446, the domain is characterized as WH2.
+At position 58 to 358, the domain is characterized as ABC transmembrane type-1.
+At position 391 to 592, the domain is characterized as ABC transporter.
+At position 179 to 272, the domain is characterized as Fe2OG dioxygenase.
+At position 169 to 324, the domain is characterized as C1q.
+At position 118 to 303, the domain is characterized as FAD-binding PCMH-type.
+At position 27 to 71, the domain is characterized as P-type 1.
+At position 77 to 120, the domain is characterized as P-type 2.
+At position 705 to 783, the domain is characterized as ACT 1.
+At position 10 to 94, the domain is characterized as Toprim.
+At position 1 to 126, the domain is characterized as ENTH.
+At position 7 to 65, the domain is characterized as CBS 1.
+At position 69 to 129, the domain is characterized as CBS 2.
+At position 153 to 246, the domain is characterized as Ig-like C2-type 2.
+At position 254 to 356, the domain is characterized as Ig-like C2-type 3.
+At position 208 to 354, the domain is characterized as Plastocyanin-like 2.
+At position 369 to 712, the domain is characterized as F5/8 type A 2.
+At position 369 to 554, the domain is characterized as Plastocyanin-like 3.
+At position 724 to 1055, the domain is characterized as F5/8 type A 3.
+At position 902 to 1051, the domain is characterized as Plastocyanin-like 6.
+At position 240 to 322, the domain is characterized as KH 2.
+At position 45 to 298, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 669 to 858, the domain is characterized as ATP-grasp 2.
+At position 927 to 1020, the domain is characterized as MGS-like.
+At position 132 to 212, the domain is characterized as Ig-like C2-type 2.
+At position 244 to 417, the domain is characterized as tr-type G.
+At position 42 to 145, the domain is characterized as C-type lectin.
+At position 30 to 181, the domain is characterized as MRH.
+At position 4 to 35, the domain is characterized as Chitin-binding type-1.
+At position 131 to 218, the domain is characterized as Ig-like C2-type 2.
+At position 223 to 307, the domain is characterized as Ig-like C2-type 3.
+At position 312 to 407, the domain is characterized as Ig-like C2-type 4.
+At position 416 to 502, the domain is characterized as Ig-like C2-type 5.
+At position 637 to 734, the domain is characterized as Fibronectin type-III 2.
+At position 739 to 835, the domain is characterized as Fibronectin type-III 3.
+At position 29 to 216, the domain is characterized as B30.2/SPRY.
+At position 247 to 279, the domain is characterized as LisH.
+At position 285 to 342, the domain is characterized as CTLH.
+At position 219 to 303, the domain is characterized as Death.
+At position 179 to 237, the domain is characterized as Sushi 1.
+At position 251 to 300, the domain is characterized as Sushi 2.
+At position 301 to 363, the domain is characterized as Sushi 3.
+At position 364 to 422, the domain is characterized as Sushi 4.
+At position 12 to 337, the domain is characterized as Protein kinase.
+At position 83 to 227, the domain is characterized as Clp R.
+At position 9 to 145, the domain is characterized as Nudix hydrolase.
+At position 186 to 221, the domain is characterized as EF-hand 4.
+At position 227 to 262, the domain is characterized as EF-hand 5.
+At position 263 to 298, the domain is characterized as EF-hand 6.
+At position 6 to 106, the domain is characterized as Glutaredoxin.
+At position 6 to 120, the domain is characterized as VOC 1.
+At position 143 to 263, the domain is characterized as VOC 2.
+At position 59 to 120, the domain is characterized as SH3.
+At position 126 to 218, the domain is characterized as SH2.
+At position 240 to 495, the domain is characterized as Protein kinase.
+At position 58 to 192, the domain is characterized as SCP.
+At position 22 to 232, the domain is characterized as DHFR.
+At position 514 to 700, the domain is characterized as DUF724.
+At position 1 to 65, the domain is characterized as KRAB.
+At position 107 to 288, the domain is characterized as ATP-grasp.
+At position 438 to 617, the domain is characterized as Lon proteolytic.
+At position 291 to 383, the domain is characterized as BRCT.
+At position 1 to 489, the domain is characterized as SMP-LTD.
+At position 247 to 451, the domain is characterized as Histidine kinase.
+At position 5 to 181, the domain is characterized as Brix.
+At position 34 to 106, the domain is characterized as EamA.
+At position 324 to 379, the domain is characterized as DEK-C.
+At position 383 to 524, the domain is characterized as Tyrosine-protein phosphatase.
+At position 58 to 194, the domain is characterized as Nudix hydrolase.
+At position 307 to 383, the domain is characterized as HSA.
+At position 482 to 647, the domain is characterized as Helicase ATP-binding.
+At position 795 to 956, the domain is characterized as Helicase C-terminal.
+At position 1270 to 1340, the domain is characterized as Bromo.
+At position 274 to 432, the domain is characterized as Helicase C-terminal.
+At position 127 to 421, the domain is characterized as AB hydrolase-1.
+At position 699 to 798, the domain is characterized as DMAP1-binding.
+At position 1005 to 1040, the domain is characterized as EF-hand.
+At position 348 to 670, the domain is characterized as Kinesin motor.
+At position 25 to 233, the domain is characterized as YjeF N-terminal.
+At position 235 to 515, the domain is characterized as YjeF C-terminal.
+At position 482 to 578, the domain is characterized as Fibronectin type-III.
+At position 726 to 808, the domain is characterized as SUEL-type lectin.
+At position 14 to 97, the domain is characterized as GS beta-grasp.
+At position 103 to 444, the domain is characterized as GS catalytic.
+At position 122 to 297, the domain is characterized as Helicase ATP-binding.
+At position 325 to 470, the domain is characterized as Helicase C-terminal.
+At position 15 to 237, the domain is characterized as Peptidase S1.
+At position 124 to 237, the domain is characterized as PilZ.
+At position 195 to 385, the domain is characterized as Peptidase M12B.
+At position 392 to 478, the domain is characterized as Disintegrin.
+At position 616 to 649, the domain is characterized as EGF-like.
+At position 356 to 613, the domain is characterized as Protein kinase.
+At position 236 to 430, the domain is characterized as Helicase C-terminal.
+At position 148 to 200, the domain is characterized as LIM zinc-binding 1.
+At position 210 to 263, the domain is characterized as LIM zinc-binding 2.
+At position 6 to 72, the domain is characterized as NAC-A/B.
+At position 208 to 329, the domain is characterized as SET.
+At position 544 to 645, the domain is characterized as tRNA-binding.
+At position 234 to 434, the domain is characterized as Helicase C-terminal.
+At position 258 to 490, the domain is characterized as ABC transporter 2.
+At position 125 to 477, the domain is characterized as TTL.
+At position 35 to 79, the domain is characterized as Fibronectin type-II 1.
+At position 80 to 128, the domain is characterized as Fibronectin type-II 2.
+At position 37 to 199, the domain is characterized as Nudix hydrolase.
+At position 6 to 74, the domain is characterized as BTB.
+At position 128 to 223, the domain is characterized as Ig-like C2-type 2.
+At position 234 to 317, the domain is characterized as Ig-like C2-type 3.
+At position 322 to 406, the domain is characterized as Ig-like C2-type 4.
+At position 412 to 499, the domain is characterized as Ig-like C2-type 5.
+At position 504 to 598, the domain is characterized as Ig-like C2-type 6.
+At position 605 to 703, the domain is characterized as Fibronectin type-III 1.
+At position 708 to 805, the domain is characterized as Fibronectin type-III 2.
+At position 810 to 907, the domain is characterized as Fibronectin type-III 3.
+At position 911 to 1003, the domain is characterized as Fibronectin type-III 4.
+At position 29 to 195, the domain is characterized as FAD-binding PCMH-type.
+At position 14 to 321, the domain is characterized as Peptidase A1.
+At position 664 to 739, the domain is characterized as ACT.
+At position 66 to 134, the domain is characterized as POTRA.
+At position 350 to 426, the domain is characterized as ACT.
+At position 196 to 274, the domain is characterized as RRM.
+At position 47 to 159, the domain is characterized as Ig-like C2-type 1.
+At position 1345 to 1530, the domain is characterized as PIK helical.
+At position 1617 to 1884, the domain is characterized as PI3K/PI4K catalytic.
+At position 547 to 687, the domain is characterized as SET.
+At position 696 to 712, the domain is characterized as Post-SET.
+At position 831 to 850, the domain is characterized as UIM.
+At position 100 to 351, the domain is characterized as Protein kinase.
+At position 70 to 179, the domain is characterized as Cadherin 1.
+At position 180 to 295, the domain is characterized as Cadherin 2.
+At position 296 to 411, the domain is characterized as Cadherin 3.
+At position 412 to 528, the domain is characterized as Cadherin 4.
+At position 529 to 643, the domain is characterized as Cadherin 5.
+At position 824 to 927, the domain is characterized as Cadherin 6.
+At position 928 to 1087, the domain is characterized as Cadherin 7.
+At position 1171 to 1284, the domain is characterized as Cadherin 8.
+At position 1285 to 1389, the domain is characterized as Cadherin 9.
+At position 1411 to 1520, the domain is characterized as Cadherin 10.
+At position 1534 to 1660, the domain is characterized as Cadherin 11.
+At position 1661 to 1774, the domain is characterized as Cadherin 12.
+At position 1 to 126, the domain is characterized as ADF-H.
+At position 127 to 303, the domain is characterized as Tyr recombinase.
+At position 137 to 366, the domain is characterized as Radical SAM core.
+At position 107 to 258, the domain is characterized as N-acetyltransferase.
+At position 125 to 440, the domain is characterized as IF rod.
+At position 25 to 125, the domain is characterized as SSB.
+At position 1 to 211, the domain is characterized as Radical SAM core.
+At position 459 to 598, the domain is characterized as Thioredoxin.
+At position 127 to 403, the domain is characterized as Peptidase S8.
+At position 355 to 636, the domain is characterized as USP.
+At position 153 to 347, the domain is characterized as Histidine kinase.
+At position 22 to 128, the domain is characterized as Ig-like 1.
+At position 152 to 239, the domain is characterized as CBM-cenC.
+At position 322 to 529, the domain is characterized as MCM.
+At position 193 to 263, the domain is characterized as EB1 C-terminal.
+At position 14 to 247, the domain is characterized as ABC transporter.
+At position 479 to 822, the domain is characterized as Kinesin motor.
+At position 22 to 137, the domain is characterized as Rhodanese.
+At position 158 to 300, the domain is characterized as Tyrosine-protein phosphatase.
+At position 26 to 62, the domain is characterized as LRRNT.
+At position 140 to 190, the domain is characterized as LRRCT.
+At position 7 to 666, the domain is characterized as Myosin motor.
+At position 704 to 892, the domain is characterized as TH1.
+At position 976 to 1035, the domain is characterized as SH3.
+At position 295 to 337, the domain is characterized as EGF-like 1.
+At position 601 to 641, the domain is characterized as EGF-like 2.
+At position 902 to 942, the domain is characterized as EGF-like 3.
+At position 1213 to 1254, the domain is characterized as EGF-like 4.
+At position 1258 to 1296, the domain is characterized as LDL-receptor class A 1.
+At position 1297 to 1333, the domain is characterized as LDL-receptor class A 2.
+At position 1335 to 1371, the domain is characterized as LDL-receptor class A 3.
+At position 17 to 139, the domain is characterized as PX.
+At position 532 to 609, the domain is characterized as Carrier.
+At position 90 to 219, the domain is characterized as GST C-terminal.
+At position 212 to 478, the domain is characterized as TrmE-type G.
+At position 92 to 457, the domain is characterized as PPM-type phosphatase.
+At position 14 to 271, the domain is characterized as Protein kinase.
+At position 276 to 303, the domain is characterized as PLD phosphodiesterase.
+At position 342 to 405, the domain is characterized as S4 RNA-binding.
+At position 570 to 669, the domain is characterized as PilZ.
+At position 17 to 192, the domain is characterized as FAD-binding PCMH-type.
+At position 448 to 538, the domain is characterized as Spaetzle.
+At position 39 to 148, the domain is characterized as WH1.
+At position 238 to 251, the domain is characterized as CRIB.
+At position 430 to 447, the domain is characterized as WH2.
+At position 35 to 66, the domain is characterized as IQ 1.
+At position 175 to 206, the domain is characterized as IQ 2.
+At position 225 to 254, the domain is characterized as IQ 3.
+At position 248 to 277, the domain is characterized as IQ 4.
+At position 321 to 350, the domain is characterized as IQ 5.
+At position 344 to 375, the domain is characterized as IQ 6.
+At position 394 to 423, the domain is characterized as IQ 7.
+At position 417 to 446, the domain is characterized as IQ 8.
+At position 467 to 496, the domain is characterized as IQ 9.
+At position 490 to 521, the domain is characterized as IQ 10.
+At position 563 to 594, the domain is characterized as IQ 11.
+At position 613 to 642, the domain is characterized as IQ 12.
+At position 636 to 667, the domain is characterized as IQ 13.
+At position 686 to 717, the domain is characterized as IQ 14.
+At position 709 to 740, the domain is characterized as IQ 15.
+At position 759 to 790, the domain is characterized as IQ 16.
+At position 832 to 863, the domain is characterized as IQ 17.
+At position 855 to 886, the domain is characterized as IQ 18.
+At position 904 to 935, the domain is characterized as IQ 19.
+At position 927 to 958, the domain is characterized as IQ 20.
+At position 977 to 1006, the domain is characterized as IQ 21.
+At position 1000 to 1031, the domain is characterized as IQ 22.
+At position 1050 to 1081, the domain is characterized as IQ 23.
+At position 1123 to 1154, the domain is characterized as IQ 24.
+At position 1259 to 1288, the domain is characterized as IQ 25.
+At position 1282 to 1313, the domain is characterized as IQ 26.
+At position 1332 to 1361, the domain is characterized as IQ 27.
+At position 1408 to 1439, the domain is characterized as IQ 28.
+At position 1456 to 1487, the domain is characterized as IQ 29.
+At position 1506 to 1527, the domain is characterized as IQ 30.
+At position 381 to 811, the domain is characterized as Ketosynthase family 3 (KS3).
+At position 1295 to 1603, the domain is characterized as PKS/mFAS DH.
+At position 1670 to 1747, the domain is characterized as Carrier.
+At position 35 to 172, the domain is characterized as MPN.
+At position 362 to 419, the domain is characterized as HTH myb-type.
+At position 128 to 273, the domain is characterized as SGF29 C-terminal.
+At position 43 to 234, the domain is characterized as Helicase ATP-binding.
+At position 266 to 416, the domain is characterized as Helicase C-terminal.
+At position 135 to 214, the domain is characterized as PAN 1.
+At position 281 to 369, the domain is characterized as PAN 2.
+At position 378 to 465, the domain is characterized as PAN 3.
+At position 260 to 397, the domain is characterized as MPN.
+At position 109 to 336, the domain is characterized as MAGE.
+At position 133 to 194, the domain is characterized as BCNT-C.
+At position 76 to 148, the domain is characterized as S4 RNA-binding.
+At position 173 to 341, the domain is characterized as cDENN.
+At position 343 to 594, the domain is characterized as dDENN.
+At position 172 to 239, the domain is characterized as Chitin-binding type R&R.
+At position 88 to 262, the domain is characterized as FAD-binding PCMH-type.
+At position 376 to 433, the domain is characterized as CBS 1.
+At position 437 to 488, the domain is characterized as CBS 2.
+At position 157 to 331, the domain is characterized as PXA.
+At position 363 to 495, the domain is characterized as RGS.
+At position 588 to 708, the domain is characterized as PX.
+At position 6 to 328, the domain is characterized as Kinesin motor.
+At position 309 to 518, the domain is characterized as Helicase ATP-binding.
+At position 655 to 818, the domain is characterized as Helicase C-terminal.
+At position 72 to 195, the domain is characterized as Cupin type-1.
+At position 198 to 376, the domain is characterized as DH.
+At position 405 to 512, the domain is characterized as PH.
+At position 586 to 652, the domain is characterized as SH3 1.
+At position 673 to 767, the domain is characterized as SH2.
+At position 816 to 877, the domain is characterized as SH3 2.
+At position 200 to 470, the domain is characterized as Protein kinase.
+At position 23 to 65, the domain is characterized as CAP-Gly.
+At position 255 to 547, the domain is characterized as PI3K/PI4K catalytic.
+At position 932 to 1065, the domain is characterized as MGS-like.
+At position 1 to 173, the domain is characterized as FAD-binding PCMH-type.
+At position 7 to 215, the domain is characterized as YjeF N-terminal.
+At position 185 to 360, the domain is characterized as Helicase ATP-binding.
+At position 386 to 534, the domain is characterized as Helicase C-terminal.
+At position 330 to 505, the domain is characterized as Helicase C-terminal.
+At position 64 to 376, the domain is characterized as PPM-type phosphatase.
+At position 30 to 127, the domain is characterized as Ig-like C2-type 1.
+At position 219 to 326, the domain is characterized as Ig-like C2-type 3.
+At position 140 to 456, the domain is characterized as IF rod.
+At position 3 to 255, the domain is characterized as Chorismate mutase.
+At position 35 to 289, the domain is characterized as CoA carboxyltransferase C-terminal.
+At position 1 to 25, the domain is characterized as Alpha-carbonic anhydrase.
+At position 208 to 332, the domain is characterized as NlpC/P60.
+At position 1087 to 1337, the domain is characterized as Glutamine amidotransferase type-1.
+At position 127 to 158, the domain is characterized as EF-hand 4.
+At position 170 to 483, the domain is characterized as IF rod.
+At position 1 to 142, the domain is characterized as N-acetyltransferase.
+At position 20 to 115, the domain is characterized as PPIase FKBP-type.
+At position 227 to 319, the domain is characterized as RRM.
+At position 11 to 235, the domain is characterized as Radical SAM core.
+At position 355 to 546, the domain is characterized as E2.
+At position 1 to 59, the domain is characterized as HTH myb-type 1.
+At position 62 to 109, the domain is characterized as HTH myb-type 2.
+At position 250 to 352, the domain is characterized as Ig-like V-type 3.
+At position 364 to 458, the domain is characterized as Ig-like V-type 4.
+At position 462 to 561, the domain is characterized as Ig-like V-type 5.
+At position 735 to 764, the domain is characterized as IQ 1.
+At position 783 to 812, the domain is characterized as IQ 3.
+At position 806 to 835, the domain is characterized as IQ 4.
+At position 831 to 860, the domain is characterized as IQ 5.
+At position 854 to 883, the domain is characterized as IQ 6.
+At position 1146 to 1447, the domain is characterized as Dilute.
+At position 123 to 229, the domain is characterized as Rieske.
+At position 39 to 158, the domain is characterized as RGS.
+At position 201 to 366, the domain is characterized as Helicase ATP-binding.
+At position 941 to 1002, the domain is characterized as SANT 2.
+At position 2 to 190, the domain is characterized as CNNM transmembrane.
+At position 208 to 268, the domain is characterized as CBS 1.
+At position 273 to 333, the domain is characterized as CBS 2.
+At position 308 to 557, the domain is characterized as Glutamine amidotransferase type-1.
+At position 190 to 393, the domain is characterized as TR mART core.
+At position 35 to 115, the domain is characterized as Ubiquitin-like.
+At position 122 to 357, the domain is characterized as NR LBD.
+At position 110 to 350, the domain is characterized as Radical SAM core.
+At position 24 to 117, the domain is characterized as LCCL.
+At position 162 to 347, the domain is characterized as VWFA 1.
+At position 364 to 534, the domain is characterized as VWFA 2.
+At position 10 to 221, the domain is characterized as HD Cas3-type.
+At position 62 to 348, the domain is characterized as PPM-type phosphatase.
+At position 157 to 217, the domain is characterized as SAM.
+At position 795 to 941, the domain is characterized as VPS9.
+At position 303 to 738, the domain is characterized as FH2.
+At position 328 to 382, the domain is characterized as EGF-like.
+At position 456 to 544, the domain is characterized as Ig-like C2-type 4.
+At position 547 to 638, the domain is characterized as Ig-like C2-type 5.
+At position 645 to 751, the domain is characterized as Fibronectin type-III 1.
+At position 756 to 853, the domain is characterized as Fibronectin type-III 2.
+At position 858 to 957, the domain is characterized as Fibronectin type-III 3.
+At position 961 to 1055, the domain is characterized as Fibronectin type-III 4.
+At position 1059 to 1154, the domain is characterized as Fibronectin type-III 5.
+At position 1159 to 1254, the domain is characterized as Fibronectin type-III 6.
+At position 1259 to 1359, the domain is characterized as Fibronectin type-III 7.
+At position 1363 to 1457, the domain is characterized as Fibronectin type-III 8.
+At position 1463 to 1566, the domain is characterized as Fibronectin type-III 9.
+At position 1571 to 1671, the domain is characterized as Fibronectin type-III 10.
+At position 1673 to 1775, the domain is characterized as Fibronectin type-III 11.
+At position 1776 to 1872, the domain is characterized as Fibronectin type-III 12.
+At position 1873 to 2004, the domain is characterized as Fibronectin type-III 13.
+At position 105 to 206, the domain is characterized as RRM 1.
+At position 228 to 310, the domain is characterized as RRM 2.
+At position 22 to 309, the domain is characterized as ABC transporter.
+At position 1 to 114, the domain is characterized as Plastocyanin-like 1.
+At position 124 to 279, the domain is characterized as Plastocyanin-like 2.
+At position 389 to 523, the domain is characterized as Plastocyanin-like 3.
+At position 246 to 442, the domain is characterized as PCI.
+At position 37 to 181, the domain is characterized as RUN.
+At position 658 to 781, the domain is characterized as PX.
+At position 32 to 112, the domain is characterized as GS beta-grasp.
+At position 119 to 369, the domain is characterized as GS catalytic.
+At position 77 to 366, the domain is characterized as ABC transmembrane type-1 1.
+At position 401 to 637, the domain is characterized as ABC transporter 1.
+At position 1030 to 1266, the domain is characterized as ABC transporter 2.
+At position 104 to 334, the domain is characterized as Radical SAM core.
+At position 16 to 94, the domain is characterized as EH.
+At position 51 to 84, the domain is characterized as EF-hand 2.
+At position 194 to 430, the domain is characterized as Dynamin-type G.
+At position 181 to 248, the domain is characterized as PUB.
+At position 349 to 433, the domain is characterized as UBX.
+At position 241 to 403, the domain is characterized as Helicase C-terminal.
+At position 145 to 211, the domain is characterized as Ig-like C2-type.
+At position 183 to 380, the domain is characterized as ATP-grasp.
+At position 578 to 735, the domain is characterized as N-acetyltransferase.
+At position 712 to 764, the domain is characterized as GPS.
+At position 107 to 206, the domain is characterized as BMC circularly permuted 2.
+At position 704 to 904, the domain is characterized as Helicase ATP-binding.
+At position 1067 to 1232, the domain is characterized as Helicase C-terminal.
+At position 97 to 199, the domain is characterized as DUSP.
+At position 364 to 1110, the domain is characterized as USP.
+At position 274 to 486, the domain is characterized as Ku.
+At position 613 to 647, the domain is characterized as SAP.
+At position 79 to 158, the domain is characterized as RRM 1.
+At position 365 to 441, the domain is characterized as RRM 2.
+At position 30 to 314, the domain is characterized as Protein kinase.
+At position 392 to 648, the domain is characterized as PPM-type phosphatase.
+At position 27 to 67, the domain is characterized as LRRNT 1.
+At position 320 to 361, the domain is characterized as LRRNT 2.
+At position 517 to 568, the domain is characterized as LRRCT 2.